Full text data of AKR1E2
AKR1E2
(AKR1CL2, AKRDC1)
[Confidence: low (only semi-automatic identification from reviews)]
1,5-anhydro-D-fructose reductase; AF reductase; 1.1.1.263 (Aldo-keto reductase family 1 member C-like protein 2; Aldo-keto reductase family 1 member E2; LoopADR; Testis-specific protein; hTSP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
1,5-anhydro-D-fructose reductase; AF reductase; 1.1.1.263 (Aldo-keto reductase family 1 member C-like protein 2; Aldo-keto reductase family 1 member E2; LoopADR; Testis-specific protein; hTSP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96JD6
ID AKCL2_HUMAN Reviewed; 320 AA.
AC Q96JD6; Q86Z16; Q86Z17; Q86Z18; Q9BU71;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-NOV-2009, sequence version 2.
DT 22-JAN-2014, entry version 89.
DE RecName: Full=1,5-anhydro-D-fructose reductase;
DE Short=AF reductase;
DE EC=1.1.1.263;
DE AltName: Full=Aldo-keto reductase family 1 member C-like protein 2;
DE AltName: Full=Aldo-keto reductase family 1 member E2;
DE AltName: Full=LoopADR;
DE AltName: Full=Testis-specific protein;
DE Short=hTSP;
GN Name=AKR1E2; Synonyms=AKR1CL2, AKRDC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5),
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=12604216; DOI=10.1016/S0009-2797(02)00187-4;
RA Nishinaka T., Azuma Y., Ushijima S., Miki T., Yabe-Nishimura C.;
RT "Human testis specific protein: a new member of aldo-keto reductase
RT superfamily.";
RL Chem. Biol. Interact. 143:299-305(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Small intestine;
RA Hyndman D.J., Li L., Flynn T.G.;
RT "LoopADR: a novel human aldo-keto reductase.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 1,5-anhydro-
CC D-fructose (AF) to 1,5-anhydro-D-glucitol. Can also catalyze the
CC reduction of various aldehydes and quinones (By similarity). Has
CC low NADPH-dependent reductase activity towards 9,10-
CC phenanthrenequinone (in vitro).
CC -!- CATALYTIC ACTIVITY: 1,5-anhydro-D-glucitol + NADP(+) = 1,5-
CC anhydro-D-fructose + NADPH.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.1 uM for 9,10-phenanthrenequinone with NADPH as cofactor;
CC Vmax=0.42 nmol/min/mg enzyme towards 9,10-phenanthrenequinone
CC with NADPH as cofactor;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96JD6-1; Sequence=Displayed;
CC Name=2; Synonyms=HTSP2;
CC IsoId=Q96JD6-2; Sequence=VSP_025615;
CC Name=3; Synonyms=HTSP1;
CC IsoId=Q96JD6-3; Sequence=VSP_025615, VSP_025616, VSP_025617;
CC Name=4; Synonyms=HTSP4;
CC IsoId=Q96JD6-4; Sequence=VSP_025616, VSP_025617;
CC Name=5; Synonyms=HTSP3;
CC IsoId=Q96JD6-5; Sequence=VSP_025614;
CC -!- TISSUE SPECIFICITY: Testis-specific.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB040820; BAC54565.1; -; mRNA.
DR EMBL; AB040821; BAC54566.1; -; mRNA.
DR EMBL; AB040822; BAC54567.1; -; mRNA.
DR EMBL; AB055603; BAC54568.1; -; mRNA.
DR EMBL; AF263242; AAK58523.1; -; mRNA.
DR EMBL; AC091817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002862; AAH02862.1; -; mRNA.
DR RefSeq; NP_001035267.1; NM_001040177.2.
DR RefSeq; NP_001257950.1; NM_001271021.1.
DR RefSeq; NP_001257954.1; NM_001271025.1.
DR UniGene; Hs.657944; -.
