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Conserved domains on  [gi|214010212|ref|NP_001135753|]
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coatomer subunit delta isoform 2 [Homo sapiens]

Protein Classification

AP_delta-COPI_MHD domain-containing protein( domain architecture ID 13604245)

AP_delta-COPI_MHD domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AP_delta-COPI_MHD cd09254
Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit; COPI ...
184-420 3.50e-135

Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit; COPI complex-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. COPI complex-coated vesicles consist of a small GTPase, ADP-ribosylation factor 1 (ARF1) and a heteroheptameric coatomer composed of two subcomplexes, F-COPI and B-COPI. ARF1 regulates COPI vesicle formation by recruiting the coatomer onto Golgi membranes to initiate its coat function. Coatomer complexes then bind cargo molecules and self-assemble to form spherical cages that yield COPI-coated vesicles. The heterotetrameric F-COPI subcomplex contains beta-, gamma-, delta-, and zeta-COP subunits, where beta- and gamma-COP subunits are related to the large AP subunits, and delta- and zeta-COP subunits are related to the medium and small AP subunits, respectively. Due to the sequence similarity to the AP complexes, the F-COPI subcomplex might play a role in the cargo-binding. The heterotrimeric B-COPI contains alpha-, beta-, and epsilon-COP subunits, which are not related to the adaptins. This subcomplex is thought to participate in the cage-forming and might serve a function similar to that of clathrin. This family corresponds to the mu homology domain of delta-subunit of COPI complex (delta-COP), which is distantly related to the C-terminal domain of mu chains among AP complexes. The delta-COP subunit appears tightly associated with the beta-COP subunit to confer its interaction with ARF1. In addition, both delta- and beta-COP subunits contribute to a common binding site for arginine (R)-based signals, which are sorting motifs conferring transient endoplasmic reticulum (ER) localization to unassembled subunits of multimeric membrane proteins.


:

Pssm-ID: 271162  Cd Length: 237  Bit Score: 387.35  E-value: 3.50e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212 184 ESVHMKIEEKITLTCGRDGGLQNMELHGMIMLRISDDKYGRIRLHVENEDKKGVQLQTHPNVDKKLFTAESLIGLKNPEK 263
Cdd:cd09254    1 EGVHITVEEKISATLSRDGGLESLEVKGTLSLRINDEELAHIKLQLANNSDKGFQFKTHPNVDKKLFTSDSVLGLKDPSK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212 264 SFPVNSDVGVLKWRLQTTEESFIPLTINCWPSESGNGCDVNIEYELQEDNLELNDVVITIPLPSGvGAPVIGEIDGEYRH 343
Cdd:cd09254   81 PFPVNDPVGVLKWRLQGSDESLLPLTINCWPSESGGGCDVTIEYELNRDDLELNDVVISIPLPSG-DAPVVNSIDGNYEY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 214010212 344 DSRRNTLEWCLPVIDAKNKSGSLEFSI-AGQPNDFFPVQVSFVSKKNYCNIQVTKVTQVDGNSPVRFSTETTFLVDKY 420
Cdd:cd09254  160 DSRKNVLEWKIPVIDASNSSGSLEFSIpADDEDAFFPISVSFTSSKTFCGVKVVEVVSADDGEPVPFSLETSLVADKY 237
longin-like super family cl38905
Longin-like domains; Longin-like domains are small protein domains present in a variety of ...
2-45 6.41e-20

Longin-like domains; Longin-like domains are small protein domains present in a variety of proteins and members of protein complexes involved in or required for different steps during the transport of proteins from the ribosome to the ER to the plasma membrane, via the Golgi apparatus. Examples are mu and sigma subunits of the heterotetrameric adaptor protein (AP) complex, zeta and delta subunits of the heterotetrameric F-COPI complex, a subgroup of R-SNARE proteins, a subfamily of the transport protein particle (TRAPP), and the signal recognition particle receptor subunit alpha (SR-alpha).


