ERG24_BOVIN
ID ERG24_BOVIN Reviewed; 418 AA.
AC Q8WMV1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Delta(14)-sterol reductase TM7SF2;
DE Short=Delta-14-SR;
DE EC=1.3.1.70 {ECO:0000269|PubMed:11784322};
DE AltName: Full=3-beta-hydroxysterol Delta (14)-reductase {ECO:0000303|PubMed:16784888};
DE AltName: Full=C-14 sterol reductase;
DE AltName: Full=Sterol C14-reductase;
DE AltName: Full=Transmembrane 7 superfamily member 2;
GN Name=TM7SF2;
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 [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11784322; DOI=10.1046/j.0014-2956.2001.02646.x;
RA Roberti R., Bennati A.M., Galli G., Caruso D., Maras B., Aisa C.,
RA Beccari T., Della Fazia M.A., Servillo G.;
RT "Cloning and expression of sterol Delta14-reductase from bovine liver.";
RL Eur. J. Biochem. 269:283-290(2002).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16784888; DOI=10.1016/j.bbalip.2006.05.004;
RA Bennati A.M., Castelli M., Della Fazia M.A., Beccari T., Caruso D.,
RA Servillo G., Roberti R.;
RT "Sterol dependent regulation of human TM7SF2 gene expression: role of the
RT encoded 3beta-hydroxysterol Delta14-reductase in human cholesterol
RT biosynthesis.";
RL Biochim. Biophys. Acta 1761:677-685(2006).
CC -!- FUNCTION: Catalyzes the reduction of the C14-unsaturated bond of
CC lanosterol, as part of the metabolic pathway leading to cholesterol
CC biosynthesis. {ECO:0000269|PubMed:11784322,
CC ECO:0000269|PubMed:16784888}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) =
CC 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + H(+) + NADPH;
CC Xref=Rhea:RHEA:18561, ChEBI:CHEBI:15378, ChEBI:CHEBI:17813,
CC ChEBI:CHEBI:18364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.70;
CC Evidence={ECO:0000269|PubMed:11784322};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-cholest-8,14-dien-3beta-ol + H(+) + NADPH = 5alpha-
CC cholest-8-en-3beta-ol + NADP(+); Xref=Rhea:RHEA:46456,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16608, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:86131;
CC Evidence={ECO:0000269|PubMed:11784322, ECO:0000269|PubMed:16784888};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,4-dimethyl-8,14-cholestadien-3beta-ol + H(+) + NADPH = 4,4-
CC dimethyl-5alpha-cholest-8-en-3beta-ol + NADP(+);
CC Xref=Rhea:RHEA:46812, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78904, ChEBI:CHEBI:87044;
CC Evidence={ECO:0000269|PubMed:11784322};
CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:Q71KT5}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11784322}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and brain.
CC {ECO:0000269|PubMed:11784322}.
CC -!- SIMILARITY: Belongs to the ERG4/ERG24 family. {ECO:0000305}.
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DR EMBL; AY039681; AAK91505.1; -; mRNA.
DR AlphaFoldDB; Q8WMV1; -.
DR SMR; Q8WMV1; -.
DR STRING; 9913.ENSBTAP00000006683; -.
DR SwissLipids; SLP:000001238; -.
DR PaxDb; Q8WMV1; -.
DR eggNOG; KOG1435; Eukaryota.
DR InParanoid; Q8WMV1; -.
DR UniPathway; UPA00063; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005637; C:nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0050613; F:delta14-sterol reductase activity; IDA:UniProtKB.
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:0006695; P:cholesterol biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cholesterol biosynthesis; Cholesterol metabolism;
KW Direct protein sequencing; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Microsome; NADP; Oxidoreductase;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..418
FT /note="Delta(14)-sterol reductase TM7SF2"
FT /id="PRO_0000244771"
FT TRANSMEM 13..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 311
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 315
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 338
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 343
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 350..351
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 390
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 394..398
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 405
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
SQ SEQUENCE 418 AA; 46751 MW; 30DE297CFB09568C CRC64;
MAPPQGSRAP LEFGGPLGAA ALMLLLPVTM FHLLLVARSG PARLLGPPPY LPGPEELWSP
WALLLCLTWL GLQAALYLLP ARKVAEGQEL KDKSRLRYPT NGFQALVLTA LLVGLGVSAG
LPLSALPEML LPLAFAATLT AFIFSLLLYL KALLAPASAL APGGNSGNLI YDFFLGRELN
PRICSFDFKY FCELRPGLIG WVLINLALLI QEAELRGSPS LAMWLVNGFQ LLYVGDALWY
EEAVLTTMDI IHDGFGFMLA FGDLAWVPFT YSLQAQFLLY HPQPLGWPLA SFICLINAVG
YYIFRGANSQ KNTFRKNPSD PRVADLETIS TATGRRLLVS GWWGMVRHPN YLGDLIMALA
WSLPCGVFHL LPYFYFLYFT ALLVHREDRD ERQCRQKYGL AWHEYCRRVP YRIVPYVY
