RDH11_HUMAN
ID RDH11_HUMAN Reviewed; 318 AA.
AC Q8TC12; A6NDK3; A8K062; B2RB26; B4DDW0; Q0QD40; Q6IAH5; Q9NRW0; Q9Y391;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Retinol dehydrogenase 11;
DE EC=1.1.1.300 {ECO:0000269|PubMed:12036956, ECO:0000269|PubMed:12226107};
DE AltName: Full=Androgen-regulated short-chain dehydrogenase/reductase 1 {ECO:0000303|PubMed:11245473};
DE AltName: Full=HCV core-binding protein HCBP12;
DE AltName: Full=Prostate short-chain dehydrogenase/reductase 1;
DE AltName: Full=Retinal reductase 1 {ECO:0000303|PubMed:12036956};
DE Short=RalR1 {ECO:0000303|PubMed:12036956};
DE AltName: Full=Short chain dehydrogenase/reductase family 7C member 1;
GN Name=RDH11; Synonyms=ARSDR1, PSDR1, SDR7C1; ORFNames=CGI-82;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Prostate;
RX PubMed=11245473;
RA Lin B., White J.T., Ferguson C., Wang S., Vessella R., Bumgarner R.,
RA True L.D., Hood L., Nelson P.S.;
RT "Prostate short-chain dehydrogenase reductase 1 (PSDR1): a new member of
RT the short-chain steroid dehydrogenase/reductase family highly expressed in
RT normal and neoplastic prostate epithelium.";
RL Cancer Res. 61:1611-1618(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Li K., Wang L., Cheng J., Zhang L., Lu Y., Liu Y., Duan H.;
RT "Screening of HCV core binding protein from human liver cDNA library by
RT using yeast two hybrid system.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Synovium, and Urinary bladder;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Muscle, Placenta, and Prostate;
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-171 (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=17286855; DOI=10.1186/1471-2164-8-42;
RA Roni V., Carpio R., Wissinger B.;
RT "Mapping of transcription start sites of human retina expressed genes.";
RL BMC Genomics 8:42-42(2007).
RN [11]
RP IDENTIFICATION AS A RETINAL REDUCTASE, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TOPOLOGY.
RX PubMed=12036956; DOI=10.1074/jbc.m202588200;
RA Kedishvili N.Y., Chumakova O.V., Chetyrkin S.V., Belyaeva O.V.,
RA Lapshina E.A., Lin D.W., Matsumura M., Nelson P.S.;
RT "Evidence that the human gene for prostate short-chain
RT dehydrogenase/reductase (PSDR1) encodes a novel retinal reductase
RT (RalR1).";
RL J. Biol. Chem. 277:28909-28915(2002).
RN [12]
RP CATALYTIC ACTIVITY, FUNCTION, SUBSTRATE SPECIFICITY, AND TOPOLOGY.
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).
RN [13]
RP CAUTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15865448; DOI=10.1021/bi050226k;
RA Belyaeva O.V., Korkina O.V., Stetsenko A.V., Kim T., Nelson P.S.,
RA Kedishvili N.Y.;
RT "Biochemical properties of purified human retinol dehydrogenase 12 (RDH12):
RT catalytic efficiency toward retinoids and C9 aldehydes and effects of
RT cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-
RT binding protein (CRALBP) on the oxidation and reduction of retinoids.";
RL Biochemistry 44:7035-7047(2005).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP INVOLVEMENT IN RDJCSS.
RX PubMed=24916380; DOI=10.1093/hmg/ddu291;
RA Xie Y.A., Lee W., Cai C., Gambin T., Noupuu K., Sujirakul T., Ayuso C.,
RA Jhangiani S., Muzny D., Boerwinkle E., Gibbs R., Greenstein V.C.,
RA Lupski J.R., Tsang S.H., Allikmets R.;
RT "New syndrome with retinitis pigmentosa is caused by nonsense mutations in
RT retinol dehydrogenase RDH11.";
RL Hum. Mol. Genet. 23:5774-5780(2014).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP INTERACTION WITH SELENOF, ACTIVITY REGULATION, CATALYTIC ACTIVITY, AND
RP FUNCTION.