DR ProteinModelPortal; Q96JD6; -.
DR SMR; Q96JD6; 4-317.
DR PhosphoSite; Q96JD6; -.
DR DMDM; 269849539; -.
DR PaxDb; Q96JD6; -.
DR PRIDE; Q96JD6; -.
DR DNASU; 83592; -.
DR Ensembl; ENST00000298375; ENSP00000298375; ENSG00000165568.
DR Ensembl; ENST00000334019; ENSP00000335034; ENSG00000165568.
DR Ensembl; ENST00000345253; ENSP00000335603; ENSG00000165568.
DR Ensembl; ENST00000463345; ENSP00000436794; ENSG00000165568.
DR Ensembl; ENST00000532248; ENSP00000432947; ENSG00000165568.
DR GeneID; 83592; -.
DR KEGG; hsa:83592; -.
DR UCSC; uc001ihi.4; human.
DR CTD; 83592; -.
DR GeneCards; GC10P004829; -.
DR H-InvDB; HIX0008606; -.
DR HGNC; HGNC:23437; AKR1E2.
DR HPA; HPA037822; -.
DR neXtProt; NX_Q96JD6; -.
DR PharmGKB; PA165548224; -.
DR eggNOG; COG0656; -.
DR HOGENOM; HOG000250272; -.
DR HOVERGEN; HBG000020; -.
DR InParanoid; Q96JD6; -.
DR KO; K13981; -.
DR OMA; GFKPPHP; -.
DR PhylomeDB; Q96JD6; -.
DR BioCyc; MetaCyc:MONOMER-17140; -.
DR GenomeRNAi; 83592; -.
DR NextBio; 72513; -.
DR PRO; PR:Q96JD6; -.
DR ArrayExpress; Q96JD6; -.
DR Bgee; Q96JD6; -.
DR CleanEx; HS_AKR1CL2; -.
DR Genevestigator; Q96JD6; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050571; F:1,5-anhydro-D-fructose reductase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR001395; Aldo/ket_red.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR020471; Aldo/keto_reductase_subgr.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR PANTHER; PTHR11732; PTHR11732; 1.
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; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; NADP;
KW Oxidoreductase; Polymorphism; Reference proteome.
FT CHAIN 1 320 1,5-anhydro-D-fructose reductase.
FT /FTId=PRO_0000287880.
FT NP_BIND 269 277 NADP (By similarity).
FT ACT_SITE 40 40 Proton donor (By similarity).
FT BINDING 35 35 NADP (By similarity).
FT BINDING 102 102 Substrate (By similarity).
FT BINDING 193 193 NADP (By similarity).
FT SITE 69 69 Lowers pKa of active site Tyr (By
FT similarity).
FT VAR_SEQ 154 251 Missing (in isoform 5).
FT /FTId=VSP_025614.
FT VAR_SEQ 194 250 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_025615.
FT VAR_SEQ 307 307 I -> M (in isoform 3 and isoform 4).
FT /FTId=VSP_025616.
FT VAR_SEQ 308 320 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_025617.
FT VARIANT 52 52 C -> G (in dbSNP:rs35429729).
FT /FTId=VAR_032356.
FT VARIANT 86 86 K -> R (in dbSNP:rs17133693).
FT /FTId=VAR_032357.
FT CONFLICT 312 312 K -> N (in Ref. 2; AAK58523).
SQ SEQUENCE 320 AA; 36589 MW; A73E06225E7F15DD CRC64;
MGDIPAVGLS SWKASPGKVT EAVKEAIDAG YRHFDCAYFY HNEREVGAGI RCKIKEGAVR
REDLFIATKL WCTCHKKSLV ETACRKSLKA LKLNYLDLYL IHWPMGFKPP HPEWIMSCSE
LSFCLSHPRV QDLPLDESNM VIPSDTDFLD TWEAMEDLVI TGLVKNIGVS NFNHEQLERL
LNKPGLRFKP LTNQIECHPY LTQKNLISFC QSRDVSVTAY RPLGGSCEGV DLIDNPVIKR
IAKEHGKSPA QILIRFQIQR NVIVIPGSIT PSHIKENIQV FDFELTQHDM DNILSLNRNL
RLAMFPITKN HKDYPFHIEY
//
ID AKCL2_HUMAN Reviewed; 320 AA.
