位置:首页 > 蛋白库 > DHC24_RAT
DHC24_RAT
ID   DHC24_RAT               Reviewed;         516 AA.
AC   Q5BQE6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Delta(24)-sterol reductase;
DE            EC=1.3.1.72 {ECO:0000250|UniProtKB:Q15392};
DE   AltName: Full=24-dehydrocholesterol reductase;
DE   AltName: Full=3-beta-hydroxysterol Delta-24-reductase;
DE   Flags: Precursor;
GN   Name=Dhcr24;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=IGS BR;
RA   Samara A., Maggi R.;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reduction of the delta-24 double bond of sterol
CC       intermediates during cholesterol biosynthesis. In addition to its
CC       cholesterol-synthesizing activity, can protect cells from oxidative
CC       stress by reducing caspase 3 activity during apoptosis induced by
CC       oxidative stress. Also protects against amyloid-beta peptide-induced
CC       apoptosis. {ECO:0000250|UniProtKB:Q15392}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cholesterol + NADP(+) = desmosterol + H(+) + NADPH;
CC         Xref=Rhea:RHEA:36391, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113,
CC         ChEBI:CHEBI:17737, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.72;
CC         Evidence={ECO:0000250|UniProtKB:Q15392};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:36393;
CC         Evidence={ECO:0000250|UniProtKB:Q15392};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + lanosterol + NADPH = 24,25-dihydrolanosterol + NADP(+);
CC         Xref=Rhea:RHEA:33919, ChEBI:CHEBI:15378, ChEBI:CHEBI:16521,
CC         ChEBI:CHEBI:28113, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:Q15392};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33920;
CC         Evidence={ECO:0000250|UniProtKB:Q15392};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5alpha-cholest-8-en-3beta-ol + NADP(+) = H(+) + NADPH +
CC         zymosterol; Xref=Rhea:RHEA:36399, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16608, ChEBI:CHEBI:18252, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.3.1.72;
CC         Evidence={ECO:0000250|UniProtKB:Q8VCH6};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:36401;
CC         Evidence={ECO:0000250|UniProtKB:Q8VCH6};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC       {ECO:0000250|UniProtKB:Q15392}.
CC   -!- SUBUNIT: Interacts with DHCR7; this interaction regulates DHCR7
CC       activity. {ECO:0000250|UniProtKB:Q15392}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q15392}; Single-pass membrane protein
CC       {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q15392};
CC       Single-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC       4 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY921220; AAX29968.2; -; mRNA.
DR   AlphaFoldDB; Q5BQE6; -.
DR   SMR; Q5BQE6; -.
DR   STRING; 10116.ENSRNOP00000009402; -.
DR   jPOST; Q5BQE6; -.
DR   PaxDb; Q5BQE6; -.
DR   PRIDE; Q5BQE6; -.
DR   Ensembl; ENSRNOT00000009402; ENSRNOP00000009402; ENSRNOG00000006787.
DR   UCSC; RGD:1306529; rat.
DR   RGD; 1306529; Dhcr24.
DR   eggNOG; KOG1262; Eukaryota.
DR   GeneTree; ENSGT00390000008338; -.
DR   HOGENOM; CLU_025883_4_0_1; -.
DR   InParanoid; Q5BQE6; -.
DR   OMA; YIPSRHY; -.
DR   PhylomeDB; Q5BQE6; -.
DR   TreeFam; TF313170; -.
DR   BRENDA; 1.3.1.72; 5301.
DR   Reactome; R-RNO-191273; Cholesterol biosynthesis.
DR   Reactome; R-RNO-6807047; Cholesterol biosynthesis via desmosterol.
DR   Reactome; R-RNO-6807062; Cholesterol biosynthesis via lathosterol.
DR   UniPathway; UPA00063; -.
DR   PRO; PR:Q5BQE6; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000006787; Expressed in liver and 19 other tissues.
DR   Genevisible; Q5BQE6; RN.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005856; C:cytoskeleton; IDA:RGD.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0000246; F:delta24(24-1) sterol reductase activity; ISO:RGD.
DR   GO; GO:0050614; F:delta24-sterol reductase activity; ISO:RGD.
DR   GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; NAS:RGD.
DR   GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; ISO:RGD.
DR   GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB.
DR   GO; GO:0042987; P:amyloid precursor protein catabolic process; ISO:RGD.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0033489; P:cholesterol biosynthetic process via desmosterol; ISO:RGD.
DR   GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD.
DR   GO; GO:0030539; P:male genitalia development; ISO:RGD.
DR   GO; GO:0061024; P:membrane organization; ISO:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR   GO; GO:0031639; P:plasminogen activation; ISO:RGD.
DR   GO; GO:0008104; P:protein localization; ISO:RGD.
DR   GO; GO:0007265; P:Ras protein signal transduction; IMP:RGD.
DR   GO; GO:0009725; P:response to hormone; IEP:RGD.
DR   GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR   GO; GO:0043588; P:skin development; ISS:UniProtKB.
DR   GO; GO:0008202; P:steroid metabolic process; IMP:RGD.
DR   GO; GO:0016125; P:sterol metabolic process; ISO:RGD.
DR   GO; GO:0009888; P:tissue development; ISS:UniProtKB.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR040165; Diminuto-like.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR10801; PTHR10801; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   2: Evidence at transcript level;
KW   Cholesterol biosynthesis; Cholesterol metabolism; Endoplasmic reticulum;
KW   FAD; Flavoprotein; Golgi apparatus; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; NADP; Oxidoreductase; Reference proteome; Signal;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..516
FT                   /note="Delta(24)-sterol reductase"
FT                   /id="PRO_0000320301"
FT   TOPO_DOM        23..31
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q15392"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..516
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q15392"
FT   DOMAIN          58..234
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   BINDING         163..175
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   SITE            122..123
FT                   /note="Cleavage; by caspase"
FT                   /evidence="ECO:0000255"
FT   SITE            383..384
FT                   /note="Cleavage; by caspase"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   516 AA;  60047 MW;  48CC4401E730569E CRC64;
     MEPAVSLAVC ALLFLLWVRV KGLEFVLIHQ RWVFVCLFLL PLSLIFDIYY YVRAWVVFKL
     SSAPRLHEQR VQDIQKQVRE WKEQGSKTFM CTGRPGWLTV SLRVGKYKKT HKNIMINLMD
     ILEVDTKKQI VRVEPLVSMG QVTALLNSIG WTLPVLPELD DLTVGGLIMG TGIESSSHKY
     GLFQHICTAY ELILADGSFV RCTPSENSDL FYAVPWSCGT LGFLVAAEIR IIPAKKYVKL
     RFEPVRGLEA ICEKFTHESQ RLENHFVEGL LYSLDEAVIM TGVMTDDVEP SKLNSIGSYY
     KPWFFKHVEN YLKTNREGLE YIPLRHYYHR HTRSIFWELQ DIIPFGNNPI FRYLFGWMVP
     PKISLLKLTQ GETLRKLYEQ HHVVQDMLVP MKCLSQALHT FQNDIHVYPI WLCPFILPSQ
     PGLVHPKGDE AELYVDIGAY GEPRVKHFEA RSCMRQLEKF VRSVHGFQML YADCYMNREE
     FWEMFDGSLY HKLRKQLGCQ DAFPEVYDKI CKAARH
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024