SUR2_YEAST
ID SUR2_YEAST Reviewed; 349 AA.
AC P38992; D6VSS6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Sphingolipid C4-hydroxylase SUR2;
DE EC=1.-.-.-;
DE AltName: Full=Syringomycin response protein 2;
GN Name=SUR2; Synonyms=SYR2; OrderedLocusNames=YDR297W; ORFNames=D9740.8;
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.
RC STRAIN=ATCC 44827 / SKQ2N;
RA Desfarges L., Durrens P., Juguelin H., Cassagne C., Bonneu M., Aigle M.;
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=KZ1-1C;
RX PubMed=8868422; DOI=10.1099/13500872-142-3-477;
RA Cliften P., Wang Y., Mochizuki D., Miyakawa T., Wangspa R., Hughes J.,
RA Takemoto J.Y.;
RT "SYR2, a gene necessary for syringomycin growth inhibition of Saccharomyces
RT cerevisiae.";
RL Microbiology 142:477-484(1996).
RN [3]
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 [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, AND CATALYTIC ACTIVITY.
RX PubMed=9368039; DOI=10.1074/jbc.272.47.29704;
RA Haak D., Gable K., Beeler T., Dunn T.;
RT "Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and
RT Scs7p.";
RL J. Biol. Chem. 272:29704-29710(1997).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9556590; DOI=10.1074/jbc.273.18.11062;
RA Grilley M.M., Stock S.D., Dickson R.C., Lester R.L., Takemoto J.Y.;
RT "Syringomycin action gene SYR2 is essential for sphingolipid 4-
RT hydroxylation in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:11062-11068(1998).
RN [7]
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).
CC -!- FUNCTION: Required for hydroxylation of C-4 in the sphingoid moiety of
CC ceramide. Catalyzes the conversion of sphinganine to phytosphingosine
CC in sphingolipid biosynthesis. Involved in the response to syringomycin.
CC {ECO:0000269|PubMed:9368039, ECO:0000269|PubMed:9556590}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + sphinganine = (4R)-
CC hydroxysphinganine + 2 Fe(III)-[cytochrome b5] + H2O;
CC Xref=Rhea:RHEA:33519, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:64124; Evidence={ECO:0000269|PubMed:9556590};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33520;
CC Evidence={ECO:0000305|PubMed:9556590};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC = an N-acyl-(4R)-4-hydroxysphinganine + 2 Fe(III)-[cytochrome b5] +
CC H2O; Xref=Rhea:RHEA:46364, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:31488,
CC ChEBI:CHEBI:31998; Evidence={ECO:0000269|PubMed:9368039,
CC ECO:0000269|PubMed:9556590};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46365;
CC Evidence={ECO:0000305|PubMed:9368039, ECO:0000305|PubMed:9556590};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyleicosasphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+)
CC + O2 = 2 Fe(III)-[cytochrome b5] + H2O + N-acyl-4-
CC hydroxyeicosasphinganine; Xref=Rhea:RHEA:55476, Rhea:RHEA-COMP:10438,
CC Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:71984, ChEBI:CHEBI:71985;
CC Evidence={ECO:0000269|PubMed:9556590};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55477;
CC Evidence={ECO:0000305|PubMed:9556590};
CC -!- PATHWAY: Membrane lipid metabolism; sphingolipid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:8868422}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 54300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR EMBL; U07171; AAA16608.1; -; Unassigned_DNA.
DR EMBL; U10427; AAB41115.1; -; Genomic_DNA.
DR EMBL; U28374; AAB64733.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12136.1; -; Genomic_DNA.
DR PIR; S48533; S48533.
DR RefSeq; NP_010583.1; NM_001180605.1.
DR AlphaFoldDB; P38992; -.
DR BioGRID; 32349; 225.
DR DIP; DIP-7741N; -.
DR IntAct; P38992; 34.
DR MINT; P38992; -.
DR STRING; 4932.YDR297W; -.
DR SwissLipids; SLP:000000370; -.
DR MaxQB; P38992; -.
DR PaxDb; P38992; -.
DR PRIDE; P38992; -.
DR EnsemblFungi; YDR297W_mRNA; YDR297W; YDR297W.
DR GeneID; 851891; -.
DR KEGG; sce:YDR297W; -.
DR SGD; S000002705; SUR2.
DR VEuPathDB; FungiDB:YDR297W; -.
DR eggNOG; KOG0874; Eukaryota.
DR HOGENOM; CLU_043293_1_1_1; -.
DR InParanoid; P38992; -.
DR OMA; FHIIDVY; -.
DR BioCyc; MetaCyc:YDR297W-MON; -.
DR BioCyc; YEAST:YDR297W-MON; -.
DR BRENDA; 1.14.18.5; 984.
DR UniPathway; UPA00786; -.
DR PRO; PR:P38992; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P38992; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IBA:GO_Central.
DR GO; GO:0000170; F:sphingosine hydroxylase activity; IMP:SGD.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006665; P:sphingolipid metabolic process; IMP:SGD.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..349
FT /note="Sphingolipid C4-hydroxylase SUR2"
FT /id="PRO_0000072316"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 162..297
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
SQ SEQUENCE 349 AA; 40734 MW; 406D778092CA75C1 CRC64;
MNVTSNATAA GSFPLAFGLK TSFGFMHYAK APAINLRPKE SLLPEMSDGV LALVAPVVAY
WALSGIFHVI DTFHLAEKYR IHPSEEVAKR NKASRMHVFL EVILQHIIQT IVGLIFMHFE
PIYMTGFEEN AMWKLRADLP RIIPDAAIYY GYMYGMSALK IFAGFLFVDT WQYFLHRLMH
MNKTLYKWFH SVHHELYVPY AYGALFNNPV EGFLLDTLGT GIAMTLTHLT HREQIILFTF
ATMKTVDDHC GYALPLDPFQ WLFPNNAVYH DIHHQQFGIK TNFAQPFFTF WDNLFQTNFK
GFEEYQKKQR RVTIDKYKEF LQERELEKKE KLKNFKAMNA AENEVKKEK
