DHRS7_HUMAN
ID DHRS7_HUMAN Reviewed; 339 AA.
AC Q9Y394; B2R896; Q9UKU2;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Dehydrogenase/reductase SDR family member 7 {ECO:0000303|PubMed:19027726};
DE EC=1.1.1.- {ECO:0000269|PubMed:24246760, ECO:0000269|PubMed:26466768, ECO:0000269|PubMed:28457967, ECO:0000269|PubMed:28687384};
DE AltName: Full=Retinal short-chain dehydrogenase/reductase 4 {ECO:0000303|PubMed:10800688};
DE Short=retSDR4 {ECO:0000303|PubMed:10800688};
DE AltName: Full=Short chain dehydrogenase/reductase family 34C member 1 {ECO:0000303|PubMed:19027726};
DE Short=Protein SDR34C1 {ECO:0000303|PubMed:19027726};
DE Flags: Precursor;
GN Name=DHRS7 {ECO:0000312|HGNC:HGNC:21524};
GN Synonyms=DHRS7A, RETSDR4 {ECO:0000303|PubMed:10800688},
GN SDR34C1 {ECO:0000303|PubMed:19027726}; ORFNames=CGI-86, UNQ285/PRO3448;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
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 [9]
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 [10]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=24246760; DOI=10.1016/j.cbi.2013.11.003;
RA Stambergova H., Skarydova L., Dunford J.E., Wsol V.;
RT "Biochemical properties of human dehydrogenase/reductase (SDR family)
RT member 7.";
RL Chem. Biol. Interact. 207:52-57(2014).
RN [11]
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 [12]
RP FUNCTION.
RX PubMed=26311046; DOI=10.1002/cam4.517;
RA Seibert J.K., Quagliata L., Quintavalle C., Hammond T.G., Terracciano L.,
RA Odermatt A.;
RT "A role for the dehydrogenase DHRS7 (SDR34C1) in prostate cancer.";
RL Cancer Med. 4:1717-1729(2015).
RN [13]
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 [14]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=26466768; DOI=10.1016/j.jsbmb.2015.09.041;
RA Stambergova H., Zemanova L., Lundova T., Malcekova B., Skarka A., Safr M.,
RA Wsol V.;
RT "Human DHRS7, promising enzyme in metabolism of steroids and retinoids?";
RL J. Steroid Biochem. Mol. Biol. 155:112-119(2016).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=28687384; DOI=10.1016/j.ijbiomac.2017.07.012;
RA Zemanova L., Kirubakaran P., Pato I.H., Stambergova H., Vondrasek J.;
RT "The identification of new substrates of human DHRS7 by molecular modeling
RT and in vitro testing.";
RL Int. J. Biol. Macromol. 105:171-182(2017).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=28457967; DOI=10.1016/j.jsbmb.2017.04.013;
RA Araya S., Kratschmar D.V., Tsachaki M., Stuecheli S., Beck K.R.,
RA Odermatt A.;
RT "DHRS7 (SDR34C1) - A new player in the regulation of androgen receptor
RT function by inactivation of 5alpha-dihydrotestosterone?";
RL J. Steroid Biochem. Mol. Biol. 171:288-295(2017).
CC -!- FUNCTION: NADPH-dependent oxidoreductase which catalyzes the reduction
CC of a variety of compounds bearing carbonyl groups including steroids,
CC retinoids and xenobiotics (PubMed:24246760, PubMed:26466768,
CC PubMed:28687384, PubMed:28457967). Catalyzes the reduction/inactivation
CC of 5alpha-dihydrotestosterone to 3alpha-androstanediol, with a possible
CC role in the modulation of androgen receptor function (PubMed:28687384,
CC PubMed:28457967). Involved in the reduction of all-trans-retinal to
CC all-trans-retinol (PubMed:26466768). Converts cortisone to 20beta-
CC dihydrocortisone in vitro, although the physiological relevance of this
CC activity is questionable (PubMed:28457967). Reduces exogenous compounds
CC such as quinones (1,2-naphtoquinone, 9,10-phenantrenequinone and
CC benzoquinone) and other xenobiotics (alpha-diketones) in vitro,
CC suggesting a role in the biotransformation of xenobiotics with carbonyl
CC group (PubMed:24246760, PubMed:26466768). A dehydrogenase activity has
CC not been detected so far (PubMed:24246760). May play a role as tumor
CC suppressor (PubMed:26311046). {ECO:0000269|PubMed:24246760,
CC ECO:0000269|PubMed:26311046, ECO:0000269|PubMed:26466768,
CC ECO:0000269|PubMed:28457967, ECO:0000269|PubMed:28687384}.
