DHCR7_BOVIN
ID DHCR7_BOVIN Reviewed; 475 AA.
AC Q5E9J5; A6QR24;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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 -!- SUBUNIT: Interacts with DHCR24; this interaction regulates DHCR7
CC activity. {ECO:0000250|UniProtKB:Q9UBM7}.
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; BT020925; AAX08942.1; -; mRNA.
DR EMBL; BC150084; AAI50085.1; -; mRNA.
DR RefSeq; NP_001014927.1; NM_001014927.1.
DR RefSeq; XP_015316829.1; XM_015461343.1.
DR AlphaFoldDB; Q5E9J5; -.
DR SMR; Q5E9J5; -.
DR STRING; 9913.ENSBTAP00000021892; -.
DR PaxDb; Q5E9J5; -.
DR PRIDE; Q5E9J5; -.
DR Ensembl; ENSBTAT00000021892; ENSBTAP00000021892; ENSBTAG00000016465.
DR Ensembl; ENSBTAT00000078608; ENSBTAP00000065333; ENSBTAG00000016465.
DR GeneID; 514745; -.
DR KEGG; bta:514745; -.
DR CTD; 1717; -.
DR VEuPathDB; HostDB:ENSBTAG00000016465; -.
DR VGNC; VGNC:28034; DHCR7.
DR eggNOG; KOG1435; Eukaryota.
DR GeneTree; ENSGT00390000000417; -.
DR InParanoid; Q5E9J5; -.
DR OMA; TSGFWGW; -.
DR OrthoDB; 532774at2759; -.
DR UniPathway; UPA00063; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000016465; Expressed in diaphragm and 107 other tissues.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:Ensembl.
DR GO; GO:0047598; F:7-dehydrocholesterol reductase activity; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IBA:GO_Central.
DR GO; GO:0009918; F:sterol delta7 reductase activity; IBA:GO_Central.
DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
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 Phosphoprotein; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..475
FT /note="7-dehydrocholesterol reductase"
FT /id="PRO_0000207501"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 358
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 362
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 395
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 400
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 407..408
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 447
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 451..455
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 462
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBM7"
SQ SEQUENCE 475 AA; 54271 MW; 4712E8DBA76D0A91 CRC64;
MAAKSQPSAP KTKSTSGLTN GNAAAQGQWG RAWEVDWFSL ASVIFLLLFA PFIVYYFIMA
CDQYGCSLTV PVADLATGRA RLADIWARTP PVTAKAAQIY TAWVTLQVLL YMLLPDFCHK
FLPGYVGGVQ EGAVTPAGAV NKYEINGLQA WLLTHLLWFA NAHLLGWFSP TIIFDNWIPL
LWCANILGYT VSTFAMVKGY LFPTDARECK FTGNFFYNYM MGVEFNPRIG KWFDFKLFFN
GRPGIVAWTL INLSFAAKQQ ELYGHVTNSM VLVNILQAIY VLDFFWNETW YLKTIDICHD
HFGWYLGWGD CVWLPYLYTL QGLYLVYHPV QLPTYYALGV LLLGLLGYYI FRMTNHQKDL
FRRTDGRCLI WGRKPKAIEC SYTSADGQRH HSKLLVSGFW GVARHFNYTG DLMGSLAYCL
ACGGGHLLPY FYIIFMAILL THRCLRDEHR CANKYGRDWE HYTAAVPYRL LPGIF
