EXP1_YEAST
ID EXP1_YEAST Reviewed; 149 AA.
AC Q07541; D6VRM9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=ER export of PMA1 protein 1 {ECO:0000303|PubMed:28727280};
GN Name=EXP1 {ECO:0000303|PubMed:28727280}; OrderedLocusNames=YDL121C;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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=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).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH PMA1
RP AND PSG1, AND TOPOLOGY.
RX PubMed=28727280; DOI=10.1111/tra.12503;
RA Geva Y., Crissman J., Arakel E.C., Gomez-Navarro N., Chuartzman S.G.,
RA Stahmer K.R., Schwappach B., Miller E.A., Schuldiner M.;
RT "Two novel effectors of trafficking and maturation of the yeast plasma
RT membrane H+ -ATPase.";
RL Traffic 18:672-682(2017).
CC -!- FUNCTION: Specific cargo receptor protein for the plasma membrane
CC ATPase PMA1 that acts with PSG1 to promote the transport and maturation
CC of PMA1 (PubMed:28727280). EXP1 and PSG1 probably act sequentially to
CC promote PMA1 sorting between the ER and the Golgi, with EXP1 promoting
CC PMA1 export from the ER to the Golgi while PSG1 has a role in PMA1
CC maturation or quality control in the Golgi (PubMed:28727280).
CC {ECO:0000269|PubMed:28727280}.
CC -!- SUBUNIT: Interacts with PMA1 and PSG1. {ECO:0000269|PubMed:28727280}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:28727280}; Single-pass type I membrane protein
CC {ECO:0000305|PubMed:28727280}. Cytoplasmic vesicle, COPI-coated vesicle
CC membrane {ECO:0000269|PubMed:28727280}; Single-pass type I membrane
CC protein {ECO:0000305|PubMed:28727280}. Cytoplasmic vesicle, COPII-
CC coated vesicle membrane {ECO:0000269|PubMed:28727280}; Single-pass type
CC I membrane protein {ECO:0000305|PubMed:28727280}. Golgi apparatus
CC membrane {ECO:0000269|PubMed:28727280}; Single-pass type I membrane
CC protein {ECO:0000305|PubMed:28727280}. Note=Cycles between the ER and
CC the Golgi apparatus. {ECO:0000269|PubMed:28727280}.
CC -!- DISRUPTION PHENOTYPE: Lead to ER retention of PMA1.
CC {ECO:0000269|PubMed:28727280}.
CC -!- MISCELLANEOUS: Present with 3260 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z74169; CAA98689.1; -; Genomic_DNA.
DR EMBL; AY558161; AAS56487.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11739.1; -; Genomic_DNA.
DR PIR; S67664; S67664.
DR RefSeq; NP_010162.1; NM_001180180.1.
DR AlphaFoldDB; Q07541; -.
DR SMR; Q07541; -.
DR BioGRID; 31942; 114.
DR DIP; DIP-5038N; -.
DR IntAct; Q07541; 3.
DR STRING; 4932.YDL121C; -.
DR iPTMnet; Q07541; -.
DR MaxQB; Q07541; -.
DR PaxDb; Q07541; -.
DR PRIDE; Q07541; -.
DR TopDownProteomics; Q07541; -.
DR EnsemblFungi; YDL121C_mRNA; YDL121C; YDL121C.
DR GeneID; 851436; -.
DR KEGG; sce:YDL121C; -.
DR SGD; S000002279; YDL121C.
DR VEuPathDB; FungiDB:YDL121C; -.
DR eggNOG; ENOG502SA5C; Eukaryota.
DR HOGENOM; CLU_150136_0_0_1; -.
DR InParanoid; Q07541; -.
DR OMA; CNGKERE; -.
DR BioCyc; YEAST:G3O-29520-MON; -.
DR PRO; PR:Q07541; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07541; protein.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..149
FT /note="ER export of PMA1 protein 1"
FT /id="PRO_0000240867"
FT TOPO_DOM 1..6
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:28727280"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28727280"
SQ SEQUENCE 149 AA; 16947 MW; B86CAB0D5779690A CRC64;
MNLYGYFLLL IIVIAFIALL PLFSGIGTFK LTKPKSSATA QSATGKLGKR EYLKKKLDHT
NVLKFDLKDT EESLGHDSAS ASSASRKFEI DSKTGLKRRV IGQYNKDPND FDFDIDDLIN
EDELDERREE EKKLKKYNGK KNEAYEGFV
