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Conserved domains on  [gi|1543734124|ref|XP_027464525|]
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AP-1 complex subunit sigma-2 isoform X4 [Zalophus californianus]

Protein Classification

AP-1 complex subunit sigma( domain architecture ID 13000692)

AP-1 complex subunit sigma is a subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes

Gene Ontology:  GO:0035615|GO:0030121|GO:0016192
PubMed:  16788044|23424177

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AP1_sigma cd14831
AP-1 complex subunit sigma; AP-1 complex sigma subunit is part of the heterotetrameric adaptor ...
 2-144 3.66e-104

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: 294.08  E-value: 3.66e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543734124   2 QFMLLFSRQGKLRLQKWYVPLSDKEKKKITRELVQTVLARKPKMCSFLEWRDLKIVYKRYASLYFCCAIEDQDNELITLE 81
Cdd:cd14831     1 HFLLLFSRQGKVRLSKWYSAYSQKEKAKITREVSTLVLARKPKMCNFLEWRDLKIVYKRYASLYFVCCVDKDDNELITLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1543734124  82 IIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSKKNVLKAIEQADLLQEEA 144
Cdd:cd14831    81 IIHRYVEILDKYFGNVCELDIIFNFHKAYFILDELLLGGELQETSKKNVLRAIEAQDLLQEEE 143
 
Name Accession Description Interval E-value
AP1_sigma cd14831
AP-1 complex subunit sigma; AP-1 complex sigma subunit is part of the heterotetrameric adaptor ...
 2-144 3.66e-104

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: 294.08  E-value: 3.66e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543734124   2 QFMLLFSRQGKLRLQKWYVPLSDKEKKKITRELVQTVLARKPKMCSFLEWRDLKIVYKRYASLYFCCAIEDQDNELITLE 81
Cdd:cd14831     1 HFLLLFSRQGKVRLSKWYSAYSQKEKAKITREVSTLVLARKPKMCNFLEWRDLKIVYKRYASLYFVCCVDKDDNELITLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1543734124  82 IIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSKKNVLKAIEQADLLQEEA 144
Cdd:cd14831    81 IIHRYVEILDKYFGNVCELDIIFNFHKAYFILDELLLGGELQETSKKNVLRAIEAQDLLQEEE 143
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
1-141 7.37e-70

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 207.21  E-value: 7.37e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543734124   1 MQFMLLFSRQGKLRLQKWYVPLSDKEKKKITRELVQTVLARKPKMCSFLEWRDLKIVYKRYASLYFCCAIEDQDNELITL 80
Cdd:pfam01217   2 IKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSNFIEFNDLKVIYKRYATLYFVVIVDDQDNELIIL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1543734124  81 EIIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSKKNVLKAIEQADLLQ 141
Cdd:pfam01217  82 ELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVALLDELA 142
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
1-149 7.04e-67

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


Pssm-ID: 227363  Cd Length: 152  Bit Score: 199.94  E-value: 7.04e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543734124   1 MQFMLLFSRQGKLRLQKWYVPLSDKEKKKITRELVQTVLARKPKMCSFLEWRDLKIVYKRYASLYFCCAIEDQDNELITL 80
Cdd:COG5030     2 IKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIEGKNEKIVYRRYATLYFVFGVDNDDNELIIL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1543734124  81 EIIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSKKNVLKAIEQADLLQEEAETPRS 149
Cdd:COG5030    82 ELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYALDAESTDDKIGRS 150
 
Name Accession Description Interval E-value
AP1_sigma cd14831
AP-1 complex subunit sigma; AP-1 complex sigma subunit is part of the heterotetrameric adaptor ...
 2-144 3.66e-104

