FYV8_YEAST
ID FYV8_YEAST Reviewed; 817 AA.
AC P46949; D6VUX8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Protein FYV8;
DE AltName: Full=Function required for yeast viability protein 8;
GN Name=FYV8; OrderedLocusNames=YGR196C; ORFNames=G7589;
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 204508 / S288c;
RX PubMed=7502584; DOI=10.1002/yea.320111110;
RA Guerreiro P., Maia e Silva A., Barreiros T., Arroyo J., Garcia-Gonzalez M.,
RA Garcia-Saez M.I., Rodrigues-Pousada C., Nombela C.;
RT "The complete sequence of a 9000 bp fragment of the right arm of
RT Saccharomyces cerevisiae chromosome VII contains four previously unknown
RT open reading frames.";
RL Yeast 11:1087-1091(1995).
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 FUNCTION.
RX PubMed=12663529; DOI=10.1093/genetics/163.3.875;
RA Page N., Gerard-Vincent M., Menard P., Beaulieu M., Azuma M.,
RA Dijkgraaf G.J.P., Li H., Marcoux J., Nguyen T., Dowse T., Sdicu A.-M.,
RA Bussey H.;
RT "A Saccharomyces cerevisiae genome-wide mutant screen for altered
RT sensitivity to K1 killer toxin.";
RL Genetics 163:875-894(2003).
RN [5]
RP FUNCTION.
RX PubMed=16380504; DOI=10.1158/1541-7786.mcr-05-0181;
RA Chen Y., Feldman D.E., Deng C., Brown J.A., De Giacomo A.F., Gaw A.F.,
RA Shi G., Le Q.T., Brown J.M., Koong A.C.;
RT "Identification of mitogen-activated protein kinase signaling pathways that
RT confer resistance to endoplasmic reticulum stress in Saccharomyces
RT cerevisiae.";
RL Mol. Cancer Res. 3:669-677(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP 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-92; SER-100; SER-134;
RP SER-163; SER-180; SER-182; SER-237 AND SER-238, AND IDENTIFICATION BY MASS
RP 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-92; SER-100; SER-163;
RP SER-180; SER-182 AND SER-532, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Required for survival upon exposure to K1 killer toxin.
CC Involved in the resistance to unfolded protein response (UPR)-inducing
CC agents. {ECO:0000269|PubMed:12663529, ECO:0000269|PubMed:16380504}.
CC -!- SIMILARITY: Belongs to the FYV8 family. {ECO:0000305}.
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DR EMBL; X82775; CAA58019.1; -; Genomic_DNA.
DR EMBL; Z72981; CAA97222.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08289.1; -; Genomic_DNA.
DR PIR; S53919; S53919.
DR RefSeq; NP_011712.1; NM_001181325.1.
DR AlphaFoldDB; P46949; -.
DR BioGRID; 33449; 217.
DR DIP; DIP-4795N; -.
DR IntAct; P46949; 6.
DR MINT; P46949; -.
DR STRING; 4932.YGR196C; -.
DR iPTMnet; P46949; -.
DR MaxQB; P46949; -.
DR PaxDb; P46949; -.
DR PRIDE; P46949; -.
DR EnsemblFungi; YGR196C_mRNA; YGR196C; YGR196C.
DR GeneID; 853110; -.
DR KEGG; sce:YGR196C; -.
DR SGD; S000003428; FYV8.
DR VEuPathDB; FungiDB:YGR196C; -.
DR eggNOG; ENOG502QPM9; Eukaryota.
DR HOGENOM; CLU_009686_0_0_1; -.
DR InParanoid; P46949; -.
DR OMA; GIQTWIN; -.
DR BioCyc; YEAST:G3O-30882-MON; -.
DR PRO; PR:P46949; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P46949; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR InterPro; IPR026248; Fyv8.
DR PRINTS; PR02076; PROTEINFYV8.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..817
FT /note="Protein FYV8"
FT /id="PRO_0000202842"
FT REGION 1..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..422
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 817 AA; 90798 MW; E52C5D659D63BEBB CRC64;
MSTEQVGRKK SYRWVSASQA SYDGAGWDSS DEYDYSSEDG TKGSEIHKQK ISNLPSLPKL
NYTDVNGEHD ENTGENKDSN DNNVSKSDIS PSDKEVGYLS DGVPKLMASR ESVELQAKKS
SEHSKSDYLS STASLKSPSE NKKSPHTNRA VNEDLDNLIE QISREMTPEI RQTSDFRRDS
DSCDEIQNEA PLGEAVPSSS SPVEEDEKSH SLGVSMDTNE ADTTFNTPTR NGNEHLSSDG
DVSEQKDDEF KVSERGYLAD ILPAEKEENL QQEDDGEVES SGALEKKEKS EEKTSIRNRN
STSSGQDKVA KPKPVANETK TSDNGYRNSF FNDYQHSSDS EEDDNNEGNS GSSDDDNRSS
VSDKHADINR QSKQLDTTDD DALSYTESIK YSTNETEEED NEDNESIEDK NEDNESIEDE
NEDTDSYKFS NREKGSILLT SDEEEEEKGM SSDSDEGSLK APKSGYFSKM IGNDDKGDSA
LQPNQIDTIE NTNLSNSGSE LENSDGSDEE DHINEDKVLE ESSVKDSTDV DSWKPDSEAL
RSGFVQDTAN KKAPPGYVID SNGKLVDLTP ASMKPRVVST YSEMESTWDA FPSKGEDDDL
ETIRDTKTIY DNNTIYNVPG LIGNQSNLPP LPMDAQEQLN AGNDNSTTDN DNSNNTANDL
AARSASFKSE NRTVSQGEMT SVHEPSTEEM AKLGQQNNLP KLDMNKLLNS KTSHAGKIEQ
LRNYKRELDE YDTGIQTWIN YTLKSSSNKD KDFIAEEYKQ HSHVREAYAN ADDLSKKHTV
INTVASVNQN VTHLRRKVFQ HSMKPKDLFA SIGKKKL
