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Conserved domains on  [gi|2024414731|ref|XP_040558108|]
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AP-4 complex subunit sigma-1 isoform X1 [Gallus gallus]

Protein Classification

AP-4 complex subunit sigma( domain architecture ID 13000705)

AP-4 complex subunit sigma is a component of the adaptor protein complex 4 (AP-4) that is a vesicle coat component involved both in vesicle formation and cargo selection

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AP4_sigma cd14832
AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor ...
 3-140 1.22e-84

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: 244.06  E-value: 1.22e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024414731   3 KFFLMVNKQGQTRLSRYYEHIEIHKRTMLEAEVIKHCLSRSKDQCSFIEYKDFKLVYRQYAALFVVVGINETENEMAVYE 82
Cdd:cd14832     1 KFILMVNKQGQTRLAQYYEFLSIEERVALEGEIIRKCLSRSEKQCSFLEYRGYKLVYRRYASLYFIVGVDEDENELAILE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024414731  83 LIHNFVEVLDKYFSRVSELDIMFNLDRVHIILDEMVLNGCIVETNPNRILAPLFVLDK 140
Cdd:cd14832    81 FIHNLVETLDKYFENVCELDIMFNLEKAHFILDEMVMNGCIVETNKSNILAPILLMDK 138
 
Name Accession Description Interval E-value
AP4_sigma cd14832
AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor ...
 3-140 1.22e-84

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: 244.06  E-value: 1.22e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024414731   3 KFFLMVNKQGQTRLSRYYEHIEIHKRTMLEAEVIKHCLSRSKDQCSFIEYKDFKLVYRQYAALFVVVGINETENEMAVYE 82
Cdd:cd14832     1 KFILMVNKQGQTRLAQYYEFLSIEERVALEGEIIRKCLSRSEKQCSFLEYRGYKLVYRRYASLYFIVGVDEDENELAILE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024414731  83 LIHNFVEVLDKYFSRVSELDIMFNLDRVHIILDEMVLNGCIVETNPNRILAPLFVLDK 140
Cdd:cd14832    81 FIHNLVETLDKYFENVCELDIMFNLEKAHFILDEMVMNGCIVETNKSNILAPILLMDK 138
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
1-143 4.60e-49

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


Pssm-ID: 227363  Cd Length: 152  Bit Score: 154.49  E-value: 4.60e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024414731   1 MIKFFLMVNKQGQTRLSRYYEHIEIHKRTMLEAEVIKHCLSRSKDQCSFIEYKDFKLVYRQYAALFVVVGINETENEMAV 80
Cdd:COG5030     1 MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIEGKNEKIVYRRYATLYFVFGVDNDDNELII 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024414731  81 YELIHNFVEVLDKYFSRVSELDIMFNLDRVHIILDEMVLNGCIVETNPNRILAPLFVLDKVAE 143
Cdd:COG5030    81 LELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYALDAEST 143
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
1-142 1.19e-42

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 137.87  E-value: 1.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024414731   1 MIKFFLMVNKQGQTRLSRYYEHIEIHKRTMLEAEVIKHCLSRSKDQCSFIEYKDFKLVYRQYAALFVVVGINETENEMAV 80
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSNFIEFNDLKVIYKRYATLYFVVIVDDQDNELII 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024414731  81 YELIHNFVEVLDKYFSRVSELDIMFNLDRVHIILDEMVLNGCIVETNPNRILAPLFVLDKVA 142
Cdd:pfam01217  81 LELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVALLDELA 142
 
Name Accession Description Interval E-value
AP4_sigma cd14832
AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor ...
 3-140 1.22e-84

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: 244.06  E-value: 1.22e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024414731   3 KFFLMVNKQGQTRLSRYYEHIEIHKRTMLEAEVIKHCLSRSKDQCSFIEYKDFKLVYRQYAALFVVVGINETENEMAVYE 82
Cdd:cd14832     1 KFILMVNKQGQTRLAQYYEFLSIEERVALEGEIIRKCLSRSEKQCSFLEYRGYKLVYRRYASLYFIVGVDEDENELAILE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024414731  83 LIHNFVEVLDKYFSRVSELDIMFNLDRVHIILDEMVLNGCIVETNPNRILAPLFVLDK 140
Cdd:cd14832    81 FIHNLVETLDKYFENVCELDIMFNLEKAHFILDEMVMNGCIVETNKSNILAPILLMDK 138
AP2_sigma cd14833
AP-2 complex subunit sigma; AP-2 complex sigma subunit is part of the heterotetrameric adaptor ...
 1-140 6.61e-51

