AP1M1_YEAST
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 03-AUG-2022, entry version 177.
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; 216.
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; Q00776; -.
DR PRIDE; Q00776; -.
DR EnsemblFungi; YPL259C_mRNA; YPL259C; YPL259C.
DR GeneID; 855869; -.
DR KEGG; sce:YPL259C; -.
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; CRAKAQI; -.
DR BioCyc; YEAST:G3O-34144-MON; -.
DR Reactome; R-SCE-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
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:0031410; C:cytoplasmic 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; IC:ComplexPortal.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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 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