The actual alignment was detected with superfamily member cd14830:

Pssm-ID: 365781  Cd Length: 130  Bit Score: 85.26  E-value: 6.41e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 214010212   2 IPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTF 45
Cdd:cd14830   87 VPEYCPSVDEEEILKNAFDLIFAFDEVISLGYRENVTLSQIKTF 130
 
Name Accession Description Interval E-value
AP_delta-COPI_MHD cd09254
Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit; COPI ...
184-420 3.50e-135

Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit; COPI complex-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. COPI complex-coated vesicles consist of a small GTPase, ADP-ribosylation factor 1 (ARF1) and a heteroheptameric coatomer composed of two subcomplexes, F-COPI and B-COPI. ARF1 regulates COPI vesicle formation by recruiting the coatomer onto Golgi membranes to initiate its coat function. Coatomer complexes then bind cargo molecules and self-assemble to form spherical cages that yield COPI-coated vesicles. The heterotetrameric F-COPI subcomplex contains beta-, gamma-, delta-, and zeta-COP subunits, where beta- and gamma-COP subunits are related to the large AP subunits, and delta- and zeta-COP subunits are related to the medium and small AP subunits, respectively. Due to the sequence similarity to the AP complexes, the F-COPI subcomplex might play a role in the cargo-binding. The heterotrimeric B-COPI contains alpha-, beta-, and epsilon-COP subunits, which are not related to the adaptins. This subcomplex is thought to participate in the cage-forming and might serve a function similar to that of clathrin. This family corresponds to the mu homology domain of delta-subunit of COPI complex (delta-COP), which is distantly related to the C-terminal domain of mu chains among AP complexes. The delta-COP subunit appears tightly associated with the beta-COP subunit to confer its interaction with ARF1. In addition, both delta- and beta-COP subunits contribute to a common binding site for arginine (R)-based signals, which are sorting motifs conferring transient endoplasmic reticulum (ER) localization to unassembled subunits of multimeric membrane proteins.


Pssm-ID: 271162  Cd Length: 237  Bit Score: 387.35  E-value: 3.50e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212 184 ESVHMKIEEKITLTCGRDGGLQNMELHGMIMLRISDDKYGRIRLHVENEDKKGVQLQTHPNVDKKLFTAESLIGLKNPEK 263
Cdd:cd09254    1 EGVHITVEEKISATLSRDGGLESLEVKGTLSLRINDEELAHIKLQLANNSDKGFQFKTHPNVDKKLFTSDSVLGLKDPSK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212 264 SFPVNSDVGVLKWRLQTTEESFIPLTINCWPSESGNGCDVNIEYELQEDNLELNDVVITIPLPSGvGAPVIGEIDGEYRH 343
Cdd:cd09254   81 PFPVNDPVGVLKWRLQGSDESLLPLTINCWPSESGGGCDVTIEYELNRDDLELNDVVISIPLPSG-DAPVVNSIDGNYEY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 214010212 344 DSRRNTLEWCLPVIDAKNKSGSLEFSI-AGQPNDFFPVQVSFVSKKNYCNIQVTKVTQVDGNSPVRFSTETTFLVDKY 420
Cdd:cd09254  160 DSRKNVLEWKIPVIDASNSSGSLEFSIpADDEDAFFPISVSFTSSKTFCGVKVVEVVSADDGEPVPFSLETSLVADKY 237
Adap_comp_sub pfam00928
Adaptor complexes medium subunit family; This family also contains members which are coatomer ...
178-422 7.73e-58

Adaptor complexes medium subunit family; This family also contains members which are coatomer subunits.


