ID   RD10B_DANRE             Reviewed;         336 AA.
AC   Q7T2D1; B0V2U0;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Retinol dehydrogenase 10-B;
DE            EC=1.1.1.300;
GN   Name=rdh10b; Synonyms=rdh10; ORFNames=si:ch211-193n21.3;
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 GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2003) 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}.
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DR   EMBL; CT027743; CAQ15477.1; -; Genomic_DNA.
DR   EMBL; BC054596; AAH54596.1; -; mRNA.
DR   RefSeq; NP_958488.1; NM_201331.1.
DR   AlphaFoldDB; Q7T2D1; -.
DR   SMR; Q7T2D1; -.
DR   STRING; 7955.ENSDARP00000104887; -.
DR   PaxDb; Q7T2D1; -.
DR   Ensembl; ENSDART00000004903; ENSDARP00000011528; ENSDARG00000012369.
DR   GeneID; 378722; -.
DR   KEGG; dre:378722; -.
DR   CTD; 378722; -.
DR   ZFIN; ZDB-GENE-030909-7; rdh10b.
DR   eggNOG; KOG1201; Eukaryota.
DR   GeneTree; ENSGT00940000157063; -.
DR   HOGENOM; CLU_010194_2_5_1; -.
DR   InParanoid; Q7T2D1; -.
DR   OMA; SVEGQVC; -.
DR   OrthoDB; 1373099at2759; -.
DR   PhylomeDB; Q7T2D1; -.
DR   TreeFam; TF312837; -.
DR   UniPathway; UPA00912; -.
DR   PRO; PR:Q7T2D1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 2.
DR   Bgee; ENSDARG00000012369; Expressed in cleaving embryo and 34 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; 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; Lipid metabolism; Membrane; Microsome; NADP;
KW   Oxidoreductase; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..336
FT                   /note="Retinol dehydrogenase 10-B"
FT                   /id="PRO_0000307685"
FT   TRANSMEM        7..27
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        205
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         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        96
FT                   /note="S -> R (in Ref. 2; AAH54596)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   336 AA;  37819 MW;  A952DCB314366262 CRC64;
     MNIATELFVV TFKIIWSFVL AGAKWFIRPR EKSVEGQVCV ITGAGSGLGR LFALEFARRR
     ATLVLWDINR QSNEETAEMA REIYRQLKPS TGSSDSVQEL PLLQPKVYTY MCDVSKRESV
     YLTAEKVRSE VGDIDLLINN AGVVSGRHLL DCPDELIERT MMVNCHAHFW TTKAFLPKML
     ELNHGHIVTV ASSLGLFTTA GVEDYCASKF GAIGFHESLS HELKAADKDG IKMTLVCPFL
     VDTGMFEGCK IRKEMAPFFP PLKPEYCVKQ AMRAILTDQP MICTPRVMYM VTFMKTVLPF
     DAIVCMYKFI GADKCMYPFL AQRKESTNNN ESKTGI