NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|969812503|ref|NP_001305020|]
View 

AP-3 complex subunit sigma-1 isoform 4 [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 ...
 1-122 7.03e-87

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: 250.99  E-value: 7.03e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969812503   1 MIKAILIFNNHGKPRLSKFYQPYSEDTQQQIIRETFHLVSKRDENVCNFLEGGLLIGGSDNKLIYRHYATLYFVFCVDSS 80
Cdd:cd14834    1 MIKAILIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKRDDNVCNFLEGGSLIGGSDTKLIYRHYATLYFVFCVDSS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 969812503  81 ESELGILDLIQV------------------------HNILAEMVMGGMVLETNMNEIVTQIDAQNK 122
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 ...
 1-122 7.03e-87

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: 250.99  E-value: 7.03e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969812503   1 MIKAILIFNNHGKPRLSKFYQPYSEDTQQQIIRETFHLVSKRDENVCNFLEGGLLIGGSDNKLIYRHYATLYFVFCVDSS 80
Cdd:cd14834    1 MIKAILIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKRDDNVCNFLEGGSLIGGSDTKLIYRHYATLYFVFCVDSS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 969812503  81 ESELGILDLIQV------------------------HNILAEMVMGGMVLETNMNEIVTQIDAQNK 122
Cdd:cd14834   81 ESELGILDLIQVfvetldkcfenvceldlifhvdkvHYILDEIVMGGMVLETNMTEILTAIEEQNK 146
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
1-128 5.71e-41

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


Pssm-ID: 227363  Cd Length: 152  Bit Score: 134.85  E-value: 5.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969812503   1 MIKAILIFNNHGKPRLSKFYQPYSEDTQQQIIRETFHLVSKRDENVCNFLEgglligGSDNKLIYRHYATLYFVFCVDSS 80
Cdd:COG5030    1 MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIE------GKNEKIVYRRYATLYFVFGVDND 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 969812503  81 ESELGILDLIQ------------------------VHNILAEMVMGGMVLETNMNEIVTQIDAQNKLEKSEA 128
Cdd:COG5030   75 DNELIILELIHnfveildrffgnvceldlifnfqkVYAILDEMILGGEIIESSKNEVLEHVYALDAESTDDK 146
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
1-124 9.17e-40

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 131.32  E-value: 9.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969812503    1 MIKAILIFNNHGKPRLSKFYQPYSEDTQQQIIRETFHLVSKRDENVCNFLEgglligGSDNKLIYRHYATLYFVFCVDSS 80
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSNFIE------FNDLKVIYKRYATLYFVVIVDDQ 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 969812503   81 ESELGILDLIQ------------------------VHNILAEMVMGGMVLETNMNEIVTQIDAQNKLE 124
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 ...
 1-122 7.03e-87

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: 250.99  E-value: 7.03e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969812503   1 MIKAILIFNNHGKPRLSKFYQPYSEDTQQQIIRETFHLVSKRDENVCNFLEGGLLIGGSDNKLIYRHYATLYFVFCVDSS 80
Cdd:cd14834    1 MIKAILIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKRDDNVCNFLEGGSLIGGSDTKLIYRHYATLYFVFCVDSS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 969812503  81 ESELGILDLIQV------------------------HNILAEMVMGGMVLETNMNEIVTQIDAQNK 122
Cdd:cd14834   81 ESELGILDLIQVfvetldkcfenvceldlifhvdkvHYILDEIVMGGMVLETNMTEILTAIEEQNK 146
AP_sigma cd14827
AP complex subunit sigma; AP complex sigma subunits are part of the heterotetrameric adaptor ...
 3-122 3.46e-47

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: 150.28  E-value: 3.46e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969812503   3 KAILIFNNHGKPRLSKFYQPYSEDTQQQIIRETFHLVSKRDENVCNFLEGGlliggsDNKLIYRHYATLYFVFCVDSSES 82
Cdd:cd14827    1 RFILLFNRQGKTRLAKWYMQFDDDERQKLIEEIVQVVLSRDAKHCNFVEFR------NYKLIYRRYASLYFCICVDSNDN 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 969812503  83 ELGILDLIQ------------------------VHNILAEMVMGGMVLETNMNEIVTQIDAQNK 122
Cdd:cd14827   75 ELAILEAIHnfvetldkyfenvceldlifnfekVYFIVDEMVLGGEIRETSQTKILKQIEMLDK 138
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
1-128 5.71e-41

