DHRS9_HUMAN
ID DHRS9_HUMAN Reviewed; 319 AA.
AC Q9BPW9; B7Z416; D3DPC1; Q5RKX1; Q9NRA9; Q9NRB0;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Dehydrogenase/reductase SDR family member 9;
DE EC=1.1.1.209 {ECO:0000269|PubMed:11294878};
DE EC=1.1.1.53 {ECO:0000269|PubMed:11294878};
DE AltName: Full=3-alpha hydroxysteroid dehydrogenase;
DE Short=3-alpha-HSD;
DE AltName: Full=NADP-dependent retinol dehydrogenase/reductase;
DE AltName: Full=RDH-E2;
DE AltName: Full=RDHL;
DE AltName: Full=Retinol dehydrogenase 15;
DE EC=1.1.1.105 {ECO:0000269|PubMed:11304534};
DE AltName: Full=Short chain dehydrogenase/reductase family 9C member 4 {ECO:0000303|PubMed:19027726};
DE AltName: Full=Short-chain dehydrogenase/reductase retSDR8;
DE AltName: Full=Tracheobronchial epithelial cell-specific retinol dehydrogenase {ECO:0000303|PubMed:11304534};
DE Short=RDH-TBE {ECO:0000303|PubMed:11304534};
DE Flags: Precursor;
GN Name=DHRS9; Synonyms=RDH15, SDR9C4 {ECO:0000303|PubMed:19027726};
GN ORFNames=UNQ835/PRO1773;
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), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Heart, and Liver;
RX PubMed=11294878; DOI=10.1074/jbc.m102076200;
RA Chetyrkin S.V., Belyaeva O.V., Gough W.H., Kedishvili N.Y.;
RT "Characterization of a novel type of human microsomal 3alpha-hydroxysteroid
RT dehydrogenase. Unique tissue distribution and catalytic properties.";
RL J. Biol. Chem. 276:22278-22286(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
RC TISSUE=Tracheobronchial epithelium;
RX PubMed=11304534; DOI=10.1074/jbc.m100332200;
RA Soref C.M., Di Y.-P., Hayden L., Zhao Y.H., Satre M.A., Wu R.;
RT "Characterization of a novel airway epithelial cell-specific short chain
RT alcohol dehydrogenase/reductase gene whose expression is up-regulated by
RT retinoids and is involved in the metabolism of retinol.";
RL J. Biol. Chem. 276:24194-24202(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Keratinocyte;
RX PubMed=12618084; DOI=10.1016/s1096-7192(02)00226-3;
RA Markova N.G., Pinkas-Sarafova A., Karaman-Jurukovska N., Jurukovski V.,
RA Simon M.;
RT "Expression pattern and biochemical characteristics of a major epidermal
RT retinol dehydrogenase.";
RL Mol. Genet. Metab. 78:119-135(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=10800688; DOI=10.1016/s0076-6879(00)16736-9;
RA Haeseleer F., Palczewski K.;
RT "Short-chain dehydrogenases/reductases in retina.";
RL Methods Enzymol. 316:372-383(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Neuroblastoma;
RA Zhang J.W., Liu T.X., Shen Y., Chen S.J., Chen Z.;
RT "Human retinol dehydrogenase homolog gene.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Colon;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [9]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [11]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19027726; DOI=10.1016/j.cbi.2008.10.040;
RA Persson B., Kallberg Y., Bray J.E., Bruford E., Dellaporta S.L.,
RA Favia A.D., Duarte R.G., Joernvall H., Kavanagh K.L., Kedishvili N.,
RA Kisiela M., Maser E., Mindnich R., Orchard S., Penning T.M., Thornton J.M.,
RA Adamski J., Oppermann U.;
RT "The SDR (short-chain dehydrogenase/reductase and related enzymes)
RT nomenclature initiative.";
RL Chem. Biol. Interact. 178:94-98(2009).
RN [12]
RP MUTAGENESIS OF TYR-176 AND LYS-180, AND CATALYTIC ACTIVITY.
