Full text data of RDH11
RDH11
(ARSDR1, PSDR1)
[Confidence: high (present in two of the MS resources)]
Retinol dehydrogenase 11; 1.1.1.300 (Androgen-regulated short-chain dehydrogenase/reductase 1; HCV core-binding protein HCBP12; Prostate short-chain dehydrogenase/reductase 1; Retinal reductase 1; RalR1)
Retinol dehydrogenase 11; 1.1.1.300 (Androgen-regulated short-chain dehydrogenase/reductase 1; HCV core-binding protein HCBP12; Prostate short-chain dehydrogenase/reductase 1; Retinal reductase 1; RalR1)
UniProt
Q8TC12
ID RDH11_HUMAN Reviewed; 318 AA.
AC Q8TC12; A6NDK3; A8K062; B2RB26; B4DDW0; Q0QD40; Q6IAH5; Q9NRW0;
read moreAC Q9Y391;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Retinol dehydrogenase 11;
DE EC=1.1.1.300;
DE AltName: Full=Androgen-regulated short-chain dehydrogenase/reductase 1;
DE AltName: Full=HCV core-binding protein HCBP12;
DE AltName: Full=Prostate short-chain dehydrogenase/reductase 1;
DE AltName: Full=Retinal reductase 1;
DE Short=RalR1;
GN Name=RDH11; Synonyms=ARSDR1, PSDR1; ORFNames=CGI-82;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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
RT of the short-chain steroid dehydrogenase/reductase family highly
RT expressed in 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
RT by 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA 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.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA 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.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT genes.";
RL BMC Genomics 8:42-42(2007).
RN [11]
RP IDENTIFICATION AS A RETINAL REDUCTASE, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [13]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Exhibits an oxidoreductive catalytic activity towards
CC retinoids. Most efficient as an NADPH-dependent retinal reductase.
CC Displays high activity towards 9-cis and all-trans-retinol. Also
CC involved in the metabolism of short-chain aldehydes. No steroid
CC dehydrogenase activity detected.
CC -!- CATALYTIC ACTIVITY: All-trans-retinol + NADP(+) = all-trans-
CC retinal + NADPH.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.23 uM for NADPH;
CC KM=0.8 uM for NADP;
CC KM=0.5 uM for all-trans-retinal;
CC KM=0.62 uM for 13-cis-retinal;
CC KM=0.19 uM for 9-cis-retinal;
CC KM=1.3 uM for all-trans-retinol;
CC Vmax=18 nmol/min/mg enzyme with all-trans-retinal as substrate;
CC Vmax=7 nmol/min/mg enzyme with 13-cis-retinal as substrate;
CC Vmax=1.6 nmol/min/mg enzyme with 9-cis-retinal as substrate;
CC Vmax=0.95 nmol/min/mg enzyme with all-trans-retinol as
CC substrate;
CC Note=Vmax is measured per mg microsomal protein;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type II membrane protein.
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 Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q8TC12-3; Sequence=VSP_046403;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the epithelial
CC cells of prostate, in both basal and luminal secretory cell
CC populations. Expressed at low levels in spleen, thymus, testis,
CC ovary, small intestine, colon, peripherical blood leukocytes,
CC kidney, adrenal gland and fetal liver. Not detected in prostatic
CC fibromuscular stromal cells, endothelial cells, or infiltrating
CC lymphocytes.
CC -!- INDUCTION: By androgens in prostate cancer cells.
CC -!- PTM: Not glycosylated.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC (SDR) family.
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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 RefSeq; NP_001239579.1; NM_001252650.1.
DR RefSeq; NP_057110.3; NM_016026.3.
DR RefSeq; XP_005267789.1; XM_005267732.1.
DR UniGene; Hs.719925; -.
DR ProteinModelPortal; Q8TC12; -.
DR SMR; Q8TC12; 39-297.
DR IntAct; Q8TC12; 5.
DR STRING; 9606.ENSP00000370750; -.
DR DrugBank; DB00162; Vitamin A.
DR PhosphoSite; Q8TC12; -.