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 Evidence={ECO:0000269|PubMed:26466768};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25035;
CC Evidence={ECO:0000305|PubMed:26466768};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-androstane-3alpha,17beta-diol + NADP(+) = 17beta-
CC hydroxy-5alpha-androstan-3-one + H(+) + NADPH; Xref=Rhea:RHEA:42116,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:28457967, ECO:0000269|PubMed:28687384};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42118;
CC Evidence={ECO:0000305|PubMed:28457967, ECO:0000305|PubMed:28687384};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20.47 uM for NADPH {ECO:0000269|PubMed:24246760};
CC KM=30.08 uM for NADH {ECO:0000269|PubMed:24246760};
CC KM=24.30 uM for all-trans-retinal {ECO:0000269|PubMed:26466768};
CC KM=48.40 uM for 17beta-hydroxy-5alpha-androstan-3-one
CC {ECO:0000269|PubMed:28687384};
CC Vmax=10.58 nmol/min/mg enzyme with NADPH as substrate
CC {ECO:0000269|PubMed:24246760};
CC Vmax=2.38 nmol/min/mg enzyme with NADH as substrate
CC {ECO:0000269|PubMed:24246760};
CC Vmax=270.30 nmol/min/mg enzyme for the NADPH-dependent reduction of
CC all-trans-retinal {ECO:0000269|PubMed:26466768};
CC Vmax=34.40 nmol/min/mg enzyme for the NADPH-dependent reduction of
CC 17beta-hydroxy-5alpha-androstan-3-one to 5alpha-androstane-
CC 3alpha,17beta-diol {ECO:0000269|PubMed:28687384};
CC Note=kcat is 10.22 min(-1) for the NADPH-dependent reduction of all-
CC trans-retinal. {ECO:0000269|PubMed:26466768};
CC -!- INTERACTION:
CC Q9Y394; Q9NTJ5: SACM1L; NbExp=3; IntAct=EBI-1387800, EBI-3917235;
CC Q9Y394; Q9BXJ8: TMEM120A; NbExp=3; IntAct=EBI-1387800, EBI-727322;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24246760, ECO:0000269|PubMed:28457967}. Note=Bound
CC to the endoplasmic reticulum membrane, possibly through a N-terminus
CC anchor. The main bulk of the polypeptide chain was first reported to be
CC facing toward the lumen of the endoplasmic reticulum (PubMed:24246760).
CC However, it was later shown to be facing the cytosol (PubMed:28457967).
CC {ECO:0000269|PubMed:24246760, ECO:0000269|PubMed:28457967}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y394-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y394-2; Sequence=VSP_008103;
CC -!- TISSUE SPECIFICITY: Found predominantly in the adrenal glands, liver,
CC thyroid, prostate, small intestine, colon, stomach, kidney and brain
CC (PubMed:26466768). Lower levels observed in skeletal muscle, the lung
CC and the spleen (PubMed:26466768). {ECO:0000269|PubMed:26466768}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- CAUTION: DHRS7 was originally reported to be anchored in the
CC endoplasmic reticulum membrane and facing the lumen (PubMed:24246760).
CC However, the catalytic moiety was later shown to be facing the cytosol
CC (PubMed:28457967). {ECO:0000269|PubMed:24246760,
CC ECO:0000269|PubMed:28457967}.
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; AF151844; AAD34081.1; -; mRNA.
DR EMBL; AF126782; AAF06941.1; -; mRNA.
DR EMBL; AY359031; AAQ89390.1; -; mRNA.
DR EMBL; AK313285; BAG36093.1; -; mRNA.
DR EMBL; AL163853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW80770.1; -; Genomic_DNA.
DR EMBL; BC000637; AAH00637.1; -; mRNA.
DR EMBL; BC007337; AAH07337.1; -; mRNA.
DR CCDS; CCDS81810.1; -. [Q9Y394-2]
DR CCDS; CCDS9743.1; -. [Q9Y394-1]
DR RefSeq; NP_001309209.1; NM_001322280.1. [Q9Y394-2]
DR RefSeq; NP_057113.1; NM_016029.3. [Q9Y394-1]
DR AlphaFoldDB; Q9Y394; -.
DR SMR; Q9Y394; -.
