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Conserved domains on  [gi|72534838|ref|NP_689973|]
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sorting nexin-32 [Homo sapiens]

Protein Classification

PX and BAR domain-containing protein( domain architecture ID 10246349)

PX (Phox homology) and BAR (Bin/Amphiphysin/Rvs) domain-containing protein, similar to sorting nexins that are involved in regulating membrane traffic and protein sorting in the endosomal system

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR_SNX5_6 cd07621
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6; BAR domains are dimerization, ...
 180-400 1.19e-128

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Members of this subfamily include SNX5, SNX6, the mammalian SNX32, and similar proteins. SNX5 and SNX6 may be components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. The function of SNX32 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


:

Pssm-ID: 153305  Cd Length: 219  Bit Score: 369.35  E-value: 1.19e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 180 GFLRNIVKSADEALItgMSGLKEVDDFFEHERTFLLEYHTRIRDACLRADRVMRAHKCLADDYIPISAALSSLGTQEVNQ 259
Cdd:cd07621   1 GFLKSISKSADEELL--LSGQKDVDEFFEQEKNFLVEYHNRIKDATAKADKMTRKHKDVADSYIKISAALTQLATSEPTP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 260 LRTSFLKLAELFERLRKLEGRVASDEDLKLSDMLRYYMRDSQAAKDLLYRRLRALADYENANKALDKARTRNREVRPAES 339
Cdd:cd07621  79 LDKFLLKVAETFEKLRKLEGRVASDEDLKLSDTLRYYMRDTQAAKDLLYRRLRCLANYENANKNLEKARAKNKDVHAAEA 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 72534838 340 HQQLCCQRFERLSDSAKQELMDFKSRRVSSFRKNLIELAELELKHAKASTLILRNTLVALK 400
Cdd:cd07621 159 AQQEACEKFESMSESAKQELLDFKTRRVAAFRKNLVELAELEIKHAKAQIQLLKNCLAALK 219
PX_domain super family cl02563
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 25-163 3.43e-85

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


The actual alignment was detected with superfamily member cd07291:

Pssm-ID: 470617  Cd Length: 141  Bit Score: 255.76  E-value: 3.43e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838  25 SLQVEISDAVSERDKVKFTVQTKSCLPHFAQTEFSVVRQHEEFIWLHDAYVENEEYAGLIIPPAPPRPDFEASREKLQKL 104
Cdd:cd07291   2 SLQIDIPDALSERDKVKFTVHTKTTLPSFQSPDFSVTRQHEDFIWLHDALIETEDYAGLIIPPAPPKPDFDGPREKMQKL 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 72534838 105 GEGDSSVTREEFAKMKQELEAEYLAIFKKTVAMHEVFLQRLAAHPTLRRDHNFFVFLEY 163
Cdd:cd07291  82 GEGEGSMTKEEFAKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPSLSKDRNFHIFLEY 140
 
Name Accession Description Interval E-value
BAR_SNX5_6 cd07621
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6; BAR domains are dimerization, ...
 180-400 1.19e-128

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Members of this subfamily include SNX5, SNX6, the mammalian SNX32, and similar proteins. SNX5 and SNX6 may be components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. The function of SNX32 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153305  Cd Length: 219  Bit Score: 369.35  E-value: 1.19e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 180 GFLRNIVKSADEALItgMSGLKEVDDFFEHERTFLLEYHTRIRDACLRADRVMRAHKCLADDYIPISAALSSLGTQEVNQ 259
Cdd:cd07621   1 GFLKSISKSADEELL--LSGQKDVDEFFEQEKNFLVEYHNRIKDATAKADKMTRKHKDVADSYIKISAALTQLATSEPTP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 260 LRTSFLKLAELFERLRKLEGRVASDEDLKLSDMLRYYMRDSQAAKDLLYRRLRALADYENANKALDKARTRNREVRPAES 339
Cdd:cd07621  79 LDKFLLKVAETFEKLRKLEGRVASDEDLKLSDTLRYYMRDTQAAKDLLYRRLRCLANYENANKNLEKARAKNKDVHAAEA 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 72534838 340 HQQLCCQRFERLSDSAKQELMDFKSRRVSSFRKNLIELAELELKHAKASTLILRNTLVALK 400
Cdd:cd07621 159 AQQEACEKFESMSESAKQELLDFKTRRVAAFRKNLVELAELEIKHAKAQIQLLKNCLAALK 219
PX_SNX5 cd07291
The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a ...
 25-163 3.43e-85

The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. The PX domain of SNX5 binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,4)P2. SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels.


