NVD_HEMPU
ID NVD_HEMPU Reviewed; 469 AA.
AC F7J188;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Cholesterol 7-desaturase nvd;
DE EC=1.14.19.21 {ECO:0000269|PubMed:21632547};
DE AltName: Full=Neverland {ECO:0000303|PubMed:21632547};
DE Short=Nvd_Hp {ECO:0000303|PubMed:21632547};
DE Flags: Precursor;
GN Name=nvd-Hp {ECO:0000312|EMBL:BAK39963.1};
OS Hemicentrotus pulcherrimus (Sea urchin) (Strongylocentrotus pulcherrimus).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Hemicentrotus.
OX NCBI_TaxID=7650;
RN [1] {ECO:0000312|EMBL:BAK39963.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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).
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}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cholesterol 7-desaturase family.
CC {ECO:0000305}.
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DR EMBL; AB607954; BAK39963.1; -; mRNA.
DR AlphaFoldDB; F7J188; -.
DR SMR; F7J188; -.
DR SwissLipids; SLP:000001123; -.
DR BRENDA; 1.14.19.21; 2635.
DR UniPathway; UPA01020; -.
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; Signal; Steroid metabolism;
KW Sterol metabolism; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..469
FT /note="Cholesterol 7-desaturase nvd"
FT /id="PRO_5003363022"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 132..238
FT /note="Rieske"
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 BINDING 174
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 192
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 195
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 469 AA; 53055 MW; AFD6FF4BA936CC9F CRC64;
MASFCASKFL PGLLMLGLGL AVALASSTPT LSLLKDNLKV MNMPLGDWLH ILATNFTNFV
ASQTLLTLTI FGVASFILRY LYQLFLKPLN LDRALGDVGY VLDGKKKRDV VNDIRRRRKS
GDLPPIYPNG WIPLVASQDL VKGDVKYISA VGNEFAVYRG EDGEAYAVDA YCPHLGANMA
IGGMVKGNCL TCPFHGWVFE GKEGKCVDIP YQEKGKSVPA QAKVKSWSVI EQNGFVLVWH
DVEGREPSWF PENIEEEKWG KMYYHGTTKH TVCAHVEEIS ENGADCAHLT FVHGAFMGSG
NDLRYMGSKL WSWASHSWGG KWEQDPDHKH VGVMTVYHAF SLFGMPIEVT RTESTARQNG
PAHVLLSFSL PFGKATIAIG VTPIEPLTQI VTQHVYASRF IPRWLAKSFL YAEYVQFERD
IMVWNYKTYQ RKPLLVFEDR LISKHRRWYS QFFSENSPKF EDMKKTLDW
