RDH10_MOUSE
ID RDH10_MOUSE Reviewed; 341 AA.
AC Q8VCH7; Q8CJ68;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Retinol dehydrogenase 10;
DE EC=1.1.1.300;
GN Name=Rdh10;
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], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=12407145;
RA Wu B.X., Chen Y., Chen Y., Fan J., Rohrer B., Crouch R.K., Ma J.-X.;
RT "Cloning and characterization of a novel all-trans retinol short-chain
RT dehydrogenase/reductase from the RPE.";
RL Invest. Ophthalmol. Vis. Sci. 43:3365-3372(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 TISSUE SPECIFICITY.
RX PubMed=15505029; DOI=10.1167/iovs.03-1302;
RA Wu B.X., Moiseyev G., Chen Y., Rohrer B., Crouch R.K., Ma J.-X.;
RT "Identification of RDH10, an all-trans retinol dehydrogenase, in retinal
RT Mueller cells.";
RL Invest. Ophthalmol. Vis. Sci. 45:3857-3862(2004).
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=17473173; DOI=10.1101/gad.1533407;
RA Sandell L.L., Sanderson B.W., Moiseyev G., Johnson T., Mushegian A.,
RA Young K., Rey J.-P., Ma J.-X., Staehling-Hampton K., Trainor P.A.;
RT "RDH10 is essential for synthesis of embryonic retinoic acid and is
RT required for limb, craniofacial, and organ development.";
RL Genes Dev. 21:1113-1124(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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 Converts all-trans-retinol to all-trans-retinal. Has no detectable
CC activity towards 11-cis-retinol, 9-cis-retinol and 13-cis-retinol (By
CC similarity). Required for normal embryonic development. {ECO:0000250,
CC ECO:0000269|PubMed:17473173}.
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;
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in retinal pigment epithelium (at protein
CC level). {ECO:0000269|PubMed:12407145, ECO:0000269|PubMed:15505029}.
CC -!- DEVELOPMENTAL STAGE: First detected in the neural groove at 8.0 dpc. At
CC 8.5 dpc, detected in lateral plate mesoderm, the dorsal region of the
CC somites, the floor plate of the neural tube and in head mesenchyme. At
CC 9.5 dpc, detected in dorsal paraxial mesoderm, lateral plate mesoderm
CC and in nephrogenic cord tissues. At 10.5 dpc, detected in lung buds,
CC developing mesonephros, mesodermal tissue surrounding dorsal root
CC ganglia and adjacent to the forlimb buds.
CC {ECO:0000269|PubMed:17473173}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF456767; AAN64749.1; -; mRNA.
DR EMBL; BC019796; AAH19796.2; -; mRNA.
DR CCDS; CCDS14830.1; -.
DR RefSeq; NP_598593.1; NM_133832.3.
DR AlphaFoldDB; Q8VCH7; -.
DR SMR; Q8VCH7; -.
DR STRING; 10090.ENSMUSP00000027053; -.
DR iPTMnet; Q8VCH7; -.
DR PhosphoSitePlus; Q8VCH7; -.
DR SwissPalm; Q8VCH7; -.
DR jPOST; Q8VCH7; -.
DR MaxQB; Q8VCH7; -.
DR PaxDb; Q8VCH7; -.
DR PeptideAtlas; Q8VCH7; -.
DR PRIDE; Q8VCH7; -.
DR ProteomicsDB; 253188; -.
DR Antibodypedia; 42541; 153 antibodies from 24 providers.
DR DNASU; 98711; -.
DR Ensembl; ENSMUST00000027053; ENSMUSP00000027053; ENSMUSG00000025921.
DR GeneID; 98711; -.
DR KEGG; mmu:98711; -.
DR UCSC; uc007ajm.1; mouse.
DR CTD; 157506; -.
DR MGI; MGI:1924238; Rdh10.
DR VEuPathDB; HostDB:ENSMUSG00000025921; -.
DR eggNOG; KOG1201; Eukaryota.
DR GeneTree; ENSGT00940000157063; -.
DR HOGENOM; CLU_010194_2_5_1; -.
DR InParanoid; Q8VCH7; -.
DR OMA; VCTPRII; -.
DR OrthoDB; 1373099at2759; -.
DR PhylomeDB; Q8VCH7; -.
DR TreeFam; TF312837; -.
DR BRENDA; 1.1.1.300; 3474.
DR BRENDA; 1.1.1.315; 3474.
DR Reactome; R-MMU-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-MMU-5365859; RA biosynthesis pathway.
DR UniPathway; UPA00912; -.
DR BioGRID-ORCS; 98711; 2 hits in 75 CRISPR screens.
DR PRO; PR:Q8VCH7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8VCH7; protein.
DR Bgee; ENSMUSG00000025921; Expressed in pigmented layer of retina and 332 other tissues.
DR Genevisible; Q8VCH7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IMP:MGI.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0060449; P:bud elongation involved in lung branching; IMP:MGI.
DR GO; GO:0043583; P:ear development; IMP:MGI.
DR GO; GO:0031076; P:embryonic camera-type eye development; IMP:MGI.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI.
DR GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:MGI.
DR GO; GO:0008406; P:gonad development; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0001656; P:metanephros development; IMP:MGI.
DR GO; GO:0014032; P:neural crest cell development; IMP:MGI.
DR GO; GO:0043584; P:nose development; IMP:MGI.
DR GO; GO:1900054; P:positive regulation of retinoic acid biosynthetic process; ISO:MGI.
DR GO; GO:0060431; P:primary lung bud formation; IMP:MGI.
DR GO; GO:0042574; P:retinal metabolic process; ISO:MGI.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; IMP:MGI.
DR GO; GO:0042572; P:retinol metabolic process; ISO:MGI.
DR GO; GO:0007601; P:visual perception; ISO:MGI.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032970; RDH10.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR24322:SF731; PTHR24322:SF731; 1.
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; Lipid metabolism; Membrane; Microsome; NADP;
KW Oxidoreductase; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..341
FT /note="Retinol dehydrogenase 10"
FT /id="PRO_0000307683"
FT TRANSMEM 3..23
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT ACT_SITE 210
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 40..64
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 341 AA; 38075 MW; D0FEDDBE9915EA89 CRC64;
MNIVVEFFVV TFKVLWAFVL AAARWLVRPK EKSVAGQVCL ITGAGSGLGR LFALEFARRR
ALLVLWDINT QSNEETAGMV RHIYRDLEAA DAAALQAGKG EEEILPPCNL QVFTYTCDVG
KRENVYLTAE RVRKEVGEVS VLVNNAGVVS GHHLLECPDE LIERTMMVNC HAHFWTTKAF
LPTMLEINHG HIVTVASSLG LFSTAGVEDY CASKFGVVGF HESLSHELKA AEKDGIKTTL
VCPYLVDTGM FRGCRIRKEI EPFLPPLKPD YCVKQAMRAI LTDQPMVCTP RLMYIVTFMK
SILPFEAVVC MYRFLGADKC MYPFIAQRKQ ATNNNEAKNG I
