AST1_YEAST
ID AST1_YEAST Reviewed; 429 AA.
AC P35183; D6VPT2; P89492;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein AST1 {ECO:0000305};
DE AltName: Full=ATPAse stabilizing protein 1 {ECO:0000303|PubMed:7822420};
GN Name=AST1 {ECO:0000303|PubMed:7822420};
GN OrderedLocusNames=YBL069W {ECO:0000312|SGD:S000000165};
GN ORFNames=YBL06.04, YBL0617;
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], FUNCTION, AND INTERACTION WITH PMA1.
RX PubMed=7822420; DOI=10.1083/jcb.128.1.39;
RA Chang A., Fink G.R.;
RT "Targeting of the yeast plasma membrane [H+]ATPase: a novel gene AST1
RT prevents mislocalization of mutant ATPase to the vacuole.";
RL J. Cell Biol. 128:39-49(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7992509; DOI=10.1002/yea.320100811;
RA Logghe M., Molemans F., Fiers W., Contreras R.;
RT "The two genes encoding yeast ribosomal protein S8 reside on different
RT chromosomes, and are closely linked to the hsp70 stress protein genes SSA3
RT and SSA4.";
RL Yeast 10:1093-1100(1994).
RN [3]
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 [4]
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 [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PMA1.
RX PubMed=11739806; DOI=10.1091/mbc.12.12.4129;
RA Bagnat M., Chang A., Simons K.;
RT "Plasma membrane proton ATPase Pma1p requires raft association for surface
RT delivery in yeast.";
RL Mol. Biol. Cell 12:4129-4138(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29897761; DOI=10.1021/acs.jproteome.8b00032;
RA He C., Jia C., Zhang Y., Xu P.;
RT "Enrichment-based proteogenomics identifies microproteins, missing
RT proteins, and novel smORFs in Saccharomyces cerevisiae.";
RL J. Proteome Res. 17:2335-2344(2018).
CC -!- FUNCTION: Lipid raft-associated protein involved in the targeting of
CC PMA1 from Golgi to the plasma membrane (PubMed:7822420,
CC PubMed:11739806). May induce clustering of PMA1, which facilitates
CC partition of PMA1 into lipid rafts after leaving the ER and its
CC transport to the cell surface (PubMed:11739806).
CC {ECO:0000269|PubMed:11739806, ECO:0000269|PubMed:7822420}.
CC -!- SUBUNIT: Interacts with PMA1. {ECO:0000269|PubMed:11739806,
CC ECO:0000269|PubMed:7822420}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11739806};
CC Peripheral membrane protein {ECO:0000305|PubMed:7822420}. Membrane raft
CC {ECO:0000269|PubMed:11739806}; Peripheral membrane protein
CC {ECO:0000305|PubMed:7822420}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:11739806}; Peripheral membrane protein
CC {ECO:0000305|PubMed:7822420}. Late endosome membrane
CC {ECO:0000269|PubMed:11739806}; Peripheral membrane protein
CC {ECO:0000305|PubMed:7822420}.
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DR EMBL; X81843; CAA57435.1; -; Genomic_DNA.
DR EMBL; Z26879; CAA81522.1; -; Genomic_DNA.
DR EMBL; Z35831; CAA84891.1; -; Genomic_DNA.
DR EMBL; Z35829; CAA84889.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07052.1; -; Genomic_DNA.
DR PIR; S45588; S45588.
DR RefSeq; NP_009484.2; NM_001178309.1.
DR AlphaFoldDB; P35183; -.
DR SMR; P35183; -.
DR BioGRID; 32631; 56.
DR IntAct; P35183; 2.
DR STRING; 4932.YBL069W; -.
DR iPTMnet; P35183; -.
DR MaxQB; P35183; -.
DR PaxDb; P35183; -.
DR PRIDE; P35183; -.
DR EnsemblFungi; YBL069W_mRNA; YBL069W; YBL069W.
DR GeneID; 852209; -.
DR KEGG; sce:YBL069W; -.
DR SGD; S000000165; AST1.
DR VEuPathDB; FungiDB:YBL069W; -.
DR eggNOG; KOG1198; Eukaryota.
DR GeneTree; ENSGT00940000176396; -.
DR HOGENOM; CLU_026673_4_0_1; -.
DR InParanoid; P35183; -.
DR OMA; WSYNYTH; -.
DR BioCyc; YEAST:G3O-28964-MON; -.
DR PRO; PR:P35183; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P35183; protein.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0005770; C:late endosome; IDA:SGD.
DR GO; GO:0045121; C:membrane raft; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006612; P:protein targeting to membrane; IGI:SGD.
DR GO; GO:0032596; P:protein transport into membrane raft; IMP:SGD.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endosome; Golgi apparatus; Membrane; Reference proteome.
FT CHAIN 1..429
FT /note="Protein AST1"
FT /id="PRO_0000064710"
FT CONFLICT 326..429
FT /note="TVGDYVANYKEDIFDSWDNPSANARKMFGSIIWSYNYTHYYFDPNAKTASAN
FT NDWIEQCGDFLKNGTVKCVVDKVYDWKDHKEAFSYMATQRAQGKLIMNVEKF -> HCR
FT (in Ref. 2; CAA81522)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 48349 MW; 9F2126C2230AE20D CRC64;
MAKDILKNQD PKLQAMIVEH SAPAPKEIPM DAPVLKRVAR PLRHVKFIPI KSLIFHTKTG
PMDFSYEKKI KTPIPKNKIV VRVSNVGLNP VDMKIRNGYT SSIYGEIGLG REYSGVITEV
GENLNYAWHV GDEVYGIYYH PHLAVGCLQS SILVDPKVDP ILLRPESVSA EEAAGSLFCL
ATGYNILNKL SKNKYLKQDS NVLINGGTSS VGMFVIQLLK RHYKLQKKLV IVTSANGPQV
LQEKFPDLAD EMIFIDYLTC RGKSSKPLRK MLEEKKISQY DPVEDKETIL NYNEGKFDVV
LDFVGGYDIL SHSSSLIHGG GAYVTTVGDY VANYKEDIFD SWDNPSANAR KMFGSIIWSY
NYTHYYFDPN AKTASANNDW IEQCGDFLKN GTVKCVVDKV YDWKDHKEAF SYMATQRAQG
KLIMNVEKF
