AP2A_YEAST
ID AP2A_YEAST Reviewed; 1025 AA.
AC P38065; D6VPW2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=AP-2 complex subunit alpha;
DE AltName: Full=Alpha-adaptin;
DE AltName: Full=Clathrin assembly protein complex 2 alpha large chain;
DE AltName: Full=Clathrin assembly protein large alpha chain;
GN Name=APL3; OrderedLocusNames=YBL037W; ORFNames=YBL0412;
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 204508 / S288c;
RX PubMed=7871888; DOI=10.1002/yea.320101113;
RA de Wergifosse P., Jacques B., Jonniaux J.-L., Purnelle B., Skala J.,
RA Goffeau A.;
RT "The sequence of a 22.4 kb DNA fragment from the left arm of yeast
RT chromosome II reveals homologues to bacterial proline synthetase and murine
RT alpha-adaptin, as well as a new permease and a DNA-binding protein.";
RL Yeast 10:1489-1496(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-727, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-727 AND SER-733, 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: Adaptins are components of the adaptor complexes which link
CC clathrin to receptors in coated vesicles. Clathrin-associated protein
CC complexes are believed to interact with the cytoplasmic tails of
CC membrane proteins, leading to their selection and concentration. Alpha
CC adaptin is a subunit of the plasma membrane adaptor. Facilitates
CC interaction between APL1 and APS2. {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 -!- INTERACTION:
CC P38065; Q00381: APS2; NbExp=3; IntAct=EBI-2181, EBI-2608;
CC -!- SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit; Peripheral
CC membrane protein; Cytoplasmic side. Note=Component of the coat
CC surrounding the cytoplasmic face of coated vesicles in the plasma
CC membrane.
CC -!- MISCELLANEOUS: Present with 1590 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; X78214; CAA55057.1; -; Genomic_DNA.
DR EMBL; Z35798; CAA84857.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07082.1; -; Genomic_DNA.
DR PIR; S50293; S50293.
DR RefSeq; NP_009516.1; NM_001178277.1.
DR AlphaFoldDB; P38065; -.
DR SMR; P38065; -.
DR BioGRID; 32660; 82.
DR ComplexPortal; CPX-534; Adapter complex AP-2.
DR DIP; DIP-2634N; -.
DR IntAct; P38065; 28.
DR MINT; P38065; -.
DR STRING; 4932.YBL037W; -.
DR iPTMnet; P38065; -.
DR MaxQB; P38065; -.
DR PaxDb; P38065; -.
DR PRIDE; P38065; -.
DR EnsemblFungi; YBL037W_mRNA; YBL037W; YBL037W.
DR GeneID; 852243; -.
DR KEGG; sce:YBL037W; -.
DR SGD; S000000133; APL3.
DR VEuPathDB; FungiDB:YBL037W; -.
DR eggNOG; KOG1077; Eukaryota.
DR GeneTree; ENSGT00950000182838; -.
DR HOGENOM; CLU_003824_1_0_1; -.
DR InParanoid; P38065; -.
DR OMA; SPIEQFM; -.
DR BioCyc; YEAST:G3O-28939-MON; -.
DR Reactome; R-SCE-437239; Recycling pathway of L1.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
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:P38065; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38065; protein.
DR GO; GO:0030122; C:AP-2 adaptor complex; IMP:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0140312; F:cargo adaptor activity; IBA:GO_Central.
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:0006886; P:intracellular protein transport; IC:SGD.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR InterPro; IPR017104; AP2_complex_asu.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR012295; TBP_dom_sf.
DR Pfam; PF01602; Adaptin_N; 1.
DR PIRSF; PIRSF037091; AP2_complex_alpha; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coated pit; Endocytosis; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1025
FT /note="AP-2 complex subunit alpha"
FT /id="PRO_0000193737"
FT REGION 713..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 727
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1025 AA; 115012 MW; 629DF3C7C5AF88E5 CRC64;
MDRKKTLINS SVSNNNSTIK GLQLFIADLR SAQQAQEQEK RIQSEIVKIK QHFDAAKKKQ
GNHDRLGGYQ RKKYVAKLAY IYITSNTTKL NEILFGLEQT VELLKSSIFS EKFIGYMTLE
LLYERSEVVA KVNDEVNYQL MKDLSSSDDN FVMLALNFVG VVGELTNRLA YNDDITTGVF
KILRSPTSSI YLKKKSALSF LALLKSNHSI LTEDLQRKQL WIQRILSLLD DTENYRLTLA
TIPLIEFIAK YIDPSYCTRL LPQLTEILYN CVVVGTSRSS DNQFPLEYTF ANMPNPWLIT
KVVSLLSILI ASPTERDSGS LLQTNNIDNE LLNKLRKCVS VAIELGTRQA QDPMERIVQN
TVLFSLINFA SKLDPSDEAI SNSVTALCSL LTSKEINIRY LTLDSLVKLC SSSGKPAIDA
VRYKNLDMIF HLLNTERDSS IVRKVVDLLY TFTDVENVKI IVDGLLQYIL SPKNLAEPQI
KSDIAVKIAI LTEKYATDIN WFVIISLQLL SLTSNTTIND DEIWQRLCQI VVNNPSLHRI
TCERLVDYLC KKQASEAIIK AAAFLLGEYS SLITDRISSA NLFTLFAEKY FSAPNVAKAM
ILTTMIKLYK TSPEIGSNVI KFFQLELNSL DIELQTRSFE YLNIIQLAKV NGNTDILQIL
FEPMPPFNSK SNPLLKRLGS LPASAGSTTL INTPSEASSS TPDLLSKRAN SSRSIMVPMP
PPSRRNTIDD VNSKISSSED FSGKDSYYSR QILAPNWREG FTRMISHKQG VLFTSSLMKV
FYRITTPDAQ QPYVFHISLA FINLTEWEIT GLSTQIIPSK TQGNPEYLIM NINTPSTATI
GPHKRAEQSY EVSIRKPFDV EDSPILAIHF KCGGSTNTIN LKTAIGMTTT LISSDVNPSM
HLNLAQFISR WKTLSDALGK EGEYQKSGIK LNKDFRKVET ISLEDGLLLL TQTVKRLGFD
IVDQTSVRST LFVSGIIHTK SEGNFGCLMK IQYQVNGTVN VTCKTTTAGP LAKYIVECIK
NVLTK
