NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|5031581|ref|NP_005820|]
View 

AP-3 complex subunit sigma-2 [Homo sapiens]

Protein Classification

AP-3 complex subunit sigma( domain architecture ID 13000718)

AP-3 complex subunit sigma is part of the AP-3 complex that is associated with the Golgi region as well as more peripheral structures

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AP3_sigma cd14834
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ...
 1-146 6.30e-108

AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large delta-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-3 binds the coat protein clathrin and the phospholipid PI(3)P and it is localized in the endosome. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


:

Pssm-ID: 341438  Cd Length: 146  Bit Score: 305.31  E-value: 6.30e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031581    1 MIQAILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGGSLIGGSDYKLIYRHYATLYFVFCVDSS 80
Cdd:cd14834   1 MIKAILIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKRDDNVCNFLEGGSLIGGSDTKLIYRHYATLYFVFCVDSS 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031581   81 ESELGILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNR 146
Cdd:cd14834  81 ESELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHYILDEIVMGGMVLETNMTEILTAIEEQNK 146
 
Name Accession Description Interval E-value
AP3_sigma cd14834
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ...
 1-146 6.30e-108

AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large delta-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-3 binds the coat protein clathrin and the phospholipid PI(3)P and it is localized in the endosome. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341438  Cd Length: 146  Bit Score: 305.31  E-value: 6.30e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031581    1 MIQAILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGGSLIGGSDYKLIYRHYATLYFVFCVDSS 80
Cdd:cd14834   1 MIKAILIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKRDDNVCNFLEGGSLIGGSDTKLIYRHYATLYFVFCVDSS 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031581   81 ESELGILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNR 146
Cdd:cd14834  81 ESELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHYILDEIVMGGMVLETNMTEILTAIEEQNK 146
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
1-148 7.98e-57

Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];


Pssm-ID: 227363  Cd Length: 152  Bit Score: 176.06  E-value: 7.98e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031581    1 MIQAILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGgsliggSDYKLIYRHYATLYFVFCVDSS 80
Cdd:COG5030   1 MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIEG------KNEKIVYRRYATLYFVFGVDND 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031581   81 ESELGILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNRLE 148
Cdd:COG5030  75 DNELIILELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYALDAES 142
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
1-148 3.28e-55

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 171.77  E-value: 3.28e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031581      1 MIQAILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGgsliggSDYKLIYRHYATLYFVFCVDSS 80
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSNFIEF------NDLKVIYKRYATLYFVVIVDDQ 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031581     81 ESELGILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNRLE 148
Cdd:pfam01217  75 DNELIILELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVALLDELA 142
 
Name Accession Description Interval E-value
AP3_sigma cd14834
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ...
 1-146 6.30e-108

AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large delta-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-3 binds the coat protein clathrin and the phospholipid PI(3)P and it is localized in the endosome. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341438  Cd Length: 146  Bit Score: 305.31  E-value: 6.30e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031581    1 MIQAILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGGSLIGGSDYKLIYRHYATLYFVFCVDSS 80
Cdd:cd14834   1 MIKAILIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKRDDNVCNFLEGGSLIGGSDTKLIYRHYATLYFVFCVDSS 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031581   81 ESELGILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNR 146
Cdd:cd14834  81 ESELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHYILDEIVMGGMVLETNMTEILTAIEEQNK 146
AP_sigma cd14827
AP complex subunit sigma; AP complex sigma subunits are part of the heterotetrameric adaptor ...
 3-146 5.35e-67

AP complex subunit sigma; AP complex sigma subunits are part of the heterotetrameric adaptor protein (AP) complex which consists of one large subunit (alpha-, gamma-, delta- or epsilon), one beta-, one mu-, and one sigma-subunit. In general, AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In most cases the coat protein is clathrin (AP1 and AP2 complex), but some of the other members of the AP complex family are associated with nonclathrin coats. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341431  Cd Length: 138  Bit Score: 201.51  E-value: 5.35e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031581    3 QAILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGGsliggsDYKLIYRHYATLYFVFCVDSSES 82
Cdd:cd14827   1 RFILLFNRQGKTRLAKWYMQFDDDERQKLIEEIVQVVLSRDAKHCNFVEFR------NYKLIYRRYASLYFCICVDSNDN 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031581   83 ELGILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNR 146
Cdd:cd14827  75 ELAILEAIHNFVETLDKYFENVCELDLIFNFEKVYFIVDEMVLGGEIRETSQTKILKQIEMLDK 138
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
1-148 7.98e-57

Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];


Pssm-ID: 227363  Cd Length: 152  Bit Score: 176.06  E-value: 7.98e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031581    1 MIQAILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGgsliggSDYKLIYRHYATLYFVFCVDSS 80
Cdd:COG5030   1 MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIEG------KNEKIVYRRYATLYFVFGVDND 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031581   81 ESELGILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNRLE 148
Cdd:COG5030  75 DNELIILELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYALDAES 142
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
1-148 3.28e-55

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 171.77  E-value: 3.28e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031581      1 MIQAILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGgsliggSDYKLIYRHYATLYFVFCVDSS 80
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSNFIEF------NDLKVIYKRYATLYFVVIVDDQ 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031581     81 ESELGILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNRLE 148
Cdd:pfam01217  75 DNELIILELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVALLDELA 142
AP1_sigma cd14831
AP-1 complex subunit sigma; AP-1 complex sigma subunit is part of the heterotetrameric adaptor ...
 5-151 2.54e-48