Pssm-ID: 132824  Cd Length: 141  Bit Score: 255.76  E-value: 3.43e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838  25 SLQVEISDAVSERDKVKFTVQTKSCLPHFAQTEFSVVRQHEEFIWLHDAYVENEEYAGLIIPPAPPRPDFEASREKLQKL 104
Cdd:cd07291   2 SLQIDIPDALSERDKVKFTVHTKTTLPSFQSPDFSVTRQHEDFIWLHDALIETEDYAGLIIPPAPPKPDFDGPREKMQKL 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 72534838 105 GEGDSSVTREEFAKMKQELEAEYLAIFKKTVAMHEVFLQRLAAHPTLRRDHNFFVFLEY 163
Cdd:cd07291  82 GEGEGSMTKEEFAKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPSLSKDRNFHIFLEY 140
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
 201-386 4.10e-12

Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.


Pssm-ID: 430527 [Multi-domain]  Cd Length: 236  Bit Score: 65.38  E-value: 4.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838   201 KEVDDFFEHERTFLLEYHTRIRDACLRADRVMRAHKCLADDYIPISAALSSLGTQEVNQLRTSFL-KLAELFERLRKLEG 279
Cdd:pfam09325  20 NEPDEWFIDKKQYIDSLESQLKKLYKALELLVSQRKELASATGEFAKSLASLASLELSTGLSRALsQLAEVEERIKELLE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838   280 RVASDEDLKLSDMLRYYMRDSQAAKDLLYRRLRALADYENANKALDKARTR------------------NREVRPAESHQ 341
Cdd:pfam09325 100 RQALQDVLTLGETIDEYLRLIGSVKAVFNQRVKAWQSWQNAEQELSKKKEQlekllranksqndklqqaKKEVEELERRV 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 72534838   342 QLCCQRFERLSDSAKQELMDFKSRRVSSFRKNLIELAELELKHAK 386
Cdd:pfam09325 180 QQAEKEFEDISELIKKELERFELERVDDFKNSVEIYLESAIESQK 224
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 50-163 1.80e-10

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 56.87  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838    50 LPHFAQTEFSVVRQHEEFIWLHDAYVENeeYAGLIIPPAPPRPDFeasreklqklgegdsSVTREEFAkmkqeleaeyla 129
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRK--FPSVIIPPLPPKRWL---------------GRYNEEFI------------ 51

                          90       100       110
                  ....*....|....*....|....*....|....
gi 72534838   130 ifKKTVAMHEVFLQRLAAHPTLRRDHNFFVFLEY 163
Cdd:pfam00787  52 --EKRRKGLEQYLQRLLQHPELRNSEVLLEFLES 83
 
Name Accession Description Interval E-value
BAR_SNX5_6 cd07621
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6; BAR domains are dimerization, ...
 180-400 1.19e-128

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Members of this subfamily include SNX5, SNX6, the mammalian SNX32, and similar proteins. SNX5 and SNX6 may be components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. The function of SNX32 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153305  Cd Length: 219  Bit Score: 369.35  E-value: 1.19e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 180 GFLRNIVKSADEALItgMSGLKEVDDFFEHERTFLLEYHTRIRDACLRADRVMRAHKCLADDYIPISAALSSLGTQEVNQ 259
Cdd:cd07621   1 GFLKSISKSADEELL--LSGQKDVDEFFEQEKNFLVEYHNRIKDATAKADKMTRKHKDVADSYIKISAALTQLATSEPTP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 260 LRTSFLKLAELFERLRKLEGRVASDEDLKLSDMLRYYMRDSQAAKDLLYRRLRALADYENANKALDKARTRNREVRPAES 339
Cdd:cd07621  79 LDKFLLKVAETFEKLRKLEGRVASDEDLKLSDTLRYYMRDTQAAKDLLYRRLRCLANYENANKNLEKARAKNKDVHAAEA 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 72534838 340 HQQLCCQRFERLSDSAKQELMDFKSRRVSSFRKNLIELAELELKHAKASTLILRNTLVALK 400
Cdd:cd07621 159 AQQEACEKFESMSESAKQELLDFKTRRVAAFRKNLVELAELEIKHAKAQIQLLKNCLAALK 219
BAR_SNX5 cd07663
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 5; BAR domains are dimerization, lipid ...
 180-400 1.71e-96

