SUR1_YEAST
ID SUR1_YEAST Reviewed; 382 AA.
AC P33300; D6W3V7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Mannosyl phosphorylinositol ceramide synthase SUR1 {ECO:0000303|PubMed:9323360};
DE EC=2.4.1.370 {ECO:0000269|PubMed:9323360};
GN Name=SUR1 {ECO:0000303|PubMed:9323360}; Synonyms=BCL21, CSG1, LPE15;
GN OrderedLocusNames=YPL057C;
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 44827 / SKQ2N;
RX PubMed=8488727; DOI=10.1002/yea.320090306;
RA Desfarges L., Durrens P., Juguelin H., Cassagne C., Bonneu M., Aigle M.;
RT "Yeast mutants affected in viability upon starvation have a modified
RT phospholipid composition.";
RL Yeast 9:267-277(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26786 / X2180-1A;
RX PubMed=7854312; DOI=10.1007/bf00288599;
RA Takita Y., Ohya Y., Anraku Y.;
RT "The CLS2 gene encodes a protein with multiple membrane-spanning domains
RT that is important Ca2+ tolerance in yeast.";
RL Mol. Gen. Genet. 246:269-281(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=9323360; DOI=10.1007/s004380050530;
RA Beeler T.J., Fu D., Rivera J., Monaghan E., Gable K., Dunn T.M.;
RT "SUR1 (CSG1/BCL21), a gene necessary for growth of Saccharomyces cerevisiae
RT in the presence of high Ca2+ concentrations at 37 degrees C, is required
RT for mannosylation of inositolphosphorylceramide.";
RL Mol. Gen. Genet. 255:570-579(1997).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=12954640; DOI=10.1074/jbc.m305498200;
RA Uemura S., Kihara A., Inokuchi J., Igarashi Y.;
RT "Csg1p and newly identified Csh1p function in mannosylinositol
RT phosphorylceramide synthesis by interacting with Csg2p.";
RL J. Biol. Chem. 278:45049-45055(2003).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, 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: Involved in the synthesis of mannosyl phosphorylinositol
CC ceramide (PubMed:9323360, PubMed:12954640). Catalyzes the addition of
CC mannosyl to phosphorylinositol ceramide. Suppressor of RVS161 mutation
CC (PubMed:9323360, PubMed:12954640). {ECO:0000269|PubMed:12954640,
CC ECO:0000269|PubMed:9323360}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1D-myo-inositol-1-phospho-N-[(R)-2-hydroxy-very-long-chain
CC fatty acyl]-(R)-4-hydroxysphingoid base + GDP-alpha-D-mannose = an
CC alpha-D-mannosyl-(1<->6)-1D-myo-inositol-1-phospho-N-[(R)-2-hydroxy-
CC very-long-chain fatty acyl]-(R)-4-hydroxysphingoid base + GDP + H(+);
CC Xref=Rhea:RHEA:64596, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:155885, ChEBI:CHEBI:155926;
CC EC=2.4.1.370; Evidence={ECO:0000269|PubMed:9323360};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64597;
CC Evidence={ECO:0000269|PubMed:9323360};
CC -!- SUBUNIT: Heterodimer of SUR1 and CSG2. {ECO:0000269|PubMed:12954640}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Leads to altered sphingolipid synthesis.
CC {ECO:0000269|PubMed:9323360}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 32 family.
CC {ECO:0000305}.
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DR EMBL; M96648; AAA68909.1; -; Genomic_DNA.
DR EMBL; D26581; BAA05628.1; -; Genomic_DNA.
DR EMBL; U39205; AAB68308.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11373.1; -; Genomic_DNA.
DR PIR; S41798; S41798.
DR RefSeq; NP_015268.1; NM_001183871.1.
DR AlphaFoldDB; P33300; -.
DR SMR; P33300; -.
DR BioGRID; 36123; 875.
DR ComplexPortal; CPX-1739; Mannosyl phosphorylinositol ceramide synthase SUR1-CSG2.
DR DIP; DIP-4557N; -.
DR IntAct; P33300; 4.
DR MINT; P33300; -.
DR STRING; 4932.YPL057C; -.
DR CAZy; GT32; Glycosyltransferase Family 32.
DR iPTMnet; P33300; -.
DR MaxQB; P33300; -.
DR PaxDb; P33300; -.
DR PRIDE; P33300; -.
DR EnsemblFungi; YPL057C_mRNA; YPL057C; YPL057C.
DR GeneID; 856050; -.
DR KEGG; sce:YPL057C; -.
DR SGD; S000005978; SUR1.
DR VEuPathDB; FungiDB:YPL057C; -.
DR eggNOG; ENOG502QS3D; Eukaryota.
DR GeneTree; ENSGT00940000176781; -.
DR HOGENOM; CLU_036369_3_2_1; -.
DR InParanoid; P33300; -.
DR OMA; WTDEMAY; -.
DR BioCyc; MetaCyc:MON3O-703; -.
DR BioCyc; YEAST:MON3O-703; -.
DR BRENDA; 2.4.1.370; 984.
DR PRO; PR:P33300; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P33300; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031501; C:mannosyltransferase complex; IDA:ComplexPortal.
DR GO; GO:0103064; F:inositol phosphorylceramide mannosyltransferase activity; IEA:RHEA.
DR GO; GO:0000030; F:mannosyltransferase activity; IMP:SGD.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; IMP:SGD.
DR GO; GO:0006676; P:mannosyl diphosphorylinositol ceramide metabolic process; IDA:ComplexPortal.
DR GO; GO:0051999; P:mannosyl-inositol phosphorylceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006675; P:mannosyl-inositol phosphorylceramide metabolic process; IMP:SGD.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:SGD.
DR InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF04488; Gly_transf_sug; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Membrane; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..382
FT /note="Mannosyl phosphorylinositol ceramide synthase SUR1"
FT /id="PRO_0000072314"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 382 AA; 44808 MW; 5A9AAB5F9A4069E3 CRC64;
MRKELKYLIC FNILLLLSII YYTFDLLTLC IDDTVKDAIL EEDLNPDAPP KPQLIPKIIH
QTYKTEDIPE HWKEGRQKCL DLHPDYKYIL WTDEMAYEFI KEEYPWFLDT FENYKYPIER
ADAIRYFILS HYGGVYIDLD DGCERKLDPL LAFPAFLRKT SPLGVSNDVM GSVPRHPFFL
KALKSLKHYD KYWFIPYMTI MGSTGPLFLS VIWKQYKRWR IPKNGTVRIL QPAYYKMHSY
SFFSITKGSS WHLDDAKLMK ALENHILSCV VTGFIFGFFI LYGEFTFYCW LCSKNFSNLT
KNWKLNAIKV RFVTILNSLG LRLKLSKSTS DTASATLLAR QQKRLRKDSN TNIVLLKSSR
KSDVYDLEKN DSSKYSLGNN SS