Pssm-ID: 395742  Cd Length: 259  Bit Score: 190.21  E-value: 7.73e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212  178 APPINMESVHMKIEEKITLTCGRDGGLQNMELHGMIMLRISDDKYGRIRLHVENEDKK----GVQLQTHPNVDKklFTAE 253
Cdd:pfam00928   7 GIKYKKNEVFLDVIERVSVIVDKDGGLLNSEVQGTIDLKCFLSGMPELRLGLNDKLLLieldDVSFHQCVNLDK--FESE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212  254 SLIGLKNPEksfpvnSDVGVLKWRLqTTEESFIPLTINCWPSESGNGCDVNIEYELQED---NLELNDVVITIPLPSGVG 330
Cdd:pfam00928  85 RVISFIPPD------GEFELMRYRL-STNEVKLPFTVKPIVSVSGDEGRVEIEVKLRSDfpkKLTAENVVISIPVPKEAS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212  331 APVIGEIDGEYRHDSRRNTLEWCLPVIDAKNK---SGSLEFSIAGQPNDFF----PVQVSFVSKKNYC-NIQVTKVTQVD 402
Cdd:pfam00928 158 SPVLRVSDGKAKYDPEENALEWSIKKIPGGNEsslSGELELSVESSSDDEFpsdpPISVEFSIPMFTAsGLKVRYLKVEE 237
                         250       260
                  ....*....|....*....|....
gi 214010212  403 GNSP----VRFSTETtflvDKYEI 422
Cdd:pfam00928 238 ENYKpykwVRYVTQS----GSYSI 257
Delta_COP_N cd14830
delta subunit of the F-COPI complex, N-terminal domain; Delta subunit of the heterotetrameric ...
2-45 6.41e-20

delta subunit of the F-COPI complex, N-terminal domain; Delta 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: 341434  Cd Length: 130  Bit Score: 85.26  E-value: 6.41e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 214010212   2 IPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTF 45
Cdd:cd14830   87 VPEYCPSVDEEEILKNAFDLIFAFDEVISLGYRENVTLSQIKTF 130
 
Name Accession Description Interval E-value
AP_delta-COPI_MHD cd09254
Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit; COPI ...
184-420 3.50e-135

Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit; COPI complex-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. COPI complex-coated vesicles consist of a small GTPase, ADP-ribosylation factor 1 (ARF1) and a heteroheptameric coatomer composed of two subcomplexes, F-COPI and B-COPI. ARF1 regulates COPI vesicle formation by recruiting the coatomer onto Golgi membranes to initiate its coat function. Coatomer complexes then bind cargo molecules and self-assemble to form spherical cages that yield COPI-coated vesicles. The heterotetrameric F-COPI subcomplex contains beta-, gamma-, delta-, and zeta-COP subunits, where beta- and gamma-COP subunits are related to the large AP subunits, and delta- and zeta-COP subunits are related to the medium and small AP subunits, respectively. Due to the sequence similarity to the AP complexes, the F-COPI subcomplex might play a role in the cargo-binding. The heterotrimeric B-COPI contains alpha-, beta-, and epsilon-COP subunits, which are not related to the adaptins. This subcomplex is thought to participate in the cage-forming and might serve a function similar to that of clathrin. This family corresponds to the mu homology domain of delta-subunit of COPI complex (delta-COP), which is distantly related to the C-terminal domain of mu chains among AP complexes. The delta-COP subunit appears tightly associated with the beta-COP subunit to confer its interaction with ARF1. In addition, both delta- and beta-COP subunits contribute to a common binding site for arginine (R)-based signals, which are sorting motifs conferring transient endoplasmic reticulum (ER) localization to unassembled subunits of multimeric membrane proteins.