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 5; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153347  Cd Length: 218  Bit Score: 287.60  E-value: 1.71e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 180 GFLRNIVKSADEALItgmSGLKEVDDFFEHERTFLLEYHTRIRDACLRADRVMRAHKCLADDYIPISAALSSLGTQEVNQ 259
Cdd:cd07663   1 GFFKNMVKSADEVLF---SGVKEVDEFFEQEKTFLVNYYNRIKDSCAKADKMTRSHKNVADDYIHISAALNSVAAEEPTV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 260 LRTSFLKLAELFERLRKLEGRVASDEDLKLSDMLRYYMRDSQAAKDLLYRRLRALADYENANKALDKARTRNREVRPAES 339
Cdd:cd07663  78 IKKYLLKVAELFEKLRKVEDRVASDQDLKLTELLRYYMLNIEAAKDLLYRRARALADYENSNKALDKARLKSKDVKQAEA 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 72534838 340 HQQLCCQRFERLSDSAKQELMDFKSRRVSSFRKNLIELAELELKHAKASTLILRNTLVALK 400
Cdd:cd07663 158 HQQECCQKFEKLSESAKQELISFKRRRVAAFRKNLIEMTELEIKHAKNNVSLLQSCIDLFK 218
BAR_SNX6 cd07662
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; BAR domains are dimerization, lipid ...
 181-400 1.17e-93

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153346  Cd Length: 218  Bit Score: 280.39  E-value: 1.17e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 181 FLRNIVKSADEALItgmSGLKEVDDFFEHERTFLLEYHTRIRDACLRADRVMRAHKCLADDYIPISAALSSLGTQEVNQL 260
Cdd:cd07662   2 FFKNVVKSADGVIV---SGVKDVDDFFEHERTFLLEYHNRVKDSSAKSDRMTRSHKSAADDYNRIGSSLYTLGTQDSTDI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 261 RTSFLKLAELFERLRKLEGRVASDEDLKLSDMLRYYMRDSQAAKDLLYRRLRALADYENANKALDKARTRNREVRPAESH 340
Cdd:cd07662  79 CKFFLKVSELFDKTRKIEARVAADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETT 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 341 QQLCCQRFERLSDSAKQELMDFKSRRVSSFRKNLIELAELELKHAKASTLILRNTLVALK 400
Cdd:cd07662 159 QQLCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQSCLAVLN 218
PX_SNX5 cd07291
The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a ...
 25-163 3.43e-85

The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. The PX domain of SNX5 binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,4)P2. SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels.


Pssm-ID: 132824  Cd Length: 141  Bit Score: 255.76  E-value: 3.43e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838  25 SLQVEISDAVSERDKVKFTVQTKSCLPHFAQTEFSVVRQHEEFIWLHDAYVENEEYAGLIIPPAPPRPDFEASREKLQKL 104
Cdd:cd07291   2 SLQIDIPDALSERDKVKFTVHTKTTLPSFQSPDFSVTRQHEDFIWLHDALIETEDYAGLIIPPAPPKPDFDGPREKMQKL 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 72534838 105 GEGDSSVTREEFAKMKQELEAEYLAIFKKTVAMHEVFLQRLAAHPTLRRDHNFFVFLEY 163
Cdd:cd07291  82 GEGEGSMTKEEFAKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPSLSKDRNFHIFLEY 140
PX_SNX5_like cd06892
The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 6; The PX domain is ...
 24-163 1.01e-84

The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 6; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Members of this subfamily include SNX5, SNX6, and similar proteins. They contain a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. SNX5 and SNX6 may be components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p.