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: 294.08  E-value: 3.66e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543734124   2 QFMLLFSRQGKLRLQKWYVPLSDKEKKKITRELVQTVLARKPKMCSFLEWRDLKIVYKRYASLYFCCAIEDQDNELITLE 81
Cdd:cd14831     1 HFLLLFSRQGKVRLSKWYSAYSQKEKAKITREVSTLVLARKPKMCNFLEWRDLKIVYKRYASLYFVCCVDKDDNELITLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1543734124  82 IIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSKKNVLKAIEQADLLQEEA 144
Cdd:cd14831    81 IIHRYVEILDKYFGNVCELDIIFNFHKAYFILDELLLGGELQETSKKNVLRAIEAQDLLQEEE 143
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
1-141 7.37e-70

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 207.21  E-value: 7.37e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543734124   1 MQFMLLFSRQGKLRLQKWYVPLSDKEKKKITRELVQTVLARKPKMCSFLEWRDLKIVYKRYASLYFCCAIEDQDNELITL 80
Cdd:pfam01217   2 IKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSNFIEFNDLKVIYKRYATLYFVVIVDDQDNELIIL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1543734124  81 EIIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSKKNVLKAIEQADLLQ 141
Cdd:pfam01217  82 ELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVALLDELA 142
AP_sigma cd14827
AP complex subunit sigma; AP complex sigma subunits are part of the heterotetrameric adaptor ...
 2-138 6.93e-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: 199.59  E-value: 6.93e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543734124   2 QFMLLFSRQGKLRLQKWYVPLSDKEKKKITRELVQTVLARKPKMCSFLEWRDLKIVYKRYASLYFCCAIEDQDNELITLE 81
Cdd:cd14827     1 RFILLFNRQGKTRLAKWYMQFDDDERQKLIEEIVQVVLSRDAKHCNFVEFRNYKLIYRRYASLYFCICVDSNDNELAILE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1543734124  82 IIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSKKNVLKAIEQAD 138
Cdd:cd14827    81 AIHNFVETLDKYFENVCELDLIFNFEKVYFIVDEMVLGGEIRETSQTKILKQIEMLD 137
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
1-149 7.04e-67

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


Pssm-ID: 227363  Cd Length: 152  Bit Score: 199.94  E-value: 7.04e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543734124   1 MQFMLLFSRQGKLRLQKWYVPLSDKEKKKITRELVQTVLARKPKMCSFLEWRDLKIVYKRYASLYFCCAIEDQDNELITL 80
Cdd:COG5030     2 IKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIEGKNEKIVYRRYATLYFVFGVDNDDNELIIL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1543734124  81 EIIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSKKNVLKAIEQADLLQEEAETPRS 149
Cdd:COG5030    82 ELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYALDAESTDDKIGRS 150
AP2_sigma cd14833
AP-2 complex subunit sigma; AP-2 complex sigma subunit is part of the heterotetrameric adaptor ...
 2-140 2.78e-62

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: 188.16  E-value: 2.78e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543734124   2 QFMLLFSRQGKLRLQKWYVPLSDKEKKKITRELVQTVLARKPKMCSFLEWRDLKIVYKRYASLYFCCAIEDQDNELITLE 81
Cdd:cd14833     3 RFILIQNRQGKTRLAKWYVPYDDDEKQKLEEEVHRLVTSRDKKHTNFVEFRNYKLVYRRYAGLFFCICVDVNDNELAYLE 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1543734124  82 IIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSKKNVLKAIEQADLL 140
Cdd:cd14833    83 AIHLFVEVLDEYFGNVCELDLVFNFYKVYAILDEMFLAGEIQETSKKVILERLKELDKL 141
AP4_sigma cd14832
AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor ...
 2-134 7.60e-50

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: 156.24  E-value: 7.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543734124   2 QFMLLFSRQGKLRLQKWYVPLSDKEKKKITRELVQTVLARKPKMCSFLEWRDLKIVYKRYASLYFCCAIEDQDNELITLE 81
Cdd:cd14832     1 KFILMVNKQGQTRLAQYYEFLSIEERVALEGEIIRKCLSRSEKQCSFLEYRGYKLVYRRYASLYFIVGVDEDENELAILE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1543734124  82 IIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSKKNVLKAI 134
Cdd:cd14832    81 FIHNLVETLDKYFENVCELDIMFNLEKAHFILDEMVMNGCIVETNKSNILAPI 133
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
 3-133 5.53e-42

