RDH14_BOVIN
ID RDH14_BOVIN Reviewed; 336 AA.
AC Q17QW3;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Retinol dehydrogenase 14;
DE EC=1.1.1.300 {ECO:0000250|UniProtKB:Q9HBH5};
GN Name=RDH14;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=12226107; DOI=10.1074/jbc.m208882200;
RA Haeseleer F., Jang G.-F., Imanishi Y., Driessen C.A.G.G., Matsumura M.,
RA Nelson P.S., Palczewski K.;
RT "Dual-substrate specificity short chain retinol dehydrogenases from the
RT vertebrate retina.";
RL J. Biol. Chem. 277:45537-45546(2002).
CC -!- FUNCTION: Retinol dehydrogenase with a clear preference for NADP.
CC Displays high activity towards 9-cis, 11-cis and all-trans-retinol.
CC Shows a very weak activity towards 13-cis-retinol. Has no activity
CC towards steroid. {ECO:0000250|UniProtKB:Q9ERI6}.
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:Q9ERI6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-cis-retinol + NADP(+) = 11-cis-retinal + H(+) + NADPH;
CC Xref=Rhea:RHEA:54912, ChEBI:CHEBI:15378, ChEBI:CHEBI:16066,
CC ChEBI:CHEBI:16302, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:Q9ERI6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-retinol + NADP(+) = 9-cis-retinal + H(+) + NADPH;
CC Xref=Rhea:RHEA:54916, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273;
CC Evidence={ECO:0000250|UniProtKB:Q9ERI6};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000250|UniProtKB:Q9ERI6}.
CC -!- TISSUE SPECIFICITY: In the retina detected in the cone and rod
CC photoreceptor outer segments, weak expression in Mueller cells.
CC {ECO:0000269|PubMed:12226107}.
CC -!- MISCELLANEOUS: Shows clear specificity for the pro-S hydrogen on C4 of
CC NADPH and the pro-R hydrogen on C15 of retinols.
CC {ECO:0000250|UniProtKB:Q9ERI6}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; DAAA02031779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC118145; AAI18146.1; -; mRNA.
DR RefSeq; NP_001068701.1; NM_001075233.1.
DR AlphaFoldDB; Q17QW3; -.
DR SMR; Q17QW3; -.
DR STRING; 9913.ENSBTAP00000006933; -.
DR PaxDb; Q17QW3; -.
DR Ensembl; ENSBTAT00000006933; ENSBTAP00000006933; ENSBTAG00000023928.
DR GeneID; 505949; -.
DR KEGG; bta:505949; -.
DR CTD; 57665; -.
DR VEuPathDB; HostDB:ENSBTAG00000023928; -.
DR eggNOG; KOG1208; Eukaryota.
DR GeneTree; ENSGT00940000160181; -.
DR HOGENOM; CLU_010194_44_5_1; -.
DR InParanoid; Q17QW3; -.
DR OMA; GVQGKCF; -.
DR OrthoDB; 921996at2759; -.
DR TreeFam; TF105429; -.
DR Reactome; R-BTA-5365859; RA biosynthesis pathway.
DR UniPathway; UPA00912; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000023928; Expressed in caput epididymis and 105 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0102354; F:11-cis-retinol dehydrogenase activity; IEA:RHEA.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0042572; P:retinol metabolic process; ISS:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
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; NADP; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..336
FT /note="Retinol dehydrogenase 14"
FT /id="PRO_0000446064"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8WNV7"
FT BINDING 48..54
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBH5"
SQ SEQUENCE 336 AA; 36625 MW; 8D053F65EBBCB338 CRC64;
MAVGTAAALL AALGGILWLA ARRFVGSSVQ RLHQGRDSGL MRGKTVLITG ANSGLGRATA
AELLRLGARV IMGCRDRERA EEAAGQLRRE VCPAGGPDSG PNSGGAGELV VKELDLASLS
SVRSFCQEML QEEPRLDVLI NNAGVFQCPY MKTEDGFEMQ FGVNHLGHFL LTNLLLGLLK
SSAPSRIVVV SSKLYKYGDI NFEDLNSEQS YNKSFCYSRS KLANILFTRE LARRLEGTSV
TVNVLHPGIV RTNLGRHIHI PLLVRPLFNL VSWAFFKTPE EGAQTAVYLA SSPEVEGVSG
RYFGDCKEEE LLPKAMDESV ARKLWDISEV MVGILK
