SUR2_SCHPO
ID SUR2_SCHPO Reviewed; 293 AA.
AC O94298;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Sphingolipid C4-hydroxylase sur2;
DE EC=1.-.-.-;
DE AltName: Full=Syringomycin response protein 2;
GN Name=sur2; ORFNames=SPBC887.15c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Required for hydroxylation of C-4 in the sphingoid moiety of
CC ceramide. Involved in the response to syringomycin (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Membrane lipid metabolism; sphingolipid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR EMBL; CU329671; CAA21900.1; -; Genomic_DNA.
DR PIR; T40740; T40740.
DR RefSeq; NP_596489.1; NM_001022409.2.
DR AlphaFoldDB; O94298; -.
DR BioGRID; 277739; 4.
DR IntAct; O94298; 1.
DR STRING; 4896.SPBC887.15c.1; -.
DR MaxQB; O94298; -.
DR PaxDb; O94298; -.
DR PRIDE; O94298; -.
DR EnsemblFungi; SPBC887.15c.1; SPBC887.15c.1:pep; SPBC887.15c.
DR GeneID; 2541225; -.
DR KEGG; spo:SPBC887.15c; -.
DR PomBase; SPBC887.15c; sur2.
DR VEuPathDB; FungiDB:SPBC887.15c; -.
DR eggNOG; KOG0874; Eukaryota.
DR HOGENOM; CLU_043293_1_1_1; -.
DR InParanoid; O94298; -.
DR OMA; FHIIDVY; -.
DR PhylomeDB; O94298; -.
DR UniPathway; UPA00786; -.
DR PRO; PR:O94298; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:PomBase.
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; ISM:PomBase.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IMP:PomBase.
DR GO; GO:0000170; F:sphingosine hydroxylase activity; IMP:PomBase.
DR GO; GO:0006675; P:mannosyl-inositol phosphorylceramide metabolic process; IMP:PomBase.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:PomBase.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..293
FT /note="Sphingolipid C4-hydroxylase sur2"
FT /id="PRO_0000317336"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 136..270
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
SQ SEQUENCE 293 AA; 34191 MW; 51923AF9876331C4 CRC64;
MVTTVEMLTT WNPVTVSLVS PVIIYWVASA FFGFLHYIEL PVFEKYRIHP PEEIARRNRV
PQMAVVKAVL FQQLCEVVVG IALAMFEGYP EPIDEAKQML RYEAFFSKNL PALLQVAPFA
PKLAYNFIVP AFQYFFAFFI IDSWQYFWHR YLHYNKKLYN MIHAHHHRLQ VPYAMGALYN
HPFEGLILDT FGAGVAYLAA GLSPQQAVIF FTLSTLKTVD DHCGYVFPYD PLQMFFANNA
RYHDLHHQPY GFQKNFSQPF FTFWDHVLGT YMPPKSETPY EKKQKAKNAK KVN
