ID   DHRS3_BOVIN             Reviewed;         302 AA.
AC   O77769; Q3MHX2;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Short-chain dehydrogenase/reductase 3;
DE            EC=1.1.1.300 {ECO:0000250|UniProtKB:O75911};
DE   AltName: Full=Retinal short-chain dehydrogenase/reductase 1;
DE            Short=retSDR1;
GN   Name=DHRS3;
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Retina;
RX   PubMed=9705317; DOI=10.1074/jbc.273.34.21790;
RA   Haeseleer F., Huang J., Lebioda L., Saari J.C., Palczewski K.;
RT   "Molecular characterization of a novel short-chain dehydrogenase/reductase
RT   that reduces all-trans-retinal.";
RL   J. Biol. Chem. 273:21790-21799(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reduction of all-trans-retinal to all-trans-
CC       retinol in the presence of NADPH. {ECO:0000250|UniProtKB:O75911}.
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:0000250|UniProtKB:O75911};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: In the retina, expressed in cone but not rod outer
CC       segments. {ECO:0000269|PubMed:9705317}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AF061742; AAC63264.1; -; mRNA.
DR   EMBL; BC104575; AAI04576.1; -; mRNA.
DR   RefSeq; NP_776605.2; NM_174180.3.
DR   AlphaFoldDB; O77769; -.
DR   SMR; O77769; -.
DR   STRING; 9913.ENSBTAP00000033930; -.
DR   PaxDb; O77769; -.
DR   GeneID; 281482; -.
DR   KEGG; bta:281482; -.
DR   CTD; 9249; -.
DR   eggNOG; KOG1201; Eukaryota.
DR   InParanoid; O77769; -.
DR   OrthoDB; 1373099at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR032969; DHRS3.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR24322:SF483; PTHR24322:SF483; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Lipid metabolism; Membrane; NADP; Oxidoreductase; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..302
FT                   /note="Short-chain dehydrogenase/reductase 3"
FT                   /id="PRO_0000054643"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        56
FT                   /note="R -> L (in Ref. 2; AAI04576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="P -> L (in Ref. 2; AAI04576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        295
FT                   /note="I -> M (in Ref. 2; AAI04576)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   302 AA;  33496 MW;  855FD2488ACB243E CRC64;
     MVWKRLGALV VFPLQMIYLV VKAAVGLVLP AKLRDLSREN VLITGGGRGI GRQLAREFAE
     RGARKIVLWG RTEKCLKETT EEIRQMGTEC HYFICDVGNR EEVYQTAKAV REKVGDITIL
     VNNAAVVHGK SLMDSDDDAL PKSQHINTLG QFWTTKAFLP RMLELQNGHI VCLNSVLALS
     AIPGAIDYCT SKASAFAFME SLTLGLLDCP GVSATTVLPF HTSTEMFQGM RVRFPNLFPP
     LKPETVARRT VEAVQLNQAL LLLPWTMHAL IILKSILPQA ALEEIHKFSG TYTCINTFKG
     RT