NVD2_CIOIN
ID NVD2_CIOIN Reviewed; 452 AA.
AC F7J187; A0A1W2W3G7; F6QUZ6;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 2.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Cholesterol 7-desaturase nvd 2;
DE EC=1.14.19.21 {ECO:0000269|PubMed:21632547};
DE AltName: Full=Neverland 2 {ECO:0000303|PubMed:21632547};
DE Short=Nvd-Ci-2 {ECO:0000303|PubMed:21632547};
GN Name=nvd-Ci-2 {ECO:0000312|EMBL:BAK39962.1};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC TISSUE=Embryo {ECO:0000312|EMBL:BAK39962.1};
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].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
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. Essential regulator of steroid
CC biosynthesis as this reaction is the first step in the synthesis of the
CC 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAAA01003003; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB607953; BAK39962.1; -; mRNA.
DR EMBL; EAAA01003003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001265912.1; NM_001278983.1.
DR AlphaFoldDB; F7J187; -.
DR SMR; F7J187; -.
DR STRING; 7719.NP_001265912.1; -.
DR SwissLipids; SLP:000001122; -.
DR GeneID; 100176071; -.
DR KEGG; cin:100176071; -.
DR eggNOG; ENOG502QS20; Eukaryota.
DR HOGENOM; CLU_037178_0_0_1; -.
DR OrthoDB; 1199207at2759; -.
DR TreeFam; TF313257; -.
DR UniPathway; UPA01020; -.
DR Proteomes; UP000008144; Unassembled WGS sequence.
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:UniProtKB-KW.
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; Cholesterol metabolism; Iron; Iron-sulfur; Lipid metabolism;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome;
KW Steroid metabolism; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..452
FT /note="Cholesterol 7-desaturase nvd 2"
FT /id="PRO_0000452608"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 107..212
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 148
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 150
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 169
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 172
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT CONFLICT 117
FT /note="K -> E (in Ref. 1; BAK39962)"
FT CONFLICT 152
FT /note="L -> G (in Ref. 1; BAK39962)"
SQ SEQUENCE 452 AA; 51977 MW; 020B5E55C7AB3354 CRC64;
MLIEYLIRIT VMVITSERLL ILMGLCDESF HFPVMIRVVF NAAVAIVIAL VMSKLYKVLF
APLDLRRKLE DVGYVHHDHS VSREENIRDT QRRKKLGNTP PVFPNGWFKV ADSTWIKKGQ
VKSIYFFGEQ LALFRNKRGL LRALDAYCPH LLANMAAGGK VVNSDCLECP FHGWKFSGET
GKLVDVPYAQ KVPTFVSVKK WSCCEVDGMA YLWYHCDGGE PKWVLPSSVT INTLKYAGKT
EHIINSHIQD IPENAADISH LDHLHKPVIG SDVEKTNESL LNNLIFHSIQ ASWKPPTDPN
EPHRSTMSIK DNIHLSIFNI KIPLLYLEFE IDQIGPGAVH IHVRTPFFRG LMLQNVTPIE
PFVQKLTHSF YVSPWVPVCI AKAFYLLETT QIERDILMWN NKTYFRQPVL VKEESALAKH
RRWYQQFYSE NSPRMNHRGD LVYPGKPKLA DW
