RDH5_MOUSE
ID RDH5_MOUSE Reviewed; 318 AA.
AC O55240;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 174.
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:10588954};
DE EC=1.1.1.53 {ECO:0000250|UniProtKB:Q92781};
DE AltName: Full=11-cis retinol dehydrogenase {ECO:0000312|EMBL:CAA66347.1};
DE Short=11-cis RDH {ECO:0000250|UniProtKB:Q27979};
DE Short=11-cis RoDH {ECO:0000303|PubMed:9654122};
DE AltName: Full=9-cis retinol dehydrogenase {ECO:0000312|EMBL:AAC25951.1};
DE AltName: Full=Cis-retinol dehydrogenase {ECO:0000303|PubMed:10588954};
GN Name=Rdh5 {ECO:0000312|EMBL:EDL24632.1,
GN ECO:0000312|Ensembl:ENSMUSP00000026406, ECO:0000312|MGI:MGI:1201412};
GN Synonyms=cRDH {ECO:0000303|PubMed:10588954},
GN rdh {ECO:0000312|EMBL:CAA66347.1}, Rdh4 {ECO:0000303|PubMed:10739682};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000269|PubMed:9654122, ECO:0000312|EMBL:CAA66347.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ {ECO:0000312|EMBL:CAA66347.1};
RC TISSUE=Liver {ECO:0000269|PubMed:9654122};
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 [2] {ECO:0000269|PubMed:9539749, ECO:0000312|EMBL:AAC25951.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Liver {ECO:0000312|EMBL:AAC25951.1};
RX PubMed=9539749; DOI=10.1073/pnas.95.8.4404;
RA Romert A., Tuvendal P., Simon A., Dencker L., Eriksson U.;
RT "The identification of a 9-cis retinol dehydrogenase in the mouse embryo
RT reveals a pathway for synthesis of 9-cis retinoic acid.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4404-4409(1998).
RN [3] {ECO:0000269|PubMed:10588954, ECO:0000312|EMBL:AAC00491.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ {ECO:0000269|PubMed:10588954},
RC BALB/cJ {ECO:0000312|EMBL:AAC00491.1}, and
RC C57BL/6J {ECO:0000312|EMBL:AAC00492.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAC00491.1}, and
RC Liver {ECO:0000312|EMBL:AAC00492.1};
RX PubMed=10588954;
RA Gamble M.V., Shang E., Zott R.P., Mertz J.R., Wolgemuth D.J., Blaner W.S.;
RT "Biochemical properties, tissue expression, and gene structure of a short
RT chain dehydrogenase/reductase able to catalyze cis-retinol oxidation.";
RL J. Lipid Res. 40:2279-2292(1999).
RN [4] {ECO:0000312|EMBL:BAE22435.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE22435.1};
RC TISSUE=Cerebellum {ECO:0000312|EMBL:BAE22435.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5] {ECO:0000312|Ensembl:ENSMUSP00000026406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000026406};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6] {ECO:0000312|EMBL:EDL24632.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000312|EMBL:AAH21372.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH21372.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH21372.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8] {ECO:0000269|PubMed:10739682}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP TOPOLOGY.
RX PubMed=10739682; DOI=10.1006/excr.2000.4817;
RA Romert A., Tuvendal P., Tryggvason K., Dencker L., Eriksson U.;
RT "Gene structure, expression analysis, and membrane topology of RDH4.";
RL Exp. Cell Res. 256:338-345(2000).
RN [9] {ECO:0000269|PubMed:10825191}
RP DISRUPTION PHENOTYPE.
RX PubMed=10825191; DOI=10.1128/mcb.20.12.4275-4287.2000;
RA Driessen C.A., Winkens H.J., Hoffmann K., Kuhlmann L.D., Janssen B.P.,
RA Van Vugt A.H., Van Hooser J.P., Wieringa B.E., Deutman A.F., Palczewski K.,
RA Ruether K., Janssen J.J.;
RT "Disruption of the 11-cis-retinol dehydrogenase gene leads to accumulation
RT of cis-retinols and cis-retinyl esters.";
RL Mol. Cell. Biol. 20:4275-4287(2000).
