SUR7_YEAST
ID SUR7_YEAST Reviewed; 302 AA.
AC P54003; D6VZC3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Protein SUR7;
GN Name=SUR7; OrderedLocusNames=YML052W; ORFNames=YM9958.11;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9219339;
RX DOI=10.1002/(sici)1097-0061(19970630)13:8<747::aid-yea137>3.0.co;2-l;
RA Sivadon P., Peypouquet M.-F., Doignon F., Aigle M., Crouzet M.;
RT "Cloning of the multicopy suppressor gene SUR7: evidence for a functional
RT relationship between the yeast actin-binding protein Rvs167 and a putative
RT membranous protein.";
RL Yeast 13:747-761(1997).
RN [5]
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 [6]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12469340;
RX DOI=10.1002/1615-9861(200212)2:12<1706::aid-prot1706>3.0.co;2-k;
RA Navarre C., Degand H., Bennett K.L., Crawford J.S., Moertz E., Boutry M.;
RT "Subproteomics: identification of plasma membrane proteins from the yeast
RT Saccharomyces cerevisiae.";
RL Proteomics 2:1706-1714(2002).
RN [7]
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 [8]
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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=15536122; DOI=10.1242/jcs.01493;
RA Malinska K., Malinsky J., Opekarova M., Tanner W.;
RT "Distribution of Can1p into stable domains reflects lateral protein
RT segregation within the plasma membrane of living S. cerevisiae cells.";
RL J. Cell Sci. 117:6031-6041(2004).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=16496001; DOI=10.1038/nature04472;
RA Walther T.C., Brickner J.H., Aguilar P.S., Bernales S., Pantoja C.,
RA Walter P.;
RT "Eisosomes mark static sites of endocytosis.";
RL Nature 439:998-1003(2006).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-301, 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. Probably involved in endocytosis.
CC {ECO:0000269|PubMed:11784867}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11784867,
CC ECO:0000269|PubMed:12469340, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15536122, ECO:0000269|PubMed:16496001}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:11784867,
CC ECO:0000269|PubMed:12469340, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15536122, ECO:0000269|PubMed:16496001}.
CC Note=Localizes at eisosomes, structures which colocalize with sites of
CC protein and lipid endocytosis.
CC -!- MISCELLANEOUS: Present with 17000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SUR7 family. {ECO:0000305}.
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DR EMBL; Z46729; CAA86724.1; -; Genomic_DNA.
DR EMBL; AY557986; AAS56312.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09847.1; -; Genomic_DNA.
DR PIR; S49809; S49809.
DR RefSeq; NP_013660.1; NM_001182410.1.
DR AlphaFoldDB; P54003; -.
DR BioGRID; 35116; 137.
DR IntAct; P54003; 3.
DR MINT; P54003; -.
DR STRING; 4932.YML052W; -.
DR TCDB; 1.H.1.7.1; the claudin tight junction (claudin1) family.
DR TCDB; 8.A.148.1.1; the plasma membrane organizing center, eisosome (eisosome) family.
DR iPTMnet; P54003; -.
DR MaxQB; P54003; -.
DR PaxDb; P54003; -.
DR PRIDE; P54003; -.
DR DNASU; 854953; -.
DR EnsemblFungi; YML052W_mRNA; YML052W; YML052W.
DR GeneID; 854953; -.
DR KEGG; sce:YML052W; -.
DR SGD; S000004516; SUR7.
DR VEuPathDB; FungiDB:YML052W; -.
DR eggNOG; ENOG502RKFF; Eukaryota.
DR HOGENOM; CLU_059603_1_0_1; -.
DR InParanoid; P54003; -.
DR OMA; PLNKFYW; -.
DR BioCyc; YEAST:G3O-32649-MON; -.
DR PRO; PR:P54003; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P54003; protein.
DR GO; GO:0005938; C:cell cortex; IDA:SGD.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0032126; C:eisosome; IDA: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; IDA: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; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR GO; GO:0097446; P:protein localization to eisosome filament; 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; Endocytosis; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Sporulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..302
FT /note="Protein SUR7"
FT /id="PRO_0000072317"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 302 AA; 33830 MW; 14625FD6A48F515A CRC64;
MVKVWNIVLR LVVLLFLAGN TLLLILMIIS GATDHYPVNR FYWVQGNTTG IPNAGDETRW
TFWGACLQDK DGSDTCTSNL APAYPISPVD NFNTHINVPH QFISKRDAFY YLTRFSFCFF
WIALAFVGVS FILYVLTWCS KMLSEMVLIL MSFGFVFNTA AVVLQTAASA MAKNAFHDDH
RSAQLGASMM GMAWASVFLC IVEFILLVFW SVRARLASTY SIDNSRYRTS SRWNPFHREK
EQATDPILTA TGPEDMQQSA SIVGPSSNAN PVTATAATEN QPKGINFFTI RKSHERPDDV
SV
