RDH11_MOUSE
ID RDH11_MOUSE Reviewed; 316 AA.
AC Q9QYF1; Q3UXM9; Q9D0U5;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Retinol dehydrogenase 11;
DE EC=1.1.1.300 {ECO:0000269|PubMed:12807874, ECO:0000269|PubMed:29567832};
DE AltName: Full=Androgen-regulated short-chain dehydrogenase/reductase 1;
DE AltName: Full=Cell line MC/9.IL4-derived protein 1;
DE AltName: Full=M42C60;
DE AltName: Full=Prostate short-chain dehydrogenase/reductase 1 {ECO:0000303|PubMed:12137953};
DE AltName: Full=Retinal reductase 1;
DE Short=RalR1;
DE AltName: Full=Short-chain aldehyde dehydrogenase {ECO:0000303|PubMed:12807874};
DE Short=SCALD {ECO:0000303|PubMed:12807874};
GN Name=Rdh11; Synonyms=Arsdr1, Mdt1, Psdr1 {ECO:0000303|PubMed:12137953};
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Mast cell;
RX PubMed=8018917;
RA Hara T., Harada N., Mitsui H., Miura T., Ishizaka T., Miyajima A.;
RT "Characterization of cell phenotype by a novel cDNA library subtraction
RT system: expression of CD8 alpha in a mast cell-derived interleukin-4-
RT dependent cell line.";
RL Blood 84:189-199(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=12137953; DOI=10.1016/s0378-1119(02)00718-7;
RA Moore S., Pritchard C., Lin B., Ferguson C., Nelson P.S.;
RT "Isolation and characterization of the murine prostate short-chain
RT dehydrogenase/reductase 1 (Psdr1) gene, a new member of the short-chain
RT steroid dehydrogenase/reductase family.";
RL Gene 293:149-160(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, INDUCTION, AND
RP TOPOLOGY.
RX PubMed=12807874; DOI=10.1074/jbc.m304969200;
RA Kasus-Jacobi A., Ou J., Bashmakov Y.K., Shelton J.M., Richardson J.A.,
RA Goldstein J.L., Brown M.S.;
RT "Characterization of mouse short-chain aldehyde reductase (SCALD), an
RT enzyme regulated by sterol regulatory element-binding proteins.";
RL J. Biol. Chem. 278:32380-32389(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Muellerian duct;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [6]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=15790565; DOI=10.1074/jbc.m413789200;
RA Kasus-Jacobi A., Ou J., Birch D.G., Locke K.G., Shelton J.M.,
RA Richardson J.A., Murphy A.J., Valenzuela D.M., Yancopoulos G.D.,
RA Edwards A.O.;
RT "Functional characterization of mouse RDH11 as a retinol dehydrogenase
RT involved in dark adaptation in vivo.";
RL J. Biol. Chem. 280:20413-20420(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND
RP CATALYTIC ACTIVITY.
RX PubMed=29567832; DOI=10.1074/jbc.ra117.001646;
RA Belyaeva O.V., Wu L., Shmarakov I., Nelson P.S., Kedishvili N.Y.;
RT "Retinol dehydrogenase 11 is essential for the maintenance of retinol
RT homeostasis in liver and testis in mice.";
RL J. Biol. Chem. 293:6996-7007(2018).
CC -!- FUNCTION: Retinol dehydrogenase with a clear preference for NADP
CC (PubMed:12807874, PubMed:29567832). Displays high activity towards 9-
CC cis, 11-cis and all-trans-retinol, and to a lesser extent on 13-cis-
CC retinol (By similarity) (PubMed:12807874). Exhibits also reductive
CC activity towards toxic lipid peroxidation products such as medium-chain
CC aldehydes trans-2-nonenal, nonanal, and cis-6-nonenal
CC (PubMed:12807874). Has no dehydrogenase activity towards steroid
CC (PubMed:12807874). Seems to be required for homeostasis of retinol in
CC liver and testis (PubMed:29567832). {ECO:0000250|UniProtKB:Q8TC12,
CC ECO:0000269|PubMed:12807874, ECO:0000269|PubMed:29567832}.
