DHCR7_XENLA
ID DHCR7_XENLA Reviewed; 473 AA.
AC Q7ZXH1;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=7-dehydrocholesterol reductase;
DE Short=7-DHC reductase;
DE EC=1.3.1.21 {ECO:0000250|UniProtKB:O88455};
DE AltName: Full=Sterol Delta(7)-reductase;
GN Name=dhcr7;
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 [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 7-dehydrocholesterol reductase of the cholesterol
CC biosynthetic pathway reducing the C7-C8 double bond of cholesta-5,7-
CC dien-3beta-ol (7-dehydrocholesterol/7-DHC) and cholesta-5,7,24-trien-
CC 3beta-ol, two intermediates in that pathway.
CC {ECO:0000250|UniProtKB:Q9UBM7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + NADP(+) = 7-dehydrocholesterol + H(+) + NADPH;
CC Xref=Rhea:RHEA:23984, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:17759, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.21;
CC Evidence={ECO:0000250|UniProtKB:Q9UBM7};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23986;
CC Evidence={ECO:0000250|UniProtKB:Q9UBM7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-dehydrodesmosterol + H(+) + NADPH = desmosterol + NADP(+);
CC Xref=Rhea:RHEA:46740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17737,
CC ChEBI:CHEBI:27910, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:O88455};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46741;
CC Evidence={ECO:0000250|UniProtKB:O88455};
CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC {ECO:0000250|UniProtKB:O88455}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9UBM7}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ERG4/ERG24 family. {ECO:0000305}.
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DR EMBL; BC044995; AAH44995.1; -; mRNA.
DR RefSeq; NP_001079586.1; NM_001086117.1.
DR RefSeq; XP_018114839.1; XM_018259350.1.
DR AlphaFoldDB; Q7ZXH1; -.
DR SMR; Q7ZXH1; -.
DR DNASU; 379273; -.
DR GeneID; 379273; -.
DR KEGG; xla:379273; -.
DR CTD; 379273; -.
DR Xenbase; XB-GENE-17334842; dhcr7.S.
DR OMA; KSIWPMP; -.
DR OrthoDB; 532774at2759; -.
DR UniPathway; UPA00063; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 379273; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047598; F:7-dehydrocholesterol reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR001171; ERG24_DHCR-like.
DR InterPro; IPR018083; Sterol_reductase_CS.
DR Pfam; PF01222; ERG4_ERG24; 1.
DR PROSITE; PS01017; STEROL_REDUCT_1; 1.
DR PROSITE; PS01018; STEROL_REDUCT_2; 1.
PE 2: Evidence at transcript level;
KW Cholesterol biosynthesis; Cholesterol metabolism; Endoplasmic reticulum;
KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..473
FT /note="7-dehydrocholesterol reductase"
FT /id="PRO_0000207506"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 356
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 360
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 393
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 398
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 405..406
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 445
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 449..453
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 460
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
SQ SEQUENCE 473 AA; 54823 MW; 8EB14E8186BDC463 CRC64;
MGERRRANAS RGDKKVANGE KQHVGQWGRA WEVDYFSLAS VIFLLAFAPL IVYYFVMSCD
QYQCALTAPV LDLYSGKARL SDIWDKTPAL TWTAVKIYLA WVSFQVFLYM FLPDILHKFV
PGYEGGVQEG ARTPAGLINK YQVNGLQAWT ITHLLWFANA YHFHWFSPTI VIDNWIPLLW
CANLLGYSVA TFALVKANFF PTNANDCKFT GNFFYDYMMG IEFNPRIGKW FDFKLFFNGR
PGIVAWTLIN LSYAAKQQEL YGQVTNSMIL VNVLQAIYVV DFFWNESWYL KTIDICHDHF
GWYLGWGDCV WLPYLYTLQG LYLVYNPVEL STTAAVAVLL LGLIGYYIFR MTNHQKDLFR
RTNGNCKIWG KKPKSIECFY VSADGKRHYS KLMISGFWGV ARHLNYTGDL MGSLAYCLAC
GFDHLLPYFY FIYMTILLVH RCIRDEHRCS SKYGKDWKLY TSAVPYRLLP GLF