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: 158.50  E-value: 6.61e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024414731   1 MIKFFLMVNKQGQTRLSRYYEHIEIHKRTMLEAEVIKHCLSRSKDQCSFIEYKDFKLVYRQYAALFVVVGINETENEMAV 80
Cdd:cd14833     1 MIRFILIQNRQGKTRLAKWYVPYDDDEKQKLEEEVHRLVTSRDKKHTNFVEFRNYKLVYRRYAGLFFCICVDVNDNELAY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024414731  81 YELIHNFVEVLDKYFSRVSELDIMFNLDRVHIILDEMVLNGCIVETNPNRILAPLFVLDK 140
Cdd:cd14833    81 LEAIHLFVEVLDEYFGNVCELDLVFNFYKVYAILDEMFLAGEIQETSKKVILERLKELDK 140
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
1-143 4.60e-49

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


Pssm-ID: 227363  Cd Length: 152  Bit Score: 154.49  E-value: 4.60e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024414731   1 MIKFFLMVNKQGQTRLSRYYEHIEIHKRTMLEAEVIKHCLSRSKDQCSFIEYKDFKLVYRQYAALFVVVGINETENEMAV 80
Cdd:COG5030     1 MIKFVLIFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESNFIEGKNEKIVYRRYATLYFVFGVDNDDNELII 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024414731  81 YELIHNFVEVLDKYFSRVSELDIMFNLDRVHIILDEMVLNGCIVETNPNRILAPLFVLDKVAE 143
Cdd:COG5030    81 LELIHNFVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYALDAEST 143
AP_sigma cd14827
AP complex subunit sigma; AP complex sigma subunits are part of the heterotetrameric adaptor ...
 3-140 1.02e-48

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: 152.98  E-value: 1.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024414731   3 KFFLMVNKQGQTRLSRYYEHIEIHKRTMLEAEVIKHCLSRSKDQCSFIEYKDFKLVYRQYAALFVVVGINETENEMAVYE 82
Cdd:cd14827     1 RFILLFNRQGKTRLAKWYMQFDDDERQKLIEEIVQVVLSRDAKHCNFVEFRNYKLIYRRYASLYFCICVDSNDNELAILE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024414731  83 LIHNFVEVLDKYFSRVSELDIMFNLDRVHIILDEMVLNGCIVETNPNRILAPLFVLDK 140
Cdd:cd14827    81 AIHNFVETLDKYFENVCELDLIFNFEKVYFIVDEMVLGGEIRETSQTKILKQIEMLDK 138
AP1_sigma cd14831
AP-1 complex subunit sigma; AP-1 complex sigma subunit is part of the heterotetrameric adaptor ...
 3-132 2.94e-45

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: 144.24  E-value: 2.94e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024414731   3 KFFLMVNKQGQTRLSRYYEHIEIHKRTMLEAEVIKHCLSRSKDQCSFIEYKDFKLVYRQYAALFVVVGINETENEMAVYE 82
Cdd:cd14831     1 HFLLLFSRQGKVRLSKWYSAYSQKEKAKITREVSTLVLARKPKMCNFLEWRDLKIVYKRYASLYFVCCVDKDDNELITLE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024414731  83 LIHNFVEVLDKYFSRVSELDIMFNLDRVHIILDEMVLNGCIVETNPNRIL 132
Cdd:cd14831    81 IIHRYVEILDKYFGNVCELDIIFNFHKAYFILDELLLGGELQETSKKNVL 130
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
1-142 1.19e-42

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 137.87  E-value: 1.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024414731   1 MIKFFLMVNKQGQTRLSRYYEHIEIHKRTMLEAEVIKHCLSRSKDQCSFIEYKDFKLVYRQYAALFVVVGINETENEMAV 80
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSNFIEFNDLKVIYKRYATLYFVVIVDDQDNELII 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024414731  81 YELIHNFVEVLDKYFSRVSELDIMFNLDRVHIILDEMVLNGCIVETNPNRILAPLFVLDKVA 142
Cdd:pfam01217  81 LELIHRFVESLDRYFGNVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVALLDELA 142
AP3_sigma cd14834
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ...
 1-133 1.24e-38