RX PubMed=29541409; DOI=10.18632/oncotarget.24107;
RA Fiandalo M.V., Stocking J.J., Pop E.A., Wilton J.H., Mantione K.M., Li Y.,
RA Attwood K.M., Azabdaftari G., Wu Y., Watt D.S., Wilson E.M., Mohler J.L.;
RT "Inhibition of dihydrotestosterone synthesis in prostate cancer by combined
RT frontdoor and backdoor pathway blockade.";
RL Oncotarget 9:11227-11242(2018).
CC -!- FUNCTION: 3-alpha-hydroxysteroid dehydrogenase that converts 3-alpha-
CC tetrahydroprogesterone (allopregnanolone) to dihydroxyprogesterone and
CC 3-alpha-androstanediol to dihydroxyprogesterone (PubMed:11294878,
CC PubMed:29541409). Also plays a role in the biosynthesis of retinoic
CC acid from retinaldehyde (PubMed:11304534, PubMed:12618084). Can utilize
CC both NADH and NADPH. {ECO:0000250|UniProtKB:Q8VD48,
CC ECO:0000269|PubMed:11294878, ECO:0000269|PubMed:11304534,
CC ECO:0000269|PubMed:12618084, ECO:0000269|PubMed:29541409}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3beta-hydroxy-5alpha-pregnane-20-one + NAD(+) = 5alpha-
CC pregnane-3,20-dione + H(+) + NADH; Xref=Rhea:RHEA:41988,
CC ChEBI:CHEBI:11909, ChEBI:CHEBI:15378, ChEBI:CHEBI:28952,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:11294878};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-hydroxy-5alpha-androstan-3-one + NAD(+) = 5alpha-
CC androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:41992,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16330,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:11294878};
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:0000269|PubMed:11294878, ECO:0000269|PubMed:29541409};
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:0000269|PubMed:11294878};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH;
CC Xref=Rhea:RHEA:21284, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.105; Evidence={ECO:0000269|PubMed:11304534};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3alpha-hydroxy-5alpha-pregnan-20-one + NAD(+) = 5alpha-
CC pregnane-3,20-dione + H(+) + NADH; Xref=Rhea:RHEA:41980,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28952, ChEBI:CHEBI:50169,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:11294878};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9 uM for NADH tested with dihydrotestosterone
CC {ECO:0000269|PubMed:11294878};
CC KM=72 uM for NAD tested with allopregnanolone
CC {ECO:0000269|PubMed:11294878};
CC KM=5 uM for allopregnanolone {ECO:0000269|PubMed:11294878};
CC KM=7.5 uM for 3-alpha-androstanediol {ECO:0000269|PubMed:11294878};
CC KM=14 uM for dehydroepiandrosterone {ECO:0000269|PubMed:11294878};
CC KM=24 uM for androsterone {ECO:0000269|PubMed:11294878};
CC KM=12 uM for dihydrotestosterone {ECO:0000269|PubMed:11294878};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9BPW9-4; P23560-2: BDNF; NbExp=3; IntAct=EBI-19157435, EBI-12275524;
CC Q9BPW9-4; P04406: GAPDH; NbExp=3; IntAct=EBI-19157435, EBI-354056;
CC Q9BPW9-4; Q9UNK0: STX8; NbExp=3; IntAct=EBI-19157435, EBI-727240;
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:11294878,
CC ECO:0000269|PubMed:11304534, ECO:0000269|PubMed:12618084}. Endoplasmic
CC reticulum membrane {ECO:0000305}. Note=Associated with microsomal
CC membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BPW9-1; Sequence=Displayed;
CC Name=2; Synonyms=Retinol dehydrogenase homolog isoform-2;
CC IsoId=Q9BPW9-2; Sequence=VSP_015875;
CC Name=3; Synonyms=Retinol dehydrogenase homolog isoform-1;
CC IsoId=Q9BPW9-3; Sequence=VSP_015876;
CC Name=4;
CC IsoId=Q9BPW9-4; Sequence=VSP_054357;
CC -!- TISSUE SPECIFICITY: Highly expressed in trachea and epidermis. Detected
CC at lower levels in spinal cord, bone marrow, brain, tongue, esophagus,
CC heart, colon, testis, placenta, lung, skeletal muscle and lymph node.
CC {ECO:0000269|PubMed:11294878, ECO:0000269|PubMed:11304534,
CC ECO:0000269|PubMed:12618084}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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; AF343729; AAK37528.1; -; mRNA.
