ALD2_MOUSE
ID ALD2_MOUSE Reviewed; 316 AA.
AC P45377; Q99JN4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Aldose reductase-related protein 2;
DE Short=AR;
DE EC=1.1.1.21;
DE AltName: Full=Aldehyde reductase;
DE AltName: Full=Fibroblast growth factor-regulated protein;
DE AltName: Full=Protein FR-1;
GN Name=Akr1b8; Synonyms=Fgfrp;
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 STRAIN=BALB/cJ;
RX PubMed=7510692; DOI=10.1016/s0021-9258(17)37237-x;
RA Donohue P.J., Alberts G.F., Hampton B.S., Winkles J.A.;
RT "A delayed-early gene activated by fibroblast growth factor-1 encodes a
RT protein related to aldose reductase.";
RL J. Biol. Chem. 269:8604-8609(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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=Brown adipose tissue, Heart, Lung, 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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NADPH AND INHIBITOR.
RX PubMed=7578036; DOI=10.1021/bi00044a009;
RA Wilson D.K., Nakano T., Petrash M., Quiocho F.A.;
RT "1.7-A structure of FR-1, a fibroblast growth factor-induced member of the
RT aldo-keto reductase family, complexed with coenzyme and inhibitor.";
RL Biochemistry 34:14323-14330(1995).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alditol + NAD(+) = an aldose + H(+) + NADH;
CC Xref=Rhea:RHEA:12785, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.21;
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: By FGF-1.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; U04204; AAA16953.1; -; mRNA.
DR EMBL; BC005789; AAH05789.1; -; mRNA.
DR CCDS; CCDS19991.1; -.
DR PIR; A53440; A53440.
DR RefSeq; NP_032038.1; NM_008012.1.
DR PDB; 1FRB; X-ray; 1.70 A; A=2-316.
DR PDBsum; 1FRB; -.
DR AlphaFoldDB; P45377; -.
DR SMR; P45377; -.
DR STRING; 10090.ENSMUSP00000040244; -.
DR SwissLipids; SLP:000001939; -.
DR iPTMnet; P45377; -.
DR PhosphoSitePlus; P45377; -.
DR SwissPalm; P45377; -.
DR REPRODUCTION-2DPAGE; IPI00273096; -.
DR REPRODUCTION-2DPAGE; P45377; -.
DR EPD; P45377; -.
DR jPOST; P45377; -.
DR MaxQB; P45377; -.
DR PaxDb; P45377; -.
DR PeptideAtlas; P45377; -.
DR PRIDE; P45377; -.
DR ProteomicsDB; 296393; -.
DR DNASU; 14187; -.
DR Ensembl; ENSMUST00000038406; ENSMUSP00000040244; ENSMUSG00000029762.
DR GeneID; 14187; -.
DR KEGG; mmu:14187; -.
DR UCSC; uc009bgz.1; mouse.
DR CTD; 14187; -.
DR MGI; MGI:107673; Akr1b8.
DR VEuPathDB; HostDB:ENSMUSG00000029762; -.
DR eggNOG; KOG1577; Eukaryota.
DR GeneTree; ENSGT00940000154773; -.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; P45377; -.
DR OMA; ECGEGVA; -.
DR OrthoDB; 1016440at2759; -.
DR PhylomeDB; P45377; -.
DR TreeFam; TF106492; -.
DR Reactome; R-MMU-193144; Estrogen biosynthesis.
DR BioGRID-ORCS; 14187; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Akr1b8; mouse.
DR EvolutionaryTrace; P45377; -.
DR PRO; PR:P45377; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P45377; protein.
DR Bgee; ENSMUSG00000029762; Expressed in pyloric antrum and 212 other tissues.
DR Genevisible; P45377; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO: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:0004303; F:estradiol 17-beta-dehydrogenase activity; ISO:MGI.
DR GO; GO:0045550; F:geranylgeranyl reductase activity; ISO:MGI.
DR GO; GO:0047718; F:indanol dehydrogenase activity; ISO:MGI.
DR GO; GO:0070401; F:NADP+ binding; IEA:Ensembl.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; ISO:MGI.
DR GO; GO:0070402; F:NADPH binding; IEA:Ensembl.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; ISO:MGI.
DR GO; GO:0016918; F:retinal binding; IEA:Ensembl.
DR GO; GO:0001758; F:retinal dehydrogenase activity; ISO:MGI.
DR GO; GO:0019751; P:polyol metabolic process; IEA:Ensembl.
DR GO; GO:0042574; P:retinal metabolic process; IEA:Ensembl.
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 3D-structure; Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..316
FT /note="Aldose reductase-related protein 2"
FT /id="PRO_0000124631"
FT ACT_SITE 49
FT /note="Proton donor"
FT BINDING 111
FT /ligand="substrate"
FT BINDING 211..273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:7578036"
FT SITE 78
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT CONFLICT 242
FT /note="E -> K (in Ref. 2; AAH05789)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1FRB"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:1FRB"
FT HELIX 25..37
FT /evidence="ECO:0007829|PDB:1FRB"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1FRB"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1FRB"
FT HELIX 52..64
FT /evidence="ECO:0007829|PDB:1FRB"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1FRB"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1FRB"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1FRB"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:1FRB"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:1FRB"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:1FRB"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:1FRB"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:1FRB"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1FRB"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:1FRB"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1FRB"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1FRB"
FT HELIX 232..240
FT /evidence="ECO:0007829|PDB:1FRB"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:1FRB"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:1FRB"
FT HELIX 267..274
FT /evidence="ECO:0007829|PDB:1FRB"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:1FRB"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1FRB"
SQ SEQUENCE 316 AA; 36121 MW; 0C6F0A7BA806497C CRC64;
MATFVELSTK AKMPIVGLGT WKSPPNQVKE AVKAAIDAGY RHIDCAYAYC NENEVGEAIQ
EKIKEKAVQR EDLFIVSKLW PTCFEKKLLK EAFQKTLTDL KLDYLDLYLI HWPQGLQPGK
ELFPKDDQGR ILTSKTTFLE AWEGMEELVD QGLVKALGVS NFNHFQIERL LNKPGLKHKP
VTNQVECHPY LTQEKLIQYC HSKGISVTAY SPLGSPDRPS AKPEDPSLLE DPKIKEIAAK
HEKTSAQVLI RFHIQRNVVV IPKSVTPSRI QENIQVFDFQ LSDEEMATIL SFNRNWRACL
LPETVNMEEY PYDAEY
