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Conserved domains on  [gi|119601109|gb|EAW80703|]
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chromosome 14 open reading frame 108, isoform CRA_c [Homo sapiens]

Protein Classification

adaptor complexes medium subunit family protein; AP-1 complex subunit mu( domain architecture ID 10174169)

adaptor complexes medium subunit family protein similar to Homo sapiens archain that forms part of a protein complex and might be involved in vesicle assembly or sorting| AP-1 complex subunit mu is a subunit of the clathrin-associated adaptor protein complex 1 that plays a role in protein sorting at the trans-Golgi network and early endosomes (TGN/EE)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AP_MuD_MHD cd09256
Mu-homology domain (MHD) of a adaptor protein (AP) encoded by mu-2 related death-inducing gene, ...
2-236 3.16e-121

Mu-homology domain (MHD) of a adaptor protein (AP) encoded by mu-2 related death-inducing gene, MuD (also known as MUDENG); This family corresponds to the MHD found in a protein encoded by MuD (also known as Adapter-related protein complex 5 subunit mu-1), which is distantly related to the C-terminal domain of the mu2 subunit of AP complexes that participates in clathrin-mediated endocytosis. MuD is evolutionary conserved from mammals to amphibians. It is able to induce cell death by itself and plays an important role in cell death in various tissues.


:

Pssm-ID: 271164  Cd Length: 276  Bit Score: 345.91  E-value: 3.16e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601109   2 PNVTISLSLPTNgSPLQDILVHPCVTSLDSAIltsssidamddSAFSGPYKFPFTPPLESFNLCFYTSQ-VPVPPILGFY 80
Cdd:cd09256   52 PEVTVSLSVPAN-SPLQAIIVHPCVQSPESGM-----------LAFSGPYKIRFSPPLGNFVLCRYQSQsVPVPPILGFY 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601109  81 QMKEEEVQLRITINLKLHESVKNNFEFCEAHIPFYNRGPITHLEYKTSFGQLEVFREKSLLIWIIGQKFPKSMEISLSGT 160
Cdd:cd09256  120 QMKGDEKHVKFLIQLKLHESVKNSFEYCEVHIPFPNRGLIKHVSATPSNGQLEVSKEKRRLVWNIGQKFPKSLEATLSGT 199
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119601109 161 VTFGAKSHE-KQPFDPICTGETAYLKLHFRILDYTLTGCYADQHSVQVFASGKPKISAHRKLISSDYYIWNSKAPAP 236
Cdd:cd09256  200 VNFGSESNRrADPEDPFCVGLNAYVKLFFKISDYTLSGCSIDPKSVQIYPSAKTKIITSREVVSSDYIIWNSLGDAP 276
 
Name Accession Description Interval E-value
AP_MuD_MHD cd09256
Mu-homology domain (MHD) of a adaptor protein (AP) encoded by mu-2 related death-inducing gene, ...
2-236 3.16e-121

Mu-homology domain (MHD) of a adaptor protein (AP) encoded by mu-2 related death-inducing gene, MuD (also known as MUDENG); This family corresponds to the MHD found in a protein encoded by MuD (also known as Adapter-related protein complex 5 subunit mu-1), which is distantly related to the C-terminal domain of the mu2 subunit of AP complexes that participates in clathrin-mediated endocytosis. MuD is evolutionary conserved from mammals to amphibians. It is able to induce cell death by itself and plays an important role in cell death in various tissues.


Pssm-ID: 271164  Cd Length: 276  Bit Score: 345.91  E-value: 3.16e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601109   2 PNVTISLSLPTNgSPLQDILVHPCVTSLDSAIltsssidamddSAFSGPYKFPFTPPLESFNLCFYTSQ-VPVPPILGFY 80
Cdd:cd09256   52 PEVTVSLSVPAN-SPLQAIIVHPCVQSPESGM-----------LAFSGPYKIRFSPPLGNFVLCRYQSQsVPVPPILGFY 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601109  81 QMKEEEVQLRITINLKLHESVKNNFEFCEAHIPFYNRGPITHLEYKTSFGQLEVFREKSLLIWIIGQKFPKSMEISLSGT 160
Cdd:cd09256  120 QMKGDEKHVKFLIQLKLHESVKNSFEYCEVHIPFPNRGLIKHVSATPSNGQLEVSKEKRRLVWNIGQKFPKSLEATLSGT 199
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119601109 161 VTFGAKSHE-KQPFDPICTGETAYLKLHFRILDYTLTGCYADQHSVQVFASGKPKISAHRKLISSDYYIWNSKAPAP 236
Cdd:cd09256  200 VNFGSESNRrADPEDPFCVGLNAYVKLFFKISDYTLSGCSIDPKSVQIYPSAKTKIITSREVVSSDYIIWNSLGDAP 276
Adap_comp_sub pfam00928
Adaptor complexes medium subunit family; This family also contains members which are coatomer ...
1-229 7.70e-39

