AP1G1_YEAST
ID AP1G1_YEAST Reviewed; 832 AA.
AC Q12028; D6W439;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=AP-1 complex subunit gamma-1;
DE AltName: Full=Clathrin assembly protein complex 1 gamma large chain;
DE AltName: Full=Clathrin assembly protein large gamma chain;
DE AltName: Full=Gamma-adaptin;
GN Name=APL4; OrderedLocusNames=YPR029C;
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 [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 [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=26658609; DOI=10.1091/mbc.e15-09-0621;
RA Whitfield S.T., Burston H.E., Bean B.D., Raghuram N., Maldonado-Baez L.,
RA Davey M., Wendland B., Conibear E.;
RT "The alternate AP-1 adaptor subunit Apm2 interacts with the Mil1 regulatory
RT protein and confers differential cargo sorting.";
RL Mol. Biol. Cell 27:588-598(2016).
CC -!- FUNCTION: Adaptins are components of the adapter complexes which link
CC clathrin to receptors in coated vesicles (PubMed:10564262). Clathrin-
CC associated protein complexes are believed to interact with the
CC cytoplasmic tails of membrane proteins, leading to their selection and
CC concentration (PubMed:10564262). The AP-1 complex interacts directly
CC with clathrin (PubMed:10564262). Component of the AP-1-related (AP-1R)
CC complex, an adapter protein complex that mediates sorting of cargo
CC SNARE SNC1 (PubMed:26658609). In contrast to the APM1-containing AP-1
CC complex, AP-1R is incapable of sorting CHS3 (PubMed:26658609).
CC {ECO:0000269|PubMed:10564262, ECO:0000269|PubMed:26658609}.
CC -!- SUBUNIT: Adapter 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) (PubMed:10564262). AP-1 interacts with
CC clathrin (PubMed:10564262). Also a component of the AP-1R complex
CC composed of at least APM2, APL4 and APS1 (PubMed:26658609).
CC {ECO:0000269|PubMed:10564262, ECO:0000269|PubMed:26658609}.
CC -!- INTERACTION:
CC Q12028; P36000: APL2; NbExp=5; IntAct=EBI-33025, EBI-2206;
CC Q12028; P35181: APS1; NbExp=4; IntAct=EBI-33025, EBI-2612;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or
CC polymerized on the cytoplasmic side of the Golgi, as well as on the
CC vesicles/buds originating from it. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 4850 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z71255; CAA95025.1; -; Genomic_DNA.
DR EMBL; Z49274; CAA89283.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11455.1; -; Genomic_DNA.
DR PIR; S54503; S54503.
DR RefSeq; NP_015354.1; NM_001184126.1.
DR AlphaFoldDB; Q12028; -.
DR SMR; Q12028; -.
DR BioGRID; 36207; 191.
DR ComplexPortal; CPX-532; Adaptor complex AP-1.
DR ComplexPortal; CPX-533; Adaptor complex AP-1R.
DR DIP; DIP-3913N; -.
DR IntAct; Q12028; 30.
DR MINT; Q12028; -.
DR STRING; 4932.YPR029C; -.
DR iPTMnet; Q12028; -.
DR MaxQB; Q12028; -.
DR PaxDb; Q12028; -.
DR PRIDE; Q12028; -.
DR EnsemblFungi; YPR029C_mRNA; YPR029C; YPR029C.
DR GeneID; 856141; -.
DR KEGG; sce:YPR029C; -.
DR SGD; S000006233; APL4.
DR VEuPathDB; FungiDB:YPR029C; -.
DR eggNOG; KOG1062; Eukaryota.
DR GeneTree; ENSGT00950000182838; -.
DR HOGENOM; CLU_003824_0_1_1; -.
DR InParanoid; Q12028; -.
DR OMA; NEFKPVM; -.
DR BioCyc; YEAST:G3O-34188-MON; -.
DR Reactome; R-SCE-432720; Lysosome Vesicle Biogenesis.
DR PRO; PR:Q12028; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12028; protein.
DR GO; GO:0030121; C:AP-1 adaptor complex; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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: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:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:0048203; P:vesicle targeting, trans-Golgi to endosome; IMP:ComplexPortal.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR017107; AP1_complex_gsu.
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 Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR PIRSF; PIRSF037094; AP1_complex_gamma; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..832
FT /note="AP-1 complex subunit gamma-1"
FT /id="PRO_0000193764"
FT DOMAIN 733..832
FT /note="GAE"
SQ SEQUENCE 832 AA; 93624 MW; ABB619E9DC4F565C CRC64;
MGSSLRSFIK DVRGAKTLAD ERAIITKQSA KIRTKLRDDH LPHEKRRVNI QKLLYLYILG
EKTHFGQVES INLIASDDFV DKRLGYLAAT LLLDESEDLL TLLTNMLNND LHHPNKYAVS
LALTSLGFLS SPELARDLYP DVENIIKNSR DPFLLKKALQ CAAKLIFKDV SLLEIFNIED
ITKILSSHSI CTHGVLLGVT KIIQSILLIG LNRKKDEDED EDGIDYSNDI LSPLSLLLRD
FFIRLENMNS KNIEPGYDVQ GICDPFLQCE IIYTLKLYFQ VGELLNSNNV LDYKDNFCDL
LTRIATNTDS TKNSGQAILY ETVKTIFSLD LNQPLRVLGI NILAKFLAGK DNNTKYVSLN
TLLKVVPQEP TAVQRHRKFI SHCLQDTDVS IRMRALELSF AILDDSNLVE LVNELMKFLA
KQDEDSKDLI IYTIDHLIDT FDTRVVKDES WKLDVFFNIL KLVGSFINYE KINDILIIIN
NTSQLSDKSE FLRKMLTISL NGTSAEISEE NIGWQLVLIW CIGEYGDLVL NEGNKNGADI
INESSITDYL LTLQELYTAT NLKIINYILT AALKLSVRFH DAKNIEKLRQ LILSYTDSTD
LSLQMKSNQY EIFFNQSISV KKIILETMPK FEKITEEQDN GKALSKNLIS NEPVDLLSDL
LGEDSKAESK ASTGDNVKPI DILEEIFGEK NDIAQVPKNA NKEESINHSS AVEANSGVTL
PLDANKIYDS SSLNVYASLL SANSGLAHLD LYFQAKSLIS DLKTFCAVPK AQKLTLGQLY
PSSTINASQI CKQSLKISGS GKLKLRVKLD FHLNGSSSIT NEQFDHKFDE TL
