YG35_YEAST
ID YG35_YEAST Reviewed; 1036 AA.
AC P53273; D6VUQ7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Uncharacterized vacuolar membrane protein YGR125W;
GN OrderedLocusNames=YGR125W; ORFNames=G6362;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046098;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<171::aid-yea57>3.0.co;2-v;
RA van Dyck L., Tettelin H., Purnelle B., Goffeau A.;
RT "An 18.3 kb DNA fragment from yeast chromosome VII carries four unknown
RT open reading frames, the gene for an Asn synthase, remnants of Ty and three
RT tRNA genes.";
RL Yeast 13:171-176(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-149; SER-152;
RP SER-153; SER-842 AND THR-847, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-842 AND THR-847, AND
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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-127; THR-130;
RP SER-140; SER-144; SER-149; SER-842 AND THR-847, AND IDENTIFICATION BY MASS
RP 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).
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095};
CC Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1420 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X83099; CAA58161.1; -; Genomic_DNA.
DR EMBL; Z72910; CAA97136.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08218.1; -; Genomic_DNA.
DR PIR; S55984; S55984.
DR RefSeq; NP_011641.1; NM_001181254.1.
DR AlphaFoldDB; P53273; -.
DR SMR; P53273; -.
DR BioGRID; 33373; 123.
DR DIP; DIP-7435N; -.
DR IntAct; P53273; 3.
DR MINT; P53273; -.
DR STRING; 4932.YGR125W; -.
DR TCDB; 2.A.53.3.10; the sulfate permease (sulp) family.
DR iPTMnet; P53273; -.
DR MaxQB; P53273; -.
DR PaxDb; P53273; -.
DR PRIDE; P53273; -.
DR EnsemblFungi; YGR125W_mRNA; YGR125W; YGR125W.
DR GeneID; 853026; -.
DR KEGG; sce:YGR125W; -.
DR SGD; S000003357; YGR125W.
DR VEuPathDB; FungiDB:YGR125W; -.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01050000244925; -.
DR HOGENOM; CLU_003182_0_2_1; -.
DR InParanoid; P53273; -.
DR OMA; ISFIPIC; -.
DR BioCyc; YEAST:G3O-30831-MON; -.
DR PRO; PR:P53273; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53273; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR036533; BAG_dom_sf.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR11814; PTHR11814; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR SUPFAM; SSF63491; SSF63491; 1.
DR PROSITE; PS50801; STAS; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Vacuole.
FT CHAIN 1..1036
FT /note="Uncharacterized vacuolar membrane protein YGR125W"
FT /id="PRO_0000202819"
FT TOPO_DOM 1..213
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..269
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..338
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..405
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..515
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 568
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..664
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 665..685
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 686..1036
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 660..781
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 842
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 847
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1036 AA; 116971 MW; 91A50225CA7FFCB1 CRC64;
MGRTIRRRRS NSSLSEAISV SLGINQDSSV NKMHRASVSA MSPPLCRSYM SGFFTGGNSP
MINNLSDSKL PISNKQHPKV IHGSENLHRQ TAQLSNEFCS SSVEENSPTI KDYMDIIGNG
DRKDDQSMRT IEENIDEEYS DEYSRLLLSP ASSNVDDDRN RGLQNSSLPE LEDGYAGGYQ
SLRPSHNLRF RPRNLWHMCT SFPSKFAHYL PAAVLGLLLN ILDALSYGMI IFPITEPVFS
HLGPTGISMF YISTIISQAV YSGGWSSFPS GIGSEMIEIT PFYHTMALAI KEALAGNDDE
IITTTIFCYV ISSMLTGVVF YALGKLRLGK IVGFFPRHIL IGCIGGVGYF LIITGIEVTT
RVAKFEYSWP FFSGLFTDYD TLAKWLLPVL LTVVLIGTQR YFKNSLVLPS FYILTLVLFH
FIVAIIPTLS LDALRQAGWI FPIANSDSKW YDHYRLFNVH KVHWSLVLQQ IPTMMALTFF
GILHVPINVP ALAMSLQMDK YDVDRELIAH GYSNFFSGLL GSVQNYLVYT NSVLFIRAGA
DSPFAGFLLI ALTICIMIIG PVIISFIPIC IVGSLIFLLG YELLVEALVD TWNKLNRFEY
LTVVIIVFTM GIFDFVLGII VGILIACFSF LVDSTKLQTI NGEYNGNVAR STVYRDYVQT
KFLDGIGEQI YVLKLQNLLF FGTIISIEEK IERLLQISNK DATKRRIKYL ILDFKNINAD
NIDYSAAEGF NRIKRFTETK RIKLIISSIK ERDRIYNAFN NVGLLNDVEL FADLNSALEW
CENEFLFQYK QLRKKAKERL EEGKQNNVVS AVIAATKNKK IDTIGNGLNR GSNGDTARNL
MSLPTNTPRN YQILSVAQNV FVNDEQAVKN FKKEYKDDEP VLPILLFALK QYRPDIISEV
QKVREKEIKF WAQLCPYFTR RRLASQSHLL HADNIFFLVE TGMLKATYEL PQGTLYEIFS
NGTCFGKIIA PGNAMPREQK LTIETETDSV LWVIDSSSLN KLKEDNLALY VEVALMVMCI
KDTRFKELLG YTLVSA