Pssm-ID: 271162  Cd Length: 237  Bit Score: 387.35  E-value: 3.50e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212 184 ESVHMKIEEKITLTCGRDGGLQNMELHGMIMLRISDDKYGRIRLHVENEDKKGVQLQTHPNVDKKLFTAESLIGLKNPEK 263
Cdd:cd09254    1 EGVHITVEEKISATLSRDGGLESLEVKGTLSLRINDEELAHIKLQLANNSDKGFQFKTHPNVDKKLFTSDSVLGLKDPSK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212 264 SFPVNSDVGVLKWRLQTTEESFIPLTINCWPSESGNGCDVNIEYELQEDNLELNDVVITIPLPSGvGAPVIGEIDGEYRH 343
Cdd:cd09254   81 PFPVNDPVGVLKWRLQGSDESLLPLTINCWPSESGGGCDVTIEYELNRDDLELNDVVISIPLPSG-DAPVVNSIDGNYEY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 214010212 344 DSRRNTLEWCLPVIDAKNKSGSLEFSI-AGQPNDFFPVQVSFVSKKNYCNIQVTKVTQVDGNSPVRFSTETTFLVDKY 420
Cdd:cd09254  160 DSRKNVLEWKIPVIDASNSSGSLEFSIpADDEDAFFPISVSFTSSKTFCGVKVVEVVSADDGEPVPFSLETSLVADKY 237
AP_MHD_Cterm cd07954
C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); ...
185-419 1.07e-85

C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); This family corresponds to the C-terminal domain of heterotetrameric AP complexes medium mu subunits and its homologs existing in monomeric stonins, delta-subunit of the heteroheptameric coat protein I (delta-COPI), a protein encoded by a pro-death gene referred as MuD (also known as MUDENG, mu-2 related death-inducing gene), an endocytic adaptor syp1, the mammalian FCH domain only proteins (FCHo1/2), SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related proteins. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. Stonins have been characterized as clathrin-dependent AP-2 mu chain related factors and may act as cargo-specific sorting adaptors in endocytosis. Coat protein complex I (COPI)-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. MuD is distantly related to the C-terminal domain of mu2 subunit of AP-2. It is able to induce cell death by itself and plays an important role in cell death in various tissues. Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis, promotes vesicle tabulation, and contributes to cell polarity and stress responses. It shares the same domain architecture with its two ubiquitously expressed mammalian counterparts, FCHo1/2, which represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Another mammalian neuronal-specific protein SGIP1 does have a C-terminal MHD and has been classified into this family as well. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


Pssm-ID: 271157  Cd Length: 245  Bit Score: 261.57  E-value: 1.07e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212 185 SVHMKIEEKITLTCGRDGGLQNMELHGMIMLRISDDKYGRIRLHVENED--KKGVQLQTHPNVDKKLFTAESLIGLKNPE 262
Cdd:cd07954    1 EVFLDVVEKVNLLISKDGSLLNSEVQGEIALKSFLSGMPEIRLGLNNPDvgIKLDDVSFHPCVRLKRFESERVISFIPPD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212 263 KSFPVNSDVGVLKWrlqtteeSFIPLTINCWPSESGNGCDVNIEYELQED-NLELNDVVITIPLPSGVGAPVIGEIDGEY 341
Cdd:cd07954   81 GEFELMSYRTVEPW-------SILPITIFPVVSEEGSQLEVVITLKLSESlQLTAENVEVHIPLPSGVTSLKSKPSDGQA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212 342 RHDSRRNTLEWCLPVIDAKNKSGSLEFSIAGQPN------DFFPVQVSFVSKKN-YCNIQVTKVTQVD-------GNSPV 407
Cdd:cd07954  154 KFDPEKNALVWRIKRIPVGGKEQSLSAHVELGSLahecpeEAPPVSVSFEIPETtGSGIQVRSLQVFDeknpghdPIKWV 233
                        250
                 ....*....|..
gi 214010212 408 RFSTETTFLVDK 419
Cdd:cd07954  234 RYITHTGKYVAR 245
Adap_comp_sub pfam00928
Adaptor complexes medium subunit family; This family also contains members which are coatomer ...
178-422 7.73e-58

Adaptor complexes medium subunit family; This family also contains members which are coatomer subunits.