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: 127.73  E-value: 1.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024414731   1 MIKFFLMVNKQGQTRLSRYYEHIEIHKRTMLEAEVIKHCLSRSKDQCSFIEY------KDFKLVYRQYAALFVVVGINET 74
Cdd:cd14834     1 MIKAILIFNNHGKPRLSKFYQHYSEEKQQQIIRETFQLVSKRDDNVCNFLEGgsliggSDTKLIYRHYATLYFVFCVDSS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024414731  75 ENEMAVYELIHNFVEVLDKYFSRVSELDIMFNLDRVHIILDEMVLNGCIVETNPNRILA 133
Cdd:cd14834    81 ESELGILDLIQVFVETLDKCFENVCELDLIFHVDKVHYILDEIVMGGMVLETNMTEILT 139
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
 3-131 1.50e-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: 76.02  E-value: 1.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024414731   3 KFFLMVNKQGQTRLSRYYehIEIHKRTMLEAEVIKHCL-SRSKDQCSFIEYKDFKLVYRQYAALFVVVGINETENEMAVY 81
Cdd:cd14823     1 KAILVLDNDGKRLFAKYY--DDTYPSVKEQKAFEKNIFnKKHRTDSEIVLLEGLRVVYKSSIDLYFVVIGSKNENELLLL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024414731  82 ELIHNFVEVLDKYFSRVSELDIMFNLDRVHIILDEMVLNGCIVETNPNRI 131
Cdd:cd14823    79 EVLNCLVDVLSEYFRKVEERAILENFEGLYFALDEIVDGGYIQETDPKQV 128
RET3 COG5541
Vesicle coat complex COPI, zeta subunit [Posttranslational modification, protein turnover, ...
 2-135 3.70e-06

Vesicle coat complex COPI, zeta subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227828  Cd Length: 187  Bit Score: 44.16  E-value: 3.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024414731   2 IKFFLMVNKQGQTRLSRYYE-------HIEIHKRTMLEAEVIKHCLSRS-KDQCSFIEYKDFKLVYRQYA-ALFVVVGIN 72
Cdd:COG5541     8 VEALLILDSQGERIYRKYYQpphrsegHQLVFNSVKKEKEFEKKLAEKTaKDRESILMFYDRLVMCKRLDdVLLYIVSPM 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024414731  73 EtENEMAVYELIHNFVEVLDKYFSRVS-ELDIMFNLDRVHIILDEMVLNGCIVETNPNRILAPL 135
Cdd:COG5541    88 E-ENEPFLGQVFDEIRAALILIVKTPTdKRNVWENYDQIVLLVDETIDEGVILETKSDEIADRV 150
AP_Mu_N cd14828
AP complex subunit mu N-terminal domain; AP complex mu subunits are part of the ...
 49-129 1.23e-05

AP complex subunit mu N-terminal domain; AP complex mu 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 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: 341432  Cd Length: 136  Bit Score: 42.18  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024414731  49 FIEYKDFKLVYRQYAALFVVVGINETENEMAVYELIHNFVEVLDKYF--SRVSELDIMFNLDRVHIILDEMVLNGCIVET 126
Cdd:cd14828    46 IISSNGWNFIYIKRDDLYFVSVTQTNVNLMSVLVFLDQFYDLLKDYFgvKKLDKNSIIDNFVLIYELIDESIDFGIIQLT 125


                  ...
gi 2024414731 127 NPN 129
Cdd:cd14828   126 DYN 128
Zeta-COP cd14829
zeta subunit of the F-COPI complex; Zeta subunit of the heterotetrameric F-COPI complex, which ...
 58-131 3.76e-05

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: 40.61  E-value: 3.76e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024414731  58 VYRQYAAL-FVVVGiNETENEMAVYELIHNFVEVLDKYF-SRVSELDIMFNLDRVHIILDEMVLNGCIVETNPNRI 131
Cdd:cd14829    55 VYKSNIDLtFYVVG-SSDENELILASVLNCLYDALSLLLrKNVEKRALLENLDLVLLALDEIVDGGIILETDPTAI 129
AP3_Mu_N cd14837
AP-3 complex subunit mu N-terminal domain; AP-3 complex mu subunit is part of the ...
 65-129 2.38e-04

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: 38.65  E-value: 2.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024414731  65 LFVVVGINETEnEMAVYELIHNFVEVLDKYFSRVSELDIMFNLDRVHIILDEMVLNGCIVETNPN 129
Cdd:cd14837    63 YFLAVVTSEVP-PLLVIEFLHRIVDVLEDYFGSLSESTIKENFVVVYQLLEEMLDNGFPLTTEPN 126
AP1_Mu_N cd14835
AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the ...
 58-122 5.49e-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: 34.83  E-value: 5.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024414731  58 VYRQYAALFVVVGINETENEMAVYELIHNFVEVLDKYFSRVSELDIMFNLDRVHIILDEMVLNGC 122
Cdd:cd14835    55 IYIKHNNLYLLAVTKKNANAAMVLSFLYKLVEVFKEYFKELEEESIRDNFVIIYELLDEMMDFGY 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.
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