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:12807874,
CC ECO:0000269|PubMed:29567832};
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:Q8TC12};
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:0000269|PubMed:12807874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-cis-retinol + NADP(+) = 13-cis-retinal + H(+) + NADPH;
CC Xref=Rhea:RHEA:54920, ChEBI:CHEBI:15378, ChEBI:CHEBI:45479,
CC ChEBI:CHEBI:45487, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:Q8TC12};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium-chain primary fatty alcohol + NADP(+) = a medium-
CC chain fatty aldehyde + H(+) + NADPH; Xref=Rhea:RHEA:58364,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:142605, ChEBI:CHEBI:142621;
CC Evidence={ECO:0000269|PubMed:12807874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6Z)-nona-2,6-dien-1-ol + NADP(+) = (2E,6Z)-nona-2,6-dienal
CC + H(+) + NADPH; Xref=Rhea:RHEA:58368, ChEBI:CHEBI:7610,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:142615; Evidence={ECO:0000269|PubMed:12807874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-oct-2-en-1-ol + NADP(+) = (2E)-octenal + H(+) + NADPH;
CC Xref=Rhea:RHEA:58372, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:61748, ChEBI:CHEBI:142616;
CC Evidence={ECO:0000269|PubMed:12807874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-non-2-en-1-ol + NADP(+) = (E)-non-2-enal + H(+) + NADPH;
CC Xref=Rhea:RHEA:58332, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:142592, ChEBI:CHEBI:142604;
CC Evidence={ECO:0000269|PubMed:12807874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=heptan-1-ol + NADP(+) = H(+) + heptanal + NADPH;
CC Xref=Rhea:RHEA:58400, ChEBI:CHEBI:15378, ChEBI:CHEBI:34787,
CC ChEBI:CHEBI:43003, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:12807874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexan-1-ol + NADP(+) = H(+) + hexanal + NADPH;
CC Xref=Rhea:RHEA:58404, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:87393, ChEBI:CHEBI:88528;
CC Evidence={ECO:0000269|PubMed:12807874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decan-1-ol + NADP(+) = decanal + H(+) + NADPH;
CC Xref=Rhea:RHEA:58376, ChEBI:CHEBI:15378, ChEBI:CHEBI:28903,
CC ChEBI:CHEBI:31457, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:12807874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + nonan-1-ol = H(+) + NADPH + nonanal;
CC Xref=Rhea:RHEA:58380, ChEBI:CHEBI:15378, ChEBI:CHEBI:35986,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:84268;
CC Evidence={ECO:0000269|PubMed:12807874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + octan-1-ol = H(+) + NADPH + octanal;
CC Xref=Rhea:RHEA:58384, ChEBI:CHEBI:15378, ChEBI:CHEBI:16188,
CC ChEBI:CHEBI:17935, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:12807874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(Z)-non-6-en-1-ol + NADP(+) = (Z)-non-6-enal + H(+) + NADPH;
CC Xref=Rhea:RHEA:58328, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:142591, ChEBI:CHEBI:142603;
CC Evidence={ECO:0000269|PubMed:12807874};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=57 uM for all-trans-retinal {ECO:0000269|PubMed:12807874};
CC KM=14 uM for 9-cis-retinal {ECO:0000269|PubMed:12807874};
CC KM=30 uM for nonan-1-ol {ECO:0000269|PubMed:12807874};
CC KM=20 uM for NADPH {ECO:0000269|PubMed:12807874};
CC Note=kcat is 167 min(-1) for NADPH as substrate.
CC {ECO:0000269|PubMed:12807874};
CC pH dependence:
CC Optimum pH is between 6.5 and 7.5 for nonanal as substrate.
CC {ECO:0000269|PubMed:12807874};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000269|PubMed:12807874}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12807874}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:12807874}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=Q9QYF1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed at high level in liver and testis
CC (PubMed:12807874, PubMed:15790565, PubMed:29567832). Expressed at lower
CC levels in smooth muscle, thymus, submaxillary gland and epididymis. In
CC testis, expression is restricted to pachytene spermatocytes. Also
CC expressed in four layers of the retina, including the outer segment of
CC rods and cones (PubMed:12807874, PubMed:15790565).
CC {ECO:0000269|PubMed:12807874, ECO:0000269|PubMed:15790565,
CC ECO:0000269|PubMed:29567832}.
CC -!- INDUCTION: Down-regulated in liver by fasting and rose by refeeding.
CC {ECO:0000269|PubMed:12807874, ECO:0000269|PubMed:29567832}.
CC -!- PTM: Not glycosylated. {ECO:0000250|UniProtKB:Q8TC12}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice are fertile and developed normally
CC but exhibit delayed dark adaptation vision (PubMed:15790565). Testis
CC and livers of deficient mice exhibit a lower rate of all-trans-retinal
CC conversion to all-trans-retinol (PubMed:29567832).
CC {ECO:0000269|PubMed:15790565, ECO:0000269|PubMed:29567832}.
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:Q8TC12}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA88521.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB035959; BAA88521.1; ALT_FRAME; mRNA.
DR EMBL; AY039032; AAK91516.1; -; mRNA.
