ID   RDH10_BOVIN             Reviewed;         341 AA.
AC   Q8HZT6;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Retinol dehydrogenase 10;
DE            EC=1.1.1.300;
GN   Name=RDH10;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Retinal pigment epithelium;
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].
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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).
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). {ECO:0000250}.
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). Detected in retina, retinal pigment epithelium, and at lower
CC       levels in cornea, liver, kidney, pancreas, lung, brain and skeletal
CC       muscle. {ECO:0000269|PubMed:12407145, ECO:0000269|PubMed:15505029}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AF456766; AAN64748.1; -; mRNA.
DR   EMBL; BC134557; AAI34558.1; -; mRNA.
DR   RefSeq; NP_777159.1; NM_174734.2.
DR   AlphaFoldDB; Q8HZT6; -.
DR   SMR; Q8HZT6; -.
DR   STRING; 9913.ENSBTAP00000026830; -.
DR   PaxDb; Q8HZT6; -.
DR   PRIDE; Q8HZT6; -.
DR   Ensembl; ENSBTAT00000026830; ENSBTAP00000026830; ENSBTAG00000020143.
DR   GeneID; 282852; -.
DR   KEGG; bta:282852; -.
DR   CTD; 157506; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020143; -.
DR   VGNC; VGNC:33841; RDH10.
DR   eggNOG; KOG1201; Eukaryota.
DR   GeneTree; ENSGT00940000157063; -.
DR   HOGENOM; CLU_010194_2_5_1; -.
DR   InParanoid; Q8HZT6; -.
DR   OMA; VCTPRII; -.
DR   OrthoDB; 1373099at2759; -.
DR   TreeFam; TF312837; -.
DR   BRENDA; 1.1.1.315; 908.
DR   Reactome; R-BTA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR   Reactome; R-BTA-5365859; RA biosynthesis pathway.
DR   UniPathway; UPA00912; -.
DR   Proteomes; UP000009136; Chromosome 14.
DR   Bgee; ENSBTAG00000020143; Expressed in uterine horn and 105 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR   GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IEA:Ensembl.
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:0060449; P:bud elongation involved in lung branching; IEA:Ensembl.
DR   GO; GO:0043583; P:ear development; IEA:Ensembl.
DR   GO; GO:0031076; P:embryonic camera-type eye development; IEA:Ensembl.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
DR   GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR   GO; GO:0008406; P:gonad development; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0001656; P:metanephros development; IEA:Ensembl.
DR   GO; GO:0014032; P:neural crest cell development; IEA:Ensembl.
DR   GO; GO:0043584; P:nose development; IEA:Ensembl.
DR   GO; GO:0060431; P:primary lung bud formation; IEA:Ensembl.
DR   GO; GO:0042574; P:retinal metabolic process; IEA:Ensembl.
DR   GO; GO:0002138; P:retinoic acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0007601; P:visual perception; IEA:Ensembl.
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_0000307681"
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;  38087 MW;  D10ABE05E7D11FC6 CRC64;
     MNIVVEFFVV TFKVLWAFVL AAARWLVRPK EKSVAGQVCL ITGAGSGLGR LFALEFARRR
     ALLVLWDINT QSNEETAGMV RHIYRDLEAA DAAALQAGNG EEEILPHCNL QVFTYTCDVG
     KRENVYLTAE RVRKEVGEVS VLVNNAGVVS GHHLLECPDE LIERTMMVNC HAHFWTTKAF
     LPTMLEINHG HIVTVASSLG LFSTAGVEDY CASKFGVVGF HESLSHELKA AEKDGIKTTL
     VCPYLVDTGM FRGCRIRKEI EPFLPPLKPD YCVKQAMKAI LTDQPMICTP RLMYIVTFMK
     SILPFEAVVC MYRFLGADKC MYPFIAQRKQ ATNNNEAKNG I