SCS7_SCHPO
ID SCS7_SCHPO Reviewed; 347 AA.
AC O13846;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ceramide very long chain fatty acid hydroxylase scs7;
DE Short=Ceramide VLCFA hydroxylase scs7;
DE EC=1.14.18.-;
GN Name=scs7 {ECO:0000312|PomBase:SPAC19G12.08}; ORFNames=SPAC19G12.08;
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: Ceramide hydroxylase involved in the hydroxylation of
CC sphingolipid-associated very long chain fatty acids. Postulated to
CC hydroxylate the very long chain fatty acid of dihydroceramides and
CC phytoceramides at C-2. {ECO:0000250|UniProtKB:Q03529}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q03529};
CC Note=Binds 2 Zn(2+) ions per subunit that likely form a catalytic
CC dimetal center. {ECO:0000250|UniProtKB:Q03529};
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000250|UniProtKB:Q03529}.
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. SCS7 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved N-terminal cytochrome b5 heme-binding
CC domain. Its enzyme activity is therefore unsure. {ECO:0000305}.
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DR EMBL; CU329670; CAB10119.1; -; Genomic_DNA.
DR PIR; T37995; T37995.
DR RefSeq; NP_594423.1; NM_001019852.2.
DR AlphaFoldDB; O13846; -.
DR SMR; O13846; -.
DR BioGRID; 278977; 210.
DR STRING; 4896.SPAC19G12.08.1; -.
DR iPTMnet; O13846; -.
DR MaxQB; O13846; -.
DR PaxDb; O13846; -.
DR PRIDE; O13846; -.
DR EnsemblFungi; SPAC19G12.08.1; SPAC19G12.08.1:pep; SPAC19G12.08.
DR GeneID; 2542519; -.
DR KEGG; spo:SPAC19G12.08; -.
DR PomBase; SPAC19G12.08; scs7.
DR VEuPathDB; FungiDB:SPAC19G12.08; -.
DR eggNOG; KOG0539; Eukaryota.
DR HOGENOM; CLU_034756_0_1_1; -.
DR InParanoid; O13846; -.
DR OMA; VFFWTII; -.
DR PhylomeDB; O13846; -.
DR Reactome; R-SPO-1660661; Sphingolipid de novo biosynthesis.
DR PRO; PR:O13846; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0080132; F:fatty acid alpha-hydroxylase activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0000170; F:sphingosine hydroxylase activity; ISO:PomBase.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006675; P:mannosyl-inositol phosphorylceramide metabolic process; IMP:PomBase.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IC:PomBase.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR InterPro; IPR014430; Scs7.
DR PANTHER; PTHR12863; PTHR12863; 1.
DR Pfam; PF04116; FA_hydroxylase; 1.
DR PIRSF; PIRSF005149; IPC-B_HD; 1.
PE 3: Inferred from homology;
KW Electron transport; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Zinc.
FT CHAIN 1..347
FT /note="Ceramide very long chain fatty acid hydroxylase
FT scs7"
FT /id="PRO_0000362158"
FT TOPO_DOM 1..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03529"
SQ SEQUENCE 347 AA; 40229 MW; B713353AC6FFB251 CRC64;
MASVTSEKCV ILSDGTEYDV TNYLVANKDA ADLLRRYHRQ EVADILNATS KSKHSEAVVE
ILKSAKVPLK NKEFSDLVDQ NIGVGYGNEF IVKPTDLDKD FEKNHFLDLK KPLLPQILFG
NIKKDVYLDQ VHRPRHYRGS GSAPLFGNFL EPLTKTPWYM IPLIWVPCVT YGFLYACTGI
PFSVAITFFI IGLFTWTLVE YTMHRFLFHL DEYTPDHPIF LTMHFAFHGC HHFLPADKYR
LVMPPALFLI FATPWYHFIQ LVLPHYIGVA GFSGAILGYV FYDLTHYFLH HRRMPNAYLT
DLKTWHLDHH YKDYKSAYGI TSWFWDRVFG TEGPLFNEQG KISTKAK