RN [10]
RP TOPOLOGY, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=11279029; DOI=10.1074/jbc.m100215200;
RA Tryggvason K., Romert A., Eriksson U.;
RT "Biosynthesis of 9-cis-retinoic acid in vivo. The roles of different
RT retinol dehydrogenases and a structure-activity analysis of microsomal
RT retinol dehydrogenases.";
RL J. Biol. Chem. 276:19253-19258(2001).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=16223484; DOI=10.1016/j.yexcr.2005.07.032;
RA Liden M., Tryggvason K., Eriksson U.;
RT "The C-terminal region of cis-retinol/androgen dehydrogenase 1 (CRAD1)
RT confers ER localization and in vivo enzymatic function.";
RL Exp. Cell Res. 311:205-217(2005).
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:10588954, PubMed:9539749). Has no activity towards all-trans
CC retinal (By similarity). Plays a significant role in 11-cis retinol
CC oxidation in the retinal pigment epithelium cells (RPE). Also
CC recognizes steroids (androsterone, androstanediol) as its substrates
CC (By similarity). {ECO:0000250|UniProtKB:Q27979,
CC ECO:0000250|UniProtKB:Q92781, ECO:0000269|PubMed:10588954,
CC ECO:0000269|PubMed:9539749}.
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:10588954};
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:10588954, ECO:0000269|PubMed:11279029,
CC ECO:0000269|PubMed:9539749};
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:10588954};
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:0000269|PubMed:10588954}.
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000303|PubMed:9539749}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q92781}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10739682, ECO:0000269|PubMed:11279029}; Multi-pass
CC membrane protein {ECO:0000255}; Lumenal side
CC {ECO:0000269|PubMed:10739682, ECO:0000269|PubMed:11279029,
CC ECO:0000269|PubMed:16223484}.
CC -!- TISSUE SPECIFICITY: Expressed in eye, liver, kidney, brain, intestine,
CC placenta, epididymus and submaxillary gland. In eye, strongly expressed
CC in the retinal pigment epithelium, with lower expression levels
CC detected in the inner segment of the photoreceptor cells and in the
CC outer plexiform layer. In kidney, strong expression detected in the
CC distal tubules and the transitional epithelium in the renal pelvis,
CC with weaker expression detected in the epithelium of the outer stripe
CC of the outer zone of the medulla. In liver, detected in hepatocytes in
CC the centrilobular area. In lung, present in Clara cells in the
CC epithelium of the bronchiole, in parenchyma and in cartilage
CC surrounding the secondary bronchi. In skin, expressed in epidermis,
CC hair follicles and mast cells in the dermis. Expressed in heart
CC (PubMed:10588954 and PubMed:10739682). Not detected in heart
CC (PubMed:9539749). Not detected in lung, spleen, skeletal muscle and
CC testis. {ECO:0000269|PubMed:10588954, ECO:0000269|PubMed:10739682,
CC ECO:0000269|PubMed:9539749, ECO:0000269|PubMed:9654122}.
CC -!- DEVELOPMENTAL STAGE: Abundantly expressed during embryonic development,
CC especially in the developing central nervous system and sensory organs,
CC cranial and spinal ganglia and endoderm of foregut and hindgut. At 10
CC dpc, detected along the entire neural tube, the mid- and hindbrain
CC floor, the central canal of the brain vesicles, spinal cord, lung
CC mesenchyme, the trabecular layer of the heart ventricles, endoderm and
CC endodermally-derived structures such as tracheal epithelium and liver.
CC At 11 dpc, expressed in the brain vesicles, along the spinal cord,
CC myotome, migrating muscle progenitor cells in the body wall, cells of
CC the genital ridge, spinal ganglion, liver, cerebellar primordium, basal
CC cells of the neuroepithelium of the mesenchephalic flexure, collections
CC of cells in the pons, Rathke's pouch, spinal and cranial ganglia and
CC the floor plate, retina, lens, optic stalks and the neural crest-
CC derived mesenchyme in the anterior eye segment. During eye development,
CC expression restricted to the retinal pigment epithelium of the
CC posterior hemisphere at 18 dpc, with expression levels increasing
CC postnatally to P16. {ECO:0000269|PubMed:10739682,
CC ECO:0000269|PubMed:9539749}.
