ID   RDH8_BOVIN              Reviewed;         312 AA.
AC   Q9N126;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Retinol dehydrogenase 8;
DE            EC=1.1.1.300 {ECO:0000269|PubMed:10753906};
DE   AltName: Full=Photoreceptor outer segment all-trans retinol dehydrogenase;
GN   Name=RDH8; Synonyms=PRRDH;
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], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Retina;
RX   PubMed=10753906; DOI=10.1074/jbc.275.15.11034;
RA   Rattner A., Smallwood P.M., Nathans J.;
RT   "Identification and characterization of all-trans-retinol dehydrogenase
RT   from photoreceptor outer segments, the visual cycle enzyme that reduces
RT   all-trans-retinal to all-trans-retinol.";
RL   J. Biol. Chem. 275:11034-11043(2000).
CC   -!- FUNCTION: Retinol dehydrogenase with a clear preference for NADP.
CC       Converts all-trans-retinal to all-trans-retinol. May play a role in the
CC       regeneration of visual pigment at high light intensity.
CC       {ECO:0000269|PubMed:10753906}.
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:10753906};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:10753906}; Multi-
CC       pass membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Detected in photoreceptor outer segments in the
CC       retina (at protein level). {ECO:0000269|PubMed:10753906}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AF229846; AAF63161.1; -; mRNA.
DR   RefSeq; NP_776592.1; NM_174167.2.
DR   AlphaFoldDB; Q9N126; -.
DR   SMR; Q9N126; -.
DR   STRING; 9913.ENSBTAP00000013443; -.
DR   PaxDb; Q9N126; -.
DR   PRIDE; Q9N126; -.
DR   Ensembl; ENSBTAT00000013443; ENSBTAP00000013443; ENSBTAG00000010188.
DR   GeneID; 281449; -.
DR   KEGG; bta:281449; -.
DR   CTD; 50700; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010188; -.
DR   VGNC; VGNC:52817; RDH8.
DR   eggNOG; KOG1205; Eukaryota.
DR   GeneTree; ENSGT00940000155412; -.
DR   HOGENOM; CLU_010194_2_9_1; -.
DR   InParanoid; Q9N126; -.
DR   OMA; QGVMFND; -.
DR   OrthoDB; 1313182at2759; -.
DR   TreeFam; TF105451; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000010188; Expressed in retina and 14 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042622; C:photoreceptor outer segment membrane; TAS:Reactome.
DR   GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0052650; F:NADP-retinol dehydrogenase activity; TAS:Reactome.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0006703; P:estrogen biosynthetic process; IEA:InterPro.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0042572; P:retinol metabolic process; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR011348; 17beta_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PIRSF; PIRSF000095; 17beta-HSD; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Lipid metabolism; Membrane; NADP; Oxidoreductase; Reference proteome;
KW   Sensory transduction; Transmembrane; Transmembrane helix; Vision.
FT   CHAIN           1..312
FT                   /note="Retinol dehydrogenase 8"
FT                   /id="PRO_0000305971"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        156
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         9..18
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q12634"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   312 AA;  33956 MW;  36481039FF71874D CRC64;
     MADAPRTVLI SGCSSGIGLE LAVQLAHDPR QRYQVVATMR DLGKKGTLET AAGEALGQTL
     TVAQLDVCSD ESVAQCLNCI QGGEVDVLVN NAGVGLVGPL EGLSLAAMQN VFDTNFFGAV
     RLVKAVLPSM KRRRQGHIVV VSSVMGLQGV VFNEVYAASK FAMEGFFESL AVQLLQFNIF
     ISLVEPGPVV TEFEGKLLEQ VSTAEFPGTD PDTLSYFRDL YLPASRELFH NVGQSPQDVA
     KVIVKVIGSA RPPLRRRTNT RYTPLIALKA MDPSGSLYVR TSHCLLFRWP RLLNLGLRCL
     ACSCFRTPVW PR