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


Pssm-ID: 395742  Cd Length: 259  Bit Score: 135.51  E-value: 7.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601109    1 MPNVTISLSLPTNGSPLQDILVHPCVtsldsailtsssidamDDSAFSGPYKFPFTPPLESFNLCFY---TSQVPVP-PI 76
Cdd:pfam00928  51 MPELRLGLNDKLLLIELDDVSFHQCV----------------NLDKFESERVISFIPPDGEFELMRYrlsTNEVKLPfTV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601109   77 LGFYQMKEEEVQLRITINLKLHESVKNNFEFCEAHIPFYNRgpITHLEYKTSFGQLEVFREKSLLIWIIGqKFPKSMEIS 156
Cdd:pfam00928 115 KPIVSVSGDEGRVEIEVKLRSDFPKKLTAENVVISIPVPKE--ASSPVLRVSDGKAKYDPEENALEWSIK-KIPGGNESS 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119601109  157 LSGTVTFGAKSHEKQPFDPICTgetayLKLHFRILDYTLTGCYADQHSVQVfASGKPKISAHRKLISSDYYIW 229
Cdd:pfam00928 192 LSGELELSVESSSDDEFPSDPP-----ISVEFSIPMFTASGLKVRYLKVEE-ENYKPYKWVRYVTQSGSYSIR 258
 
Name Accession Description Interval E-value
AP_MuD_MHD cd09256
Mu-homology domain (MHD) of a adaptor protein (AP) encoded by mu-2 related death-inducing gene, ...
2-236 3.16e-121

Mu-homology domain (MHD) of a adaptor protein (AP) encoded by mu-2 related death-inducing gene, MuD (also known as MUDENG); This family corresponds to the MHD found in a protein encoded by MuD (also known as Adapter-related protein complex 5 subunit mu-1), which is distantly related to the C-terminal domain of the mu2 subunit of AP complexes that participates in clathrin-mediated endocytosis. MuD is evolutionary conserved from mammals to amphibians. It is able to induce cell death by itself and plays an important role in cell death in various tissues.


Pssm-ID: 271164  Cd Length: 276  Bit Score: 345.91  E-value: 3.16e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601109   2 PNVTISLSLPTNgSPLQDILVHPCVTSLDSAIltsssidamddSAFSGPYKFPFTPPLESFNLCFYTSQ-VPVPPILGFY 80
Cdd:cd09256   52 PEVTVSLSVPAN-SPLQAIIVHPCVQSPESGM-----------LAFSGPYKIRFSPPLGNFVLCRYQSQsVPVPPILGFY 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601109  81 QMKEEEVQLRITINLKLHESVKNNFEFCEAHIPFYNRGPITHLEYKTSFGQLEVFREKSLLIWIIGQKFPKSMEISLSGT 160
Cdd:cd09256  120 QMKGDEKHVKFLIQLKLHESVKNSFEYCEVHIPFPNRGLIKHVSATPSNGQLEVSKEKRRLVWNIGQKFPKSLEATLSGT 199
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119601109 161 VTFGAKSHE-KQPFDPICTGETAYLKLHFRILDYTLTGCYADQHSVQVFASGKPKISAHRKLISSDYYIWNSKAPAP 236
Cdd:cd09256  200 VNFGSESNRrADPEDPFCVGLNAYVKLFFKISDYTLSGCSIDPKSVQIYPSAKTKIITSREVVSSDYIIWNSLGDAP 276
AP_MHD_Cterm cd07954
C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); ...
1-236 8.30e-76

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: 229.60  E-value: 8.30e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601109   1 MPNVTISLSLPTNGSPLQDILVHPCVTSLDsailtsssidamddsaFSGPYKFPFTPPLESFNLCFYTSQVP--VPPILG 78
Cdd:cd07954   38 MPEIRLGLNNPDVGIKLDDVSFHPCVRLKR----------------FESERVISFIPPDGEFELMSYRTVEPwsILPITI 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601109  79 FYQMKEEEVQLRITINLKLHESVKNNFEFCEAHIPFYNRgpITHLEYKTSFGQLEVFREKSLLIWIIGQKFPKSMEISLS 158
Cdd:cd07954  102 FPVVSEEGSQLEVVITLKLSESLQLTAENVEVHIPLPSG--VTSLKSKPSDGQAKFDPEKNALVWRIKRIPVGGKEQSLS 179
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119601109 159 GTVTFGAKSHEkqpfdpiCTGETAYLKLHFRILDYTLTGCYADqhSVQVFASGKPkisAHRKLISSDYYIWNSKAPAP 236
Cdd:cd07954  180 AHVELGSLAHE-------CPEEAPPVSVSFEIPETTGSGIQVR--SLQVFDEKNP---GHDPIKWVRYITHTGKYVAR 245
Adap_comp_sub pfam00928
Adaptor complexes medium subunit family; This family also contains members which are coatomer ...
1-229 7.70e-39

