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RDH14_MOUSE
ID   RDH14_MOUSE             Reviewed;         334 AA.
AC   Q9ERI6;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Retinol dehydrogenase 14;
DE            EC=1.1.1.300 {ECO:0000269|PubMed:12226107};
DE   AltName: Full=Alcohol dehydrogenase PAN2 {ECO:0000303|Ref.1};
GN   Name=Rdh14; Synonyms=Pan2 {ECO:0000303|Ref.1};
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].
RC   STRAIN=C57BL/6J; TISSUE=Fetus;
RA   Li K.X., Brereton P.S., Obeyesekere V.R., Krozowski Z.S.;
RT   "Cloning of the mouse Pan2 cDNA: a novel member of the short chain alcohol
RT   dehydrogenase superfamily.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
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   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=12226107; DOI=10.1074/jbc.m208882200;
RA   Haeseleer F., Jang G.-F., Imanishi Y., Driessen C.A.G.G., Matsumura M.,
RA   Nelson P.S., Palczewski K.;
RT   "Dual-substrate specificity short chain retinol dehydrogenases from the
RT   vertebrate retina.";
RL   J. Biol. Chem. 277:45537-45546(2002).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC   Testis;
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: Retinol dehydrogenase with a clear preference for NADP.
CC       Displays high activity towards 9-cis, 11-cis and all-trans-retinol.
CC       Shows a very weak activity towards 13-cis-retinol. Has no activity
CC       towards steroids. {ECO:0000269|PubMed:12226107}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) +
CC         NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC         ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.300; Evidence={ECO:0000269|PubMed:12226107};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=11-cis-retinol + NADP(+) = 11-cis-retinal + H(+) + NADPH;
CC         Xref=Rhea:RHEA:54912, ChEBI:CHEBI:15378, ChEBI:CHEBI:16066,
CC         ChEBI:CHEBI:16302, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000269|PubMed:12226107};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=9-cis-retinol + NADP(+) = 9-cis-retinal + H(+) + NADPH;
CC         Xref=Rhea:RHEA:54916, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273;
CC         Evidence={ECO:0000269|PubMed:12226107};
CC   -!- MISCELLANEOUS: Shows clear specificity for the pro-S hydrogen on C4 of
CC       NADPH and the pro-R hydrogen on C15 of retinols.
CC       {ECO:0000269|PubMed:12226107}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AF303831; AAG30904.1; -; mRNA.
DR   EMBL; BC020094; AAH20094.1; -; mRNA.
DR   CCDS; CCDS25811.1; -.
DR   RefSeq; NP_076186.1; NM_023697.2.
DR   AlphaFoldDB; Q9ERI6; -.
DR   SMR; Q9ERI6; -.
DR   BioGRID; 222748; 1.
DR   STRING; 10090.ENSMUSP00000020947; -.
DR   SwissLipids; SLP:000001820; -.
DR   iPTMnet; Q9ERI6; -.
DR   PhosphoSitePlus; Q9ERI6; -.
DR   SwissPalm; Q9ERI6; -.
DR   EPD; Q9ERI6; -.
DR   jPOST; Q9ERI6; -.
DR   MaxQB; Q9ERI6; -.
DR   PaxDb; Q9ERI6; -.
DR   PeptideAtlas; Q9ERI6; -.
DR   PRIDE; Q9ERI6; -.
DR   ProteomicsDB; 255140; -.
DR   Antibodypedia; 47311; 111 antibodies from 17 providers.
DR   DNASU; 105014; -.
DR   Ensembl; ENSMUST00000020947; ENSMUSP00000020947; ENSMUSG00000020621.
DR   GeneID; 105014; -.
DR   KEGG; mmu:105014; -.
DR   UCSC; uc007nar.2; mouse.
DR   CTD; 57665; -.
DR   MGI; MGI:1920402; Rdh14.
DR   VEuPathDB; HostDB:ENSMUSG00000020621; -.
DR   eggNOG; KOG1208; Eukaryota.
DR   GeneTree; ENSGT00940000160181; -.
DR   HOGENOM; CLU_010194_44_5_1; -.
DR   InParanoid; Q9ERI6; -.
DR   OMA; GVQGKCF; -.
DR   OrthoDB; 921996at2759; -.
DR   PhylomeDB; Q9ERI6; -.
DR   TreeFam; TF105429; -.
DR   Reactome; R-MMU-5365859; RA biosynthesis pathway.
DR   BioGRID-ORCS; 105014; 4 hits in 76 CRISPR screens.
DR   PRO; PR:Q9ERI6; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q9ERI6; protein.
DR   Bgee; ENSMUSG00000020621; Expressed in interventricular septum and 235 other tissues.
DR   Genevisible; Q9ERI6; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0102354; F:11-cis-retinol dehydrogenase activity; IEA:RHEA.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:MGI.
DR   GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0042572; P:retinol metabolic process; IDA:UniProtKB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Lipid metabolism; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..334
FT                   /note="Retinol dehydrogenase 14"
FT                   /id="PRO_0000054771"
FT   ACT_SITE        215
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WNV7"
FT   BINDING         51..57
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   334 AA;  36366 MW;  A05653655E70802D CRC64;
     MAVASVAAAL LAALGGALWL AARRFSGPRN QRQQGGGDPG LMHGKTVLIT GANSGLGRAT
     AAELLRLGAR VIMGCRDRAR AEEAAGQLRQ ELCQAGGAGP DGTDGQLVVK ELDLASLRSV
     RAFCQELLQE EPRLDVLINN AGVFHCPYTK TEDGFEMQFG VNHLGHFLLT NLLLGLLKSS
     APSRIVVVSS KLYKYGEINF EDLNSEQSYN KSFCYSRSKL ANILFTRELA RRLEGTNVTV
     NVLHPGIVRT NLGRHIHIPL LARPLFNLVS WAFFKTPLEG AQTSIYLACS PDVEGVSGRY
     FGDCKEEELL PKAMDESVAR KLWDISEVMV GILK
 
 
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