NVD_XENLA
ID NVD_XENLA Reviewed; 454 AA.
AC F7J184;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Cholesterol 7-desaturase nvd {ECO:0000305};
DE EC=1.14.19.21 {ECO:0000269|PubMed:21632547};
DE AltName: Full=Protein neverland {ECO:0000303|PubMed:21632547};
DE Short=Nvd protein {ECO:0000303|PubMed:21632547};
DE Short=nvd-Xl {ECO:0000303|PubMed:21632547};
GN Name=nvd; ORFNames=XELAEV_18041408mg {ECO:0000303|PubMed:27762356};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=21632547; DOI=10.1074/jbc.m111.244384;
RA Yoshiyama-Yanagawa T., Enya S., Shimada-Niwa Y., Yaguchi S., Haramoto Y.,
RA Matsuya T., Shiomi K., Sasakura Y., Takahashi S., Asashima M., Kataoka H.,
RA Niwa R.;
RT "The conserved Rieske oxygenase DAF-36/Neverland is a novel cholesterol-
RT metabolizing enzyme.";
RL J. Biol. Chem. 286:25756-25762(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J;
RX PubMed=27762356; DOI=10.1038/nature19840;
RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL Nature 538:336-343(2016).
CC -!- FUNCTION: Catalyzes the production of 7-dehydrocholesterol (7-DHC or
CC cholesta-5,7-dien-3beta-ol) by inserting a double bond (desaturating)
CC at the C7-C8 single bond of cholesterol. This reaction is the first
CC step in the synthesis of the steroid hormone Delta(7)-dafachronic acid.
CC {ECO:0000269|PubMed:21632547}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + H(+) + NADPH + O2 = 7-dehydrocholesterol + 2 H2O
CC + NADP(+); Xref=Rhea:RHEA:45024, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:17759, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.14.19.21; Evidence={ECO:0000269|PubMed:21632547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45025;
CC Evidence={ECO:0000305|PubMed:21632547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + H(+) + NADH + O2 = 7-dehydrocholesterol + 2 H2O
CC + NAD(+); Xref=Rhea:RHEA:51644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:17759,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.19.21;
CC Evidence={ECO:0000269|PubMed:21632547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51645;
CC Evidence={ECO:0000305|PubMed:21632547};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
CC -!- PATHWAY: Steroid hormone biosynthesis; dafachronic acid biosynthesis.
CC {ECO:0000305|PubMed:21632547}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cholesterol 7-desaturase family.
CC {ECO:0000305}.
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DR EMBL; AB607950; BAK39959.1; -; mRNA.
DR EMBL; CM004481; OCT65169.1; -; Genomic_DNA.
DR AlphaFoldDB; F7J184; -.
DR SMR; F7J184; -.
DR STRING; 8355.F7J184; -.
DR SwissLipids; SLP:000000091; -.
DR OMA; AVYQMRR; -.
DR BRENDA; 1.14.19.21; 6725.
DR UniPathway; UPA01020; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:InterPro.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR045605; KshA-like_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF19298; KshA_C; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Iron; Iron-sulfur; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..454
FT /note="Cholesterol 7-desaturase nvd"
FT /id="PRO_0000451465"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 117..221
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 158
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 160
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 178
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 181
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 454 AA; 51761 MW; DB3E737E20243643 CRC64;
MESVGHSLLT LSVLCPVGAL LLCWVGSVLL GAGLLPSLTL STRDPSTTLS RTPWLVVLVP
LLVLWGWRWL SRPMELLRSP EEVGYIPERG RSRAQTANLV RRRRMKGELP PIYPNGWYRA
LDSHLLPPGT VQDCTLLGEQ LAVYRTLEGK VYVVDAYCPH LGANLAVGGK VVGDCIECPF
HGWQFRGEDG KCTRIPYAEK VPDFAKIKTR PSCELNGMVF VWYHCDGIEP TWSVPEQEEI
TKKEWVYHGR TEHYVNAHIE EIPENAADIA HLDFLHTPGI LSGVDLRYTK SRIWDFVKHS
WKVQWIPEPA PNKHCSQMLL AHSILLFGKH FPLLDVNVVA RQVGPGIVFL HFKHAFLGEG
VIVHCVTPVE PLLQKVSHSI YYQKNIPALI PKFILKAECI QFERDVMIWN NKKYISKPML
VKEDAAIQKH RRWFSQFYSN NSPQITFQQE GLDW