DR EMBL; AY017349; AAG49422.1; -; mRNA.
DR EMBL; AF529286; AAN04008.1; -; mRNA.
DR EMBL; AF529287; AAN04009.1; -; mRNA.
DR EMBL; AF529288; AAN04010.1; -; mRNA.
DR EMBL; AF295380; AAL37037.1; -; mRNA.
DR EMBL; AF240697; AAF82747.1; -; mRNA.
DR EMBL; AF240698; AAF82748.1; -; mRNA.
DR EMBL; AY359046; AAQ89405.1; -; mRNA.
DR EMBL; AK296625; BAH12402.1; -; mRNA.
DR EMBL; AC007556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471058; EAX11282.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11283.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11284.1; -; Genomic_DNA.
DR EMBL; BC058883; AAH58883.1; -; mRNA.
DR CCDS; CCDS2231.1; -. [Q9BPW9-1]
DR CCDS; CCDS74600.1; -. [Q9BPW9-4]
DR RefSeq; NP_001135742.1; NM_001142270.1. [Q9BPW9-1]
DR RefSeq; NP_001135743.1; NM_001142271.1. [Q9BPW9-1]
DR RefSeq; NP_001276692.1; NM_001289763.1. [Q9BPW9-4]
DR RefSeq; NP_954674.1; NM_199204.1. [Q9BPW9-1]
DR RefSeq; XP_011508777.1; XM_011510475.1. [Q9BPW9-1]
DR AlphaFoldDB; Q9BPW9; -.
DR SMR; Q9BPW9; -.
DR BioGRID; 115472; 24.
DR IntAct; Q9BPW9; 14.
DR STRING; 9606.ENSP00000389241; -.
DR BindingDB; Q9BPW9; -.
DR ChEMBL; CHEMBL5974; -.
DR DrugCentral; Q9BPW9; -.
DR SwissLipids; SLP:000000793; -.
DR PhosphoSitePlus; Q9BPW9; -.
DR BioMuta; DHRS9; -.
DR DMDM; 74752227; -.
DR EPD; Q9BPW9; -.
DR jPOST; Q9BPW9; -.
DR MassIVE; Q9BPW9; -.
DR MaxQB; Q9BPW9; -.
DR PaxDb; Q9BPW9; -.
DR PeptideAtlas; Q9BPW9; -.
DR PRIDE; Q9BPW9; -.
DR ProteomicsDB; 6563; -.
DR ProteomicsDB; 78582; -. [Q9BPW9-1]
DR ProteomicsDB; 78583; -. [Q9BPW9-2]
DR ProteomicsDB; 78584; -. [Q9BPW9-3]
DR Antibodypedia; 33805; 240 antibodies from 27 providers.
DR DNASU; 10170; -.
DR Ensembl; ENST00000357546.6; ENSP00000350154.2; ENSG00000073737.17. [Q9BPW9-1]
DR Ensembl; ENST00000412271.1; ENSP00000407747.1; ENSG00000073737.17. [Q9BPW9-1]
DR Ensembl; ENST00000421653.5; ENSP00000388066.1; ENSG00000073737.17. [Q9BPW9-2]
DR Ensembl; ENST00000428522.5; ENSP00000388564.1; ENSG00000073737.17. [Q9BPW9-1]
DR Ensembl; ENST00000432060.6; ENSP00000389241.2; ENSG00000073737.17. [Q9BPW9-4]
DR Ensembl; ENST00000436483.6; ENSP00000407167.2; ENSG00000073737.17. [Q9BPW9-1]
DR Ensembl; ENST00000602501.5; ENSP00000473337.1; ENSG00000073737.17. [Q9BPW9-1]
DR Ensembl; ENST00000674881.1; ENSP00000502399.1; ENSG00000073737.17. [Q9BPW9-1]
DR GeneID; 10170; -.
DR KEGG; hsa:10170; -.
DR MANE-Select; ENST00000674881.1; ENSP00000502399.1; NM_001376924.1; NP_001363853.1.
DR UCSC; uc002ueq.3; human. [Q9BPW9-1]
DR CTD; 10170; -.
DR DisGeNET; 10170; -.
DR GeneCards; DHRS9; -.
DR HGNC; HGNC:16888; DHRS9.
DR HPA; ENSG00000073737; Tissue enhanced (intestine).