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


Pssm-ID: 395742  Cd Length: 259  Bit Score: 135.51  E-value: 7.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601109    1 MPNVTISLSLPTNGSPLQDILVHPCVtsldsailtsssidamDDSAFSGPYKFPFTPPLESFNLCFY---TSQVPVP-PI 76
Cdd:pfam00928  51 MPELRLGLNDKLLLIELDDVSFHQCV----------------NLDKFESERVISFIPPDGEFELMRYrlsTNEVKLPfTV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601109   77 LGFYQMKEEEVQLRITINLKLHESVKNNFEFCEAHIPFYNRgpITHLEYKTSFGQLEVFREKSLLIWIIGqKFPKSMEIS 156
Cdd:pfam00928 115 KPIVSVSGDEGRVEIEVKLRSDFPKKLTAENVVISIPVPKE--ASSPVLRVSDGKAKYDPEENALEWSIK-KIPGGNESS 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119601109  157 LSGTVTFGAKSHEKQPFDPICTgetayLKLHFRILDYTLTGCYADQHSVQVfASGKPKISAHRKLISSDYYIW 229
Cdd:pfam00928 192 LSGELELSVESSSDDEFPSDPP-----ISVEFSIPMFTASGLKVRYLKVEE-ENYKPYKWVRYVTQSGSYSIR 258
AP-3_Mu3_Cterm cd09252
C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes ...
1-197 8.49e-06

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: 45.65  E-value: 8.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601109   1 MPNVTISLSLPtngSPLQDILVHPCVtsldsailtsssidamDDSAFSGPYKFPFTPPLESFNLCFYTSQVPVPPILGFY 80
Cdd:cd09252   51 MPDLLLSFNNP---RLLDDPSFHPCV----------------RYSRWESERVLSFIPPDGKFTLMSYRVDLNSLVSLPVY 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601109  81 ---QMKEEEVQLRITINLKLHESVKNNFEFCEAHIPFynrGP------ITHLEYKTSFGQLevfreKSLLIWIIGqKFPK 151
Cdd:cd09252  112 vkpQISFSGSSGRFEITVGSRQNLGKSIENVVVEIPL---PKgvkslrLTASHGSFSFDSS-----TKTLVWNIG-KLTP 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 119601109 152 SMEISLSGTVTFGAKSHEkqpfdpicTGETAYLKLHFRILDYTLTG 197
Cdd:cd09252  183 GKTPTLRGSVSLSSGLEA--------PSESPSISVQFKIPGYTPSG 220
AP-1_Mu1B_Cterm cd09259
C-terminal domain of medium Mu1B subunit in epithelial cell-specific clathrin-associated ...
17-174 3.66e-04

C-terminal domain of medium Mu1B subunit in epithelial cell-specific clathrin-associated adaptor protein (AP) complex AP-1; 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 different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1B subunit encoded by ap1m2 gene exclusively expressed in polarized epithelial cells. Epithelial cell-specific AP-1 is used to sort proteins to the basolateral plasma membrane, which involves the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1). The phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those 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-1 mu1B 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 reside-binding. Besides, AP-1 mu1B subunit mediates the basolateral recycling of low-density lipoprotein receptor (LDLR) and transferrin receptor (TfR) from the sorting endosomes, where the basolateral sorting signal does not belong to the tyrosine-based signals. Thus, the binding site in mu1B subunit of AP-1 for the signals of LDLR and TfR might be distinct from that for YXXPhi signals.


Pssm-ID: 271167  Cd Length: 268  Bit Score: 40.77  E-value: 3.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601109  17 LQDILVHPCVTSldsailtsssidamddSAFSGPYKFPFTPPLESFNLCFYTSQVPVPPILGFYQMKEEEVQLRITINLK 96
Cdd:cd09259   80 LEDVKFHQCVRL----------------SRFENDRTISFIPPDGDFELMSYRLNTQVKPLIWIESVIEKFSHSRVEIMVK 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119601109  97 LH-----ESVKNNFEFcEAHIPFYNRGPithlEYKTSFGQLEVFREKSLLIWIIgQKFPKSMEISLSGtvTFGAKSHEKQ 171
Cdd:cd09259  144 AKgqfkkQSVANNVEI-RVPVPSDADSP----KFKTSVGSAKYVPEKNVVVWSI-KSFPGGKEYLMRA--HFGLPSVENE 215

                 ...
gi 119601109 172 PFD 174
Cdd:cd09259  216 ELE 218
 
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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