RX PubMed=29410696; DOI=10.1186/s12986-017-0235-x;
RA Tian J., Liu J., Li J., Zheng J., Chen L., Wang Y., Liu Q., Ni J.;
RT "The interaction of selenoprotein F (SELENOF) with retinol dehydrogenase 11
RT (RDH11) implied a role of SELENOF in vitamin A metabolism.";
RL Nutr. Metab. 15:7-7(2018).
CC -!- FUNCTION: Retinol dehydrogenase with a clear preference for NADP.
CC Displays high activity towards 9-cis, 11-cis and all-trans-retinol, and
CC to a lesser extent on 13-cis-retinol (PubMed:12226107, PubMed:12036956,
CC PubMed:29410696). Exhibits a low reductive activity towards unsaturated
CC medium-chain aldehydes such as cis -6-nonenal and no activity toward
CC nonanal or 4-hydroxy-nonenal (PubMed:15865448). Has no dehydrogenase
CC activity towards steroid (PubMed:12226107, PubMed:12036956).
CC {ECO:0000269|PubMed:12036956, ECO:0000269|PubMed:12226107,
CC ECO:0000269|PubMed:15865448, ECO:0000269|PubMed:29410696}.
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:12036956,
CC ECO:0000269|PubMed:12226107, ECO:0000269|PubMed:29410696};
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:0000269|PubMed:12036956, ECO:0000269|PubMed:12226107};
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:12036956, ECO:0000269|PubMed:12226107};
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:0000269|PubMed:12036956, ECO:0000269|PubMed:12226107};
CC -!- ACTIVITY REGULATION: SELENOF decreases the retinol dehydrogenase
CC activity. {ECO:0000269|PubMed:29410696}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.23 uM for NADPH {ECO:0000269|PubMed:12036956};
CC KM=0.8 uM for NADP {ECO:0000269|PubMed:12036956};
CC KM=0.5 uM for all-trans-retinal {ECO:0000269|PubMed:12036956};
CC KM=0.62 uM for 13-cis-retinal {ECO:0000269|PubMed:12036956};
CC KM=0.19 uM for 9-cis-retinal {ECO:0000269|PubMed:12036956};
CC KM=1.3 uM for all-trans-retinol {ECO:0000269|PubMed:12036956};
CC KM=5 uM for (Z)-non-6-enol {ECO:0000269|PubMed:15865448};
CC Vmax=18 nmol/min/mg enzyme with all-trans-retinal as substrate
CC {ECO:0000269|PubMed:12036956};
CC Vmax=7 nmol/min/mg enzyme with 13-cis-retinal as substrate
CC {ECO:0000269|PubMed:12036956};
CC Vmax=1.6 nmol/min/mg enzyme with 9-cis-retinal as substrate
CC {ECO:0000269|PubMed:12036956};
CC Vmax=0.95 nmol/min/mg enzyme with all-trans-retinol as substrate
CC {ECO:0000269|PubMed:12036956};
CC Vmax=19 nmol/min/mg enzyme with (Z)-non-6-enol
CC {ECO:0000269|PubMed:15865448};
CC Note=Vmax is measured per mg microsomal protein.;
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000269|PubMed:12036956, ECO:0000269|PubMed:12226107}.
CC -!- SUBUNIT: Interacts with SELENOF. {ECO:0000269|PubMed:29410696}.
CC -!- INTERACTION:
CC Q8TC12; O60613: SELENOF; NbExp=5; IntAct=EBI-2823756, EBI-1052797;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12036956}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:12036956}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TC12-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TC12-2; Sequence=VSP_008159;
CC Name=3;
CC IsoId=Q8TC12-3; Sequence=VSP_046403;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the epithelial cells of
CC prostate, in both basal and luminal secretory cell populations.
CC Expressed at low levels in spleen, thymus, testis, ovary, small
CC intestine, colon, peripherical blood leukocytes, kidney, adrenal gland
CC and fetal liver. Not detected in prostatic fibromuscular stromal cells,
CC endothelial cells, or infiltrating lymphocytes.
CC {ECO:0000269|PubMed:11245473}.
CC -!- INDUCTION: By androgens in prostate cancer cells.
CC {ECO:0000269|PubMed:11245473}.
CC -!- PTM: Not glycosylated. {ECO:0000269|PubMed:11245473}.
