ID   RDH10_HUMAN             Reviewed;         341 AA.
AC   Q8IZV5;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 169.
DE   RecName: Full=Retinol dehydrogenase 10;
DE            EC=1.1.1.300;
DE   AltName: Full=Short chain dehydrogenase/reductase family 16C member 4;
GN   Name=RDH10; Synonyms=SDR16C4; ORFNames=UNQ9375/PRO34191;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Retina;
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].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
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   TISSUE SPECIFICITY.
RX   PubMed=14596915; DOI=10.1016/s0014-5793(03)01089-5;
RA   Picozzi P., Marozzi A., Fornasari D., Benfante R., Barisani D.,
RA   Meneveri R., Ginelli E.;
RT   "Genomic organization and transcription of the human retinol dehydrogenase
RT   10 (RDH10) gene.";
RL   FEBS Lett. 554:59-66(2003).
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.
CC       {ECO:0000269|PubMed:12407145}.
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:12407145};
CC   -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC   -!- INTERACTION:
CC       Q8IZV5; Q96CM8: ACSF2; NbExp=3; IntAct=EBI-11913715, EBI-2876502;
CC       Q8IZV5; Q9BW61: DDA1; NbExp=3; IntAct=EBI-11913715, EBI-2510241;
CC       Q8IZV5; Q05329: GAD2; NbExp=3; IntAct=EBI-11913715, EBI-9304251;
CC       Q8IZV5; Q96LZ7: RMDN2; NbExp=3; IntAct=EBI-11913715, EBI-2806908;
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 retina, kidney, liver, small intestine,
CC       placenta, lung, heart and skeletal muscle.
CC       {ECO:0000269|PubMed:12407145, ECO:0000269|PubMed:14596915}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AF456765; AAN64747.1; -; mRNA.
DR   EMBL; AY358270; AAQ88637.1; -; mRNA.
DR   EMBL; BC067131; AAH67131.1; -; mRNA.
DR   CCDS; CCDS6213.1; -.
DR   RefSeq; NP_742034.1; NM_172037.4.
DR   AlphaFoldDB; Q8IZV5; -.
DR   SMR; Q8IZV5; -.
DR   BioGRID; 127600; 48.
DR   IntAct; Q8IZV5; 6.
DR   MINT; Q8IZV5; -.
DR   STRING; 9606.ENSP00000240285; -.
DR   SwissLipids; SLP:000001866; -.
DR   GlyGen; Q8IZV5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8IZV5; -.
DR   PhosphoSitePlus; Q8IZV5; -.
DR   SwissPalm; Q8IZV5; -.
DR   BioMuta; RDH10; -.
DR   DMDM; 74750799; -.
DR   EPD; Q8IZV5; -.
DR   jPOST; Q8IZV5; -.
DR   MassIVE; Q8IZV5; -.
DR   MaxQB; Q8IZV5; -.
DR   PaxDb; 9606-ENSP00000240285; -.
DR   PeptideAtlas; Q8IZV5; -.
DR   ProteomicsDB; 71436; -.
DR   Pumba; Q8IZV5; -.
DR   Antibodypedia; 42541; 166 antibodies from 24 providers.
DR   DNASU; 157506; -.
DR   Ensembl; ENST00000240285.10; ENSP00000240285.5; ENSG00000121039.10.
DR   GeneID; 157506; -.
DR   KEGG; hsa:157506; -.
DR   MANE-Select; ENST00000240285.10; ENSP00000240285.5; NM_172037.5; NP_742034.1.
DR   UCSC; uc003xzi.4; human.
DR   AGR; HGNC:19975; -.
DR   CTD; 157506; -.
DR   DisGeNET; 157506; -.
DR   GeneCards; RDH10; -.
DR   HGNC; HGNC:19975; RDH10.
DR   HPA; ENSG00000121039; Low tissue specificity.
DR   MIM; 607599; gene.
DR   neXtProt; NX_Q8IZV5; -.
DR   OpenTargets; ENSG00000121039; -.
DR   PharmGKB; PA134989620; -.
DR   VEuPathDB; HostDB:ENSG00000121039; -.
DR   eggNOG; KOG1201; Eukaryota.
DR   GeneTree; ENSGT00940000157063; -.
DR   HOGENOM; CLU_010194_2_5_1; -.
DR   InParanoid; Q8IZV5; -.
DR   OMA; TVCPTYI; -.
DR   OrthoDB; 6845at2759; -.
DR   PhylomeDB; Q8IZV5; -.
DR   TreeFam; TF312837; -.
DR   BioCyc; MetaCyc:ENSG00000121039-MONOMER; -.
DR   BRENDA; 1.1.1.105; 2681.
DR   BRENDA; 1.1.1.300; 2681.
DR   BRENDA; 1.1.1.315; 2681.
DR   PathwayCommons; Q8IZV5; -.
DR   Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR   Reactome; R-HSA-5365859; RA biosynthesis pathway.
DR   SignaLink; Q8IZV5; -.
DR   SIGNOR; Q8IZV5; -.
DR   UniPathway; UPA00912; -.
DR   BioGRID-ORCS; 157506; 15 hits in 1165 CRISPR screens.
DR   ChiTaRS; RDH10; human.
DR   GenomeRNAi; 157506; -.
DR   Pharos; Q8IZV5; Tbio.
DR   PRO; PR:Q8IZV5; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q8IZV5; Protein.
DR   Bgee; ENSG00000121039; Expressed in nasal cavity epithelium and 174 other cell types or tissues.
DR   ExpressionAtlas; Q8IZV5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0052650; F:NADP-retinol dehydrogenase activity; TAS:Reactome.
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:1900054; P:positive regulation of retinoic acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0060431; P:primary lung bud formation; IEA:Ensembl.
DR   GO; GO:0042574; P:retinal metabolic process; IDA:UniProtKB.
DR   GO; GO:0002138; P:retinoic acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
DR   GO; GO:0042572; P:retinol metabolic process; IDA:UniProtKB.
DR   GO; GO:0007601; P:visual perception; IDA:MGI.
DR   CDD; cd05339; 17beta-HSDXI-like_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR24322; PKSB; 1.
DR   PANTHER; PTHR24322:SF736; RETINOL DEHYDROGENASE 10; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
DR   Genevisible; Q8IZV5; HS.
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_0000307682"
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
//