ID M3YHI0_MUSPF Unreviewed; 452 AA.
AC M3YHI0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=AP-4 complex subunit mu-1 {ECO:0000256|ARBA:ARBA00041045, ECO:0000256|PIRNR:PIRNR005992};
GN Name=AP4M1 {ECO:0000313|Ensembl:ENSMPUP00000010787.1,
GN ECO:0000313|RefSeq:XP_004781874.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000010787.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000010787.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004781874.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004781874.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the adaptor protein complex 4 (AP-4). Adaptor
CC protein complexes are vesicle coat components involved both in vesicle
CC formation and cargo selection. They control the vesicular transport of
CC proteins in different trafficking pathways. AP-4 forms a non clathrin-
CC associated coat on vesicles departing the trans-Golgi network (TGN) and
CC may be involved in the targeting of proteins from the trans-Golgi
CC network (TGN) to the endosomal-lysosomal system. It is also involved in
CC protein sorting to the basolateral membrane in epithelial cells and the
CC proper asymmetric localization of somatodendritic proteins in neurons.
CC Within AP-4, the mu-type subunit AP4M1 is directly involved in the
CC recognition and binding of tyrosine-based sorting signals found in the
CC cytoplasmic part of cargos. The adaptor protein complex 4 (AP-4) may
CC also recognize other types of sorting signal.
CC {ECO:0000256|PIRNR:PIRNR005992}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000256|ARBA:ARBA00004412,
CC ECO:0000256|PIRNR:PIRNR005992}. Endosome
CC {ECO:0000256|ARBA:ARBA00004177}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000256|ARBA:ARBA00004150,
CC ECO:0000256|PIRNR:PIRNR005992}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004150, ECO:0000256|PIRNR:PIRNR005992}.
CC Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000256|ARBA:ARBA00005324, ECO:0000256|PIRNR:PIRNR005992}.
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DR EMBL; AEYP01103964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004781874.1; XM_004781817.3.
DR STRING; 9669.ENSMPUP00000010787; -.
DR Ensembl; ENSMPUT00000010966.1; ENSMPUP00000010787.1; ENSMPUG00000010875.1.
DR GeneID; 101673602; -.
DR KEGG; mpuf:101673602; -.
DR CTD; 9179; -.
DR eggNOG; KOG0937; Eukaryota.
DR GeneTree; ENSGT00940000159929; -.
DR HOGENOM; CLU_026996_5_0_1; -.
DR OMA; DYGYIQN; -.
DR OrthoDB; 5353102at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0030124; C:AP-4 adaptor complex; IEA:Ensembl.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0000045; P:autophagosome assembly; IEA:Ensembl.
DR GO; GO:0006895; P:Golgi to endosome transport; IEA:Ensembl.
DR GO; GO:0090160; P:Golgi to lysosome transport; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006622; P:protein targeting to lysosome; IEA:Ensembl.
DR CDD; cd09253; AP-4_Mu4_Cterm; 1.
DR CDD; cd14838; AP4_Mu_N; 1.
DR Gene3D; 3.30.450.60; -; 1.
DR Gene3D; 2.60.40.1170; Mu homology domain, subdomain B; 2.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR001392; Clathrin_mu.
DR InterPro; IPR018240; Clathrin_mu_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
DR PANTHER; PTHR10529; AP COMPLEX SUBUNIT MU; 1.
DR PANTHER; PTHR10529:SF270; AP-4 COMPLEX SUBUNIT MU-1; 1.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR PIRSF; PIRSF005992; Clathrin_mu; 1.
DR PRINTS; PR00314; CLATHRINADPT.
DR SUPFAM; SSF49447; Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor; 1.
DR SUPFAM; SSF64356; SNARE-like; 1.
DR PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR PROSITE; PS51072; MHD; 1.
PE 3: Inferred from homology;
KW Endosome {ECO:0000256|ARBA:ARBA00022753, ECO:0000256|PIRNR:PIRNR005992};
KW Golgi apparatus {ECO:0000256|PIRNR:PIRNR005992};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR005992};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|PIRNR:PIRNR005992};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005992}.
FT DOMAIN 184..451
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
SQ SEQUENCE 452 AA; 49955 MW; 230A0C8DD6B0A795 CRC64;
MISQFFILSS KGDPLIYKDF RGDTGGRDVA ELFYRKLTGL SGDESPVVMH HDDRHFIHIR
HSGLYLVATT SENISPFSLL ELLSRLATLL GDYCGSLNEG TISRNVALVY ELLDEVLDYG
YVQTTSMEML RNFIQTEAVV SKPFSLFDLS SVGLFGAETQ QSKVAPSSAA SRPVLASRSD
QSQKNEVFLD VVERLSVLIA SNGSLLKVDV QGEIRLKSFL PSGSEMRIGL TEEFCVGKSE
LRGYGPGIRV DEVSFHSSVL LEEFESHRIL RLQPPQGELT VMRYQLSDDL PSPLPFRLFP
SVQWDRGSGR LQVYLKLRCD LPPKSQALNV RLHLPLPRGV ISLSQELSGP EQKAELGEGA
LRWDLPRVQG GSQLSGLFQM DVPGLPGPPG QGPSTSAPLG LGPASLSFEL PRHTCSGLQV
RFLRLAFRPC GNTNPHKWVR HLSHSDAYVI RI
//
