AKCL2_PIG
ID AKCL2_PIG Reviewed; 301 AA.
AC P82125; Q1KLB5;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=1,5-anhydro-D-fructose reductase;
DE Short=AF reductase;
DE EC=1.1.1.263 {ECO:0000269|PubMed:9504428};
DE AltName: Full=Aldo-keto reductase family 1 member C-like protein 2;
DE Short=Aldo-keto reductase family 1 member CL2;
DE AltName: Full=Aldo-keto reductase family 1 member E2;
GN Name=AKR1E2; Synonyms=AKR1CL2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX PubMed=16970816; DOI=10.1186/1746-6148-2-28;
RA Nonneman D.J., Wise T.H., Ford J.J., Kuehn L.A., Rohrer G.A.;
RT "Characterization of the aldo-keto reductase 1C gene cluster on pig
RT chromosome 10: possible associations with reproductive traits.";
RL BMC Vet. Res. 2:28-28(2006).
RN [2]
RP PROTEIN SEQUENCE OF 3-69; 92-131; 171-185; 188-223 AND 253-298, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND ACTIVITY
RP REGULATION.
RC TISSUE=Liver;
RX PubMed=9504428; DOI=10.1093/oxfordjournals.jbchem.a021909;
RA Sakuma M., Kametani S., Akanuma H.;
RT "Purification and some properties of a hepatic NADPH-dependent reductase
RT that specifically acts on 1,5-anhydro-D-fructose.";
RL J. Biochem. 123:189-193(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 169-301 (ISOFORM LONG).
RX PubMed=14681463; DOI=10.1093/nar/gkh037;
RA Uenishi H., Eguchi T., Suzuki K., Sawazaki T., Toki D., Shinkai H.,
RA Okumura N., Hamasima N., Awata T.;
RT "PEDE (Pig EST Data Explorer): construction of a database for ESTs derived
RT from porcine full-length cDNA libraries.";
RL Nucleic Acids Res. 32:D484-D488(2004).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-
CC fructose (AF) to 1,5-anhydro-D-glucitol. {ECO:0000269|PubMed:9504428}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,5-anhydro-D-glucitol + NADP(+) = 1,5-anhydro-D-fructose +
CC H(+) + NADPH; Xref=Rhea:RHEA:20665, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16070, ChEBI:CHEBI:16715, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.1.1.263;
CC Evidence={ECO:0000269|PubMed:9504428};
CC -!- ACTIVITY REGULATION: Inhibited by p-chloromercuribenzoic acid and
CC alkyliodines. {ECO:0000269|PubMed:9504428}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.44 mM for 1,5-anhydro-D-fructose {ECO:0000269|PubMed:9504428};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:9504428};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:9504428};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9504428}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P82125-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P82125-2; Sequence=VSP_037445, VSP_037446;
CC -!- MISCELLANEOUS: [Isoform Short]: Due to exon inclusion. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; DQ474064; ABF18830.1; -; mRNA.
DR EMBL; DB808243; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001038033.2; NM_001044568.2. [P82125-1]
DR RefSeq; XP_013835805.1; XM_013980351.1. [P82125-1]
DR RefSeq; XP_013835806.1; XM_013980352.1. [P82125-1]
DR RefSeq; XP_013835811.1; XM_013980357.1.
DR RefSeq; XP_013835812.1; XM_013980358.1.
DR AlphaFoldDB; P82125; -.
DR SMR; P82125; -.
DR STRING; 9823.ENSSSCP00000011891; -.
DR PaxDb; P82125; -.
DR PeptideAtlas; P82125; -.
DR PRIDE; P82125; -.
DR Ensembl; ENSSSCT00000012204; ENSSSCP00000011891; ENSSSCG00000036941. [P82125-1]
DR Ensembl; ENSSSCT00000052191; ENSSSCP00000046702; ENSSSCG00000036941. [P82125-2]
DR Ensembl; ENSSSCT00005029791; ENSSSCP00005018130; ENSSSCG00005018482. [P82125-1]
DR Ensembl; ENSSSCT00005029824; ENSSSCP00005018154; ENSSSCG00005018482. [P82125-1]
DR Ensembl; ENSSSCT00005029849; ENSSSCP00005018168; ENSSSCG00005018482. [P82125-1]
DR Ensembl; ENSSSCT00025032851; ENSSSCP00025013710; ENSSSCG00025024226. [P82125-1]
DR Ensembl; ENSSSCT00035029808; ENSSSCP00035011546; ENSSSCG00035022798. [P82125-1]
DR Ensembl; ENSSSCT00045048830; ENSSSCP00045033959; ENSSSCG00045028552. [P82125-1]
DR Ensembl; ENSSSCT00055002173; ENSSSCP00055001633; ENSSSCG00055001205. [P82125-1]
DR Ensembl; ENSSSCT00060086891; ENSSSCP00060037590; ENSSSCG00060063649. [P82125-1]
DR Ensembl; ENSSSCT00065085447; ENSSSCP00065037345; ENSSSCG00065062289. [P82125-1]
DR Ensembl; ENSSSCT00065085458; ENSSSCP00065037352; ENSSSCG00065062289. [P82125-1]
DR Ensembl; ENSSSCT00070011622; ENSSSCP00070009575; ENSSSCG00070006087. [P82125-1]
DR Ensembl; ENSSSCT00070011628; ENSSSCP00070009581; ENSSSCG00070006087. [P82125-1]
DR GeneID; 733633; -.
DR KEGG; ssc:733633; -.
DR CTD; 83592; -.
DR eggNOG; KOG1577; Eukaryota.
DR GeneTree; ENSGT00940000153272; -.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; P82125; -.
DR OMA; AEMYANE; -.
DR OrthoDB; 1016440at2759; -.
DR TreeFam; TF106492; -.
DR BioCyc; MetaCyc:MON-17139; -.
DR Proteomes; UP000008227; Chromosome 10.
DR Proteomes; UP000314985; Chromosome 10.
DR Bgee; ENSSSCG00000036941; Expressed in metanephros cortex and 35 other tissues.
DR ExpressionAtlas; P82125; baseline and differential.
DR Genevisible; P82125; SS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050571; F:1,5-anhydro-D-fructose reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR CDD; cd19110; AKR_AKR1E1-2; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044484; AKR1E2.
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; 2.
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 Alternative splicing; Direct protein sequencing; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..301
FT /note="1,5-anhydro-D-fructose reductase"
FT /id="PRO_0000124674"
FT ACT_SITE 40
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT BINDING 35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT BINDING 175
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT BINDING 246..258
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT SITE 69
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:P14550"
FT VAR_SEQ 288
FT /note="I -> M (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:16970816"
FT /id="VSP_037445"
FT VAR_SEQ 289..301
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:16970816"
FT /id="VSP_037446"
SQ SEQUENCE 301 AA; 34107 MW; 1B7D0FDFD141ED2E CRC64;
MEKIPVLGLG TWQAAPGEVT EAVKVAIDTG YRHFDCAYLY HNENEVGVGI QAKIDEGVVR
REDLFIVSKL WCTCHKKSLV KSACTRSLKA LKLQYLDLYL IHWPMGFKPG EVDLPVDRSG
MIVASNTDFL DTWEAMEDLV IEGLVRAIGV SNFNHEQLER LLNKPNLRVK PVTNQIECHP
YLTQKKLISF CQSRNVSVTA YRPLGGSSEG VPLLEDPVIQ TIAQKHGKSA AQILIRFQIQ
RNVIVIPKSV NPKRILENFQ VFDFELSEQD MTDLLGLDRN LRLSAFPIAE NHKDYPFKAE
Y
