ALD1_MOUSE
ID ALD1_MOUSE Reviewed; 316 AA.
AC P21300;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Aldo-keto reductase family 1 member B7;
DE EC=1.1.1.21 {ECO:0000250|UniProtKB:Q5RJP0};
DE AltName: Full=Aldehyde reductase;
DE Short=AR;
DE AltName: Full=Aldose reductase-related protein 1 {ECO:0000303|PubMed:1637719};
DE AltName: Full=MVDP {ECO:0000303|PubMed:1637719};
DE AltName: Full=Vas deferens androgen-dependent protein;
GN Name=Akr1b7; Synonyms=Avdp;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Vas deferens;
RX PubMed=1637719; DOI=10.1016/0960-0760(92)90445-o;
RA Pailhoux E.A., Veyssiere G.M., Fabre S., Tournaire C., Jean C.G.;
RT "The genomic organization and DNA sequence of the mouse vas deferens
RT androgen regulated protein gene.";
RL J. Steroid Biochem. Mol. Biol. 42:561-568(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1; TISSUE=Vas deferens;
RX PubMed=2123194; DOI=10.1016/s0021-9258(17)45463-9;
RA Pailhoux E.A., Martinez A., Veyssiere G.M., Jean C.G.;
RT "Androgen-dependent protein from mouse vas deferens. cDNA cloning and
RT protein homology with the aldo-keto reductase superfamily.";
RL J. Biol. Chem. 265:19932-19936(1990).
RN [3]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=19010934; DOI=10.1093/jb/mvn152;
RA Kabututu Z., Manin M., Pointud J.C., Maruyama T., Nagata N., Lambert S.,
RA Lefrancois-Martinez A.M., Martinez A., Urade Y.;
RT "Prostaglandin F2alpha synthase activities of aldo-keto reductase 1B1, 1B3
RT and 1B7.";
RL J. Biochem. 145:161-168(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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: Reduces a broad range of aliphatic and aromatic aldehydes to
CC the corresponding alcohols. Reduces prostaglandins (PubMed:19010934).
CC May play a role in the metabolism of xenobiotic aromatic aldehydes (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:19010934}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alditol + NADP(+) = an aldose + H(+) + NADPH;
CC Xref=Rhea:RHEA:12789, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.21;
CC Evidence={ECO:0000250|UniProtKB:Q5RJP0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin
CC H2; Xref=Rhea:RHEA:45312, ChEBI:CHEBI:15378, ChEBI:CHEBI:57404,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:19010934};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.8 uM for prostaglandin H2 {ECO:0000269|PubMed:19010934};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in the epithelial cells of
CC the deferent duct. {ECO:0000269|PubMed:1637719}.
CC -!- INDUCTION: Castration resulted in a marked decrease in the level of the
CC mRNA coding for the protein, whereas administration of testosterone to
CC castrated males resulted in a marked increase.
CC {ECO:0000269|PubMed:2123194}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; M81448; AAA39774.1; -; Genomic_DNA.
DR EMBL; J05663; AAA39773.1; -; mRNA.
DR CCDS; CCDS19993.1; -.
DR PIR; A37990; A37990.
DR RefSeq; NP_033861.2; NM_009731.2.
DR AlphaFoldDB; P21300; -.
DR SMR; P21300; -.
DR STRING; 10090.ENSMUSP00000007449; -.
DR SwissLipids; SLP:000001114; -.
DR iPTMnet; P21300; -.
DR PhosphoSitePlus; P21300; -.
DR SwissPalm; P21300; -.
DR REPRODUCTION-2DPAGE; P21300; -.
DR jPOST; P21300; -.
DR PaxDb; P21300; -.
DR PeptideAtlas; P21300; -.
DR PRIDE; P21300; -.
DR ProteomicsDB; 281965; -.
DR DNASU; 11997; -.
DR Ensembl; ENSMUST00000007449; ENSMUSP00000007449; ENSMUSG00000052131.
DR GeneID; 11997; -.
DR KEGG; mmu:11997; -.
DR UCSC; uc009bhd.2; mouse.
DR CTD; 11997; -.
DR MGI; MGI:101918; Akr1b7.
DR VEuPathDB; HostDB:ENSMUSG00000052131; -.
DR eggNOG; KOG1577; Eukaryota.
DR GeneTree; ENSGT00940000154773; -.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; P21300; -.
DR OMA; DCALAYQ; -.
DR OrthoDB; 1016440at2759; -.
DR PhylomeDB; P21300; -.
DR TreeFam; TF106492; -.
DR Reactome; R-MMU-193144; Estrogen biosynthesis.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR SABIO-RK; P21300; -.
DR BioGRID-ORCS; 11997; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Akr1b7; mouse.
DR PRO; PR:P21300; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P21300; protein.
DR Bgee; ENSMUSG00000052131; Expressed in adrenal gland and 84 other tissues.
DR ExpressionAtlas; P21300; baseline and differential.
DR Genevisible; P21300; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; ISO:MGI.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0045550; F:geranylgeranyl reductase activity; ISO:MGI.
DR GO; GO:0047718; F:indanol dehydrogenase activity; ISO:MGI.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; ISO:MGI.
DR GO; GO:0036130; F:prostaglandin H2 endoperoxidase reductase activity; IEA:RHEA.
DR GO; GO:0001758; F:retinal dehydrogenase activity; ISO:MGI.
DR GO; GO:0044255; P:cellular lipid metabolic process; TAS:MGI.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..316
FT /note="Aldo-keto reductase family 1 member B7"
FT /id="PRO_0000124629"
FT ACT_SITE 49
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 20..21
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 160..161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 210..215
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 263..269
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 78
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT CONFLICT 94
FT /note="Q -> D (in Ref. 2; AAA39773)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 35988 MW; 6BC46B6076969742 CRC64;
MATFVELSTK AKMPLVGLGT WKSSPGQVKE AVKAAIDAGY RHIDCAYVYH NENEVGEAIQ
EKIKENAVKR EDLFIVSKLW ATFFEKSLVK KAFQNTLSDL KLDYLDLYLV HWPQGFQAGN
ALLPKDNKGK VLLSKSTFLD AWEAMEELVD QGLVKALGIS NFNHFQIERL LNKPGLKHKP
VTNQIESHPY LTQEKLIQYC QSKGIAVTAY SPLGSPDRPY AKPEDPVVME IPKIKEIAAK
HKKTVAQVLI RFHVQRNVVV IPKSVTPSRI QENLQVFDFQ LSEEDMAAIL SFNRNWRACD
LLDARTEEDY PFHEEY