Pssm-ID: 132802  Cd Length: 141  Bit Score: 254.67  E-value: 1.01e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838  24 SSLQVEISDAVSERDKVKFTVQTKSCLPHFAQTEFSVVRQHEEFIWLHDAYVENEEYAGLIIPPAPPRPDFEASREKLQK 103
Cdd:cd06892   1 SSLQVDISDALSERDKVKFTVHTKTTLPTFQKPEFSVTRQHEEFVWLHDTLVENEDYAGLIIPPAPPKPDFDASREKLQK 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 104 LGEGDSSVTREEFAKMKQELEAEYLAIFKKTVAMHEVFLQRLAAHPTLRRDHNFFVFLEY 163
Cdd:cd06892  81 LGEGEGSMTKEEFEKMKQELEAEYLAIFKKTVAMHEVFLRRLASHPVLRNDANFRVFLEY 140
PX_SNX6 cd07292
The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; The PX domain is a ...
 24-163 1.22e-78

The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). SNX6 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs.


Pssm-ID: 132825  Cd Length: 141  Bit Score: 238.85  E-value: 1.22e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838  24 SSLQVEISDAVSERDKVKFTVQTKSCLPHFAQTEFSVVRQHEEFIWLHDAYVENEEYAGLIIPPAPPRPDFEASREKLQK 103
Cdd:cd07292   1 AALQVDISDALSERDKVKFTVHTKSSLPNFKQNEFSVVRQHEEFIWLHDSFVENEDYAGYIIPPAPPRPDFDASREKLQK 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 104 LGEGDSSVTREEFAKMKQELEAEYLAIFKKTVAMHEVFLQRLAAHPTLRRDHNFFVFLEY 163
Cdd:cd07292  81 LGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEY 140
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 202-396 1.95e-24

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 100.12  E-value: 1.95e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 202 EVDDFFEHERTFLLEYHTRIRDACLRADRVMRAHKCLADDYIPISAALSSLGTQEVNQ---LRTSFLKLAELFERLRKLE 278
Cdd:cd07596   1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEEVggeLGEALSKLGKAAEELSSLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 279 GRVASDEDLKLSDMLRYYMRDSQAAKDLLYRRLRALADYENANKALDKARTR------------------NREVRPAESH 340
Cdd:cd07596  81 EAQANQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQleklkaapgikpakveelEEELEEAESA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 72534838 341 QQLCCQRFERLSDSAKQELMDFKSRRVSSFRKNLIELAELELKHAKASTLILRNTL 396
Cdd:cd07596 161 LEEARKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESLL 216
BAR_SNX_like cd07630
The Bin/Amphiphysin/Rvs (BAR) domain of uncharacterized Sorting Nexins; BAR domains are ...
 202-386 7.75e-22

The Bin/Amphiphysin/Rvs (BAR) domain of uncharacterized Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of uncharacterized proteins with similarity to sorting nexins (SNXs), which are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153314  Cd Length: 198  Bit Score: 92.18  E-value: 7.75e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 202 EVDDFFEHERTFLLEYHTRIRDACLRADRVMRAHKCLADDYIPISAALSSLGTQE---VNQLRTSFLKLAELFERLRKLE 278
Cdd:cd07630   1 DVDEFFQKERDMNTKLSANMKEAAEKFLKIVNTEQRLANALGHLSSSLQLCVGLDeasVVALNRLCTKLSEALEEAKENI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 279 GRVASDEDLKLSDMLRYYMRDSQAAKDLLYRRLRALADYENANKALDKARTRNREVrpAESHQQLCCQRFERLSDSAKQE 358
Cdd:cd07630  81 EVVAGNNENTLGLTLDLYSRYSESEKDMLFRRTCKLIEFENASKALEKAKPQKKEQ--AEEAKKKAETEFEEISSLAKKE 158

                       170       180
                ....*....|....*....|....*...
gi 72534838 359 LMDFKSRRVSSFRKNLIELAELELKHAK 386
Cdd:cd07630 159 LERFHRQRVLELQSALVCYAESQIKNAK 186
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
 26-162 1.12e-18

The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.


