FMP45_YEAST
ID FMP45_YEAST Reviewed; 309 AA.
AC Q07651; D6VRD3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=SUR7 family protein FMP45;
GN Name=FMP45; OrderedLocusNames=YDL222C;
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=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 [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 SUBCELLULAR LOCATION.
RX PubMed=11784867; DOI=10.1128/mcb.22.3.927-934.2002;
RA Young M.E., Karpova T.S., Bruegger B., Moschenross D.M., Wang G.K.,
RA Schneiter R., Wieland F.T., Cooper J.A.;
RT "The Sur7p family defines novel cortical domains in Saccharomyces
RT cerevisiae, affects sphingolipid metabolism, and is involved in
RT sporulation.";
RL Mol. Cell. Biol. 22:927-934(2002).
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 INDUCTION.
RX PubMed=12868060; DOI=10.1002/yea.1019;
RA Runner V.M., Brewster J.L.;
RT "A genetic screen for yeast genes induced by sustained osmotic stress.";
RL Yeast 20:913-920(2003).
RN [7]
RP INDUCTION.
RX PubMed=17334841; DOI=10.1007/s00284-006-0525-4;
RA Liu X., Zhang X., Wang C., Liu L., Lei M., Bao X.;
RT "Genetic and comparative transcriptome analysis of bromodomain factor 1 in
RT the salt stress response of Saccharomyces cerevisiae.";
RL Curr. Microbiol. 54:325-330(2007).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=17078969; DOI=10.1016/j.jmb.2006.10.004;
RA White M.A., Clark K.M., Grayhack E.J., Dumont M.E.;
RT "Characteristics affecting expression and solubilization of yeast membrane
RT proteins.";
RL J. Mol. Biol. 365:621-636(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-232 AND THR-235, 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: Involved in sporulation and affects the sphingolipid
CC composition of the plasma membrane. {ECO:0000269|PubMed:11784867}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11784867,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17078969}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:11784867,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17078969}.
CC Note=Concentrates within cortical patches at the membrane.
CC -!- INDUCTION: By osmotic and salt stresses. {ECO:0000269|PubMed:12868060,
CC ECO:0000269|PubMed:17334841}.
CC -!- MISCELLANEOUS: Present with 329 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SUR7 family. {ECO:0000305}.
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DR EMBL; Z74270; CAA98801.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11643.1; -; Genomic_DNA.
DR PIR; S67785; S67785.
DR RefSeq; NP_010059.1; NM_001180282.1.
DR AlphaFoldDB; Q07651; -.
DR BioGRID; 31824; 117.
DR IntAct; Q07651; 48.
DR MINT; Q07651; -.
DR STRING; 4932.YDL222C; -.
DR iPTMnet; Q07651; -.
DR MaxQB; Q07651; -.
DR PaxDb; Q07651; -.
DR PRIDE; Q07651; -.
DR EnsemblFungi; YDL222C_mRNA; YDL222C; YDL222C.
DR GeneID; 851304; -.
DR KEGG; sce:YDL222C; -.
DR SGD; S000002381; FMP45.
DR VEuPathDB; FungiDB:YDL222C; -.
DR eggNOG; ENOG502RKFF; Eukaryota.
DR GeneTree; ENSGT00940000176556; -.
DR HOGENOM; CLU_059603_0_0_1; -.
DR InParanoid; Q07651; -.
DR OMA; FMWTAVA; -.
DR BioCyc; YEAST:G3O-29602-MON; -.
DR PRO; PR:Q07651; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07651; protein.
DR GO; GO:0005938; C:cell cortex; IDA:SGD.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0032185; P:septin cytoskeleton organization; IBA:GO_Central.
DR InterPro; IPR009571; SUR7/Rim9-like_fungi.
DR Pfam; PF06687; SUR7; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Sporulation; Stress response; Transmembrane; Transmembrane helix.
FT CHAIN 1..309
FT /note="SUR7 family protein FMP45"
FT /id="PRO_0000202591"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 253..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 309 AA; 34135 MW; DC1B0D70FA52E7A7 CRC64;
MIFKRFVNLL VFLFLLGAGL LTFFLILSGG RESGTLKNFY WLQADTNGFN SAPSTTRWYN
YNWCGYEDGQ LANCSSRAPA KPFSPRDNFG NSVNLPSSFR NNRDTYYYLS RVGWAMLLIS
LFFIVLALVP GFLATFLPFK AVPVLYCVLS WLAFFFIILA ACLYTGCYVK ARKTFRNSGR
SARLGPKNFA FIWTSVFLML VNAIWSTIFS ATHKAHSTYS DHDMYAQYES PSVDTGAQME
KSTYNSGATD GAGPITAAPV VGQPQPTTTT TPAGNGKFFQ KLKTRKQVPS AELEPAGDGG
LAGPVTVRD
