ID   RD10B_XENLA             Reviewed;         341 AA.
AC   Q6NRV4;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Retinol dehydrogenase 10-B;
DE            EC=1.1.1.300;
GN   Name=rdh10-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) 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; BC070608; AAH70608.1; -; mRNA.
DR   RefSeq; NP_001084938.1; NM_001091469.1.
DR   AlphaFoldDB; Q6NRV4; -.
DR   SMR; Q6NRV4; -.
DR   DNASU; 431995; -.
DR   GeneID; 431995; -.
DR   KEGG; xla:431995; -.
DR   CTD; 431995; -.
DR   Xenbase; XB-GENE-6251537; rdh10.S.
DR   OrthoDB; 1390068at2759; -.
DR   UniPathway; UPA00912; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 431995; Expressed in internal ear 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:0052650; F:NADP-retinol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002138; P:retinoic acid biosynthetic process; IEA:InterPro.
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..341
FT                   /note="Retinol dehydrogenase 10-B"
FT                   /id="PRO_0000307688"
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;  38530 MW;  F56598AA51239216 CRC64;
     MHIVLEFFLV TFRVLWAFVL AAAKWFVRPK DKNVAGQVCL ITGAGSGLGR LFALEFARRR
     AQLVLWDINP QSNEETADMV RDIYRQLQAE DSARRANSSA DEEVLPCCNL QVYTYTCDVG
     KRESVYSTAE RVRREVGDVY LLLNNAGVVS GHHLLECPDE LIERTMMVNC HAHFWTTKAF
     LPKMMEMNHG HIVSVASSLG LFSTAGVEDY CASKFGVVGF HESLSHELKA ADKDGIKTTL
     VCPYLVDTGM FRGCRIRKEI EPFLPPLKPD YCVKQAMRAI LTDQPMICTP RLMYIVLCMK
     SILPFEAVVC MYRFLGADKC MYPFIAQRKQ ATNNNETKNG I