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   27-MAR-2024, entry version 172.
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; 139.
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   GlyCosmos; P54003; 1 site, No reported glycans.
DR   GlyGen; P54003; 1 site.
DR   iPTMnet; P54003; -.
DR   MaxQB; P54003; -.
DR   PaxDb; 4932-YML052W; -.
DR   PeptideAtlas; P54003; -.
DR   DNASU; 854953; -.
DR   EnsemblFungi; YML052W_mRNA; YML052W; YML052W.
DR   GeneID; 854953; -.
DR   KEGG; sce:YML052W; -.
DR   AGR; SGD:S000004516; -.
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   OrthoDB; 1967464at2759; -.
DR   BioCyc; YEAST:G3O-32649-MONOMER; -.
DR   BioGRID-ORCS; 854953; 2 hits in 10 CRISPR screens.
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: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   Gene3D; 1.20.140.150; -; 1.
DR   InterPro; IPR009571; SUR7/Rim9-like_fungi.
DR   PANTHER; PTHR36414; PROTEIN SUR7; 1.
DR   PANTHER; PTHR36414:SF1; PROTEIN SUR7; 1.
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
//