DR DMDM; 34395789; -.
DR PaxDb; Q8TC12; -.
DR PRIDE; Q8TC12; -.
DR DNASU; 51109; -.
DR Ensembl; ENST00000381346; ENSP00000370750; ENSG00000072042.
DR Ensembl; ENST00000428130; ENSP00000416395; ENSG00000072042.
DR Ensembl; ENST00000553384; ENSP00000452079; ENSG00000072042.
DR GeneID; 51109; -.
DR KEGG; hsa:51109; -.
DR UCSC; uc001xjx.4; human.
DR CTD; 51109; -.
DR GeneCards; GC14M068143; -.
DR HGNC; HGNC:17964; RDH11.
DR HPA; CAB046011; -.
DR MIM; 607849; gene.
DR neXtProt; NX_Q8TC12; -.
DR PharmGKB; PA134981588; -.
DR eggNOG; COG1028; -.
DR HOVERGEN; HBG078800; -.
DR InParanoid; Q8TC12; -.
DR KO; K11152; -.
DR OMA; TTARRLW; -.
DR OrthoDB; EOG73Z2TK; -.
DR BioCyc; MetaCyc:HS01050-MONOMER; -.
DR BRENDA; 1.1.1.105; 2681.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR SABIO-RK; Q8TC12; -.
DR ChiTaRS; RDH11; human.
DR GeneWiki; RDH11; -.
DR GenomeRNAi; 51109; -.
DR NextBio; 53857; -.
DR PRO; PR:Q8TC12; -.
DR ArrayExpress; Q8TC12; -.
DR Bgee; Q8TC12; -.
DR CleanEx; HS_RDH11; -.
DR Genevestigator; Q8TC12; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IDA:MGI.
DR GO; GO:0004745; F:retinol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0007603; P:phototransduction, visible light; TAS:Reactome.
DR GO; GO:0042574; P:retinal metabolic process; IDA:MGI.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR InterPro; IPR002347; Glc/ribitol_DH.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR PROSITE; PS00061; ADH_SHORT; FALSE_NEG.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Endoplasmic reticulum; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1 318 Retinol dehydrogenase 11.
FT /FTId=PRO_0000054763.
FT TRANSMEM 1 21 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 22 318 Cytoplasmic (Potential).
FT NP_BIND 48 54 NADP (By similarity).
FT ACT_SITE 202 202 Proton acceptor (By similarity).
FT BINDING 177 177 Substrate (By similarity).
FT MOD_RES 112 112 N6-acetyllysine.
FT VAR_SEQ 52 64 Missing (in isoform 2).
FT /FTId=VSP_008159.
FT VAR_SEQ 152 221 Missing (in isoform 3).
FT /FTId=VSP_046403.
FT CONFLICT 176 176 S -> F (in Ref. 9; AAH51291).
FT CONFLICT 294 294 A -> V (in Ref. 1; AAF89632).
FT CONFLICT 316 316 P -> S (in Ref. 9; AAH26274).
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
//
ID RDH11_HUMAN Reviewed; 318 AA.
AC Q8TC12; A6NDK3; A8K062; B2RB26; B4DDW0; Q0QD40; Q6IAH5; Q9NRW0;
read moreAC Q9Y391;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Retinol dehydrogenase 11;
DE EC=1.1.1.300;
DE AltName: Full=Androgen-regulated short-chain dehydrogenase/reductase 1;
DE AltName: Full=HCV core-binding protein HCBP12;
DE AltName: Full=Prostate short-chain dehydrogenase/reductase 1;
DE AltName: Full=Retinal reductase 1;
DE Short=RalR1;
GN Name=RDH11; Synonyms=ARSDR1, PSDR1; ORFNames=CGI-82;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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
RT of the short-chain steroid dehydrogenase/reductase family highly
RT expressed in 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
RT by 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA 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.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA 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.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT genes.";
RL BMC Genomics 8:42-42(2007).
RN [11]
RP IDENTIFICATION AS A RETINAL REDUCTASE, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [13]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Exhibits an oxidoreductive catalytic activity towards
CC retinoids. Most efficient as an NADPH-dependent retinal reductase.
