ID   RD10A_DANRE             Reviewed;         339 AA.
AC   A1L1W4;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Retinol dehydrogenase 10-A;
DE            EC=1.1.1.300;
GN   Name=rdh10a; ORFNames=zgc:158459;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC129239; AAI29240.1; -; mRNA.
DR   RefSeq; NP_001074052.1; NM_001080583.1.
DR   AlphaFoldDB; A1L1W4; -.
DR   SMR; A1L1W4; -.
DR   STRING; 7955.ENSDARP00000066702; -.
DR   PaxDb; A1L1W4; -.
DR   Ensembl; ENSDART00000191533; ENSDARP00000144743; ENSDARG00000113421.
DR   GeneID; 562840; -.
DR   KEGG; dre:562840; -.
DR   CTD; 562840; -.
DR   ZFIN; ZDB-GENE-070112-2242; rdh10a.
DR   eggNOG; KOG1201; Eukaryota.
DR   InParanoid; A1L1W4; -.
DR   OrthoDB; 1373099at2759; -.
DR   PhylomeDB; A1L1W4; -.
DR   Reactome; R-DRE-2453902; The canonical retinoid cycle in rods (twilight vision).
DR   Reactome; R-DRE-5365859; RA biosynthesis pathway.
DR   UniPathway; UPA00912; -.
DR   PRO; PR:A1L1W4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   Bgee; ENSDARG00000113421; Expressed in multicellular organism and 19 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: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:0002138; P:retinoic acid biosynthetic process; IMP:ZFIN.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Microsome; NADP; Oxidoreductase;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..339
FT                   /note="Retinol dehydrogenase 10-A"
FT                   /id="PRO_0000307686"
FT   TRANSMEM        3..23
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        208
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         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   339 AA;  38232 MW;  A8A4D0D1B4A587A1 CRC64;
     MNIFVEFFLV MLKVCWAIVM AGFKWLIRPK EKSVAGQVCV ITGAGGGLGR LFAKEFARRR
     ATLVLWDINS HSNEETAEMV RQIYREQDNP MSKEGAVGGV EEVPPFQPQV YTYVLDVGKR
     ESVYSTAEKV RREVGEVDLL INNAGVVSGH HLLECPDELI ERTMVVNCHA HFWTTKAFLP
     KMLEMNHGHI VTVASSLGLF STAGVEDYCA SKFGAIGFHE SLSHEIQASE KDGIKMTLVC
     PYLVDTGMFR GCRIRKEIEP FLPPLRPEFC VKQAMRAILT DQPMICTPRI VYMVNFMKSI
     LPFEAIVCMY RFLGADKCMY PFLAQRKEAM NNNEAKNGI