AC Q96JD6; Q86Z16; Q86Z17; Q86Z18; Q9BU71;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-NOV-2009, sequence version 2.
DT 22-JAN-2014, entry version 89.
DE RecName: Full=1,5-anhydro-D-fructose reductase;
DE Short=AF reductase;
DE EC=1.1.1.263;
DE AltName: Full=Aldo-keto reductase family 1 member C-like protein 2;
DE AltName: Full=Aldo-keto reductase family 1 member E2;
DE AltName: Full=LoopADR;
DE AltName: Full=Testis-specific protein;
DE Short=hTSP;
GN Name=AKR1E2; Synonyms=AKR1CL2, AKRDC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5),
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=12604216; DOI=10.1016/S0009-2797(02)00187-4;
RA Nishinaka T., Azuma Y., Ushijima S., Miki T., Yabe-Nishimura C.;
RT "Human testis specific protein: a new member of aldo-keto reductase
RT superfamily.";
RL Chem. Biol. Interact. 143:299-305(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Small intestine;
RA Hyndman D.J., Li L., Flynn T.G.;
RT "LoopADR: a novel human aldo-keto reductase.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 1,5-anhydro-
CC D-fructose (AF) to 1,5-anhydro-D-glucitol. Can also catalyze the
CC reduction of various aldehydes and quinones (By similarity). Has
CC low NADPH-dependent reductase activity towards 9,10-
CC phenanthrenequinone (in vitro).
CC -!- CATALYTIC ACTIVITY: 1,5-anhydro-D-glucitol + NADP(+) = 1,5-
CC anhydro-D-fructose + NADPH.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.1 uM for 9,10-phenanthrenequinone with NADPH as cofactor;
CC Vmax=0.42 nmol/min/mg enzyme towards 9,10-phenanthrenequinone
CC with NADPH as cofactor;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96JD6-1; Sequence=Displayed;
CC Name=2; Synonyms=HTSP2;
CC IsoId=Q96JD6-2; Sequence=VSP_025615;
CC Name=3; Synonyms=HTSP1;
CC IsoId=Q96JD6-3; Sequence=VSP_025615, VSP_025616, VSP_025617;
CC Name=4; Synonyms=HTSP4;
CC IsoId=Q96JD6-4; Sequence=VSP_025616, VSP_025617;
CC Name=5; Synonyms=HTSP3;
CC IsoId=Q96JD6-5; Sequence=VSP_025614;
CC -!- TISSUE SPECIFICITY: Testis-specific.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB040820; BAC54565.1; -; mRNA.
DR EMBL; AB040821; BAC54566.1; -; mRNA.
DR EMBL; AB040822; BAC54567.1; -; mRNA.
DR EMBL; AB055603; BAC54568.1; -; mRNA.
DR EMBL; AF263242; AAK58523.1; -; mRNA.
DR EMBL; AC091817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002862; AAH02862.1; -; mRNA.
DR RefSeq; NP_001035267.1; NM_001040177.2.
DR RefSeq; NP_001257950.1; NM_001271021.1.
DR RefSeq; NP_001257954.1; NM_001271025.1.
DR UniGene; Hs.657944; -.
DR ProteinModelPortal; Q96JD6; -.
DR SMR; Q96JD6; 4-317.
DR PhosphoSite; Q96JD6; -.
DR DMDM; 269849539; -.
DR PaxDb; Q96JD6; -.
DR PRIDE; Q96JD6; -.
DR DNASU; 83592; -.