Pssm-ID: 132769 [Multi-domain]  Cd Length: 114  Bit Score: 81.09  E-value: 1.12e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838  26 LQVEISDAVSERDKVK----FTVQTKSCLPHFAQTEFSVVRQHEEFIWLHDAYVENeeYAGLIIPPAPprpdfeasrEKl 101
Cdd:cd06859   1 FEISVTDPVKVGDGMSayvvYRVTTKTNLPDFKKSEFSVLRRYSDFLWLYERLVEK--YPGRIVPPPP---------EK- 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 72534838 102 qklgegdSSVTReefAKMKQELeaeylaIFKKTVAMhEVFLQRLAAHPTLRRDHNFFVFLE 162
Cdd:cd06859  69 -------QAVGR---FKVKFEF------IEKRRAAL-ERFLRRIAAHPVLRKDPDFRLFLE 112
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
 26-162 2.33e-14

The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX2 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. Similar to SNX1, SNX2 contains a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX domain of SNX2 preferentially binds phosphatidylinositol-3-phosphate (PI3P), but not PI(3,4,5)P3. Studies on mice deficient with SNX1 and/or SNX2 suggest that they provide an essential function in embryogenesis and are functionally redundant.


Pssm-ID: 132815  Cd Length: 124  Bit Score: 69.31  E-value: 2.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838  26 LQVEISDAVSERDKVK----FTVQTKSCLPHFAQTEFSVVRQHEEFIWLHDAYVENEEYAGLIIPPAPPRPDFEASRekl 101
Cdd:cd07282   1 IEIGVSDPEKVGDGMNaymaYRVTTKTSLSMFSRSEFSVRRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVGMTK--- 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 72534838 102 QKLGEGDSSVTreEFAKmkqeleaeylaifKKTVAMhEVFLQRLAAHPTLRRDHNFFVFLE 162
Cdd:cd07282  78 VKVGKEDSSST--EFVE-------------KRRAAL-ERYLQRTVKHPTLLQDPDLRQFLE 122
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
 40-162 2.93e-13

The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. The PX domain of Vps5p binds phosphatidylinositol-3-phosphate (PI3P). Similar to SNX1, Vps5p contains a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1.


Pssm-ID: 132771  Cd Length: 112  Bit Score: 65.84  E-value: 2.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838  40 VKFTVQTKSCLPHFAQTEFSVVRQHEEFIWLHDAYVENeeYAGLIIPPAPprpdfeasrEKlQKLGEGDssvtrEEFakm 119
Cdd:cd06861  19 TVYTVRTRTTSPNFEVSSFSVLRRYRDFRWLYRQLQNN--HPGVIVPPPP---------EK-QSVGRFD-----DNF--- 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 72534838 120 kqeLEAEYLAIfkktvamhEVFLQRLAAHPTLRRDHNFFVFLE 162
Cdd:cd06861  79 ---VEQRRAAL--------EKMLRKIANHPVLQKDPDFRLFLE 110
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
 201-386 4.10e-12

Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.


Pssm-ID: 430527 [Multi-domain]  Cd Length: 236  Bit Score: 65.38  E-value: 4.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838   201 KEVDDFFEHERTFLLEYHTRIRDACLRADRVMRAHKCLADDYIPISAALSSLGTQEVNQLRTSFL-KLAELFERLRKLEG 279
Cdd:pfam09325  20 NEPDEWFIDKKQYIDSLESQLKKLYKALELLVSQRKELASATGEFAKSLASLASLELSTGLSRALsQLAEVEERIKELLE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838   280 RVASDEDLKLSDMLRYYMRDSQAAKDLLYRRLRALADYENANKALDKARTR------------------NREVRPAESHQ 341
Cdd:pfam09325 100 RQALQDVLTLGETIDEYLRLIGSVKAVFNQRVKAWQSWQNAEQELSKKKEQlekllranksqndklqqaKKEVEELERRV 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 72534838   342 QLCCQRFERLSDSAKQELMDFKSRRVSSFRKNLIELAELELKHAK 386
Cdd:pfam09325 180 QQAEKEFEDISELIKKELERFELERVDDFKNSVEIYLESAIESQK 224
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 50-163 1.80e-10

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 56.87  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838    50 LPHFAQTEFSVVRQHEEFIWLHDAYVENeeYAGLIIPPAPPRPDFeasreklqklgegdsSVTREEFAkmkqeleaeyla 129
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRK--FPSVIIPPLPPKRWL---------------GRYNEEFI------------ 51