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:0000269|PubMed:11279029}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice develop normally and are fertile. No
CC abnormalities can be found in the retinal structure, rhodopsin content
CC and fundus appearance of their eyes. Mice display a mild visual
CC phenotype of impaired dark adaptation and accumulation of 11-cis- and
CC 13-cis-retinols and 11-cis- and 13-cis-retinyl esters in the eyes.
CC {ECO:0000269|PubMed:10825191}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X97752; CAA66347.1; -; Genomic_DNA.
DR EMBL; AF013288; AAC25951.1; -; mRNA.
DR EMBL; AF033195; AAC00491.1; -; mRNA.
DR EMBL; AF033196; AAC00492.1; -; mRNA.
DR EMBL; AK135139; BAE22435.1; -; mRNA.
DR EMBL; AC122380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466578; EDL24632.1; -; Genomic_DNA.
DR EMBL; BC021372; AAH21372.1; -; mRNA.
DR CCDS; CCDS24298.1; -.
DR RefSeq; NP_598767.1; NM_134006.4.
DR RefSeq; XP_006513450.1; XM_006513387.2.
DR AlphaFoldDB; O55240; -.
DR SMR; O55240; -.
DR BioGRID; 202843; 1.
DR STRING; 10090.ENSMUSP00000026406; -.
DR SwissLipids; SLP:000000798; -.
DR iPTMnet; O55240; -.
DR PhosphoSitePlus; O55240; -.
DR MaxQB; O55240; -.
DR PaxDb; O55240; -.
DR PeptideAtlas; O55240; -.
DR PRIDE; O55240; -.
DR ProteomicsDB; 253191; -.
DR Antibodypedia; 27694; 101 antibodies from 28 providers.
DR DNASU; 19682; -.
DR Ensembl; ENSMUST00000026406; ENSMUSP00000026406; ENSMUSG00000025350.
DR GeneID; 19682; -.
DR KEGG; mmu:19682; -.
DR UCSC; uc007how.1; mouse.
DR CTD; 5959; -.
DR MGI; MGI:1201412; Rdh5.
DR VEuPathDB; HostDB:ENSMUSG00000025350; -.
DR eggNOG; KOG1610; Eukaryota.
DR GeneTree; ENSGT00940000161168; -.
DR InParanoid; O55240; -.
DR OMA; YLKVQRF; -.
DR OrthoDB; 1313182at2759; -.
DR PhylomeDB; O55240; -.
DR TreeFam; TF325617; -.
DR BRENDA; 1.1.1.105; 3474.
DR Reactome; R-MMU-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-MMU-5365859; RA biosynthesis pathway.
DR UniPathway; UPA00912; -.
DR BioGRID-ORCS; 19682; 1 hit in 77 CRISPR screens.
DR PRO; PR:O55240; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O55240; protein.
DR Bgee; ENSMUSG00000025350; Expressed in choroid plexus of fourth ventricle and 161 other tissues.
DR ExpressionAtlas; O55240; baseline and differential.
DR Genevisible; O55240; MM.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
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; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
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 Endoplasmic reticulum; Lipid metabolism; Membrane; NAD; Oxidoreductase;
KW Reference proteome; Sensory transduction; Steroid metabolism;
KW Transmembrane; Transmembrane helix; Vision.
FT CHAIN 1..318
FT /note="Retinol dehydrogenase 5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000419633"
FT TRANSMEM 1..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..288
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:16223484"
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; 34826 MW; AA8DB76CD0BF7DFC CRC64;
MWLPLLLGAL LWAVLWLLRD RQSLPASDAF IFITGCDSGF GRLLALQLDQ KGFQVLAGCL
TPSGAEDLQQ MASSRLHTTL LDITDPQNVQ QVAKWVKTRV GETGLFGLVN NAGVAGIIGP
TPWLTQDDFQ RVLSVNTLGP IGVTLALLPL LQQARGRVVN ITSVLGRIAA NGGGYCVSKF
GLEAFSDSLR RDMAPFGVQV SIVEPGFFRT PVTNLESLES TLKACWARLP PAIQAHYGEA
FLDTYLRVQR RIMNLICDPE LTKVTSCLEH ALTARHPRTR YSPGWDAKLL WLPASYLPAR
VVDAVLTWIL PRPAQSVS
