DHRS9_MOUSE
ID DHRS9_MOUSE Reviewed; 319 AA.
AC Q58NB6; Q8BGC7;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Dehydrogenase/reductase SDR family member 9;
DE EC=1.1.1.209 {ECO:0000250|UniProtKB:Q9BPW9};
DE EC=1.1.1.53 {ECO:0000250|UniProtKB:Q9BPW9};
DE AltName: Full=3-alpha hydroxysteroid dehydrogenase;
DE Short=3-alpha-HSD;
DE AltName: Full=Retinol dehydrogenase;
DE EC=1.1.1.105 {ECO:0000250|UniProtKB:Q9BPW9};
DE AltName: Full=Short-chain dehydrogenase/reductase retSDR8;
DE Flags: Precursor;
GN Name=Dhrs9;
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 [MRNA].
RC TISSUE=Eye;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Uterus;
RA Plumley H.C., Rexer B.N., Li X.-H., Ong D.E.;
RT "Mouse homolog of rat epithelial retinol dehydrogenase.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Liver;
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).
CC -!- FUNCTION: 3-alpha-hydroxysteroid dehydrogenase that converts 3-alpha-
CC tetrahydroprogesterone (allopregnanolone) to dihydroxyprogesterone and
CC 3-alpha-androstanediol to dihydroxyprogesterone. Also plays a role in
CC the biosynthesis of retinoic acid. Can utilize both NADH and NADPH.
CC {ECO:0000250|UniProtKB:Q8VD48, ECO:0000250|UniProtKB:Q9BPW9}.
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:0000250|UniProtKB:Q9BPW9};
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:0000250|UniProtKB:Q9BPW9};
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:0000250|UniProtKB:Q9BPW9};
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:0000250|UniProtKB:Q9BPW9};
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:0000250|UniProtKB:Q9BPW9};
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:0000250|UniProtKB:Q9BPW9};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:Q9BPW9}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9BPW9}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF361479; AAN75755.1; -; mRNA.
DR EMBL; AK050180; BAC34110.1; -; mRNA.
DR EMBL; AK080914; BAC38075.1; -; mRNA.
DR EMBL; AY936479; AAX33670.1; -; mRNA.
DR CCDS; CCDS16091.1; -.
DR RefSeq; NP_780721.1; NM_175512.2.
DR AlphaFoldDB; Q58NB6; -.
DR SMR; Q58NB6; -.
DR STRING; 10090.ENSMUSP00000069631; -.
DR PhosphoSitePlus; Q58NB6; -.
DR MaxQB; Q58NB6; -.
DR PaxDb; Q58NB6; -.
DR PRIDE; Q58NB6; -.
DR ProteomicsDB; 279528; -.
DR Antibodypedia; 33805; 240 antibodies from 27 providers.
DR DNASU; 241452; -.
DR Ensembl; ENSMUST00000063690; ENSMUSP00000069631; ENSMUSG00000027068.
DR GeneID; 241452; -.
DR KEGG; mmu:241452; -.
DR UCSC; uc008jyb.1; mouse.
DR CTD; 10170; -.
DR MGI; MGI:2442798; Dhrs9.
DR VEuPathDB; HostDB:ENSMUSG00000027068; -.
DR eggNOG; KOG1610; Eukaryota.
DR GeneTree; ENSGT00940000158665; -.
DR HOGENOM; CLU_010194_2_0_1; -.
DR InParanoid; Q58NB6; -.
DR OMA; PQTHYIA; -.
DR OrthoDB; 1313182at2759; -.
DR PhylomeDB; Q58NB6; -.
DR TreeFam; TF325617; -.
DR Reactome; R-MMU-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-MMU-5365859; RA biosynthesis pathway.
DR BioGRID-ORCS; 241452; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q58NB6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q58NB6; protein.
DR Bgee; ENSMUSG00000027068; Expressed in granulocyte and 27 other tissues.
DR ExpressionAtlas; Q58NB6; baseline and differential.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0047044; F:androstan-3-alpha,17-beta-diol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0047023; F:androsterone dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0008209; P:androgen metabolic process; ISO:MGI.
DR GO; GO:0042448; P:progesterone metabolic process; ISO:MGI.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; ISO:MGI.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid metabolism; Membrane; Microsome; NAD; NADP;
KW Oxidoreductase; Reference proteome; Signal; Steroid metabolism.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..319
FT /note="Dehydrogenase/reductase SDR family member 9"
FT /id="PRO_0000042618"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BPW9"
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 CONFLICT 3..5
FT /note="FWL -> LWV (in Ref. 2; AAX33670)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="I -> L (in Ref. 2; AAX33670)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="K -> Q (in Ref. 2; AAX33670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 35242 MW; A8111F84ED57BB19 CRC64;
MLFWLLALLF LCAFLWNYKG QLKIADIADK YVFITGCDTG FGNLAARTFD KKGFRVIAAC
LTESGSAALK AKTSERLHTV LLDVTDPENV KKTAQWVKSH VGEKGLWGLI NNAGVLGVLA
PTDWLTVDDY REPIEVNLFG LINVTLNMLP LVKKARGRVI NVSSIGGRLA FGGGGYTPSK
YAVEGFNDSL RRDMKAFGVH VSCIEPGLFK TELADPIKTT EKKLAIWKHL SPDIKQQYGE
GYIEKSLHRL KSNTSSVNLD LSLVVGCMDH ALTSLFPKTR YIAGKDAKTF WIPLSHMPAV
LQDFLLLKQK VELANPKAV