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: 136.49  E-value: 5.53e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543734124   3 FMLLFSRQGKLRLQKWYVPLSDkEKKKITRELVQTVLARKPKMCSFLEWRDLKIVYKRYASLYFCCAIEDQDNELITLEI 82
Cdd:cd14823     2 AILVLDNDGKRLFAKYYDDTYP-SVKEQKAFEKNIFNKKHRTDSEIVLLEGLRVVYKSSIDLYFVVIGSKNENELLLLEV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1543734124  83 IHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSKKNVLKA 133
Cdd:cd14823    81 LNCLVDVLSEYFRKVEERAILENFEGLYFALDEIVDGGYIQETDPKQVVHF 131
AP3_sigma cd14834
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ...
 5-138 1.80e-41

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: 135.43  E-value: 1.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543734124   5 LLFSRQGKLRLQKWYVPLSDKEKKKITRELVQTVLARKPKMCSFLE------WRDLKIVYKRYASLYFCCAIEDQDNELI 78
Cdd:cd14834     6 LIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKRDDNVCNFLEggsligGSDTKLIYRHYATLYFVFCVDSSESELG 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543734124  79 TLEIIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSKKNVLKAIEQAD 138
Cdd:cd14834    86 ILDLIQVFVETLDKCFENVCELDLIFHVDKVHYILDEIVMGGMVLETNMTEILTAIEEQN 145
AP3_Mu_N cd14837
AP-3 complex subunit mu N-terminal domain; AP-3 complex mu subunit is part of the ...
 63-120 9.55e-05

AP-3 complex subunit mu N-terminal domain; AP-3 complex mu 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 mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341441  Cd Length: 139  Bit Score: 40.20  E-value: 9.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1543734124  63 SLYFCCAIEDQDNELITLEIIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGG 120
Cdd:cd14837    61 NLYFLAVVTSEVPPLLVIEFLHRIVDVLEDYFGSLSESTIKENFVVVYQLLEEMLDNG 118
AP2_Mu_N cd14836
AP-2 complex subunit mu N-terminal domain; AP-2 complex mu subunit is part of the ...
 57-132 4.28e-04

AP-2 complex subunit mu N-terminal domain; AP-2 complex mu 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 mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341440  Cd Length: 140  Bit Score: 38.27  E-value: 4.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1543734124  57 VYKRYASLYFCcAIEDQD-NELITLEIIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSkKNVLK 132
Cdd:cd14836    56 FHVRHGNLYLV-AVTRSNvNAAMVFEFLYKLVQLFKSYFGKFNEDSIKNNFVLIYELLDEILDFGYPQNTE-PEALK 130
AP1_Mu_N cd14835
AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the ...
 57-136 2.97e-03

AP-1 complex subunit mu N-terminal domain; AP-1 complex mu 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 mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341439  Cd Length: 139  Bit Score: 35.99  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543734124  57 VYKRYASLYFCCAIEDQDNELITLEIIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSKKNVLKAIEQ 136
Cdd:cd14835    55 IYIKHNNLYLLAVTKKNANAAMVLSFLYKLVEVFKEYFKELEEESIRDNFVIIYELLDEMMDFGYPQTTESKILQEYITQ 134
AP4_Mu_N cd14838
AP-4 complex subunit mu N-terminal domain; AP-4 complex mu subunit is part of the ...
 57-133 9.78e-03

AP-4 complex subunit mu N-terminal domain; AP-4 complex mu 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 mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341442  Cd Length: 137  Bit Score: 34.45  E-value: 9.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1543734124  57 VYKRYASLYFCCAIEDQDNELITLEIIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLLGGEVQETSkKNVLKA 133
Cdd:cd14838    53 LHVKRNGLYFVATTRFNVSPSYVLELLNRIAKLIKDYCGVLNEESIRKNFVLIYELLDEILDFGYPQTTS-TEQLKS 128
 
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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