CC -!- DISEASE: Retinal dystrophy, juvenile cataracts, and short stature
CC syndrome (RDJCSS) [MIM:616108]: A disorder characterized by retinal
CC dystrophy resulting in progressive decrease in visual acuity and
CC difficulties with night vision in the first decade of life, development
CC of juvenile cataracts, facial dysmorphism, psychomotor developmental
CC delays, learning disabilities and short stature. Ophthalmological
CC findings include salt-and-pepper retinopathy, attenuation of the
CC arterioles, generalized rod-cone dysfunction, mottled macula at an
CC early age, and peripapillary sparing of the retinal pigment epithelium.
CC {ECO:0000269|PubMed:24916380}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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:0000269|PubMed:12226107}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- CAUTION: In contrast to mouse, human RDH11 exhibits little or no
CC activity towards toxic lipid peroxidation products, such as nonanal or
CC 4-hydroxy-nonenal. {ECO:0000269|PubMed:15865448}.
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DR EMBL; AF167438; AAF89632.1; -; mRNA.
DR EMBL; AF395068; AAK72049.1; -; mRNA.
DR EMBL; AF151840; AAD34077.1; -; mRNA.
DR EMBL; CR457180; CAG33461.1; -; mRNA.
DR EMBL; AK289427; BAF82116.1; -; mRNA.
DR EMBL; AK293355; BAG56871.1; -; mRNA.
DR EMBL; AK314465; BAG37073.1; -; mRNA.
DR EMBL; AK074749; BAG51997.1; -; mRNA.
DR EMBL; AL049779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW80950.1; -; Genomic_DNA.
DR EMBL; BC000112; AAH00112.1; -; mRNA.
DR EMBL; BC011727; AAH11727.1; -; mRNA.
DR EMBL; BC026274; AAH26274.1; -; mRNA.
DR EMBL; BC037302; AAH37302.1; -; mRNA.
DR EMBL; BC051291; AAH51291.1; -; mRNA.
DR EMBL; DQ426886; ABD90542.1; -; mRNA.
DR CCDS; CCDS32104.1; -. [Q8TC12-1]
DR CCDS; CCDS58326.1; -. [Q8TC12-3]
DR RefSeq; NP_001239579.1; NM_001252650.1. [Q8TC12-3]
DR RefSeq; NP_057110.3; NM_016026.3. [Q8TC12-1]
DR AlphaFoldDB; Q8TC12; -.
DR SMR; Q8TC12; -.
DR BioGRID; 119298; 142.
DR IntAct; Q8TC12; 26.
DR MINT; Q8TC12; -.
DR STRING; 9606.ENSP00000370750; -.
DR DrugBank; DB00162; Vitamin A.
DR SwissLipids; SLP:000001785; -.
DR CarbonylDB; Q8TC12; -.
DR GlyGen; Q8TC12; 1 site.
DR iPTMnet; Q8TC12; -.
DR PhosphoSitePlus; Q8TC12; -.
DR SwissPalm; Q8TC12; -.
DR BioMuta; RDH11; -.
DR DMDM; 34395789; -.
DR EPD; Q8TC12; -.
DR jPOST; Q8TC12; -.
DR MassIVE; Q8TC12; -.
DR MaxQB; Q8TC12; -.
DR PaxDb; Q8TC12; -.
DR PeptideAtlas; Q8TC12; -.
DR PRIDE; Q8TC12; -.
DR ProteomicsDB; 3897; -.
DR ProteomicsDB; 74069; -. [Q8TC12-1]
DR ProteomicsDB; 74070; -. [Q8TC12-2]
DR Antibodypedia; 12201; 242 antibodies from 28 providers.
DR DNASU; 51109; -.
DR Ensembl; ENST00000381346.9; ENSP00000370750.4; ENSG00000072042.13. [Q8TC12-1]
DR Ensembl; ENST00000428130.6; ENSP00000416395.2; ENSG00000072042.13. [Q8TC12-3]
DR Ensembl; ENST00000553384.5; ENSP00000452079.1; ENSG00000072042.13. [Q8TC12-2]
DR GeneID; 51109; -.
DR KEGG; hsa:51109; -.
