DHRS7_MOUSE
ID DHRS7_MOUSE Reviewed; 338 AA.
AC Q9CXR1;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Dehydrogenase/reductase SDR family member 7 {ECO:0000250|UniProtKB:Q9Y394};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:Q9Y394};
DE AltName: Full=Retinal short-chain dehydrogenase/reductase 4 {ECO:0000250|UniProtKB:Q9Y394};
DE Short=retSDR4 {ECO:0000250|UniProtKB:Q9Y394};
DE AltName: Full=Short chain dehydrogenase/reductase family 34C member 1 {ECO:0000250|UniProtKB:Q9Y394};
DE Short=Protein SDR34C1 {ECO:0000250|UniProtKB:Q9Y394};
DE Flags: Precursor;
GN Name=Dhrs7 {ECO:0000312|MGI:MGI:1913625}; Synonyms=Retsdr4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: NADPH-dependent oxidoreductase which catalyzes the reduction
CC of a variety of compounds bearing carbonyl groups including steroids,
CC retinoids and xenobiotics. Catalyzes the reduction/inactivation of
CC 5alpha-dihydrotestosterone to 3alpha-androstanediol, with a possible
CC role in the modulation of androgen receptor function. Involved in the
CC reduction of all-trans-retinal to all-trans-retinol. Converts cortisone
CC to 20beta-dihydrocortisone in vitro, although the physiological
CC relevance of this activity is questionable. 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. A dehydrogenase activity has not been detected so far. May play
CC a role as tumor suppressor. {ECO:0000250|UniProtKB:Q9Y394}.
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:0000250|UniProtKB:Q9Y394};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25035;
CC Evidence={ECO:0000250|UniProtKB:Q9Y394};
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:0000250|UniProtKB:Q9Y394};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42118;
CC Evidence={ECO:0000250|UniProtKB:Q9Y394};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y394}. Note=Bound to the endoplasmic reticulum
CC membrane, possibly through a N-terminus anchor. The main bulk of the
CC polypeptide chain was first reported to be facing toward the lumen of
CC the endoplasmic reticulum. However, it was later shown to be facing the
CC cytosol. {ECO:0000250|UniProtKB:Q9Y394}.
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 (By similarity).
CC However, the catalytic moiety was later shown to be facing the cytosol
CC (By similarity). {ECO:0000250|UniProtKB:Q9Y394}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16189.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB29156.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK014100; BAB29156.1; ALT_FRAME; mRNA.
DR EMBL; BC016189; AAH16189.1; ALT_INIT; mRNA.
DR CCDS; CCDS49086.1; -.
DR RefSeq; NP_079798.2; NM_025522.5.
DR AlphaFoldDB; Q9CXR1; -.
DR SMR; Q9CXR1; -.
DR BioGRID; 211424; 4.
DR STRING; 10090.ENSMUSP00000021512; -.
DR iPTMnet; Q9CXR1; -.
DR PhosphoSitePlus; Q9CXR1; -.
DR SwissPalm; Q9CXR1; -.
DR EPD; Q9CXR1; -.
DR jPOST; Q9CXR1; -.
DR MaxQB; Q9CXR1; -.
DR PaxDb; Q9CXR1; -.
DR PeptideAtlas; Q9CXR1; -.
DR PRIDE; Q9CXR1; -.
DR ProteomicsDB; 277336; -.
DR DNASU; 66375; -.
DR Ensembl; ENSMUST00000021512; ENSMUSP00000021512; ENSMUSG00000021094.
DR GeneID; 66375; -.
DR KEGG; mmu:66375; -.
DR UCSC; uc007nvs.2; mouse.
DR CTD; 51635; -.
DR MGI; MGI:1913625; Dhrs7.
DR VEuPathDB; HostDB:ENSMUSG00000021094; -.
DR eggNOG; KOG1205; Eukaryota.
DR GeneTree; ENSGT00940000155226; -.
DR HOGENOM; CLU_010194_2_1_1; -.
DR InParanoid; Q9CXR1; -.
DR OMA; WAWWLTN; -.
DR OrthoDB; 906746at2759; -.
DR PhylomeDB; Q9CXR1; -.
DR TreeFam; TF354276; -.
DR BioGRID-ORCS; 66375; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Dhrs7; mouse.
DR PRO; PR:Q9CXR1; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9CXR1; protein.
DR Bgee; ENSMUSG00000021094; Expressed in granulocyte and 232 other tissues.
DR ExpressionAtlas; Q9CXR1; baseline and differential.
DR Genevisible; Q9CXR1; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; ISS:UniProtKB.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; ISS: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 Endoplasmic reticulum; Membrane; NAD; NADP; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..338
FT /note="Dehydrogenase/reductase SDR family member 7"
FT /id="PRO_0000031969"
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 CONFLICT 10
FT /note="L -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 38167 MW; 5D12F0117BD1070D CRC64;
MSWELLLWLL ALCALILPLV QLLRFLRADA DLTLLWAEWQ GRRPEWELTD MVVWVTGASS
GIGEELAFQL SKLGVSLVLS ARRAQELERV KRRCLENGNL KEKDILVLPL DLTDTSSHEA
ATKAVLQEFG KIDILVNNGG RSQRSLVLET NLDVFKELIN LNYIGTVSLT KCVLPHMIER
KQGKIVTVNS IAGIASVSLS SGYCASKHAL RGFFNALHSE LGQYPGITFC NVYPGPVQSD
IVKNAFTEEV TKSMRNNIDQ SYKMPTSRCV RLMLISMAND LKEVWISDHP VLLGAYIWQY
MPTWAAWLNC KLGKERIQNF KNNLDPDLPY KFLKAKKD
