RDH5_BOVIN
ID RDH5_BOVIN Reviewed; 318 AA.
AC Q27979; F1ML51; Q28004;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Retinol dehydrogenase 5;
DE EC=1.1.1.209 {ECO:0000250|UniProtKB:Q92781};
DE EC=1.1.1.315 {ECO:0000269|PubMed:7544779, ECO:0000269|PubMed:7836368, ECO:0000269|PubMed:9654122};
DE EC=1.1.1.53 {ECO:0000250|UniProtKB:Q92781};
DE AltName: Full=11-cis retinol dehydrogenase;
DE Short=11-cis RDH {ECO:0000303|PubMed:9654122};
DE Short=11-cis RoDH;
DE AltName: Full=9-cis retinol dehydrogenase;
DE Short=9cRDH;
DE AltName: Full=P32 {ECO:0000303|PubMed:7836368};
GN Name=RDH5; Synonyms=RDH1;
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, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Retinal pigment epithelium;
RX PubMed=7544779;
RA Driessen C.A., Janssen B.P., Winkens H.J., van Vugt A.H., de Leeuw T.L.,
RA Janssen J.J.;
RT "Cloning and expression of a cDNA encoding bovine retinal pigment
RT epithelial 11-cis retinol dehydrogenase.";
RL Invest. Ophthalmol. Vis. Sci. 36:1988-1996(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 76-89; 192-198; 210-224;
RP 281-288 AND 301-318, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Retinal pigment epithelium;
RX PubMed=7836368; DOI=10.1074/jbc.270.34.19979;
RA Simon A., Hellman U., Wernstedt C., Eriksson U.;
RT "The retinal pigment epithelial-specific 11-cis retinol dehydrogenase
RT belongs to the family of short chain alcohol dehydrogenases.";
RL J. Biol. Chem. 270:1107-1112(1995).
RN [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9654122; DOI=10.1016/s0014-5793(98)00473-6;
RA Driessen C.A., Winkens H.J., Kuhlmann E.D., Janssen A.P., van Vugt A.H.,
RA Deutman A.F., Janssen J.J.;
RT "The visual cycle retinol dehydrogenase: possible involvement in the 9-cis
RT retinoic acid biosynthetic pathway.";
RL FEBS Lett. 428:135-140(1998).
RN [5]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=9914166; DOI=10.1242/jcs.112.4.549;
RA Simon A., Romert A., Gustafson A.L., McCaffery J.M., Eriksson U.;
RT "Intracellular localization and membrane topology of 11-cis retinol
RT dehydrogenase in the retinal pigment epithelium suggest a compartmentalized
RT synthesis of 11-cis retinaldehyde.";
RL J. Cell Sci. 112:549-558(1999).
CC -!- FUNCTION: Catalyzes the oxidation of cis-isomers of retinol, including
CC 11-cis-, 9-cis-, and 13-cis-retinol in an NAD-dependent manner
CC (PubMed:7544779, PubMed:7836368, PubMed:9654122). Has no activity
CC towards all-trans retinal (PubMed:9654122). Plays a significant role in
CC 11-cis retinol oxidation in the retinal pigment epithelium cells (RPE)
CC (By similarity). Also recognizes steroids (androsterone,
CC androstanediol) as its substrates (By similarity).
CC {ECO:0000250|UniProtKB:Q92781, ECO:0000269|PubMed:7544779,
CC ECO:0000269|PubMed:7836368, ECO:0000269|PubMed:9654122}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-cis-retinol + NAD(+) = 11-cis-retinal + H(+) + NADH;
CC Xref=Rhea:RHEA:42060, ChEBI:CHEBI:15378, ChEBI:CHEBI:16066,
CC ChEBI:CHEBI:16302, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.315; Evidence={ECO:0000269|PubMed:7544779,
CC ECO:0000269|PubMed:7836368, ECO:0000269|PubMed:9654122};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-retinol + NAD(+) = 9-cis-retinal + H(+) + NADH;
CC Xref=Rhea:RHEA:42052, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273;
CC Evidence={ECO:0000269|PubMed:7544779, ECO:0000269|PubMed:9654122};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-cis-retinol + NAD(+) = 13-cis-retinal + H(+) + NADH;
CC Xref=Rhea:RHEA:42056, ChEBI:CHEBI:15378, ChEBI:CHEBI:45479,
CC ChEBI:CHEBI:45487, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:7544779, ECO:0000269|PubMed:9654122};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3alpha-hydroxy-5alpha-androstan-17-one + NAD(+) = 5alpha-
CC androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:20381,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16032,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.209;
CC Evidence={ECO:0000250|UniProtKB:Q92781};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta-
CC hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42004,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.53;
CC Evidence={ECO:0000250|UniProtKB:Q92781};
CC -!- ACTIVITY REGULATION: Inhibited by 9-cis-, 13-cis- and all-trans-
CC retinoic acids, with the most potent inhibitor being 13-cis-retinoic
CC acid. Weakly inhibited by oleic acid. {ECO:0000250|UniProtKB:O55240}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=38 nmol/min/mg enzyme with 9-cis-retinol as substrate
CC {ECO:0000269|PubMed:9654122};
CC Vmax=38 nmol/min/mg enzyme with 11-cis-retinol as substrate
CC {ECO:0000269|PubMed:9654122};
CC Vmax=17 nmol/min/mg enzyme with 13-cis-retinol as substrate
CC {ECO:0000269|PubMed:9654122};
CC Vmax=56 nmol/min/mg enzyme with 9-cis-retinal as substrate
CC {ECO:0000269|PubMed:9654122};
CC Vmax=57 nmol/min/mg enzyme with 11-cis-retinal as substrate
CC {ECO:0000269|PubMed:9654122};
CC Vmax=57 nmol/min/mg enzyme with 13-cis-retinal as substrate
CC {ECO:0000269|PubMed:9654122};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000269|PubMed:7836368}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q92781}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:9914166}; Multi-pass membrane protein
CC {ECO:0000255}; Lumenal side {ECO:0000269|PubMed:9914166}. Microsome
CC membrane {ECO:0000269|PubMed:7836368}.
