AP1M_CAEEL
ID AP1M_CAEEL Reviewed; 422 AA.
AC P35602; O02282; Q1ZXR6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=AP-1 complex subunit mu-1-I;
DE AltName: Full=Clathrin assembly protein complex 1 mu-1-I medium chain;
DE AltName: Full=Clathrin coat assembly protein AP47;
DE AltName: Full=Clathrin coat-associated protein AP47;
DE AltName: Full=Golgi adaptor AP-1 47 kDa protein;
DE AltName: Full=HA1 47 kDa subunit;
DE AltName: Full=Mu1-I-adaptin;
DE AltName: Full=Uncoordinated protein 101;
GN Name=unc-101; ORFNames=K11D2.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Bristol N2;
RX PubMed=8288128; DOI=10.1101/gad.8.1.60;
RA Lee J., Jongeward G.D., Sternberg P.W.;
RT "unc-101, a gene required for many aspects of Caenorhabditis elegans
RT development and behavior, encodes a clathrin-associated protein.";
RL Genes Dev. 8:60-73(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, INTERACTION WITH KVS-4, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=26762178; DOI=10.1002/1873-3468.12043;
RA Zhou X., Zeng J., Ouyang C., Luo Q., Yu M., Yang Z., Wang H., Shen K.,
RA Shi A.;
RT "A novel bipartite UNC-101/AP-1 mu1 binding signal mediates KVS-4/Kv2.1
RT somatodendritic distribution in Caenorhabditis elegans.";
RL FEBS Lett. 590:76-92(2016).
CC -!- FUNCTION: Component of the adaptor complexes which link clathrin to
CC receptors in coated vesicles (Probable). Clathrin-associated protein
CC complexes are believed to interact with the cytoplasmic tails of
CC membrane proteins, leading to their selection and concentration
CC (Probable). Required for many aspects of development and behavior,
CC including negative regulation of vulval differentiation
CC (PubMed:8288128). Required for the dendritic localization of potassium
CC channel kvs-4 in the cholinergic motor neuron DA9 (PubMed:26762178).
CC {ECO:0000269|PubMed:26762178, ECO:0000269|PubMed:8288128,
CC ECO:0000305|PubMed:8288128}.
CC -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC of two large adaptins (gamma- and beta'-type subunits), a medium
CC adaptin (mu-type subunit AP47) and a small adaptin (sigma-type subunit
CC AP19) (By similarity). Interacts (via N-terminus) with kvs-4
CC (PubMed:26762178). {ECO:0000250|UniProtKB:Q9WVP1,
CC ECO:0000269|PubMed:26762178}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:26762178}.
CC Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC {ECO:0000303|PubMed:8288128}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P38153}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P38153}. Cell projection, dendrite
CC {ECO:0000305|PubMed:26762178}. Note=Component of the coat surrounding
CC the cytoplasmic face of coated vesicles located at the Golgi complex
CC (By similarity). Association with kvs-4, targets kvs-4 to dendrites
CC (PubMed:26762178). {ECO:0000250|UniProtKB:P38153,
CC ECO:0000305|PubMed:26762178}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:K11D2.3a};
CC IsoId=P35602-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:K11D2.3b};
CC IsoId=P35602-2; Sequence=VSP_020097;
CC -!- TISSUE SPECIFICITY: Expressed in the cholinergic motor neuron DA9.
CC {ECO:0000269|PubMed:26762178}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
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DR EMBL; L26291; AAA72418.1; -; mRNA.
DR EMBL; Z83115; CAB05557.3; -; Genomic_DNA.
DR EMBL; Z83115; CAJ85757.1; -; Genomic_DNA.
DR PIR; A49837; A49837.
DR PIR; T23603; T23603.
DR RefSeq; NP_001040675.1; NM_001047210.2. [P35602-1]
DR RefSeq; NP_001040676.1; NM_001047211.1. [P35602-2]
DR AlphaFoldDB; P35602; -.
DR SMR; P35602; -.
DR BioGRID; 38518; 11.
DR IntAct; P35602; 9.
DR MINT; P35602; -.
DR STRING; 6239.K11D2.3a.2; -.
DR EPD; P35602; -.
DR PaxDb; P35602; -.
DR PeptideAtlas; P35602; -.
DR EnsemblMetazoa; K11D2.3a.1; K11D2.3a.1; WBGene00006829. [P35602-1]
DR EnsemblMetazoa; K11D2.3b.1; K11D2.3b.1; WBGene00006829. [P35602-2]
DR GeneID; 173121; -.
DR KEGG; cel:CELE_K11D2.3; -.
DR UCSC; K11D2.3a.1; c. elegans. [P35602-1]
DR CTD; 173121; -.
DR WormBase; K11D2.3a; CE28050; WBGene00006829; unc-101. [P35602-1]
DR WormBase; K11D2.3b; CE40095; WBGene00006829; unc-101. [P35602-2]
DR eggNOG; KOG0937; Eukaryota.
DR GeneTree; ENSGT00940000157924; -.
DR HOGENOM; CLU_026996_0_0_1; -.
DR InParanoid; P35602; -.
DR OMA; CRAKAQI; -.
DR OrthoDB; 725236at2759; -.
DR PhylomeDB; P35602; -.
DR Reactome; R-CEL-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-CEL-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR SignaLink; P35602; -.
DR PRO; PR:P35602; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006829; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; P35602; baseline and differential.
DR GO; GO:0030121; C:AP-1 adaptor complex; NAS:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0045176; P:apical protein localization; IGI:WormBase.
DR GO; GO:0060271; P:cilium assembly; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
DR GO; GO:0097500; P:receptor localization to non-motile cilium; IMP:WormBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0040025; P:vulval development; NAS:UniProtKB.
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 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; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
DR PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasmic vesicle;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..422
FT /note="AP-1 complex subunit mu-1-I"
FT /id="PRO_0000193789"
FT DOMAIN 167..420
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT VAR_SEQ 1..364
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020097"
FT CONFLICT 400
FT /note="S -> R (in Ref. 1; AAA72418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 48229 MW; 947BF5D1EF496C8B CRC64;
MATSAMFILD LKGKTIISRN YRGDIDMTAI DKFIHLLMEK EEEGSAAPVL TYQDTNFVFI
KHTNIYLVSA CRSNVNVTMI LSFLYKCVEV FSEYFKDVEE ESVRDNFVVI YELLDEMMDF
GFPQTTESRI LQEYITQEGQ KLISAPRPPM AVTNAVSWRS EGIKYRKNEV FLDVIESVNM
LASANGTVLQ SEIVGSVKMR VYLTGMPELR LGLNDKVLFE GSGRGKSKSV ELEDVKFHQC
VRLSRFDTDR TISFIPPDGA FELMSYRLTT VVKPLIWIET SIERHSHSRV SFIIKAKSQF
KRRSTANNVE IIIPVPSDAD SPKFKTSIGS VKYTPEQSAF VWTIKNFPGG KEYLLTAHLS
LPSVMSEESE GRPPIKVKFE IPYFTTSGIQ VRYLKIIEKS GYQALPWVRY ITQNGEYEMR
MK