Pssm-ID: 395742  Cd Length: 259  Bit Score: 190.21  E-value: 7.73e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212  178 APPINMESVHMKIEEKITLTCGRDGGLQNMELHGMIMLRISDDKYGRIRLHVENEDKK----GVQLQTHPNVDKklFTAE 253
Cdd:pfam00928   7 GIKYKKNEVFLDVIERVSVIVDKDGGLLNSEVQGTIDLKCFLSGMPELRLGLNDKLLLieldDVSFHQCVNLDK--FESE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212  254 SLIGLKNPEksfpvnSDVGVLKWRLqTTEESFIPLTINCWPSESGNGCDVNIEYELQED---NLELNDVVITIPLPSGVG 330
Cdd:pfam00928  85 RVISFIPPD------GEFELMRYRL-STNEVKLPFTVKPIVSVSGDEGRVEIEVKLRSDfpkKLTAENVVISIPVPKEAS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212  331 APVIGEIDGEYRHDSRRNTLEWCLPVIDAKNK---SGSLEFSIAGQPNDFF----PVQVSFVSKKNYC-NIQVTKVTQVD 402
Cdd:pfam00928 158 SPVLRVSDGKAKYDPEENALEWSIKKIPGGNEsslSGELELSVESSSDDEFpsdpPISVEFSIPMFTAsGLKVRYLKVEE 237
                         250       260
                  ....*....|....*....|....
gi 214010212  403 GNSP----VRFSTETtflvDKYEI 422
Cdd:pfam00928 238 ENYKpykwVRYVTQS----GSYSI 257
Delta_COP_N cd14830
delta subunit of the F-COPI complex, N-terminal domain; Delta subunit of the heterotetrameric ...
2-45 6.41e-20

delta subunit of the F-COPI complex, N-terminal domain; Delta 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: 341434  Cd Length: 130  Bit Score: 85.26  E-value: 6.41e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 214010212   2 IPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTF 45
Cdd:cd14830   87 VPEYCPSVDEEEILKNAFDLIFAFDEVISLGYRENVTLSQIKTF 130
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
2-45 2.92e-16

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: 74.86  E-value: 2.92e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 214010212   2 IPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTF 45
Cdd:cd14823   88 LSEYFRKVEERAILENFEGLYFALDEIVDGGYIQETDPKQVVHF 131
AP-3_Mu3_Cterm cd09252
C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes ...
242-402 1.35e-04

C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3 subunit, which includes two closely related homologs, mu3A (P47A, encoded by ap3m1) and mu1B (P47B, encoded by ap3m2). Mu3A is ubiquitously expressed, but mu3B is specifically expressed in neurons and neuroendocrine cells. AP-3 is particularly important for targeting integral membrane proteins to lysosomes and lysome-related organelles at trans-Golgi network (TGN) and/or endosomes, such as the yeast vacuole, fly pigment granules and mammalian melanosomes, platelet dense bodies and the secretory lysosomes of cytotoxic T lymphocytes. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 271160  Cd Length: 251  Bit Score: 43.34  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212 242 HPNVDKKLFTAESLIglknpekSF-PVNSDVGVLKWRLQTTEESFIPLTINCWPSESGNGCDVNIE-YELQEDNLELNDV 319
Cdd:cd09252   70 HPCVRYSRWESERVL-------SFiPPDGKFTLMSYRVDLNSLVSLPVYVKPQISFSGSSGRFEITvGSRQNLGKSIENV 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214010212 320 VITIPLPSGVGAPVIGEIDGEYRHDSRRNTLEWCLPVIDaKNKSGSLEFSIAGQPNDFFPVQVSFVSKKnYCNIQVT--- 396
Cdd:cd09252  143 VVEIPLPKGVKSLRLTASHGSFSFDSSTKTLVWNIGKLT-PGKTPTLRGSVSLSSGLEAPSESPSISVQ-FKIPGYTpsg 220

                 ....*..
gi 214010212 397 -KVTQVD 402
Cdd:cd09252  221 lKVDSLD 227
 
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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