ID SYG1_YEAST Reviewed; 902 AA. AC P40528; D6VVN4; P40964; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 161. DE RecName: Full=Protein SYG1; GN Name=SYG1; OrderedLocusNames=YIL047C; 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, SUBCELLULAR LOCATION, AND RP INTERACTION WITH STE4. RC STRAIN=SP1; RX PubMed=7592711; DOI=10.1074/jbc.270.43.25435; RA Spain B.H., Koo D., Ramakrishnan M., Dzudzor B., Colicelli J.; RT "Truncated forms of a novel yeast protein suppress the lethality of a G RT protein alpha subunit deficiency by interacting with the beta subunit."; RL J. Biol. Chem. 270:25435-25444(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169870; RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C., RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., RA Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."; RL Nature 387:84-87(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 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 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859 AND SER-860, AND RP IDENTIFICATION BY MASS SPECTROMETRY [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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172 AND SER-179, 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859 AND SER-860, AND 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). CC -!- FUNCTION: May function in G-protein coupled signal transduction. CC {ECO:0000269|PubMed:7592711}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7592711}; CC Multi-pass membrane protein {ECO:0000269|PubMed:7592711}. CC -!- MISCELLANEOUS: Present with 1160 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U14726; AAA91621.1; -; Genomic_DNA. DR EMBL; Z46861; CAA86904.1; -; Genomic_DNA. DR EMBL; BK006942; DAA08500.1; -; Genomic_DNA. DR PIR; S49931; S49931. DR RefSeq; NP_012217.3; NM_001179397.3. DR AlphaFoldDB; P40528; -. DR SMR; P40528; -. DR BioGRID; 34943; 121. DR DIP; DIP-2383N; -. DR IntAct; P40528; 2. DR MINT; P40528; -. DR STRING; 4932.YIL047C; -. DR iPTMnet; P40528; -. DR MaxQB; P40528; -. DR PaxDb; 4932-YIL047C; -. DR PeptideAtlas; P40528; -. DR EnsemblFungi; YIL047C_mRNA; YIL047C; YIL047C. DR GeneID; 854764; -. DR KEGG; sce:YIL047C; -. DR AGR; SGD:S000001309; -. DR SGD; S000001309; SYG1. DR VEuPathDB; FungiDB:YIL047C; -. DR eggNOG; KOG1162; Eukaryota. DR GeneTree; ENSGT00500000044895; -. DR HOGENOM; CLU_006116_1_1_1; -. DR InParanoid; P40528; -. DR OMA; SIPWAHA; -. DR OrthoDB; 7162at2759; -. DR BioCyc; YEAST:G3O-31318-MONOMER; -. DR BioGRID-ORCS; 854764; 4 hits in 10 CRISPR screens. DR PRO; PR:P40528; -. DR Proteomes; UP000002311; Chromosome IX. DR RNAct; P40528; Protein. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0005886; C:plasma membrane; IDA:SGD. DR GO; GO:0000822; F:inositol hexakisphosphate binding; IBA:GO_Central. DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0016036; P:cellular response to phosphate starvation; IBA:GO_Central. DR GO; GO:0006817; P:phosphate ion transport; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; IMP:SGD. DR CDD; cd14475; SPX_SYG1_like; 1. DR InterPro; IPR004342; EXS_C. DR InterPro; IPR004331; SPX_dom. DR PANTHER; PTHR10783:SF103; XENOTROPIC AND POLYTROPIC RETROVIRUS RECEPTOR 1; 1. DR PANTHER; PTHR10783; XENOTROPIC AND POLYTROPIC RETROVIRUS RECEPTOR 1-RELATED; 1. DR Pfam; PF03124; EXS; 1. DR Pfam; PF03105; SPX; 1. DR PROSITE; PS51380; EXS; 1. DR PROSITE; PS51382; SPX; 1. PE 1: Evidence at protein level; KW Cell membrane; Membrane; Phosphoprotein; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..902 FT /note="Protein SYG1" FT /id="PRO_0000072382" FT TOPO_DOM 1..404 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 405..425 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 426..435 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 436..456 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 457..497 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 498..518 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 519..522 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 523..543 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 544..554 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 555..575 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 576 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 577..599 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 600..732 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 733..753 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 754..761 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 762..782 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 783..902 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 1..303 FT /note="SPX" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714" FT DOMAIN 606..815 FT /note="EXS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00712" FT REGION 882..902 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 172 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 179 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 859 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT MOD_RES 860 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" SQ SEQUENCE 902 AA; 104218 MW; F8D87D1DDB3AED64 CRC64; MKFADHLTES AIPEWRDKYI DYKVGKKKLR RYKEKLDAEE EQSSSYRSWM PSVSVYQTAF QQREPGKSRS DGDYRSGPAF KKDYSALQRE FVADFIEDWL ISFQLSKCNE FYLWLLKECD KKFEVLQSQL HYYSLQKNYE RDNLNRSSSN VDMSTSLYAA GLAGRSDSRV NSIDSDSRSV MYGSMPCTKE AKKPRLSLLA YCQKVLKDNR LLPSWPKRGF SLLQDLRQDA SSRGRETFAF GASFLETMTT TQARNLLSNA IIEYYLYLQL VKSFRDINVT GFRKMVKKFD KTCHTRELTT FMSYARTHYT LFKHADANVQ LVAQKMQQIT SSQPTPTSEL SSAQRDKEPI TWLETQITEW FTTALTNSPK DRKHNTHKLK KLTIQYSISE QMVHRNNRSI VQMLVVGLGI GVSMTLITYT LYLGISSEET SFTHKILFPL WGGWYMVLLI AFLFLVNCFI WHRTGINYRF IMLGEIQSKN GTQFFNNDFA TSKIPLKLYF LTFFIVPCAV CSMLSFALEK LTPLGFLYIG IVSFLFLCPS GLIPYWDKVV HTRKWLVVTL IRLMMSGFFP VEFGDFFLGD IICSLTYSIA DIAMFFCVYS HTPNNLCGSS HSRAMGVLSC LPSYWRFMQC LRRFADSGDW FPHLLNAAKY TLGIAYNATL CAYRLSDRSE QRRTPFIVCA TLNSILTSAW DLVMDWSFAH NTTSYNWLLR DDLYLAGKKN WENGSYSFSR KLVYYFAMIW DILIRFEWIV YAIAPQTIQQ SAVTSFILAL LEVLRRFVWI IFRVENEHVA NVHLFRVTGD APLPYPIAQV GDDSMDSSDL GSKAFSSLND IPITPSHDNN PHSFAEPMPA YRGTFRRRSS VFENISRSIP WAHATDFQRP TVNTVDDRSP ETDSESEVES IM //