DR MIM; 612131; gene.
DR neXtProt; NX_Q9BPW9; -.
DR OpenTargets; ENSG00000073737; -.
DR PharmGKB; PA134913654; -.
DR VEuPathDB; HostDB:ENSG00000073737; -.
DR eggNOG; KOG1610; Eukaryota.
DR GeneTree; ENSGT00940000158665; -.
DR HOGENOM; CLU_010194_2_0_1; -.
DR InParanoid; Q9BPW9; -.
DR OMA; PQTHYIA; -.
DR OrthoDB; 1313182at2759; -.
DR PhylomeDB; Q9BPW9; -.
DR TreeFam; TF325617; -.
DR BioCyc; MetaCyc:HS01113-MON; -.
DR PathwayCommons; Q9BPW9; -.
DR Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-HSA-5365859; RA biosynthesis pathway.
DR SABIO-RK; Q9BPW9; -.
DR SignaLink; Q9BPW9; -.
DR SIGNOR; Q9BPW9; -.
DR BioGRID-ORCS; 10170; 7 hits in 1074 CRISPR screens.
DR GeneWiki; DHRS9; -.
DR GenomeRNAi; 10170; -.
DR Pharos; Q9BPW9; Tbio.
DR PRO; PR:Q9BPW9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9BPW9; protein.
DR Bgee; ENSG00000073737; Expressed in nasal cavity epithelium and 160 other tissues.
DR ExpressionAtlas; Q9BPW9; baseline and differential.
DR Genevisible; Q9BPW9; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0047044; F:androstan-3-alpha,17-beta-diol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0047023; F:androsterone dehydrogenase activity; IDA: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:0016854; F:racemase and epimerase activity; NAS:UniProtKB.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0008209; P:androgen metabolic process; IDA:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; NAS:UniProtKB.
DR GO; GO:0042448; P:progesterone metabolic process; IDA:UniProtKB.
DR GO; GO:0042572; P:retinol metabolic process; IBA:GO_Central.
DR GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
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 Alternative splicing; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW Microsome; NAD; NADP; Oxidoreductase; Reference proteome; Signal;
KW Steroid metabolism.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..319
FT /note="Dehydrogenase/reductase SDR family member 9"
FT /id="PRO_0000042617"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:29541409"
FT BINDING 34..58
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..147
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_015875"
FT VAR_SEQ 1
FT /note="M -> MPEGRSHCACSITSLTLLVSLTRVTLDILQKLDPPQPAHWRHHLLVL
FT YKKGVYLSHTGGKM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054357"
FT VAR_SEQ 206..246
FT /note="PGLFKTNLADPVKVIEKKLAIWEQLSPDIKQQYGEGYIEKS -> R (in
FT isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_015876"
FT VARIANT 286
FT /note="D -> H (in dbSNP:rs11695788)"
FT /id="VAR_052320"
FT MUTAGEN 176
FT /note="Y->F: Decreases androsterone dehydrogenase activity;
FT when associated with R-180."
FT /evidence="ECO:0000269|PubMed:29541409"
FT MUTAGEN 180
FT /note="K->R: Decreases androsterone dehydrogenase activity;
FT when associated with F-176."
FT /evidence="ECO:0000269|PubMed:29541409"
FT CONFLICT 162
FT /note="V -> G (in Ref. 5; AAF82747)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="M -> L (in Ref. 5; AAF82747)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 35227 MW; DEE8CD65E5C25C6F CRC64;
MLFWVLGLLI LCGFLWTRKG KLKIEDITDK YIFITGCDSG FGNLAARTFD KKGFHVIAAC
LTESGSTALK AETSERLRTV LLDVTDPENV KRTAQWVKNQ VGEKGLWGLI NNAGVPGVLA
PTDWLTLEDY REPIEVNLFG LISVTLNMLP LVKKAQGRVI NVSSVGGRLA IVGGGYTPSK
YAVEGFNDSL RRDMKAFGVH VSCIEPGLFK TNLADPVKVI EKKLAIWEQL SPDIKQQYGE
GYIEKSLDKL KGNKSYVNMD LSPVVECMDH ALTSLFPKTH YAAGKDAKIF WIPLSHMPAA
LQDFLLLKQK AELANPKAV
