ID DHRS9_RAT Reviewed; 319 AA.
AC Q8VD48;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 145.
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:0000269|PubMed:12390888};
DE AltName: Full=Short-chain dehydrogenase/reductase retSDR8;
DE Flags: Precursor;
GN Name=Dhrs9; Synonyms=eRolDH {ECO:0000303|PubMed:12390888};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=Sprague-Dawley; TISSUE=Uterus;
RX PubMed=12390888; DOI=10.1095/biolreprod.102.007021;
RA Rexer B.N., Ong D.E.;
RT "A novel short-chain alcohol dehydrogenase from rats with retinol
RT dehydrogenase activity, cyclically expressed in uterine epithelium.";
RL Biol. Reprod. 67:1555-1564(2002).
CC -!- FUNCTION: 3-alpha-hydroxysteroid dehydrogenase that converts 3-alpha-
CC tetrahydroprogesterone (allopregnanolone) to dihydroxyprogesterone and
CC 3-alpha-androstanediol to dihydroxyprogesterone (By similarity). Plays
CC also role in the biosynthesis of retinoic acid from retinaldehyde
CC (PubMed:12390888). Can utilize both NADH and NADPH (By similarity).
CC {ECO:0000250|UniProtKB:Q9BPW9, ECO:0000269|PubMed:12390888}.
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=androsterone + NAD(+) = 5alpha-androstan-3,17-dione + H(+) +
CC NADH; Xref=Rhea:RHEA:20381, ChEBI:CHEBI:15378, ChEBI:CHEBI:15994,
CC ChEBI:CHEBI:16032, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.209; 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:0000269|PubMed:12390888};
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 -!- TISSUE SPECIFICITY: Highly expressed in epithelium of estrus uterus.
CC {ECO:0000269|PubMed:12390888}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF337953; AAL73225.1; -; mRNA.
DR RefSeq; NP_570832.1; NM_130819.1.
DR AlphaFoldDB; Q8VD48; -.
DR SMR; Q8VD48; -.
DR STRING; 10116.ENSRNOP00000069708; -.
DR BindingDB; Q8VD48; -.
DR ChEMBL; CHEMBL1075220; -.
DR DrugCentral; Q8VD48; -.
DR iPTMnet; Q8VD48; -.
DR PhosphoSitePlus; Q8VD48; -.
DR PaxDb; 10116-ENSRNOP00000008921; -.
DR Ensembl; ENSRNOT00000106393.1; ENSRNOP00000091619.1; ENSRNOG00000065735.1.
DR GeneID; 170635; -.
DR KEGG; rno:170635; -.
DR UCSC; RGD:620655; rat.
DR AGR; RGD:620655; -.
DR CTD; 10170; -.
DR RGD; 620655; Dhrs9.
DR eggNOG; KOG1610; Eukaryota.
DR GeneTree; ENSGT00940000158665; -.
DR HOGENOM; CLU_010194_2_0_1; -.
DR InParanoid; Q8VD48; -.
DR OMA; ANPNIGW; -.
DR OrthoDB; 5403248at2759; -.
DR PhylomeDB; Q8VD48; -.
DR Reactome; R-RNO-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-RNO-5365859; RA biosynthesis pathway.
DR PRO; PR:Q8VD48; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000058568; Expressed in esophagus and 13 other cell types or tissues.
DR Genevisible; Q8VD48; RN.
DR GO; GO:0005789; C: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; IMP:RGD.
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:RGD.
DR GO; GO:0042448; P:progesterone metabolic process; ISO:RGD.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; IDA:RGD.
DR GO; GO:0042573; P:retinoic acid metabolic process; NAS:RGD.
DR GO; GO:0042572; P:retinol metabolic process; IBA:GO_Central.
DR GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
DR CDD; cd09805; type2_17beta_HSD-like_SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43313:SF15; DEHYDROGENASE_REDUCTASE SDR FAMILY MEMBER 9; 1.
DR PANTHER; PTHR43313; SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY 9C; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 1: Evidence at protein 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_0000042619"
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"
SQ SEQUENCE 319 AA; 35214 MW; 2EA1B82D3F170B9B CRC64;
MLLWVLALLF LCAFLWNYKG QLKIADIADK YIFITGCDSG FGNLAARTFD RKGFRVIAAC
LTESGSEALK AKTSERLHTV LLDVTNPENV KETAQWVKSH VGEKGLWGLI NNAGVLGVLA
PTDWLTVDDY REPIEVNLFG LINVTLNMLP LVKKARGRVI NVSSIGGRLA FGGGGYTPSK
YAVEGFNDSL RRDMKAFGVH VSCIEPGLFK TGLADPIKTT EKKLAIWKHL SPDIKQQYGE
GYIEKSLHRL KSSTSSVNLD LSLVVECMDH ALTSLFPKTR YTAGKDAKTF WIPLSHMPAA
LQDFLLLKEK VELANPQAV
//