                          90       100       110
                  ....*....|....*....|....*....|....
gi 72534838   130 ifKKTVAMHEVFLQRLAAHPTLRRDHNFFVFLEY 163
Cdd:pfam00787  52 --EKRRKGLEQYLQRLLQHPELRNSEVLLEFLES 83
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
 40-162 5.66e-10

The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX1 is both membrane associated and a cytosolic protein that exists as a tetramer in protein complexes. It can associate reversibly with membranes of the endosomal compartment, thereby coating these vesicles. SNX1 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. SNX1 contains a Bin/Amphiphysin/Rvs (BAR) domain C-terminal to the PX domain. The PX domain of SNX1 specifically binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,5)P2, while the BAR domain detects membrane curvature. Both domains help determine the specific membrane-targeting of SNX1, which is localized to a microdomain in early endosomes where it regulates cation-independent mannose-6-phosphate receptor retrieval to the trans Golgi network.


Pssm-ID: 132814  Cd Length: 124  Bit Score: 56.61  E-value: 5.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838  40 VKFTVQTKSCLPHFAQTEFSVVRQHEEFIWLHDAYVENEEYAGLIIPPAPPRPDFEASReklQKLGEGDSSvtreefakm 119
Cdd:cd07281  19 VVYKVTTQTSLLMFRSKHFTVKRRFSDFLGLYEKLSEKHSQNGFIVPPPPEKSLIGMTK---VKVGKEDSS--------- 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 72534838 120 kqelEAEYLaifKKTVAMHEVFLQRLAAHPTLRRDHNFFVFLE 162
Cdd:cd07281  87 ----SAEFL---ERRRAALERYLQRIVSHPSLLQDPDVREFLE 122
PX_SNX7_30_like cd06860
The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is ...
 40-161 4.47e-09

The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. This subfamily consists of SNX7, SNX30, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of the sorting nexins in this subfamily has yet to be elucidated.


Pssm-ID: 132770  Cd Length: 116  Bit Score: 53.88  E-value: 4.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838  40 VKFTVQTKSCLPHFAQTEFSVVRQHEEFIWLHDAYVEneEYAGLIIPPAPprpdfeasrEKLQKLGEGDssvtreefaKM 119
Cdd:cd06860  19 ITYRVTTKTTRSEFDSSEYSVRRRYQDFLWLRQKLEE--SHPTHIIPPLP---------EKHSVKGLLD---------RF 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 72534838 120 KQE-LEAEYLAIFKktvamhevFLQRLAAHPTLRRDHNFFVFL 161
Cdd:cd06860  79 SPEfVATRMRALHK--------FLNRIVEHPVLSFNEHLKVFL 113
PX_Atg24p cd06863
The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation ...
 26-162 5.88e-09

The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation protein; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The yeast Atg24p is a sorting nexin (SNX) which is involved in membrane fusion events at the vacuolar surface during pexophagy. This is facilitated via binding of Atg24p to phosphatidylinositol 3-phosphate (PI3P) through its PX domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132773  Cd Length: 118  Bit Score: 53.83  E-value: 5.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838  26 LQVEISDAVSERDK-----VKFTVQTKSCLPHFAQTEFSVVRQHEEFIWLHDAYVenEEYAGLIIPPAPprpdfeaSREK 100
Cdd:cd06863   1 LECLVSDPQKELDGssdtyISYLITTKTNLPSFSRKEFKVRRRYSDFVFLHECLS--NDFPACVVPPLP-------DKHR 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 72534838 101 LQKLgEGDSsvTREEFakmkqeleaeylaIFKKTVAMHEvFLQRLAAHPTLRRDHNFFVFLE 162
Cdd:cd06863  72 LEYI-TGDR--FSPEF-------------ITRRAQSLQR-FLRRISLHPVLSQSKILHQFLE 116
PX_SNX_like cd06865
The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a ...
 41-161 1.09e-07

The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. This subfamily is composed of uncharacterized proteins, predominantly from plants, with similarity to sorting nexins. A few members show a similar domain architecture as a subfamily of sorting nexins, containing a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX-BAR structural unit is known to determine specific membrane localization.


