SRF1_YEAST
ID SRF1_YEAST Reviewed; 437 AA.
AC Q12516; D6VRL6; P89897; Q7LGS2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Regulator of phospholipase D SRF1;
DE AltName: Full=SPO14 regulatory factor 1;
GN Name=SRF1; OrderedLocusNames=YDL133W; ORFNames=D2185;
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=8972577;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1549::aid-yea42>3.0.co;2-s;
RA Woelfl S., Haneman V., Saluz H.P.;
RT "Analysis of a 26,756 bp segment from the left arm of yeast chromosome
RT IV.";
RL Yeast 12:1549-1554(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 INDUCTION.
RX PubMed=16278933; DOI=10.1002/yea.1302;
RA de Lichtenberg U., Wernersson R., Jensen T.S., Nielsen H.B., Fausboell A.,
RA Schmidt P., Hansen F.B., Knudsen S., Brunak S.;
RT "New weakly expressed cell cycle-regulated genes in yeast.";
RL Yeast 22:1191-1201(2005).
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-45, 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-167, 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 SER-45 AND SER-167, 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).
RN [9]
RP FUNCTION, AND INTERACTION WITH SPO14.
RX PubMed=21347278; DOI=10.1371/journal.pgen.1001299;
RA Kennedy M.A., Kabbani N., Lambert J.P., Swayne L.A., Ahmed F., Figeys D.,
RA Bennett S.A., Bryan J., Baetz K.;
RT "Srf1 is a novel regulator of phospholipase D activity and is essential to
RT buffer the toxic effects of C16:0 platelet activating factor.";
RL PLoS Genet. 7:E1001299-E1001299(2011).
CC -!- FUNCTION: Regulator of phospholipase D (SPO14) which is required for
CC SPO14 catalytic activity in mitotic cells. Essential to buffer the
CC toxic effects of C16:0 platelet activating factor.
CC {ECO:0000269|PubMed:21347278}.
CC -!- SUBUNIT: Interacts with SPO14. {ECO:0000269|PubMed:21347278}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: During S phase of cell cycle. {ECO:0000269|PubMed:16278933}.
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DR EMBL; X96876; CAA65627.1; -; Genomic_DNA.
DR EMBL; Z74180; CAA98703.1; -; Genomic_DNA.
DR EMBL; Z74181; CAA98704.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11726.1; -; Genomic_DNA.
DR PIR; S67679; S67679.
DR RefSeq; NP_010149.1; NM_001180192.1.
DR AlphaFoldDB; Q12516; -.
DR BioGRID; 31929; 161.
DR DIP; DIP-1802N; -.
DR IntAct; Q12516; 5.
DR MINT; Q12516; -.
DR STRING; 4932.YDL133W; -.
DR iPTMnet; Q12516; -.
DR MaxQB; Q12516; -.
DR PaxDb; Q12516; -.
DR PRIDE; Q12516; -.
DR EnsemblFungi; YDL133W_mRNA; YDL133W; YDL133W.
DR GeneID; 851423; -.
DR KEGG; sce:YDL133W; -.
DR SGD; S000002291; SRF1.
DR VEuPathDB; FungiDB:YDL133W; -.
DR eggNOG; ENOG502QPXG; Eukaryota.
DR HOGENOM; CLU_027163_1_1_1; -.
DR InParanoid; Q12516; -.
DR OMA; YICRKQR; -.
DR BioCyc; YEAST:G3O-29531-MON; -.
DR PRO; PR:Q12516; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12516; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IMP:SGD.
DR InterPro; IPR037737; Srf1.
DR PANTHER; PTHR36819; PTHR36819; 2.
PE 1: Evidence at protein level;
KW Glycoprotein; Lipid degradation; Lipid metabolism; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..437
FT /note="Regulator of phospholipase D SRF1"
FT /id="PRO_0000240873"
FT TOPO_DOM 1..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..308
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..403
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 437 AA; 49580 MW; 8442327B1ECFF883 CRC64;
MGDSNSSQEA YSDTTSTNAS RIADQNQLNL NVDLEKNQTV RKSGSLEALQ NAKIHVPKHS
DGSPLDYPKL NTYTFVPTTV PPYVLEAQFD KLRLQDKGTV DGNVTDDKNL PKEFKWGQFA
STIGCHSAYT RDQNYNPSHK SYDGYSLSSS TSSKNAALRE ILGDMCSEWG GEERLEGVLH
SEIGANLEFN TTEERKEWLQ YIEKVKDFYY GDNKKNPESP ESVHNKVYKS DWVNELNKER
EKWRRLKQRK LQQWRPPLTS LLLDNQYLIL GLRIFTGILS CISLALAIKI FQNSRSNNTI
SESKIGQQPS TIMAICVNAV AIAYIIYIAH DEFAGKPVGL RNPLSKLKLI LLDLLFIIFS
SANLALAFNT RFDKEWVCTS IRRSNGSTYG YPKIPRICRK QEALSAFLFV ALFMWVITFS
ISIVRVVEKV SSITNRN