CC Displays high activity towards 9-cis and all-trans-retinol. Also
CC involved in the metabolism of short-chain aldehydes. No steroid
CC dehydrogenase activity detected.
CC -!- CATALYTIC ACTIVITY: All-trans-retinol + NADP(+) = all-trans-
CC retinal + NADPH.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.23 uM for NADPH;
CC KM=0.8 uM for NADP;
CC KM=0.5 uM for all-trans-retinal;
CC KM=0.62 uM for 13-cis-retinal;
CC KM=0.19 uM for 9-cis-retinal;
CC KM=1.3 uM for all-trans-retinol;
CC Vmax=18 nmol/min/mg enzyme with all-trans-retinal as substrate;
CC Vmax=7 nmol/min/mg enzyme with 13-cis-retinal as substrate;
CC Vmax=1.6 nmol/min/mg enzyme with 9-cis-retinal as substrate;
CC Vmax=0.95 nmol/min/mg enzyme with all-trans-retinol as
CC substrate;
CC Note=Vmax is measured per mg microsomal protein;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type II membrane protein.
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 Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q8TC12-3; Sequence=VSP_046403;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the epithelial
CC cells of prostate, in both basal and luminal secretory cell
CC populations. Expressed at low levels in spleen, thymus, testis,
CC ovary, small intestine, colon, peripherical blood leukocytes,
CC kidney, adrenal gland and fetal liver. Not detected in prostatic
CC fibromuscular stromal cells, endothelial cells, or infiltrating
CC lymphocytes.
CC -!- INDUCTION: By androgens in prostate cancer cells.
CC -!- PTM: Not glycosylated.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC (SDR) family.
CC -----------------------------------------------------------------------
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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 RefSeq; NP_001239579.1; NM_001252650.1.
DR RefSeq; NP_057110.3; NM_016026.3.
DR RefSeq; XP_005267789.1; XM_005267732.1.
DR UniGene; Hs.719925; -.
DR ProteinModelPortal; Q8TC12; -.
DR SMR; Q8TC12; 39-297.
DR IntAct; Q8TC12; 5.
DR STRING; 9606.ENSP00000370750; -.
DR DrugBank; DB00162; Vitamin A.
DR PhosphoSite; Q8TC12; -.
DR DMDM; 34395789; -.
DR PaxDb; Q8TC12; -.
DR PRIDE; Q8TC12; -.
DR DNASU; 51109; -.
DR Ensembl; ENST00000381346; ENSP00000370750; ENSG00000072042.
DR Ensembl; ENST00000428130; ENSP00000416395; ENSG00000072042.
DR Ensembl; ENST00000553384; ENSP00000452079; ENSG00000072042.
DR GeneID; 51109; -.
DR KEGG; hsa:51109; -.
DR UCSC; uc001xjx.4; human.
DR CTD; 51109; -.
DR GeneCards; GC14M068143; -.
DR HGNC; HGNC:17964; RDH11.
DR HPA; CAB046011; -.
DR MIM; 607849; gene.
DR neXtProt; NX_Q8TC12; -.
DR PharmGKB; PA134981588; -.
DR eggNOG; COG1028; -.
DR HOVERGEN; HBG078800; -.
DR InParanoid; Q8TC12; -.
DR KO; K11152; -.
DR OMA; TTARRLW; -.
DR OrthoDB; EOG73Z2TK; -.
DR BioCyc; MetaCyc:HS01050-MONOMER; -.
DR BRENDA; 1.1.1.105; 2681.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR SABIO-RK; Q8TC12; -.
DR ChiTaRS; RDH11; human.
DR GeneWiki; RDH11; -.
DR GenomeRNAi; 51109; -.
DR NextBio; 53857; -.
DR PRO; PR:Q8TC12; -.
DR ArrayExpress; Q8TC12; -.
DR Bgee; Q8TC12; -.
DR CleanEx; HS_RDH11; -.
DR Genevestigator; Q8TC12; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IDA:MGI.