DR BioGRID; 119649; 150.
DR IntAct; Q9Y394; 50.
DR MINT; Q9Y394; -.
DR STRING; 9606.ENSP00000216500; -.
DR GlyGen; Q9Y394; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y394; -.
DR PhosphoSitePlus; Q9Y394; -.
DR SwissPalm; Q9Y394; -.
DR BioMuta; DHRS7; -.
DR DMDM; 34395856; -.
DR EPD; Q9Y394; -.
DR jPOST; Q9Y394; -.
DR MassIVE; Q9Y394; -.
DR MaxQB; Q9Y394; -.
DR PaxDb; Q9Y394; -.
DR PeptideAtlas; Q9Y394; -.
DR PRIDE; Q9Y394; -.
DR ProteomicsDB; 85986; -. [Q9Y394-1]
DR ProteomicsDB; 85987; -. [Q9Y394-2]
DR Antibodypedia; 24356; 241 antibodies from 28 providers.
DR DNASU; 51635; -.
DR Ensembl; ENST00000216500.9; ENSP00000216500.5; ENSG00000100612.14. [Q9Y394-1]
DR Ensembl; ENST00000536410.6; ENSP00000442993.2; ENSG00000100612.14. [Q9Y394-2]
DR Ensembl; ENST00000557185.6; ENSP00000451882.1; ENSG00000100612.14. [Q9Y394-1]
DR GeneID; 51635; -.
DR KEGG; hsa:51635; -.
DR MANE-Select; ENST00000557185.6; ENSP00000451882.1; NM_016029.4; NP_057113.1.
DR UCSC; uc001xes.5; human. [Q9Y394-1]
DR CTD; 51635; -.
DR DisGeNET; 51635; -.
DR GeneCards; DHRS7; -.
DR HGNC; HGNC:21524; DHRS7.
DR HPA; ENSG00000100612; Tissue enhanced (skeletal).
DR MIM; 612833; gene.
DR neXtProt; NX_Q9Y394; -.
DR OpenTargets; ENSG00000100612; -.
DR PharmGKB; PA134974539; -.
DR VEuPathDB; HostDB:ENSG00000100612; -.
DR eggNOG; KOG1205; Eukaryota.
DR GeneTree; ENSGT00940000155226; -.
DR HOGENOM; CLU_010194_2_1_1; -.
DR InParanoid; Q9Y394; -.
DR OMA; WAWWLTN; -.
DR OrthoDB; 906746at2759; -.
DR PhylomeDB; Q9Y394; -.
DR TreeFam; TF354276; -.
DR PathwayCommons; Q9Y394; -.
DR SignaLink; Q9Y394; -.
DR BioGRID-ORCS; 51635; 9 hits in 1082 CRISPR screens.
DR ChiTaRS; DHRS7; human.
DR GenomeRNAi; 51635; -.
DR Pharos; Q9Y394; Tbio.
DR PRO; PR:Q9Y394; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9Y394; protein.
DR Bgee; ENSG00000100612; Expressed in parotid gland and 202 other tissues.
DR ExpressionAtlas; Q9Y394; baseline and differential.
DR Genevisible; Q9Y394; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IDA: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; IDA:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; NAD; NADP;
KW Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..339
FT /note="Dehydrogenase/reductase SDR family member 7"
FT /id="PRO_0000031968"
FT ACT_SITE 203
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 60
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 62
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 203
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 239
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_008103"
FT VARIANT 218
FT /note="R -> Q (in dbSNP:rs34583017)"
FT /id="VAR_052319"
SQ SEQUENCE 339 AA; 38299 MW; 7B251CE5894ED70C CRC64;
MNWELLLWLL VLCALLLLLV QLLRFLRADG DLTLLWAEWQ GRRPEWELTD MVVWVTGASS
GIGEELAYQL SKLGVSLVLS ARRVHELERV KRRCLENGNL KEKDILVLPL DLTDTGSHEA
ATKAVLQEFG RIDILVNNGG MSQRSLCMDT SLDVYRKLIE LNYLGTVSLT KCVLPHMIER
KQGKIVTVNS ILGIISVPLS IGYCASKHAL RGFFNGLRTE LATYPGIIVS NICPGPVQSN
IVENSLAGEV TKTIGNNGDQ SHKMTTSRCV RLMLISMAND LKEVWISEQP FLLVTYLWQY
MPTWAWWITN KMGKKRIENF KSGVDADSSY FKIFKTKHD
