AP2B_YEAST
ID AP2B_YEAST Reviewed; 700 AA.
AC P27351; D6VWH9;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=AP-2 complex subunit beta;
DE AltName: Full=Beta-2-adaptin;
DE AltName: Full=Beta-adaptin;
DE AltName: Full=Clathrin assembly protein complex 2 beta large chain;
DE AltName: Full=Clathrin assembly protein large beta chain;
GN Name=APL1; Synonyms=YAP80; OrderedLocusNames=YJR005W; ORFNames=J1422;
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=2122239; DOI=10.1128/mcb.10.11.6089-6090.1990;
RA Kirchhausen T.;
RT "Identification of a putative yeast homolog of the mammalian beta chains of
RT the clathrin-associated protein complexes.";
RL Mol. Cell. Biol. 10:6089-6090(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 APS2.
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 SER-649; THR-652 AND SER-683, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
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. Beta
CC adaptin is a subunit of the plasma membrane adaptor.
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). Interacts with APS2.
CC {ECO:0000269|PubMed:10564262}.
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 1670 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; M64998; AAA35226.1; -; Genomic_DNA.
DR EMBL; X87611; CAA60927.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z49505; CAA89527.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08795.1; -; Genomic_DNA.
DR PIR; S57020; S57020.
DR RefSeq; NP_012538.3; NM_001181662.3.
DR AlphaFoldDB; P27351; -.
DR SMR; P27351; -.
DR BioGRID; 33761; 93.
DR ComplexPortal; CPX-534; Adapter complex AP-2.
DR DIP; DIP-915N; -.
DR IntAct; P27351; 5.
DR MINT; P27351; -.
DR STRING; 4932.YJR005W; -.
DR iPTMnet; P27351; -.
DR MaxQB; P27351; -.
DR PaxDb; P27351; -.
DR PRIDE; P27351; -.
DR TopDownProteomics; P27351; -.
DR EnsemblFungi; YJR005W_mRNA; YJR005W; YJR005W.
DR GeneID; 853461; -.
DR KEGG; sce:YJR005W; -.
DR SGD; S000003765; APL1.
DR VEuPathDB; FungiDB:YJR005W; -.
DR eggNOG; KOG1061; Eukaryota.
DR HOGENOM; CLU_006320_4_4_1; -.
DR InParanoid; P27351; -.
DR OMA; ICHEYVR; -.
DR BioCyc; YEAST:G3O-31651-MON; -.
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:P27351; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P27351; protein.
DR GO; GO:0030122; C:AP-2 adaptor complex; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0030139; C:endocytic vesicle; IDA:SGD.
DR GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR026739; AP_beta.
DR InterPro; IPR016342; AP_complex_bsu_1_2_4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR PANTHER; PTHR11134; PTHR11134; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR PIRSF; PIRSF002291; AP_complex_beta; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coated pit; Endocytosis; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..700
FT /note="AP-2 complex subunit beta"
FT /id="PRO_0000193755"
FT REGION 625..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 652
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CONFLICT 55
FT /note="V -> L (in Ref. 1; AAA35226)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="S -> N (in Ref. 1; AAA35226)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="S -> N (in Ref. 1; AAA35226)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="I -> T (in Ref. 1; AAA35226)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="F -> I (in Ref. 1; AAA35226)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 700 AA; 80453 MW; 556A8F3EF8B3930F CRC64;
MSDQKVFARY KANEIVTDLQ HFGVKKFKSN ITRRKNALRK IIANLVLGNY GEMSVLFSEL
LKFWQIEDDL EVKRICHEYI RVIGALKPQQ AREALPFIMD DFKSRDEKLQ IMALRTLVLV
PVKELSDQAF DCIISLVNHK SPPEQVTRTA IYALLDLDEI DHERVLGLSS ILHDIVKAQS
SSPEVIVAAL HTLYSIHEKN ANMEPFRIPL ELAFDMLELL PELNEWNKAT VLEVLTTSVV
PQHYLDTHEM IELALPYLQQ VNTYVVLNSL KFIMYLLNYV DVIKETLAEK LSNSVIALLD
KPPELQFLVL RNVILLLLSR ESSLLRLDIS YFFIEYNDPI YIKDTKLECL YLLANKETLP
RILEELEQYA TDIDIQMSRK SVRAIGNLAV KLDEDSVHDC VAVLLDLLEF GVDYVVQEII
SVFRNILRKY PNNFKANVTE LVKHTEVVQE PESKNAMIWI ITQYSDVIPN YLELFRVFSS
NMFSETLEVQ FSILNSAIKF FIRSPTKETE ELCMDLLKGC IDHENNPDLR DKTLMYWRLL
SLTKTSRISN AITFESLKSV LDGELPLIEM NTKLDPTVLE ELELNIGTIV SIYLKPVSHI
FRLNKTKLLP QSPILNPNKD LLPVVGNSFP PTGANRDRQN SESQSSTKSR KTAMMDDYDK
PAEKINQLKG KRKSSSNNPS KLSRKPSTLL RKLSMKRPFS
