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RDH7_MOUSE
ID   RDH7_MOUSE              Reviewed;         316 AA.
AC   O88451;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Retinol dehydrogenase 7;
DE            EC=1.1.1.105;
DE   AltName: Full=Cis-retinol/3alpha-hydroxysterol short-chain dehydrogenase isozyme 2;
DE   AltName: Full=Cis-retinol/androgen dehydrogenase type 2;
DE            Short=CRAD-2;
GN   Name=Rdh7; Synonyms=Crad2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=9651397; DOI=10.1074/jbc.273.28.17910;
RA   Su J., Chai X., Kahn B., Napoli J.L.;
RT   "cDNA cloning, tissue distribution, and substrate characteristics of a cis-
RT   retinol/3alpha-hydroxysterol short-chain dehydrogenase isozyme.";
RL   J. Biol. Chem. 273:17910-17916(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Ola; TISSUE=Liver;
RX   PubMed=10876094; DOI=10.1016/s0378-1119(00)00194-3;
RA   Tomita K., Sato M., Kajiwara K., Tanaka M., Tamiya G., Makino S.,
RA   Tomizawa M., Mizutani A., Kuwano Y., Shiina T., Ishii H., Kimura M.;
RT   "Gene structure and promoter for Crad2 encoding mouse cis-retinol/3-
RT   hydroxysterol short-chain dehydrogenase isozyme.";
RL   Gene 251:175-186(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Acts on androgens and retinols, i.e. has steroid 3-alpha- and
CC       17-beta-dehydrogenase and cis/trans-retinol catalytic activities.
CC       {ECO:0000269|PubMed:9651397}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinol--[retinol-binding protein] + NAD(+) = all-
CC         trans-retinal--[retinol-binding protein] + H(+) + NADH;
CC         Xref=Rhea:RHEA:48488, Rhea:RHEA-COMP:14428, Rhea:RHEA-COMP:14430,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83228;
CC         EC=1.1.1.105;
CC   -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC   -!- SUBCELLULAR LOCATION: Microsome {ECO:0000250}. Endoplasmic reticulum
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in liver. Also expressed in lung,
CC       eye, kidney, and brain. {ECO:0000269|PubMed:9651397}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AF056194; AAC40159.1; -; mRNA.
DR   EMBL; AB015165; BAB03717.1; -; mRNA.
DR   EMBL; AB032058; BAB03718.1; -; mRNA.
DR   EMBL; AB032057; BAB03719.1; -; Genomic_DNA.
DR   EMBL; BC024603; AAH24603.1; -; mRNA.
DR   EMBL; BC092255; AAH92255.1; -; mRNA.
DR   EMBL; BC093514; AAH93514.1; -; mRNA.
DR   CCDS; CCDS24255.1; -.
DR   RefSeq; NP_001144221.1; NM_001150749.1.
DR   RefSeq; NP_059501.1; NM_017473.4.
DR   AlphaFoldDB; O88451; -.
DR   SMR; O88451; -.
DR   IntAct; O88451; 1.
DR   STRING; 10090.ENSMUSP00000039252; -.
DR   iPTMnet; O88451; -.
DR   PhosphoSitePlus; O88451; -.
DR   SwissPalm; O88451; -.
DR   jPOST; O88451; -.
DR   MaxQB; O88451; -.
DR   PaxDb; O88451; -.
DR   PeptideAtlas; O88451; -.
DR   PRIDE; O88451; -.
DR   ProteomicsDB; 253192; -.
DR   DNASU; 54150; -.
DR   Ensembl; ENSMUST00000047199; ENSMUSP00000039252; ENSMUSG00000040134.
DR   GeneID; 54150; -.
DR   KEGG; mmu:54150; -.
DR   UCSC; uc007hkv.2; mouse.
DR   CTD; 54150; -.
DR   MGI; MGI:1860517; Rdh7.
DR   VEuPathDB; HostDB:ENSMUSG00000040134; -.
DR   eggNOG; KOG1610; Eukaryota.
DR   GeneTree; ENSGT00940000154118; -.
DR   HOGENOM; CLU_010194_2_0_1; -.
DR   InParanoid; O88451; -.
DR   OMA; FRWYQER; -.
DR   OrthoDB; 942985at2759; -.
DR   PhylomeDB; O88451; -.
DR   TreeFam; TF325617; -.
DR   BRENDA; 1.1.1.315; 3474.
DR   UniPathway; UPA00912; -.
DR   BioGRID-ORCS; 54150; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; Rdh7; mouse.
DR   PRO; PR:O88451; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; O88451; protein.
DR   Bgee; ENSMUSG00000040134; Expressed in left lobe of liver and 40 other tissues.
DR   Genevisible; O88451; MM.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0047044; F:androstan-3-alpha,17-beta-diol dehydrogenase activity; ISO:MGI.
DR   GO; GO:0047023; F:androsterone dehydrogenase activity; ISO:MGI.
DR   GO; GO:0003824; F:catalytic activity; ISS:MGI.
DR   GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016229; F:steroid dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0042572; P:retinol metabolic process; IBA:GO_Central.
DR   GO; GO:0008202; P:steroid metabolic process; ISO:MGI.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Microsome; NAD; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..316
FT                   /note="Retinol dehydrogenase 7"
FT                   /id="PRO_0000054761"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         33..57
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   316 AA;  35660 MW;  0BFB9A1C2DDE3C17 CRC64;
     MWLYLVALVG LWTLLRFFRE RQVVSHLQDK YVFITGCDSG FGNLLARQLD RRGMRVLAAC
     LTEKGAEQLR NKTSDRLETV ILDVTKTESI VAATQWVKER VGNRGLWGLV NNAGICVFAI
     NEWLKKEDFA NILDVNLLGM IEVTLSMLPL VRKARGRVVN ISSSMGRVSL CGGGYCISKY
     GVEAFSDSLR REISYFGVKV AIIEPGGFRT NVSNYERLSH SIEKLWDQTS SEVKEVYDKN
     FLDSYIKAIQ SLTDTCSDDL SVVTDCMEHA LTACHPRTRY SAGWDAKLFY LPLSYMPTFL
     VDAMLYWSSV KPAQAL
 
 
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