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FAR8_YEAST
ID   FAR8_YEAST              Reviewed;         523 AA.
AC   Q05040; D6VZK3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Factor arrest protein 8;
GN   Name=FAR8; OrderedLocusNames=YMR029C; ORFNames=YM9973.02C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
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   [3]
RP   FUNCTION, AND INTERACTION WITH FAR3; FAR7; FAR10; FAR11 AND VPS64.
RX   PubMed=12588993; DOI=10.1128/mcb.23.5.1750-1763.2003;
RA   Kemp H.A., Sprague G.F. Jr.;
RT   "Far3 and five interacting proteins prevent premature recovery from
RT   pheromone arrest in the budding yeast Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 23:1750-1763(2003).
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 THR-132, 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-115, AND IDENTIFICATION BY
RP   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 THR-132, AND IDENTIFICATION BY
RP   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: Participates in the control of the reentry into the cell
CC       cycle following pheromone treatment. {ECO:0000269|PubMed:12588993}.
CC   -!- SUBUNIT: Component of a complex at least composed of FAR3, FAR7, FAR8,
CC       FAR10, FAR11 and VPS64.
CC   -!- INTERACTION:
CC       Q05040; P46671: FAR3; NbExp=3; IntAct=EBI-28053, EBI-6789;
CC       Q05040; P02994: TEF2; NbExp=2; IntAct=EBI-28053, EBI-6314;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC       Endoplasmic reticulum {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 4010 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z49213; CAA89144.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09927.1; -; Genomic_DNA.
DR   PIR; S53945; S53945.
DR   RefSeq; NP_013742.1; NM_001182525.1.
DR   AlphaFoldDB; Q05040; -.
DR   SMR; Q05040; -.
DR   BioGRID; 35201; 125.
DR   ComplexPortal; CPX-1197; FAR complex.
DR   DIP; DIP-6343N; -.
DR   IntAct; Q05040; 10.
DR   MINT; Q05040; -.
DR   STRING; 4932.YMR029C; -.
DR   iPTMnet; Q05040; -.
DR   MaxQB; Q05040; -.
DR   PaxDb; Q05040; -.
DR   PRIDE; Q05040; -.
DR   EnsemblFungi; YMR029C_mRNA; YMR029C; YMR029C.
DR   GeneID; 855044; -.
DR   KEGG; sce:YMR029C; -.
DR   SGD; S000004631; FAR8.
DR   VEuPathDB; FungiDB:YMR029C; -.
DR   eggNOG; KOG0642; Eukaryota.
DR   GeneTree; ENSGT00950000183095; -.
DR   HOGENOM; CLU_034775_0_0_1; -.
DR   InParanoid; Q05040; -.
DR   OMA; YLQTEFT; -.
DR   BioCyc; YEAST:G3O-32734-MON; -.
DR   PRO; PR:Q05040; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q05040; protein.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR   GO; GO:0090443; C:FAR/SIN/STRIPAK complex; IC:ComplexPortal.
DR   GO; GO:0071444; P:cellular response to pheromone; IC:ComplexPortal.
DR   GO; GO:0000321; P:re-entry into mitotic cell cycle after pheromone arrest; IGI:SGD.
DR   GO; GO:0051726; P:regulation of cell cycle; IC:ComplexPortal.
DR   InterPro; IPR013258; Striatin_N.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF08232; Striatin; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Coiled coil; Cytoplasm; Endoplasmic reticulum; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..523
FT                   /note="Factor arrest protein 8"
FT                   /id="PRO_0000087193"
FT   REGION          61..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          26..76
FT                   /evidence="ECO:0000255"
FT   MOD_RES         115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         132
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   523 AA;  59301 MW;  3B2A3C95B2D575AE CRC64;
     MAINQAHVHP HYTLPGVMHY LQTEFTKNER DRITWELERS EMKARIAELE GENRDLKHQL
     NQIQSKAVSP EGEKEEKHVP DSLLQSKLAV QENVKEIIYL LKGPNTVNQL ESLNSREAGS
     ELHDLEKLNV NTPKEEGSAK TNGMDILNNA LLDTKPNPKQ GPSESPSPTK VKSLFSTANK
     RENNETISKI HSELSKVDII SSYGDCMALY DADTKSLEIH QVDANLNSKL LKKISLGQDS
     DIMKFFWVST SKLLVIEKSF HLKLFSISSA SLISDVDLLQ DSEQPFSSSD IINIDFKNKW
     LLIASKNKSQ IRIWELDNIE APEDVPINIK ETYEITHDND DDDSNDSTNI LDCILGITEK
     SLILLSSNPY QLTIYDFEGK LLQKIDLKID TILSGKPEEE GYHLFLDRKT SKLLIQLSNE
     RLLVYSFDKK KVVLKEQLTP SSTLPIQLDL NDSIITVSYS NGDFEFRNLE NLKPSIDEFV
     VADINFSERK EPVVFSSNLI VDSTPVLITV NKNNEVLLHK IKI
 
 
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