DR GO; GO:0004745; F:retinol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0007603; P:phototransduction, visible light; TAS:Reactome.
DR GO; GO:0042574; P:retinal metabolic process; IDA:MGI.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR InterPro; IPR002347; Glc/ribitol_DH.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR PROSITE; PS00061; ADH_SHORT; FALSE_NEG.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Endoplasmic reticulum; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1 318 Retinol dehydrogenase 11.
FT /FTId=PRO_0000054763.
FT TRANSMEM 1 21 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 22 318 Cytoplasmic (Potential).
FT NP_BIND 48 54 NADP (By similarity).
FT ACT_SITE 202 202 Proton acceptor (By similarity).
FT BINDING 177 177 Substrate (By similarity).
FT MOD_RES 112 112 N6-acetyllysine.
FT VAR_SEQ 52 64 Missing (in isoform 2).
FT /FTId=VSP_008159.
FT VAR_SEQ 152 221 Missing (in isoform 3).
FT /FTId=VSP_046403.
FT CONFLICT 176 176 S -> F (in Ref. 9; AAH51291).
FT CONFLICT 294 294 A -> V (in Ref. 1; AAF89632).
FT CONFLICT 316 316 P -> S (in Ref. 9; AAH26274).
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
//
MIM
607849
*RECORD*
*FIELD* NO
607849
*FIELD* TI
*607849 RETINOL DEHYDROGENASE 11; RDH11
;;PROSTATE SHORT-CHAIN DEHYDROGENASE/REDUCTASE 1; PSDR1;;
read moreRETINAL REDUCTASE 1; RALR1
*FIELD* TX
DESCRIPTION
RHD11, a member of the short-chain dehydrogenase/reductase (SDR)
superfamily of oxidoreductases, is expressed at high levels in prostate
epithelium, and its expression is regulated by androgens.
CLONING
Using microarrays, Lin et al. (2001) found that RDH11, which they
designated PSDR1, was upregulated by synthetic androgen in an
androgen-sensitive prostate cancer cell line. By database analysis and
screening of a prostate cDNA library, they cloned full-length RDH11. The
deduced protein contains 318 amino acids, and the transcript contains 2
potential polyadenylation signals. RDH11 shares conserved motifs with
the SDR family of oxidoreductases, including an N-terminal
coenzyme-binding motif, which binds NAD(H) or NADP(H), and a C-terminal
catalytic domain. RDH11 shares about 25% sequence identity with other
SDR family members. Northern blot and RNA dot blot analyses detected a
2.5-kb transcript expressed at a high level in prostate and at low
levels in other tissues, including spleen, thymus, testis, ovary, small
intestine, colon, peripheral blood leukocytes, kidney, adrenal gland,
and fetal liver. Testis expressed an additional transcript of about 0.9
kb. In situ hybridization of normal prostate detected RDH11 expression
in basal and luminal epithelial cells, but not in fibromuscular stromal
cells, endothelial cells, or infiltrating lymphocytes. Primary prostate
adenocarcinoma cells were uniformly positive for RDH11 expression.
Kedishvili et al. (2002) determined that RDH11, which they called RALR1,
localized to the endoplasmic reticulum when transfected into COS-7
cells.
Moore et al. (2002) cloned mouse Rdh11. The deduced 316-amino acid
protein shares 85% identity with human RDH11. Northern blot analysis
detected highest expression in testis and liver, where there were 2
Rdh11 isoforms. RNA dot blot analysis detected expression in all tissues
examined, with highest expression in testis.
GENE FUNCTION
Kedishvili et al. (2002) characterized the substrate specificity of
recombinant RDH11 expressed in sf9 insect cells. They determined that
RDH11 had oxidoreductase activity toward retinoids but not steroids. It
also showed a preference for NADP+ and NADPH versus NAD+ and NADH as
cofactors. The enzyme was about 50-fold more efficient in the reduction
of all-trans-retinal than in the oxidation of all-trans-retinol. RDH11
reduced all-trans-retinal in the presence of a 10-fold molar excess of
cellular retinol-binding protein-1 (180260), which was believed to
sequester all-trans-retinal from nonspecific enzymes.