AP-1 complex subunit sigma; AP-1 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large gamma-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-1 the coat protein is clathrin. AP-1 binds the phospholipid PI(4)P which plays a role in its localisation to the trans-Golgi network (TGN)/endosome. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341435  Cd Length: 143  Bit Score: 154.25  E-value: 2.54e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031581    5 ILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGgsliggSDYKLIYRHYATLYFVFCVDSSESEL 84
Cdd:cd14831   3 LLLFSRQGKVRLSKWYSAYSQKEKAKITREVSTLVLARKPKMCNFLEW------RDLKIVYKRYASLYFVCCVDKDDNEL 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031581   85 GILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNRLEKSE 151
Cdd:cd14831  77 ITLEIIHRYVEILDKYFGNVCELDIIFNFHKAYFILDELLLGGELQETSKKNVLRAIEAQDLLQEEE 143
AP2_sigma cd14833
AP-2 complex subunit sigma; AP-2 complex sigma subunit is part of the heterotetrameric adaptor ...
 1-147 2.04e-46

AP-2 complex subunit sigma; AP-2 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-2 complex which consists of one large alpha-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-2 the coat protein is clathrin. AP-2 binds the phospholipid PI(4,5)P2 which is important for its localisation to the plasma membrane. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341437  Cd Length: 141  Bit Score: 149.26  E-value: 2.04e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031581    1 MIQAILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGGSliggsdYKLIYRHYATLYFVFCVDSS 80
Cdd:cd14833   1 MIRFILIQNRQGKTRLAKWYVPYDDDEKQKLEEEVHRLVTSRDKKHTNFVEFRN------YKLVYRRYAGLFFCICVDVN 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031581   81 ESELGILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNRL 147
Cdd:cd14833  75 DNELAYLEAIHLFVEVLDEYFGNVCELDLVFNFYKVYAILDEMFLAGEIQETSKKVILERLKELDKL 141
AP4_sigma cd14832
AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor ...
 5-141 1.06e-42

AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large epsilon-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-4 does not bind the coat protein clathrin, it is associated with nonclathrin coats. Its phospholipid binding partner is unknown and it is localized in the trans-Golgi network (TGN). The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341436  Cd Length: 138  Bit Score: 139.68  E-value: 1.06e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031581    5 ILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGgsliggSDYKLIYRHYATLYFVFCVDSSESEL 84
Cdd:cd14832   3 ILMVNKQGQTRLAQYYEFLSIEERVALEGEIIRKCLSRSEKQCSFLEY------RGYKLVYRRYASLYFIVGVDEDENEL 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031581   85 GILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQI 141
Cdd:cd14832  77 AILEFIHNLVETLDKYFENVCELDIMFNLEKAHFILDEMVMNGCIVETNKSNILAPI 133
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
 4-138 4.18e-18

Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the heterotetrameric adaptor protein (AP) complex which consists of one large subunit (alpha-, gamma-, delta- or epsilon), one beta-, one mu-, and one sigma-subunit. In general, AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In most cases the coat protein is clathrin (AP1 and AP2 complex), but some of the other members of the AP complex family are associated with nonclathrin coats. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341427  Cd Length: 131  Bit Score: 76.40  E-value: 4.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031581    4 AILVFNNHGKPRLVRFYQRFPEEiQQQIVRETFHLVLKRDDNICNFLEGGSLiggsdyKLIYRHYATLYFVFCVDSSESE 83
Cdd:cd14823   2 AILVLDNDGKRLFAKYYDDTYPS-VKEQKAFEKNIFNKKHRTDSEIVLLEGL------RVVYKSSIDLYFVVIGSKNENE 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5031581   84 LGILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIV 138
Cdd:cd14823  75 LLLLEVLNCLVDVLSEYFRKVEERAILENFEGLYFALDEIVDGGYIQETDPKQVV 129
Zeta-COP cd14829
zeta subunit of the F-COPI complex; Zeta subunit of the heterotetrameric F-COPI complex, which ...
 3-138 2.21e-03

zeta subunit of the F-COPI complex; Zeta subunit of the heterotetrameric F-COPI complex, which consists of one beta-, one gamma-, one delta-, and one zeta subunit, where beta- and gamma- subunits are related to the large adaptor protein (AP) complex subunits, and delta- and zeta- subunits are related to the medium and small AP subunits, respectively. F-COPI forms a coatomer together with the B-COPI subcomplex, which assembles with a small GTPase, ADP-ribosylation factor 1 (ARF1), playing an important role in the formation of COPI complex-coated vesicles. COPI complex-coated vesicles function in the early secretory pathway mediating the retrograde transport from the Golgi to the ER, and intra-Golgi transport.


Pssm-ID: 341433  Cd Length: 132  Bit Score: 36.75  E-value: 2.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031581    3 QAILVFNNHGKPRLVRFYQR-FPEEIQQQIVRETFHLVLKRDDNICNFLEGgsliggsdYKLIYRHYATLYFVFCVDSSE 81
Cdd:cd14829   1 KAILILDNDGKRVLAKYYDDtFPTVKEQKAFEKKLFDKTHKANAEIILLDG--------LTVVYKSNIDLTFYVVGSSDE 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5031581   82 SELGILDLIQVFVETLDKCFE-NVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIV 138
Cdd:cd14829  73 NELILASVLNCLYDALSLLLRkNVEKRALLENLDLVLLALDEIVDGGIILETDPTAIA 130
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH