ID AK1C2_HUMAN Reviewed; 323 AA.
AC P52895; A8K2N9; B4DKR9; Q14133; Q5SR16; Q7M4N1; Q96A71;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 3.
DT 01-MAY-2013, entry version 134.
DE RecName: Full=Aldo-keto reductase family 1 member C2;
DE EC=1.-.-.-;
DE AltName: Full=3-alpha-HSD3;
DE AltName: Full=Chlordecone reductase homolog HAKRD;
DE AltName: Full=Dihydrodiol dehydrogenase 2;
DE Short=DD-2;
DE Short=DD2;
DE AltName: Full=Dihydrodiol dehydrogenase/bile acid-binding protein;
DE Short=DD/BABP;
DE AltName: Full=Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase;
DE EC=1.3.1.20;
DE AltName: Full=Type III 3-alpha-hydroxysteroid dehydrogenase;
DE EC=1.1.1.213;
GN Name=AKR1C2; Synonyms=DDH2;
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] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8274401; DOI=10.1016/0960-0760(93)90308-J;
RA Qin K.-N., New M.I., Cheng K.-C.;
RT "Molecular cloning of multiple cDNAs encoding human enzymes
RT structurally related to 3 alpha-hydroxysteroid dehydrogenase.";
RL J. Steroid Biochem. Mol. Biol. 46:673-679(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=8011662; DOI=10.1016/0005-2728(94)90144-9;
RA Ciaccio P.J., Tew K.D.;
RT "cDNA and deduced amino acid sequences of a human colon dihydrodiol
RT dehydrogenase.";
RL Biochim. Biophys. Acta 1186:129-132(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT TYR-46.
RX PubMed=7959017; DOI=10.1016/0378-1119(94)90176-7;
RA Qin K.-N., Khanna M., Cheng K.-C.;
RT "Structure of a gene coding for human dihydrodiol dehydrogenase/bile
RT acid-binding protein.";
RL Gene 149:357-361(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Prostate;
RX PubMed=8920937; DOI=10.1006/bbrc.1996.1684;
RA Dufort I., Soucy P., Labrie F., Luu-The V.;
RT "Molecular cloning of human type 3 3 alpha-hydroxysteroid
RT dehydrogenase that differs from 20 alpha-hydroxysteroid dehydrogenase
RT by seven amino acids.";
RL Biochem. Biophys. Res. Commun. 228:474-479(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=9716498;
RA Shiraishi H., Ishikura S., Matsuura K., Deyashiki Y., Ninomiya M.,
RA Sakai S., Hara A.;
RT "Sequence of the cDNA of a human dihydrodiol dehydrogenase isoform
RT (AKR1C2) and tissue distribution of its mRNA.";
RL Biochem. J. 334:399-405(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=10672042; DOI=10.1046/j.1365-2443.2000.00310.x;
RA Nishizawa M., Nakajima T., Yasuda K., Kanzaki H., Sasaguri Y.,
RA Watanabe K., Ito S.;
RT "Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with
RT three aldo-keto reductase genes.";
RL Genes Cells 5:111-125(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Urinary bladder;
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 [11]
RP PROTEIN SEQUENCE OF 2-31; 40-62; 69-100; 105-131; 137-153; 162-206;
RP 209-231; 250-269 AND 271-323, FUNCTION, CATALYTIC ACTIVITY, ENZYME
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8573067;
RA Hara A., Matsuura K., Tamada Y., Sato K., Miyabe Y., Deyashiki Y.,
RA Ishida N.;
RT "Relationship of human liver dihydrodiol dehydrogenases to hepatic
RT bile-acid-binding protein and an oxidoreductase of human colon
RT cells.";
RL Biochem. J. 313:373-376(1996).
RN [12]
RP PROTEIN SEQUENCE OF 10-29; 40-55; 76-101; 105-128; 137-146; 162-197;
RP 208-223; 259-270 AND 305-322.
RC TISSUE=Liver;
RX PubMed=8486699;
RA Stolz A., Hammond L., Lou H., Takikawa H., Ronk M., Shively J.E.;
RT "cDNA cloning and expression of the human hepatic bile acid-binding
RT protein. A member of the monomeric reductase gene family.";
RL J. Biol. Chem. 268:10448-10457(1993).
RN [13]
RP TISSUE SPECIFICITY, VARIANTS SRXY8 VAL-79; GLN-90; GLN-222 AND
RP THR-300, AND CHARACTERIZATION OF VARIANTS SRXY8 VAL-79; GLN-90;
RP GLN-222 AND THR-300.
RX PubMed=21802064; DOI=10.1016/j.ajhg.2011.06.009;
RA Fluck C.E., Meyer-Boni M., Pandey A.V., Kempna P., Miller W.L.,
RA Schoenle E.J., Biason-Lauber A.;
RT "Why boys will be boys: two pathways of fetal testicular androgen
RT biosynthesis are needed for male sexual differentiation.";
RL Am. J. Hum. Genet. 89:201-218(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH NADP AND
RP URSODEOXYCHOLATE.
RX PubMed=11513593; DOI=10.1021/bi010919a;
RA Jin Y., Stayrook S.E., Albert R.H., Palackal N.T., Penning T.M.,
RA Lewis M.;
RT "Crystal structure of human type III 3alpha-hydroxysteroid
RT dehydrogenase/bile acid binding protein complexed with NADP(+) and
RT ursodeoxycholate.";
RL Biochemistry 40:10161-10168(2001).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH NADP AND
RP TESTOSTERONE.
RX PubMed=11514561; DOI=10.1074/jbc.M105610200;
RA Nahoum V., Gangloff A., Legrand P., Zhu D.-W., Cantin L., Zhorov B.S.,
RA Luu-The V., Labrie F., Breton R., Lin S.X.;
RT "Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in
RT complex with testosterone and NADP at 1.25-A resolution.";
RL J. Biol. Chem. 276:42091-42098(2001).
CC -!- FUNCTION: Works in concert with the 5-alpha/5-beta-steroid
CC reductases to convert steroid hormones into the 3-alpha/5-alpha
CC and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation
CC of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-
CC DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol).
CC Has a high bile-binding ability.
CC -!- CATALYTIC ACTIVITY: Trans-1,2-dihydrobenzene-1,2-diol + NADP(+) =
CC catechol + NADPH.
CC -!- CATALYTIC ACTIVITY: A 3-alpha-hydroxysteroid + NAD(P)(+) = a 3-
CC oxosteroid + NAD(P)H.
CC -!- ENZYME REGULATION: Inhibited by hexestrol with an IC(50) of 2.8
CC uM, 1,10-phenanthroline with an IC(50) of 2100 uM, 1,7-
CC phenanthroline with an IC(50) of 1500 uM, flufenamic acid with an
CC IC(50) of 0.9 uM, indomethacin with an IC(50) of 75 uM, ibuprofen
CC with an IC(50) of 6.9 uM, lithocholic acid with an IC(50) of 0.07
CC uM, ursodeoxycholic acid with an IC(50) of 0.08 uM and
CC chenodeoxycholic acid with an IC(50) of 0.13 uM.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=260 uM for (s)-tetralol;
CC KM=520 uM for (s)-indan-1-ol;
CC KM=5000 uM for benzene dihydrodiol;
CC KM=1 uM for 5-beta-pregnane-3-alpha,20-alpha-diol;
CC KM=208 uM for 9-alpha,11-beta-PGF2;
CC KM=0.3 uM for 5-beta-androstane-3,17-dione;
CC KM=79 uM for PGD2;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P52895-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52895-2; Sequence=VSP_043779, VSP_043780;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in fetal testes. Expressed in fetal
CC and adult adrenal glands.
CC -!- DISEASE: 46,XY sex reversal 8 (SRXY8) [MIM:614279]: A disorder of
CC sex development. Affected individuals have a 46,XY karyotype but
CC present as phenotypically normal females. Note=The disease is
CC caused by mutations affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family.
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DR EMBL; S68330; AAD14013.1; -; mRNA.
DR EMBL; U05598; AAA20937.1; -; mRNA.
DR EMBL; L32592; AAB38486.1; -; Genomic_DNA.
DR EMBL; AB021654; BAA36169.1; -; mRNA.
DR EMBL; AB031084; BAA92884.1; -; mRNA.
DR EMBL; AB032153; BAA92891.1; -; Genomic_DNA.
DR EMBL; AK290304; BAF82993.1; -; mRNA.
DR EMBL; AK296686; BAG59281.1; -; mRNA.
DR EMBL; BT006653; AAP35299.1; -; mRNA.
DR EMBL; AL713867; CAI16408.1; -; Genomic_DNA.
DR EMBL; AL391427; CAI16408.1; JOINED; Genomic_DNA.
