AP2M_YEAST
ID AP2M_YEAST Reviewed; 491 AA.
AC Q99186; D6W205;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=AP-2 complex subunit mu;
DE AltName: Full=Adaptin medium chain APM4;
DE AltName: Full=Clathrin assembly protein complex 2 mu medium chain;
DE AltName: Full=Clathrin coat assembly protein AP50;
DE AltName: Full=Clathrin coat-associated protein AP50;
DE AltName: Full=Mu2-adaptin;
DE AltName: Full=Plasma membrane adaptor AP-2 50 kDa protein;
GN Name=APM4; Synonyms=AMP1; OrderedLocusNames=YOL062C; ORFNames=O1210;
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].
RC STRAIN=ATCC 90843 / S288c / FY73;
RX PubMed=8789261;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<67::aid-yea884>3.0.co;2-f;
RA Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.;
RT "Analysis of a 26 kb region on the left arm of yeast chromosome XV.";
RL Yeast 12:67-76(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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, AND SUBUNIT.
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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179; SER-180 AND SER-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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.
CC {ECO:0000269|PubMed:10564262}.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC of two large adaptins (alpha-type subunit APL3 and beta-type subunit
CC APL1), a medium chain (mu-type subunit APM4) and a small adaptin
CC (sigma-type subunit APS2). {ECO:0000269|PubMed:10564262}.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit. Cytoplasmic
CC vesicle, clathrin-coated vesicle membrane.
CC -!- MISCELLANEOUS: Present with 3410 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; X91067; CAA62522.1; -; Genomic_DNA.
DR EMBL; Z74804; CAA99071.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10721.1; -; Genomic_DNA.
DR PIR; S61715; S61715.
DR RefSeq; NP_014579.1; NM_001183317.1.
DR AlphaFoldDB; Q99186; -.
DR SMR; Q99186; -.
DR BioGRID; 34339; 52.
DR ComplexPortal; CPX-534; Adapter complex AP-2.
DR DIP; DIP-5448N; -.
DR IntAct; Q99186; 34.
DR MINT; Q99186; -.
DR STRING; 4932.YOL062C; -.
DR iPTMnet; Q99186; -.
DR MaxQB; Q99186; -.
DR PaxDb; Q99186; -.
DR PRIDE; Q99186; -.
DR EnsemblFungi; YOL062C_mRNA; YOL062C; YOL062C.
DR GeneID; 854092; -.
DR KEGG; sce:YOL062C; -.
DR SGD; S000005423; APM4.
DR VEuPathDB; FungiDB:YOL062C; -.
DR eggNOG; KOG0938; Eukaryota.
DR GeneTree; ENSGT00940000159223; -.
DR HOGENOM; CLU_026996_5_2_1; -.
DR InParanoid; Q99186; -.
DR OMA; VWKIPRI; -.
DR BioCyc; YEAST:G3O-33470-MON; -.
DR Reactome; R-SCE-196025; Formation of annular gap junctions.
DR Reactome; R-SCE-437239; Recycling pathway of L1.
DR Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-SCE-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-SCE-8866427; VLDLR internalisation and degradation.
DR Reactome; R-SCE-8964038; LDL clearance.
DR PRO; PR:Q99186; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q99186; protein.
DR GO; GO:0030122; C:AP-2 adaptor complex; IPI:SGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IC:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd09251; AP-2_Mu2_Cterm; 1.
DR CDD; cd14836; AP2_Mu_N; 1.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR043532; AP2_Mu_N.
DR InterPro; IPR001392; Clathrin_mu.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR043512; Mu2_C.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR PIRSF; PIRSF005992; Clathrin_mu; 1.
DR SUPFAM; SSF49447; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW Coated pit; Cytoplasmic vesicle; Endocytosis; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..491
FT /note="AP-2 complex subunit mu"
FT /id="PRO_0000193780"
FT DOMAIN 209..490
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 491 AA; 55387 MW; DCAF8F6BF8D43D45 CRC64;
MISGVLVYSS RGELVLNKFF KNSLKRSISD IFRVQVINNL DVRSPVLTLG STTFHHIRSR
HGDNLWLVTI TRSNANSAAI WEFLYKLDAV MNAYRLDREE ALKEEFMIVH EMLDIMLGGN
GIPIDTELNS VIAQMSVKPV RNMGGLLDSP DGNDVLSSSS SPTSSAGELH FPKFLTKRSS
SFLGQGDSTS DFYDNNKITW RPKGIIHKKD EVFLYVNERI NILVSRDGSI LKSYVDGTID
ITTHLSGTPI CRFGLNDSLG MQSEDEKKWL AQQQRHSGSD FGNKNFIPKA AAGSVLLEDC
KFHECVSLDK FNRNHIIEFV PPDGSMELMK YHVRDNINLP FKVTPIVTHS TRDNEIDYRI
TLKSLFPGKL SAKDVVLHIP VPPSTVDCKI SVSNGHCKFV PEENAMIWRF NKYNGLTENT
LSAVTVSTSD TTQLNLQQWT RPPISLEFEV MMFSNSGLVV RYFTISGKDS KHRAVKWIKY
ISKAGSYEVR Y