DR Ensembl; ENST00000298375; ENSP00000298375; ENSG00000165568.
DR Ensembl; ENST00000334019; ENSP00000335034; ENSG00000165568.
DR Ensembl; ENST00000345253; ENSP00000335603; ENSG00000165568.
DR Ensembl; ENST00000463345; ENSP00000436794; ENSG00000165568.
DR Ensembl; ENST00000532248; ENSP00000432947; ENSG00000165568.
DR GeneID; 83592; -.
DR KEGG; hsa:83592; -.
DR UCSC; uc001ihi.4; human.
DR CTD; 83592; -.
DR GeneCards; GC10P004829; -.
DR H-InvDB; HIX0008606; -.
DR HGNC; HGNC:23437; AKR1E2.
DR HPA; HPA037822; -.
DR neXtProt; NX_Q96JD6; -.
DR PharmGKB; PA165548224; -.
DR eggNOG; COG0656; -.
DR HOGENOM; HOG000250272; -.
DR HOVERGEN; HBG000020; -.
DR InParanoid; Q96JD6; -.
DR KO; K13981; -.
DR OMA; GFKPPHP; -.
DR PhylomeDB; Q96JD6; -.
DR BioCyc; MetaCyc:MONOMER-17140; -.
DR GenomeRNAi; 83592; -.
DR NextBio; 72513; -.
DR PRO; PR:Q96JD6; -.
DR ArrayExpress; Q96JD6; -.
DR Bgee; Q96JD6; -.
DR CleanEx; HS_AKR1CL2; -.
DR Genevestigator; Q96JD6; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050571; F:1,5-anhydro-D-fructose reductase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR001395; Aldo/ket_red.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR020471; Aldo/keto_reductase_subgr.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR PANTHER; PTHR11732; PTHR11732; 1.
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; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; NADP;
KW Oxidoreductase; Polymorphism; Reference proteome.
FT CHAIN 1 320 1,5-anhydro-D-fructose reductase.
FT /FTId=PRO_0000287880.
FT NP_BIND 269 277 NADP (By similarity).
FT ACT_SITE 40 40 Proton donor (By similarity).
FT BINDING 35 35 NADP (By similarity).
FT BINDING 102 102 Substrate (By similarity).
FT BINDING 193 193 NADP (By similarity).
FT SITE 69 69 Lowers pKa of active site Tyr (By
FT similarity).
FT VAR_SEQ 154 251 Missing (in isoform 5).
FT /FTId=VSP_025614.
FT VAR_SEQ 194 250 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_025615.
FT VAR_SEQ 307 307 I -> M (in isoform 3 and isoform 4).
FT /FTId=VSP_025616.
FT VAR_SEQ 308 320 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_025617.
FT VARIANT 52 52 C -> G (in dbSNP:rs35429729).
FT /FTId=VAR_032356.
FT VARIANT 86 86 K -> R (in dbSNP:rs17133693).
FT /FTId=VAR_032357.
FT CONFLICT 312 312 K -> N (in Ref. 2; AAK58523).
SQ SEQUENCE 320 AA; 36589 MW; A73E06225E7F15DD CRC64;
MGDIPAVGLS SWKASPGKVT EAVKEAIDAG YRHFDCAYFY HNEREVGAGI RCKIKEGAVR
REDLFIATKL WCTCHKKSLV ETACRKSLKA LKLNYLDLYL IHWPMGFKPP HPEWIMSCSE
LSFCLSHPRV QDLPLDESNM VIPSDTDFLD TWEAMEDLVI TGLVKNIGVS NFNHEQLERL
LNKPGLRFKP LTNQIECHPY LTQKNLISFC QSRDVSVTAY RPLGGSCEGV DLIDNPVIKR
IAKEHGKSPA QILIRFQIQR NVIVIPGSIT PSHIKENIQV FDFELTQHDM DNILSLNRNL
RLAMFPITKN HKDYPFHIEY
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