DR EMBL; BC007024; AAH07024.1; -; mRNA.
DR EMBL; BC063574; AAH63574.1; -; mRNA.
DR IPI; IPI00005668; -.
DR PIR; I73676; I73676.
DR PIR; JC5240; JC5240.
DR PIR; S61516; S61516.
DR RefSeq; NP_001128713.1; NM_001135241.2.
DR RefSeq; NP_001345.1; NM_001354.5.
DR RefSeq; NP_995317.1; NM_205845.2.
DR UniGene; Hs.460260; -.
DR UniGene; Hs.567256; -.
DR UniGene; Hs.734597; -.
DR PDB; 1IHI; X-ray; 3.00 A; A/B=1-323.
DR PDB; 1J96; X-ray; 1.25 A; A/B=2-323.
DR PDB; 1XJB; X-ray; 1.90 A; A/B=2-323.
DR PDB; 2HDJ; X-ray; 2.00 A; A/B=1-323.
DR PDB; 2IPJ; X-ray; 1.80 A; A/B=3-323.
DR PDBsum; 1IHI; -.
DR PDBsum; 1J96; -.
DR PDBsum; 1XJB; -.
DR PDBsum; 2HDJ; -.
DR PDBsum; 2IPJ; -.
DR ProteinModelPortal; P52895; -.
DR IntAct; P52895; 1.
DR STRING; 9606.ENSP00000370129; -.
DR PhosphoSite; P52895; -.
DR DMDM; 20532374; -.
DR PaxDb; P52895; -.
DR PRIDE; P52895; -.
DR DNASU; 1646; -.
DR Ensembl; ENST00000380753; ENSP00000370129; ENSG00000151632.
DR Ensembl; ENST00000407674; ENSP00000385221; ENSG00000151632.
DR Ensembl; ENST00000455190; ENSP00000408440; ENSG00000151632.
DR Ensembl; ENST00000580345; ENSP00000463185; ENSG00000265231.
DR Ensembl; ENST00000580545; ENSP00000464045; ENSG00000265231.
DR Ensembl; ENST00000585272; ENSP00000462069; ENSG00000265231.
DR GeneID; 1646; -.
DR KEGG; hsa:1646; -.
DR UCSC; uc001ihs.3; human.
DR CTD; 1646; -.
DR GeneCards; GC10M005021; -.
DR HGNC; HGNC:385; AKR1C2.
DR HPA; CAB047304; -.
DR MIM; 600450; gene.
DR MIM; 614279; phenotype.
DR neXtProt; NX_P52895; -.
DR Orphanet; 90796; 46,XY disorder of sex development due to isolated 17, 20 lyase deficiency.
DR PharmGKB; PA24678; -.
DR eggNOG; COG0656; -.
DR HOGENOM; HOG000250272; -.
DR HOVERGEN; HBG000020; -.
DR InParanoid; P52895; -.
DR KO; K00089; -.
DR KO; K00212; -.
DR OMA; HRDPEMV; -.
DR OrthoDB; EOG4Q2DG2; -.
DR PhylomeDB; P52895; -.
DR BioCyc; MetaCyc:HS07754-MONOMER; -.
DR BRENDA; 1.1.1.213; 2681.
DR SABIO-RK; P52895; -.
DR BindingDB; P52895; -.
DR ChEMBL; CHEMBL5847; -.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB01586; Ursodeoxycholic acid.
DR EvolutionaryTrace; P52895; -.
DR GenomeRNAi; 1646; -.
DR NextBio; 6772; -.
DR ArrayExpress; P52895; -.
DR Bgee; P52895; -.
DR CleanEx; HS_AKR1C2; -.
DR Genevestigator; P52895; -.
DR GermOnline; ENSG00000151632; Homo sapiens.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0047026; F:androsterone dehydrogenase (A-specific) activity; IEA:EC.
DR GO; GO:0032052; F:bile acid binding; IDA:UniProtKB.
DR GO; GO:0047086; F:ketosteroid monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:UniProtKB.
DR GO; GO:0018636; F:phenanthrene 9,10-monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0004958; F:prostaglandin F receptor activity; IDA:UniProtKB.
DR GO; GO:0047115; F:trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0071395; P:cellular response to jasmonic acid stimulus; IDA:UniProtKB.
DR GO; GO:0044597; P:daunorubicin metabolic process; IMP:UniProtKB.
DR GO; GO:0007586; P:digestion; IDA:UniProtKB.