GENE STRUCTURE
Lin et al. (2001) determined that the RDH11 gene contains 7 exons and
spans about 18.9 kb. The promoter region contains a TATA box and
putative androgen, progesterone, and interleukin-6 (IL6; 147620)
response elements.
MAPPING
By radiation hybrid analysis, Lin et al. (2001) mapped the RDH11 gene to
chromosome 14q23-q24.3. Moore et al. (2002) mapped the mouse Rdh11 gene
to chromosome 12 in a region that shows homology of synteny to human
chromosome 14q23-q24.3.
By genomic sequence analysis, Haeseleer et al. (2002) mapped the RDH11
and RDH12 (608830) genes within about 30 kb of each other.
*FIELD* RF
1. Haeseleer, F.; Jang, G.-F.; Imanishi, Y.; Driessen, C. A. G. G.;
Matsumura, M.; Nelson, P. S.; Palczewski, K.: Dual-substrate specificity
Short chain retinol dehydrogenases from the vertebrate retina. J.
Biol. Chem. 277: 45537-45546, 2002.
2. Kedishvili, N. Y.; Chumakova, O. V.; Chetyrkin, S. V.; Belyaeva,
O. V.; Lapshina, E. A.; Lin, D. W.; Matsumura, M.; Nelson, P. S.:
Evidence that the human gene for prostate short-chain dehydrogenase/reductase
(PSDR1) encodes a novel retinal reductase (RalR1). J. Biol. Chem. 277:
28909-28915, 2002.
3. Lin, B.; White, J. T.; Ferguson, C.; Wang, S.; Vessella, R.; Bumgarner,
R.; True, L. D.; Hood, L.; Nelson, P. S.: Prostate short-chain dehydrogenase
reductase 1 (PSDR1): a new member of the short-chain steroid dehydrogenase/reductase
family highly expressed in normal and neoplastic prostate epithelium. Cancer
Res. 61: 1611-1618, 2001.
4. Moore, S.; Pritchard, C.; Lin, B.; Ferguson, C.; Nelson, P. S.
: Isolation and characterization of the murine prostate short-chain
dehydrogenase/reductase 1 (Psdr1) gene, a new member of the short-chain
steroid dehydrogenase/reductase family. Gene 293: 149-160, 2002.
*FIELD* CN
Victor A. McKusick - updated: 9/9/2004
*FIELD* CD
Patricia A. Hartz: 6/4/2003
*FIELD* ED
carol: 06/06/2007
carol: 9/9/2004
terry: 9/9/2004
terry: 7/20/2004
mgross: 6/4/2003
*RECORD*
*FIELD* NO
607849
*FIELD* TI
*607849 RETINOL DEHYDROGENASE 11; RDH11
;;PROSTATE SHORT-CHAIN DEHYDROGENASE/REDUCTASE 1; PSDR1;;
read moreRETINAL REDUCTASE 1; RALR1
*FIELD* TX
DESCRIPTION
RHD11, a member of the short-chain dehydrogenase/reductase (SDR)
superfamily of oxidoreductases, is expressed at high levels in prostate
epithelium, and its expression is regulated by androgens.
CLONING
Using microarrays, Lin et al. (2001) found that RDH11, which they
designated PSDR1, was upregulated by synthetic androgen in an
androgen-sensitive prostate cancer cell line. By database analysis and
screening of a prostate cDNA library, they cloned full-length RDH11. The
deduced protein contains 318 amino acids, and the transcript contains 2
potential polyadenylation signals. RDH11 shares conserved motifs with
the SDR family of oxidoreductases, including an N-terminal
coenzyme-binding motif, which binds NAD(H) or NADP(H), and a C-terminal
catalytic domain. RDH11 shares about 25% sequence identity with other
SDR family members. Northern blot and RNA dot blot analyses detected a
2.5-kb transcript expressed at a high level in prostate and at low
levels in other tissues, including spleen, thymus, testis, ovary, small
intestine, colon, peripheral blood leukocytes, kidney, adrenal gland,
and fetal liver. Testis expressed an additional transcript of about 0.9
kb. In situ hybridization of normal prostate detected RDH11 expression
in basal and luminal epithelial cells, but not in fibromuscular stromal
cells, endothelial cells, or infiltrating lymphocytes. Primary prostate
adenocarcinoma cells were uniformly positive for RDH11 expression.