DR MANE-Select; ENST00000381346.9; ENSP00000370750.4; NM_016026.4; NP_057110.3.
DR UCSC; uc001xjv.6; human. [Q8TC12-1]
DR CTD; 51109; -.
DR DisGeNET; 51109; -.
DR GeneCards; RDH11; -.
DR HGNC; HGNC:17964; RDH11.
DR HPA; ENSG00000072042; Tissue enhanced (prostate).
DR MalaCards; RDH11; -.
DR MIM; 607849; gene.
DR MIM; 616108; phenotype.
DR neXtProt; NX_Q8TC12; -.
DR OpenTargets; ENSG00000072042; -.
DR Orphanet; 436245; Retinitis pigmentosa-juvenile cataract-short stature-intellectual disability syndrome.
DR PharmGKB; PA134981588; -.
DR VEuPathDB; HostDB:ENSG00000072042; -.
DR eggNOG; KOG1208; Eukaryota.
DR GeneTree; ENSGT00940000158191; -.
DR InParanoid; Q8TC12; -.
DR OMA; APHIRRY; -.
DR PhylomeDB; Q8TC12; -.
DR TreeFam; TF105429; -.
DR BioCyc; MetaCyc:HS01050-MON; -.
DR BRENDA; 1.1.1.300; 2681.
DR PathwayCommons; Q8TC12; -.
DR Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-HSA-5365859; RA biosynthesis pathway.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SABIO-RK; Q8TC12; -.
DR SignaLink; Q8TC12; -.
DR UniPathway; UPA00912; -.
DR BioGRID-ORCS; 51109; 14 hits in 1077 CRISPR screens.
DR ChiTaRS; RDH11; human.
DR GeneWiki; RDH11; -.
DR GenomeRNAi; 51109; -.
DR Pharos; Q8TC12; Tbio.
DR PRO; PR:Q8TC12; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q8TC12; protein.
DR Bgee; ENSG00000072042; Expressed in pigmented layer of retina and 207 other tissues.
DR ExpressionAtlas; Q8TC12; baseline and differential.
DR Genevisible; Q8TC12; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR GO; GO:0102354; F:11-cis-retinol dehydrogenase activity; IEA:RHEA.
DR GO; GO:0033721; F:aldehyde dehydrogenase (NADP+) activity; IEA:Ensembl.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; TAS:Reactome.
DR GO; GO:0016062; P:adaptation of rhodopsin mediated signaling; IEA:Ensembl.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; IDA:UniProtKB.
DR GO; GO:0042574; P:retinal metabolic process; IDA:MGI.
DR GO; GO:0001523; P:retinoid metabolic process; IDA:UniProtKB.
DR GO; GO:0042572; P:retinol metabolic process; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
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; Cataract; Dwarfism;
KW Endoplasmic reticulum; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..318
FT /note="Retinol dehydrogenase 11"
FT /id="PRO_0000054763"
FT TRANSMEM 1..21
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000269|PubMed:12036956,
FT ECO:0000269|PubMed:12226107"
FT TOPO_DOM 22..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:12036956,
FT ECO:0000269|PubMed:12226107"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
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 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 52..64
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008159"
FT VAR_SEQ 152..221
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046403"
FT CONFLICT 176
FT /note="S -> F (in Ref. 9; AAH51291)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="A -> V (in Ref. 1; AAF89632)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="P -> S (in Ref. 9; AAH26274)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 35386 MW; 5B0C366552774835 CRC64;
MVELMFPLLL LLLPFLLYMA APQIRKMLSS GVCTSTVQLP GKVVVVTGAN TGIGKETAKE
LAQRGARVYL ACRDVEKGEL VAKEIQTTTG NQQVLVRKLD LSDTKSIRAF AKGFLAEEKH
LHVLINNAGV MMCPYSKTAD GFEMHIGVNH LGHFLLTHLL LEKLKESAPS RIVNVSSLAH
HLGRIHFHNL QGEKFYNAGL AYCHSKLANI LFTQELARRL KGSGVTTYSV HPGTVQSELV
RHSSFMRWMW WLFSFFIKTP QQGAQTSLHC ALTEGLEILS GNHFSDCHVA WVSAQARNET
IARRLWDVSC DLLGLPID