DR GO; GO:0044598; P:doxorubicin metabolic process; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling cascade; IDA:UniProtKB.
DR GO; GO:0042448; P:progesterone metabolic process; IDA:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; IDA:UniProtKB.
DR GO; GO:0034694; P:response to prostaglandin stimulus; IDA:UniProtKB.
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; Aldo/ket_red; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; FALSE_NEG.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Disease mutation; Lipid metabolism; NADP;
KW Oxidoreductase; Polymorphism; Reference proteome; Steroid metabolism.
FT CHAIN 1 323 Aldo-keto reductase family 1 member C2.
FT /FTId=PRO_0000124637.
FT NP_BIND 216 280 NADP.
FT ACT_SITE 55 55 Proton donor.
FT BINDING 117 117 Substrate.
FT SITE 84 84 Lowers pKa of active site Tyr (By
FT similarity).
FT VAR_SEQ 124 139 PGEEVIPKDENGKILF -> EDIGILTWKKSPKHNS (in
FT isoform 2).
FT /FTId=VSP_043779.
FT VAR_SEQ 140 323 Missing (in isoform 2).
FT /FTId=VSP_043780.
FT VARIANT 46 46 F -> Y (in dbSNP:rs2854482).
FT /FTId=VAR_048216.
FT VARIANT 79 79 I -> V (in SRXY8; partially impaired
FT activity).
FT /FTId=VAR_066632.
FT VARIANT 90 90 H -> Q (in SRXY8; partially impaired
FT activity).
FT /FTId=VAR_066633.
FT VARIANT 172 172 L -> Q (in dbSNP:rs11474).
FT /FTId=VAR_014748.
FT VARIANT 222 222 H -> Q (in SRXY8; partially impaired
FT activity).
FT /FTId=VAR_066634.
FT VARIANT 300 300 N -> T (in SRXY8; partially impaired
FT activity).
FT /FTId=VAR_066635.
FT CONFLICT 76 76 R -> S (in Ref. 12; AA sequence).
FT CONFLICT 87 87 S -> C (in Ref. 12; AA sequence).
FT CONFLICT 93 93 E -> EE (in Ref. 12; AA sequence).
FT CONFLICT 111 111 V -> A (in Ref. 3; AAB38486).
FT CONFLICT 164 164 G -> R (in Ref. 7; BAF82993).
FT CONFLICT 179 179 K -> E (in Ref. 1; AAD14013 and 3;
FT AAB38486).
FT CONFLICT 185 185 K -> E (in Ref. 1; AAD14013 and 3;
FT AAB38486).
FT CONFLICT 188 188 C -> H (in Ref. 12; AA sequence).
FT CONFLICT 193 193 C -> H (in Ref. 12; AA sequence).
FT CONFLICT 319 319 F -> I (in Ref. 1; AAD14013 and 3;
FT AAB38486).
FT STRAND 7 9
FT STRAND 15 22
FT HELIX 32 44
FT STRAND 48 50
FT HELIX 53 55
FT HELIX 58 70
FT HELIX 76 78
FT STRAND 80 85
FT HELIX 87 89
FT HELIX 92 94
FT HELIX 95 106
FT STRAND 111 116
FT STRAND 119 122
FT STRAND 124 126
FT HELIX 144 156
FT STRAND 159 167
FT HELIX 170 177
FT STRAND 187 192
FT HELIX 200 208
FT STRAND 212 217
FT TURN 225 227
FT HELIX 235 237
FT HELIX 239 248
FT HELIX 252 262
FT STRAND 266 270
FT HELIX 274 280
FT HELIX 281 285
FT HELIX 290 297
FT HELIX 309 311
FT STRAND 318 321
SQ SEQUENCE 323 AA; 36735 MW; 0D7B6F983FCE85E1 CRC64;
MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEAVKL AIEAGFHHID SAHVYNNEEQ
VGLAIRSKIA DGSVKREDIF YTSKLWSNSH RPELVRPALE RSLKNLQLDY VDLYLIHFPV
SVKPGEEVIP KDENGKILFD TVDLCATWEA MEKCKDAGLA KSIGVSNFNH RLLEMILNKP
GLKYKPVCNQ VECHPYFNQR KLLDFCKSKD IVLVAYSALG SHREEPWVDP NSPVLLEDPV
LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTS EEMKAIDGLN
RNVRYLTLDI FAGPPNYPFS DEY
//
