SC5D_RAT
ID SC5D_RAT Reviewed; 299 AA.
AC Q9EQS5;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Lathosterol oxidase;
DE EC=1.14.19.20;
DE AltName: Full=C-5 sterol desaturase;
DE AltName: Full=Delta(7)-sterol 5-desaturase;
DE AltName: Full=Delta(7)-sterol C5(6)-desaturase;
DE AltName: Full=Lathosterol 5-desaturase;
DE AltName: Full=Sterol-C5-desaturase {ECO:0000312|EMBL:BAB19798.1};
GN Name=Sc5d {ECO:0000312|RGD:620775};
GN Synonyms=C5d {ECO:0000312|EMBL:BAB19798.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Nishino H., Hozumi K., Moromi M., Nam S., Ishibashi T.;
RT "Cloning, expression, and site-directed mutagenesis of the mammalian sterol
RT C5-desaturase.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAH81704.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=4019441; DOI=10.1093/oxfordjournals.jbchem.a135137;
RA Honjo K., Ishibashi T., Imai Y.;
RT "Partial purification and characterization of lathosterol 5-desaturase from
RT rat liver microsomes.";
RL J. Biochem. 97:955-959(1985).
RN [6]
RP CATALYTIC ACTIVITY.
RX PubMed=9056262; DOI=10.1006/abbi.1996.9871;
RA Nishino H., Nakaya J., Nishi S., Kurosawa T., Ishibashi T.;
RT "Temperature-induced differential kinetic properties between an initial
RT burst and the following steady state in membrane-bound enzymes: studies on
RT lathosterol 5-desaturase.";
RL Arch. Biochem. Biophys. 339:298-304(1997).
CC -!- FUNCTION: Catalyzes a dehydrogenation to introduce C5-6 double bond
CC into lathosterol in cholesterol biosynthesis.
CC {ECO:0000269|PubMed:4019441}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a Delta(7)-sterol + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a
CC Delta(5),Delta(7)-sterol + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:54320, 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:138130,
CC ChEBI:CHEBI:138131; EC=1.14.19.20;
CC Evidence={ECO:0000269|PubMed:4019441, ECO:0000269|PubMed:9056262};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54321;
CC Evidence={ECO:0000305|PubMed:4019441, ECO:0000305|PubMed:9056262};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + lathosterol + O2 = 7-
CC dehydrocholesterol + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46556, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17168, ChEBI:CHEBI:17759, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=1.14.19.20;
CC Evidence={ECO:0000250|UniProtKB:O75845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46557;
CC Evidence={ECO:0000250|UniProtKB:O75845};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:4019441}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR EMBL; AB052846; BAB19798.1; -; mRNA.
DR EMBL; AC133265; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473975; EDL95251.1; -; Genomic_DNA.
DR EMBL; BC081704; AAH81704.1; -; mRNA.
DR RefSeq; NP_446094.1; NM_053642.2.
DR RefSeq; XP_017450895.1; XM_017595406.1.
DR AlphaFoldDB; Q9EQS5; -.
DR STRING; 10116.ENSRNOP00000011284; -.
DR PaxDb; Q9EQS5; -.
DR Ensembl; ENSRNOT00000106582; ENSRNOP00000092291; ENSRNOG00000065944.
DR GeneID; 114100; -.
DR KEGG; rno:114100; -.
DR UCSC; RGD:620775; rat.
DR CTD; 6309; -.
DR RGD; 620775; Sc5d.
DR eggNOG; KOG0872; Eukaryota.
DR GeneTree; ENSGT00550000075101; -.
DR HOGENOM; CLU_047036_2_2_1; -.
DR InParanoid; Q9EQS5; -.
DR OMA; HTLHHMY; -.
DR OrthoDB; 1249774at2759; -.
DR PhylomeDB; Q9EQS5; -.
DR TreeFam; TF300797; -.
DR Reactome; R-RNO-6807047; Cholesterol biosynthesis via desmosterol.
DR Reactome; R-RNO-6807062; Cholesterol biosynthesis via lathosterol.
DR PRO; PR:Q9EQS5; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000008305; Expressed in liver and 20 other tissues.
DR Genevisible; Q9EQS5; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000248; F:C-5 sterol desaturase activity; IDA:RGD.
DR GO; GO:0050046; F:delta7-sterol 5(6)-desaturase activity; TAS:RGD.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0033490; P:cholesterol biosynthetic process via lathosterol; IDA:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; TAS:RGD.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Iron; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..299
FT /note="Lathosterol oxidase"
FT /id="PRO_0000434558"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 124..252
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 138..143
FT /note="Histidine box-1"
FT MOTIF 151..155
FT /note="Histidine box-2"
FT MOTIF 228..233
FT /note="Histidine box-3"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75845"
SQ SEQUENCE 299 AA; 35147 MW; AE2D03FF486A46A3 CRC64;
MDLVLSAADY YFFTPYVYPA TWPEDNIIRQ TVSLLVVTNL GAYILYFFCA TLSYYFVYDH
SLMKHPQFLK NQVSREIMFT VKSLPWISIP TVSLFLLELR GYSKLYDDIG DFPNGWIHLI
MSVISFLFFT DMLIYWIHRG LHHRLLYKHI HKPHHIWKIP TPFASHAFHP VDGFLQSLPY
HIYPFVFPLH KVVYLGLYVL VNVWTISIHD GDFRVPQIFR PFINGSAHHT DHHMLFDYNY
GQYFTLWDRI GGSFKHPSSF EGKGPHSYVK NMTEKESNSL AENGCKSKKL CNGEFTKNE