CC -!- TISSUE SPECIFICITY: Expressed in retinal pigment epithelial cells
CC (PubMed:9914166). Expression detected in smooth muscle cells of the
CC small arteries in liver, kidney, small intestine and heart, and in
CC small intestine also in the muscularis mucosae and muscularis propria
CC (at protein level; PubMed:9654122). Expressed in eye in retinal pigment
CC epithelium but not in lens capsule, iris, retina, cornea epithelium and
CC ciliary body. Not detected in adrenal gland, lung, testis, brain,
CC muscle and spleen. Not detected in liver, kidney, heart and small
CC intestine (PubMed:7544779 and PubMed:7836368).
CC {ECO:0000269|PubMed:9914166}.
CC -!- DOMAIN: The last 8 amino acids of the C-terminal tail are important for
CC a proper localization as well as for the in vivo enzymatic activity.
CC {ECO:0000250|UniProtKB:O55240}.
CC -!- PTM: Not glycosylated. {ECO:0000269|PubMed:9914166}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA80694.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=DAAA02013541; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L36533; AAA80694.1; ALT_FRAME; mRNA.
DR EMBL; X82262; CAA57715.1; -; mRNA.
DR EMBL; DAAA02013541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A55429; A55429.
DR PIR; I45845; I45845.
DR RefSeq; NP_776591.2; NM_174166.3.
DR RefSeq; XP_010803419.1; XM_010805117.2.
DR AlphaFoldDB; Q27979; -.
DR SMR; Q27979; -.
DR STRING; 9913.ENSBTAP00000056512; -.
DR SwissLipids; SLP:000001721; -.
DR PaxDb; Q27979; -.
DR Ensembl; ENSBTAT00000065932; ENSBTAP00000056512; ENSBTAG00000011927.
DR GeneID; 281448; -.
DR KEGG; bta:281448; -.
DR CTD; 5959; -.
DR VEuPathDB; HostDB:ENSBTAG00000011927; -.
DR VGNC; VGNC:33843; RDH5.
DR eggNOG; KOG1610; Eukaryota.
DR GeneTree; ENSGT00940000161168; -.
DR HOGENOM; CLU_010194_2_0_1; -.
DR InParanoid; Q27979; -.
DR OMA; YLKVQRF; -.
DR OrthoDB; 1313182at2759; -.
DR TreeFam; TF325617; -.
DR BRENDA; 1.1.1.315; 908.
DR Reactome; R-BTA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-BTA-5365859; RA biosynthesis pathway.
DR UniPathway; UPA00912; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000011927; Expressed in anterior segment of eyeball and 103 other tissues.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0047044; F:androstan-3-alpha,17-beta-diol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0047023; F:androsterone dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0001523; P:retinoid metabolic process; IBA:GO_Central.
DR GO; GO:0042572; P:retinol metabolic process; IDA:UniProtKB.
DR GO; GO:0008202; P:steroid metabolic process; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Lipid metabolism;
KW Membrane; Microsome; NAD; Oxidoreductase; Reference proteome;
KW Sensory transduction; Steroid metabolism; Transmembrane;
KW Transmembrane helix; Vision.
FT CHAIN 1..318
FT /note="Retinol dehydrogenase 5"
FT /id="PRO_0000054757"
FT TRANSMEM 1..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..288
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:9914166"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92781"
FT BINDING 32..56
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 318 AA; 35037 MW; 78B4A1E43E5FB351 CRC64;
MWLPLLLGVL LWAALWLLRD RQCLPASDAF IFITGCDSGF GRLLALRLDQ RGFRVLASCL
TPSGAEDLQR VASSRLHTTL LDVTDPQSIR QAVKWVETHV GEAGLFGLVN NAGVAGIIGP
TPWQTREDFQ RVLNVNTLGP IGVTLALLPL LLQARGRVIN ITSVLGRLAA NGGGYCVSKF
GLEAFSDSLR RDVAPFGVRV SIVEPGFFRT PVTNLETLED TLQACWARLP PATQALYGEA
FLTKYLRVQQ RIMNMICDPD LAKVSRCLEH ALTARHPRTR YSPGWDAKLL WLPASYLPAR
LVDAVLAWVL PKPAQTVY