Pssm-ID: 132775  Cd Length: 120  Bit Score: 50.11  E-value: 1.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838  41 KFTVQTKscLPHFAQTEFSVVRQHEEFIWLHDAYveNEEYAGLIIPPappRPDFEASREKLQKlgegdssvtREEFAKmk 120
Cdd:cd06865  27 KVTTRTN--IPSYTHGEFTVRRRFRDVVALADRL--AEAYRGAFVPP---RPDKSVVESQVMQ---------SAEFIE-- 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 72534838 121 qeleaeylaifKKTVAMhEVFLQRLAAHPTLRRDHNFFVFL 161
Cdd:cd06865  89 -----------QRRVAL-EKYLNRLAAHPVIGLSDELRVFL 117
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 27-162 4.18e-07

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


Pssm-ID: 132768 [Multi-domain]  Cd Length: 106  Bit Score: 48.12  E-value: 4.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838  27 QVEISDAVSERDK----VKFTVQTKSCLphfaQTEFSVVRQHEEFIWLHDAYVENeeYAGLIIPPAPPRPDFeasreklq 102
Cdd:cd06093   1 SVSIPDYEKVKDGgkkyVVYIIEVTTQG----GEEWTVYRRYSDFEELHEKLKKK--FPGVILPPLPPKKLF-------- 66

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 103 klgegdSSVTREEFAKMKQELEAeylaifkktvamhevFLQRLAAHPTLRRDHNFFVFLE 162
Cdd:cd06093  67 ------GNLDPEFIEERRKQLEQ---------------YLQSLLNHPELRNSEELKEFLE 105
PX_SNX7 cd07284
The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a ...
 40-161 7.17e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX7 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, SNX30, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of SNX7 has yet to be elucidated.


Pssm-ID: 132817  Cd Length: 116  Bit Score: 47.66  E-value: 7.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838  40 VKFTVQTKSCLPHFAQTEFSVVRQHEEFIWLHDAYveNEEYAGLIIPPAPPRPDFEASREKLQklgegdssvtrEEFAKM 119
Cdd:cd07284  19 ITYRVMTKTSRSEFDSSEFEVRRRYQDFLWLKGRL--EEAHPTLIIPPLPEKFVMKGMVERFN-----------EDFIET 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 72534838 120 KQEleaeylaifkktvAMHEvFLQRLAAHPTLRRDHNFFVFL 161
Cdd:cd07284  86 RRK-------------ALHK-FLNRIADHPTLTFNEDFKIFL 113
BAR_SNX1_2 cd07623
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, ...
 248-384 4.81e-06

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. This subfamily consists of SNX1, SNX2, and similar proteins. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153307  Cd Length: 224  Bit Score: 47.27  E-value: 4.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 248 ALSSLGTQEVNQ-LRTSFLKLAELFERLRKLEGRVASDEDLKLSDMLRYYMRDSQAAKDLLYRRLRALADYENANKALDK 326
Cdd:cd07623  55 SAAMLSNCEEHTsLSRALSQLAEVEEKIEQLHGEQADTDFYILAELLKDYIGLIGAIKDVFHERVKVWQNWQNAQQTLTK 134

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72534838 327 AR---TR-------------NREVRPAESHQQLCCQRFERLSDSAKQELMDFKSRRVSSFRKNLIELAELELKH 384
Cdd:cd07623 135 KReakAKlelsgrtdkldqaQQEIKEWEAKVDRGQKEFEEISKTIKKEIERFEKNRVKDFKDIIIKYLESLLNT 208
BAR_Vps5p cd07627
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ...
 202-374 3.25e-05

The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153311 [Multi-domain]  Cd Length: 216  Bit Score: 44.60  E-value: 3.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 202 EVDDFFEHERTFL--LEYHTRirdACLRA-DRVMRAHKCLADDYIPISAALSSLGTQEV-NQLRTSFLKLAELFERLRKL 277
Cdd:cd07627   1 EPDEWFIEKKQYLdsLESQLK---QLYKSlELVSSQRKELASATEEFAETLEALSSLELsKSLSDLLAALAEVQKRIKES 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 278 EGRVASDEDLKLSDMLRYYMRDSQAAKDLLYRRLRALADYENANKALDKARTR------------------NREVRPAES 339
Cdd:cd07627  78 LERQALQDVLTLGVTLDEYIRSIGSVRAAFAQRQKLWQYWQSAESELSKKKAQleklkrqgktqqeklnslLSELEEAER 157

