ID   AP1M1_YEAST             Reviewed;         475 AA.
AC   Q00776; D6W3B0;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   27-MAR-2024, entry version 184.
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 AP54;
DE   AltName: Full=Clathrin coat-associated protein AP54;
DE   AltName: Full=Golgi adaptor AP-1 54 kDa protein;
DE   AltName: Full=HA1 54 kDa subunit;
DE   AltName: Full=Mu(1)-adaptin;
DE   AltName: Full=Mu1-I-adaptin;
GN   Name=APM1; Synonyms=YAP54; OrderedLocusNames=YPL259C; ORFNames=P0394;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1761056; DOI=10.1111/j.1432-1033.1991.tb16409.x;
RA   Nakayama Y., Goebl M., O'Brine Greco B., Lemmon S., Pingchang C.E.,
RA   Kirchhausen T.;
RT   "The medium chains of the mammalian clathrin-associated proteins have a
RT   homolog in yeast.";
RL   Eur. J. Biochem. 202:569-574(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION, SUBUNIT, AND INTERACTION WITH CLATHRIN.
RX   PubMed=10564262; DOI=10.1091/mbc.10.11.3643;
RA   Yeung B.G., Phan H.L., Payne G.S.;
RT   "Adaptor complex-independent clathrin function in yeast.";
RL   Mol. Biol. Cell 10:3643-3659(1999).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Component of the adaptor complexes which link clathrin to
CC       receptors in coated vesicles. Clathrin-associated protein complexes are
CC       believed to interact with the cytoplasmic tails of membrane proteins,
CC       leading to their selection and concentration. The AP-1 complex
CC       interacts directly with clathrin. AP57 is probably a subunit of the
CC       Golgi membrane adaptor. {ECO:0000269|PubMed:10564262}.
CC   -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC       of two large adaptins (gamma-type subunit APL4 and beta-type subunit
CC       APL2), a medium adaptin (mu-type subunit APM1) and a small adaptin
CC       (sigma-type subunit APS1). AP-1 interacts with clathrin.
CC       {ECO:0000269|PubMed:10564262}.
CC   -!- INTERACTION:
CC       Q00776; P36000: APL2; NbExp=9; IntAct=EBI-2624, EBI-2206;
CC       Q00776; P35181: APS1; NbExp=4; IntAct=EBI-2624, EBI-2612;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle. Cytoplasmic vesicle,
CC       clathrin-coated vesicle membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Membrane,
CC       clathrin-coated pit {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 4420 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC       {ECO:0000305}.
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DR   EMBL; X60288; CAA42828.1; -; Genomic_DNA.
DR   EMBL; Z73615; CAA97989.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11176.1; -; Genomic_DNA.
DR   PIR; S65290; S65290.
DR   RefSeq; NP_015064.1; NM_001184073.1.
DR   AlphaFoldDB; Q00776; -.
DR   SMR; Q00776; -.
DR   BioGRID; 35953; 222.
DR   ComplexPortal; CPX-532; Adaptor complex AP-1.
DR   DIP; DIP-1198N; -.
DR   IntAct; Q00776; 53.
DR   MINT; Q00776; -.
DR   STRING; 4932.YPL259C; -.
DR   iPTMnet; Q00776; -.
DR   MaxQB; Q00776; -.
DR   PaxDb; 4932-YPL259C; -.
DR   PeptideAtlas; Q00776; -.
DR   EnsemblFungi; YPL259C_mRNA; YPL259C; YPL259C.
DR   GeneID; 855869; -.
DR   KEGG; sce:YPL259C; -.
DR   AGR; SGD:S000006180; -.
DR   SGD; S000006180; APM1.
DR   VEuPathDB; FungiDB:YPL259C; -.
DR   eggNOG; KOG0937; Eukaryota.
DR   GeneTree; ENSGT00940000165747; -.
DR   HOGENOM; CLU_026996_0_2_1; -.
DR   InParanoid; Q00776; -.
DR   OMA; KPLIWCD; -.
DR   OrthoDB; 6959at2759; -.
DR   BioCyc; YEAST:G3O-34144-MONOMER; -.
DR   Reactome; R-SCE-432720; Lysosome Vesicle Biogenesis.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 855869; 1 hit in 10 CRISPR screens.
DR   PRO; PR:Q00776; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q00776; Protein.
DR   GO; GO:0030121; C:AP-1 adaptor complex; IDA:SGD.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR   GO; GO:0006896; P:Golgi to vacuole transport; IMP:SGD.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0048203; P:vesicle targeting, trans-Golgi to endosome; NAS:ComplexPortal.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   CDD; cd09250; AP-1_Mu1_Cterm; 1.
DR   CDD; cd14835; AP1_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:SF262; ADAPTOR PROTEIN COMPLEX 1, MU SUBUNIT; 1.
DR   PANTHER; PTHR10529; AP COMPLEX SUBUNIT MU; 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; 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   Coated pit; Cytoplasmic vesicle; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..475
FT                   /note="AP-1 complex subunit mu-1-I"
FT                   /id="PRO_0000193778"
FT   DOMAIN          175..473
FT                   /note="MHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT   REGION          240..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        214
FT                   /note="M -> I (in Ref. 1; CAA42828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216
FT                   /note="D -> H (in Ref. 1; CAA42828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="N -> K (in Ref. 1; CAA42828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        433
FT                   /note="P -> R (in Ref. 1; CAA42828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        440
FT                   /note="I -> M (in Ref. 1; CAA42828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        450
FT                   /note="Missing (in Ref. 1; CAA42828)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   475 AA;  53874 MW;  C6B11153B845921C CRC64;
     MASAVYFCDH NGKPLLSRRY RDDIPLSAID KFPILLSDLE EQSNLIPPCL NHNGLEYLFI
     QHNDLYVVAI VTSLSANAAA IFTFLHKLVE VLSDYLKTVE EESIRDNFVI IYELLDEVMD
     YGIPQITETK MLKQYITQKS FKLVKSAKKK RNATRPPVAL TNSVSWRPEG ITHKKNEAFL
     DIVESINMLM TQKGQVLRSE IIGDVKVNSK LSGMPDLKLG INDKGIFSKY LDDDTNIPSA
     SATTSDNNTE TDKKPSITSS SATNKKKVNI ELEDLKFHQC VRLSKFENEK IITFIPPDGK
     FDLMNYRLST TIKPLIWCDV NVQVHSNSRI EIHCKAKAQI KRKSTATNVE ILIPVPDDAD
     TPTFKYSHGS LKYVPEKSAI LWKIRSFPGG KEYSMSAELG LPSISNNEDG NRTMPKSNAE
     ILKGPVQIKF QIPYFTTSGI QVRYLKINEP KLQYKSYPWV RYITQSGDDY TIRLT
//