DR EMBL; AF474027; AAL79910.1; -; mRNA.
DR EMBL; AK004413; BAB23296.1; -; mRNA.
DR EMBL; AK135443; BAE22534.1; -; mRNA.
DR EMBL; BC018261; AAH18261.1; -; mRNA.
DR CCDS; CCDS36480.1; -. [Q9QYF1-1]
DR RefSeq; NP_067532.2; NM_021557.5. [Q9QYF1-1]
DR AlphaFoldDB; Q9QYF1; -.
DR SMR; Q9QYF1; -.
DR BioGRID; 201376; 2.
DR IntAct; Q9QYF1; 1.
DR STRING; 10090.ENSMUSP00000124066; -.
DR iPTMnet; Q9QYF1; -.
DR PhosphoSitePlus; Q9QYF1; -.
DR SwissPalm; Q9QYF1; -.
DR EPD; Q9QYF1; -.
DR jPOST; Q9QYF1; -.
DR MaxQB; Q9QYF1; -.
DR PaxDb; Q9QYF1; -.
DR PeptideAtlas; Q9QYF1; -.
DR PRIDE; Q9QYF1; -.
DR ProteomicsDB; 253189; -. [Q9QYF1-1]
DR DNASU; 17252; -.
DR Ensembl; ENSMUST00000161204; ENSMUSP00000124066; ENSMUSG00000066441. [Q9QYF1-1]
DR GeneID; 17252; -.
DR KEGG; mmu:17252; -.
DR UCSC; uc007oaa.1; mouse. [Q9QYF1-1]
DR CTD; 51109; -.
DR MGI; MGI:102581; Rdh11.
DR VEuPathDB; HostDB:ENSMUSG00000066441; -.
DR eggNOG; KOG1208; Eukaryota.
DR GeneTree; ENSGT00940000158191; -.
DR InParanoid; Q9QYF1; -.
DR OMA; APHIRRY; -.
DR OrthoDB; 1032903at2759; -.
DR PhylomeDB; Q9QYF1; -.
DR TreeFam; TF105429; -.
DR BRENDA; 1.1.1.300; 3474.
DR Reactome; R-MMU-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-MMU-5365859; RA biosynthesis pathway.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR UniPathway; UPA00912; -.
DR BioGRID-ORCS; 17252; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Rdh11; mouse.
DR PRO; PR:Q9QYF1; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9QYF1; protein.
DR Bgee; ENSMUSG00000066441; Expressed in spermatocyte and 261 other tissues.
DR ExpressionAtlas; Q9QYF1; baseline and differential.
DR Genevisible; Q9QYF1; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR GO; GO:0102354; F:11-cis-retinol dehydrogenase activity; IEA:RHEA.
DR GO; GO:0033721; F:aldehyde dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; ISO:MGI.
DR GO; GO:0016062; P:adaptation of rhodopsin mediated signaling; IMP:MGI.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; IDA:UniProtKB.
DR GO; GO:0042574; P:retinal metabolic process; ISO:MGI.
DR GO; GO:0001523; P:retinoid metabolic process; ISO:MGI.
DR GO; GO:0042572; P:retinol metabolic process; IMP:UniProtKB.
DR GO; GO:0007601; P:visual perception; IMP: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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Endoplasmic reticulum; Lipid metabolism;
KW Membrane; NADP; Oxidoreductase; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..316
FT /note="Retinol dehydrogenase 11"
FT /id="PRO_0000054764"
FT TRANSMEM 1..21
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000269|PubMed:12807874"
FT TOPO_DOM 22..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:12807874"
FT ACT_SITE 199
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 45..51
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8TC12"
FT CONFLICT 238
FT /note="R -> G (in Ref. 1; BAA88521)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="S -> R (in Ref. 1; BAA88521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 35148 MW; 62FAE25585CC05FE CRC64;
MFGFLLLLSL PFILYLVTPK IRKMLSSGVC TSNVQLPGKV AIVTGANTGI GKETAKDLAQ
RGARVYLACR DVDKGELAAR EIQAVTGNSQ VFVRKLDLAD TKSIRAFAKD FLAEEKHLHL
LINNAGVMMC PYSKTADGFE MHIGVNHLGH FLLTHLLLEK LKESAPSRIV NLSSLGHHLG
RIHFHNLQGE KFYSAGLAYC HSKLANILFT KELAKRLKGS GVTTYSVHPG TVHSELTRYS
SIMRWLWQLF FVFIKTPQEG AQTSLYCALT EGLESLSGSH FSDCQLAWVS YQGRNEIIAR
RLWDVSCDLL GLPVDW