                       170       180       190
                ....*....|....*....|....*....|....*
gi 72534838 340 HQQLCCQRFERLSDSAKQELMDFKSRRVSSFRKNL 374
Cdd:cd07627 158 RASELKKEFEEVSELIKSELERFERERVEDFRNSV 192
BAR_SNX1 cd07665
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 1; BAR domains are dimerization, lipid ...
 200-379 3.26e-05

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX1 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. SNX1 is localized to a microdomain in early endosomes where it regulates cation-independent mannose-6-phosphate receptor retrieval to the trans Golgi network. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153349 [Multi-domain]  Cd Length: 234  Bit Score: 45.06  E-value: 3.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 200 LKEVDDFFEHERTFLLEYHTRIRDACLRADRVMRAHKCLADDYIPISAALSSLGTQEVNQ-LRTSFLKLAELFERLRKLE 278
Cdd:cd07665  17 MNESDVWFEEKLQEVECEEQRLRKLHAVVETLVNHRKELALNTALFAKSLAMLGSSEDNTaLSRALSQLAEVEEKIEQLH 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 279 GRVASDEDLKLSDMLRYYMRDSQAAKDLLYRRLRALADYENANKAL----------------DKARTRNREVRPAESHQQ 342
Cdd:cd07665  97 QEQANNDFFLLAELLADYIRLLSAVRGAFDQRMKTWQRWQDAQAMLqkkreaearllwankpDKLQQAKDEIAEWESRVT 176

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 72534838 343 LCCQRFERLSDSAKQELMDFKSRRVSSFRKNLIELAE 379
Cdd:cd07665 177 QYERDFERISATVRKEVIRFEKEKSKDFKNHIIKYLE 213
BAR_SNX2 cd07664
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 2; BAR domains are dimerization, lipid ...
 185-379 3.18e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX2 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153348 [Multi-domain]  Cd Length: 234  Bit Score: 41.96  E-value: 3.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 185 IVKSADEALITGMSGLKEVDDFFEHERTFLLEYHTRIRDACLRADRVMRAHKCLADDYIPISAALSSLGTQEVNQ-LRTS 263
Cdd:cd07664   2 MVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQLRKLHASVESLVCHRKELSANTAAFAKSAAMLGNSEDHTaLSRA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838 264 FLKLAELFERLRKLEGRVASDEDLKLSDMLRYYMRDSQAAKDLLYRRLRALADYENANKAL----------------DKA 327
Cdd:cd07664  82 LSQLAEVEEKIDQLHQDQAFADFYLFSELLGDYIRLIAAVKGVFDQRMKCWQKWQDAQVTLqkkreaeaklqyankpDKL 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 72534838 328 RTRNREVRPAESHQQLCCQRFERLSDSAKQELMDFKSRRVSSFRKNLIELAE 379
Cdd:cd07664 162 QQAKDEIKEWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLE 213
PX_SNX3 cd07293
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3; The PX domain is a ...
 42-162 3.68e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 3; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX3 associates with early endosomes through a PX domain-mediated interaction with phosphatidylinositol-3-phosphate (PI3P). It associates with the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, and functions as a cargo-specific adaptor for the retromer. SNX3 is required for the formation of multivesicular bodies, which function as transport intermediates to late endosomes. It also promotes cell surface expression of the amiloride-sensitive epithelial Na+ channel (ENaC), which is critical in sodium homeostasis and maintenance of extracellular fluid volume.


Pssm-ID: 132826  Cd Length: 123  Bit Score: 37.28  E-value: 3.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534838  42 FTVQTKSCLPHFAQTEFSVVRQHEEFIWLHDayvENEEYAGLIIPPAPPRPDFEasreklQKLGEGDSSVTREEF-AKMK 120
Cdd:cd07293  22 YEIRLKTNLPIFKLKESTVRRRYSDFEWLRS---ELERESKVVVPPLPGKALFR------QLPFRGDDGIFDDSFiEERK 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 72534838 121 QELEAeylaifkktvamhevFLQRLAAHPTLRRDHNFFVFLE 162
Cdd:cd07293  93 QGLEQ---------------FLNKVAGHPLAQNERCLHMFLQ 119
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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