ALD2_CRIGR
ID ALD2_CRIGR Reviewed; 316 AA.
AC O08782;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 104.
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=Aldo-keto reductase;
GN Name=AKR1B8;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=9148949; DOI=10.1074/jbc.272.20.13286;
RA Hyndman D.J., Takenoshita R., Vera N.L., Pang S.C., Flynn T.G.;
RT "Cloning, sequencing, and enzymatic activity of an inducible aldo-keto
RT reductase from Chinese hamster ovary cells.";
RL J. Biol. Chem. 272:13286-13291(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NADPH.
RX PubMed=10651037;
RX DOI=10.1002/(sici)1097-0134(20000101)38:1<41::aid-prot5>3.0.co;2-m;
RA Ye Q., Hyndman D.J., Li X., Flynn T.G., Jia Z.;
RT "Crystal structure of CHO reductase, a member of the aldo-keto reductase
RT superfamily.";
RL Proteins 38:41-48(2000).
CC -!- FUNCTION: Reductase with a preference for aliphatic substrates. Can
CC also act on small aromatic aldehydes, steroid aldehydes and some ketone
CC substrates. {ECO:0000269|PubMed:9148949}.
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 -!- TISSUE SPECIFICITY: Detected at very low levels in urinary bladder,
CC testis and jejunum. {ECO:0000269|PubMed:9148949}.
CC -!- INDUCTION: By FGF-1 (By similarity). Up-regulated by calpain inhibitor
CC I (N-acetyl-leucyl-leucyl-norleucinal/ALLN). {ECO:0000250,
CC ECO:0000269|PubMed:9148949}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; U81045; AAC53199.1; -; mRNA.
DR RefSeq; NP_001233680.1; NM_001246751.1.
DR PDB; 1C9W; X-ray; 2.40 A; A=2-316.
DR PDBsum; 1C9W; -.
DR AlphaFoldDB; O08782; -.
DR SMR; O08782; -.
DR STRING; 10029.NP_001233680.1; -.
DR PRIDE; O08782; -.
DR Ensembl; ENSCGRT00001022560; ENSCGRP00001018316; ENSCGRG00001018111.
DR GeneID; 100689318; -.
DR KEGG; cge:100689318; -.
DR CTD; 14187; -.
DR eggNOG; KOG1577; Eukaryota.
DR GeneTree; ENSGT00940000154773; -.
DR OMA; GYEATFN; -.
DR OrthoDB; 1016440at2759; -.
DR EvolutionaryTrace; O08782; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IEA:UniProtKB-EC.
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.
FT CHAIN 1..316
FT /note="Aldose reductase-related protein 2"
FT /id="PRO_0000124630"
FT ACT_SITE 49
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 211..273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10651037"
FT SITE 78
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1C9W"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:1C9W"
FT HELIX 25..38
FT /evidence="ECO:0007829|PDB:1C9W"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1C9W"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1C9W"
FT HELIX 52..64
FT /evidence="ECO:0007829|PDB:1C9W"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1C9W"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1C9W"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1C9W"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:1C9W"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:1C9W"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:1C9W"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1C9W"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1C9W"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:1C9W"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1C9W"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:1C9W"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:1C9W"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1C9W"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1C9W"
FT HELIX 232..240
FT /evidence="ECO:0007829|PDB:1C9W"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:1C9W"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:1C9W"
FT HELIX 267..273
FT /evidence="ECO:0007829|PDB:1C9W"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:1C9W"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1C9W"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1C9W"
SQ SEQUENCE 316 AA; 36340 MW; 80B4B8BF0F4FDDAE CRC64;
MSTFVELSTK AKMPIVGLGT WQSPPGQVKE AVKVAIDAGY RHIDCAYAYY NEHEVGEAIQ
EKIKEKAVRR EDLFIVSKLW PTCFERKLLK EAFQKTLTDL KLDYLDLYLI HWPQGLQPGK
ELFPKDDQGN VLTSKITFLD AWEVMEELVD EGLVKALGVS NFNHFQIERI LNKPGLKHKP
VTNQVECHPY LTQEKLIEYC HSKGITVTAY SPLGSPNRPW AKPEDPSLLE DPKIKEIAAK
HKKTSAQVLI RFHIQRNVVV IPKSVTPARI HENFQVFDFQ LSDQEMATIL GFNRNWRACL
LPETVNMEEY PYDAEY