Kedishvili et al. (2002) determined that RDH11, which they called RALR1,
localized to the endoplasmic reticulum when transfected into COS-7
cells.
Moore et al. (2002) cloned mouse Rdh11. The deduced 316-amino acid
protein shares 85% identity with human RDH11. Northern blot analysis
detected highest expression in testis and liver, where there were 2
Rdh11 isoforms. RNA dot blot analysis detected expression in all tissues
examined, with highest expression in testis.
GENE FUNCTION
Kedishvili et al. (2002) characterized the substrate specificity of
recombinant RDH11 expressed in sf9 insect cells. They determined that
RDH11 had oxidoreductase activity toward retinoids but not steroids. It
also showed a preference for NADP+ and NADPH versus NAD+ and NADH as
cofactors. The enzyme was about 50-fold more efficient in the reduction
of all-trans-retinal than in the oxidation of all-trans-retinol. RDH11
reduced all-trans-retinal in the presence of a 10-fold molar excess of
cellular retinol-binding protein-1 (180260), which was believed to
sequester all-trans-retinal from nonspecific enzymes.
GENE STRUCTURE
Lin et al. (2001) determined that the RDH11 gene contains 7 exons and
spans about 18.9 kb. The promoter region contains a TATA box and
putative androgen, progesterone, and interleukin-6 (IL6; 147620)
response elements.
MAPPING
By radiation hybrid analysis, Lin et al. (2001) mapped the RDH11 gene to
chromosome 14q23-q24.3. Moore et al. (2002) mapped the mouse Rdh11 gene
to chromosome 12 in a region that shows homology of synteny to human
chromosome 14q23-q24.3.
By genomic sequence analysis, Haeseleer et al. (2002) mapped the RDH11
and RDH12 (608830) genes within about 30 kb of each other.
*FIELD* RF
1. Haeseleer, F.; Jang, G.-F.; Imanishi, Y.; Driessen, C. A. G. G.;
Matsumura, M.; Nelson, P. S.; Palczewski, K.: Dual-substrate specificity
Short chain retinol dehydrogenases from the vertebrate retina. J.
Biol. Chem. 277: 45537-45546, 2002.
2. Kedishvili, N. Y.; Chumakova, O. V.; Chetyrkin, S. V.; Belyaeva,
O. V.; Lapshina, E. A.; Lin, D. W.; Matsumura, M.; Nelson, P. S.:
Evidence that the human gene for prostate short-chain dehydrogenase/reductase
(PSDR1) encodes a novel retinal reductase (RalR1). J. Biol. Chem. 277:
28909-28915, 2002.
3. Lin, B.; White, J. T.; Ferguson, C.; Wang, S.; Vessella, R.; Bumgarner,
R.; True, L. D.; Hood, L.; Nelson, P. S.: Prostate short-chain dehydrogenase
reductase 1 (PSDR1): a new member of the short-chain steroid dehydrogenase/reductase
family highly expressed in normal and neoplastic prostate epithelium. Cancer
Res. 61: 1611-1618, 2001.
4. Moore, S.; Pritchard, C.; Lin, B.; Ferguson, C.; Nelson, P. S.
: Isolation and characterization of the murine prostate short-chain
dehydrogenase/reductase 1 (Psdr1) gene, a new member of the short-chain
steroid dehydrogenase/reductase family. Gene 293: 149-160, 2002.
*FIELD* CN
Victor A. McKusick - updated: 9/9/2004
*FIELD* CD
Patricia A. Hartz: 6/4/2003
*FIELD* ED
carol: 06/06/2007
carol: 9/9/2004
terry: 9/9/2004
terry: 7/20/2004
mgross: 6/4/2003