AP1B1_YEAST
ID AP1B1_YEAST Reviewed; 726 AA.
AC P36000; D6VX61;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=AP-1 complex subunit beta-1;
DE AltName: Full=Beta-1-adaptin;
DE AltName: Full=Clathrin assembly protein complex 1 beta-1 large chain;
DE AltName: Full=Clathrin assembly protein large beta-1 chain;
GN Name=APL2; OrderedLocusNames=YKL135C;
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=7615679; DOI=10.1242/jcs.108.4.1605;
RA Rad M.R., Phan H.L., Kirchrath L., Tan P.K., Kirchhausen T.,
RA Hollenberg C.P., Payne G.S.;
RT "Saccharomyces cerevisiae Apl2p, a homologue of the mammalian clathrin AP
RT beta subunit, plays a role in clathrin-dependent Golgi functions.";
RL J. Cell Sci. 108:1605-1615(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(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, SUBUNIT, AND INTERACTION WITH APM2 AND CHC1.
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].
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).
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. The
CC AP-1 complex interacts directly with clathrin.
CC {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). Interacts with CHC1. Interacts with APM2,
CC probably forming an alternative AP-1-like complex.
CC {ECO:0000269|PubMed:10564262}.
CC -!- INTERACTION:
CC P36000; Q12028: APL4; NbExp=5; IntAct=EBI-2206, EBI-33025;
CC P36000; Q00776: APM1; NbExp=9; IntAct=EBI-2206, EBI-2624;
CC P36000; P38700: APM2; NbExp=6; IntAct=EBI-2206, EBI-2705;
CC P36000; P35181: APS1; NbExp=5; IntAct=EBI-2206, EBI-2612;
CC P36000; P22137: CHC1; NbExp=3; IntAct=EBI-2206, EBI-4766;
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 2690 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; Z30212; CAA82931.1; -; Genomic_DNA.
DR EMBL; Z28135; CAA81977.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09027.1; -; Genomic_DNA.
DR PIR; S37964; S37964.
DR RefSeq; NP_012787.1; NM_001179701.1.
DR AlphaFoldDB; P36000; -.
DR SMR; P36000; -.
DR BioGRID; 34001; 137.
DR ComplexPortal; CPX-532; Adaptor complex AP-1.
DR ComplexPortal; CPX-533; Adaptor complex AP-1R.
DR DIP; DIP-1199N; -.
DR IntAct; P36000; 45.
DR MINT; P36000; -.
DR STRING; 4932.YKL135C; -.
DR iPTMnet; P36000; -.
DR MaxQB; P36000; -.
DR PaxDb; P36000; -.
DR PRIDE; P36000; -.
DR EnsemblFungi; YKL135C_mRNA; YKL135C; YKL135C.
DR GeneID; 853723; -.
DR KEGG; sce:YKL135C; -.
DR SGD; S000001618; APL2.
DR VEuPathDB; FungiDB:YKL135C; -.
DR eggNOG; KOG1061; Eukaryota.
DR GeneTree; ENSGT00960000189261; -.
DR HOGENOM; CLU_006320_4_0_1; -.
DR InParanoid; P36000; -.
DR OMA; NPPEVQW; -.
DR BioCyc; YEAST:G3O-31913-MON; -.
DR Reactome; R-SCE-432720; Lysosome Vesicle Biogenesis.
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:P36000; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36000; protein.
DR GO; GO:0030121; C:AP-1 adaptor complex; IDA:SGD.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0030276; F:clathrin binding; IDA:SGD.
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; IMP: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; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..726
FT /note="AP-1 complex subunit beta-1"
FT /id="PRO_0000193753"
SQ SEQUENCE 726 AA; 81869 MW; 89893945D4EC6C4A CRC64;
MPPLDKRIKK FLKDSIRIAP KISGKGELSE LRTGLVSQYP QTRKDAIKKT IQQMTLGKDV
SSLFPDVLKN IATIDVEQKK LVYLYVMNYA ETHPELCILA VNTFITDAQD PNPLIRCMAI
RTMSMIRVDK ILEYIETPLR RTLHDDNAYV RKTAVICVAK LFQLNKDLCV ELGVVEDLVN
ALDDSNPLVI ANATAALIEI HNMDMDAVDL SSLIQSHVSQ FLLALNECTE WARIIILGTL
SEYSAKDSLE AQDIIDRVTA HLQHVNPAVV LATIKVIVRN LPQIEYSSNS LIMKRLSSAF
VSLMSTPPEM QYVALKNIRI ILEKYPELLT KELRIFYVKF NDPLYVKLEK IDILVRLVDP
SNLKQCTLLL TELKEYAMEY EPEFVSRAIQ ALSQLGIKYA QESFVSKVLD ILLELLERQD
TIKDDCCISL CDLLRHCPGN DKMAKQVCAV FNTWSNPEVL LQSDIAKCNY VWLLGQHPNN
FSDLESKINI FIENFVQEEA LTQMSLLMTI VRLHATLTGS MLQSVLELAT QQTHELDVRD
MAMMYWRCLS MPNNESLVND LCQNKLPMIS NTLEKFSPEV LEKLLMELGT ISSIYFKPDS
NRRKGKKYVQ NIVKGKHIEE LESMAKNEIS SKANDDVLLD FDERDDVTNT NAGMLNTLTT
LGDLDDLFDF GPSEDATQIN TNDTKAVQGL KELKLGGDSN GISSGGKNNP DVSGGNIVSQ
DLLDLF