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


Pssm-ID: 227363  Cd Length: 152  Bit Score: 134.85  E-value: 5.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969812503   1 MIKAILIFNNHGKPRLSKFYQPYSEDTQQQIIRETFHLVSKRDENVCNFLEgglligGSDNKLIYRHYATLYFVFCVDSS 80
Cdd:COG5030    1 MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIE------GKNEKIVYRRYATLYFVFGVDND 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 969812503  81 ESELGILDLIQ------------------------VHNILAEMVMGGMVLETNMNEIVTQIDAQNKLEKSEA 128
Cdd:COG5030   75 DNELIILELIHnfveildrffgnvceldlifnfqkVYAILDEMILGGEIIESSKNEVLEHVYALDAESTDDK 146
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
1-124 9.17e-40

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 131.32  E-value: 9.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969812503    1 MIKAILIFNNHGKPRLSKFYQPYSEDTQQQIIRETFHLVSKRDENVCNFLEgglligGSDNKLIYRHYATLYFVFCVDSS 80
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSNFIE------FNDLKVIYKRYATLYFVVIVDDQ 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 969812503   81 ESELGILDLIQ------------------------VHNILAEMVMGGMVLETNMNEIVTQIDAQNKLE 124
Cdd:pfam01217  75 DNELIILELIHrfvesldryfgnvceldlifnfekVYLILDEMVMGGEILETSKNEVLHRVALLDELA 142
AP2_sigma cd14833
AP-2 complex subunit sigma; AP-2 complex sigma subunit is part of the heterotetrameric adaptor ...
 1-123 2.60e-32

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: 112.28  E-value: 2.60e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969812503   1 MIKAILIFNNHGKPRLSKFYQPYSEDTQQQIIRETFHLVSKRDENVCNFLEgglligGSDNKLIYRHYATLYFVFCVDSS 80
Cdd:cd14833    1 MIRFILIQNRQGKTRLAKWYVPYDDDEKQKLEEEVHRLVTSRDKKHTNFVE------FRNYKLVYRRYAGLFFCICVDVN 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 969812503  81 ESELGILDLI------------------------QVHNILAEMVMGGMVLETNMNEIVTQIDAQNKL 123
Cdd:cd14833   75 DNELAYLEAIhlfvevldeyfgnvceldlvfnfyKVYAILDEMFLAGEIQETSKKVILERLKELDKL 141
AP1_sigma cd14831
AP-1 complex subunit sigma; AP-1 complex sigma subunit is part of the heterotetrameric adaptor ...
 5-127 7.59e-29

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: 103.41  E-value: 7.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969812503   5 ILIFNNHGKPRLSKFYQPYSEDTQQQIIRETFHLVSKRDENVCNFLEgglligGSDNKLIYRHYATLYFVFCVDSSESEL 84
Cdd:cd14831    3 LLLFSRQGKVRLSKWYSAYSQKEKAKITREVSTLVLARKPKMCNFLE------WRDLKIVYKRYASLYFVCCVDKDDNEL 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 969812503  85 GILDLIQ------------------------VHNILAEMVMGGMVLETNMNEIVTQIDAQNKLEKSE 127
Cdd:cd14831   77 ITLEIIHryveildkyfgnvceldiifnfhkAYFILDELLLGGELQETSKKNVLRAIEAQDLLQEEE 143
AP4_sigma cd14832
AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor ...
 3-122 6.05e-21

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: 83.05  E-value: 6.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969812503   3 KAILIFNNHGKPRLSKFYQPYSEDTQQQIIRETFHLVSKRDENVCNFLEGglliggSDNKLIYRHYATLYFVFCVDSSES 82
Cdd:cd14832    1 KFILMVNKQGQTRLAQYYEFLSIEERVALEGEIIRKCLSRSEKQCSFLEY------RGYKLVYRRYASLYFIVGVDEDEN 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 969812503  83 ELGILDLIQ------------------------VHNILAEMVMGGMVLETNMNEIVTQIDAQNK 122
Cdd:cd14832   75 ELAILEFIHnlvetldkyfenvceldimfnlekAHFILDEMVMNGCIVETNKSNILAPILLMDK 138
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
 3-115 1.49e-03

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: 36.73  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969812503   3 KAILIFNNHGKPRLSKFYQPySEDTQQQIIRETFHLVSKRDENVCNFLEGGLLiggsdnKLIYRHYATLYFVFCVDSSES 82
Cdd:cd14823    1 KAILVLDNDGKRLFAKYYDD-TYPSVKEQKAFEKNIFNKKHRTDSEIVLLEGL------RVVYKSSIDLYFVVIGSKNEN 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 969812503  83 ELGILDLIQ------------------------VHNILAEMVMGGMVLETNMNEIVT 115
Cdd:cd14823   74 ELLLLEVLNclvdvlseyfrkveerailenfegLYFALDEIVDGGYIQETDPKQVVH 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