SYG1_YEAST
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 03-AUG-2022, entry version 155.
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}.
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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; 91.
DR DIP; DIP-2383N; -.
DR IntAct; P40528; 2.
DR MINT; P40528; -.
DR STRING; 4932.YIL047C; -.
DR iPTMnet; P40528; -.
DR MaxQB; P40528; -.
DR PaxDb; P40528; -.
DR PRIDE; P40528; -.
DR EnsemblFungi; YIL047C_mRNA; YIL047C; YIL047C.
DR GeneID; 854764; -.
DR KEGG; sce:YIL047C; -.
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; YFAMIWD; -.
DR BioCyc; YEAST:G3O-31318-MON; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 InterPro; IPR004342; EXS_C.
DR InterPro; IPR004331; SPX_dom.
DR InterPro; IPR033507; Syg1.
DR PANTHER; PTHR10783:SF4; PTHR10783:SF4; 1.
DR Pfam; PF03124; EXS; 1.
DR Pfam; PF03105; SPX; 2.
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
