(data stored in ACNUC25930 zone)

HOGENOM: HS10_PE101

ID   HS10_PE101                           STANDARD;      PRT;   323 AA.
AC   HS10_PE101; P17516; Q5T6A3; Q8WW84; Q9NS54;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Aldo-keto reductase family 1 member C4; EC=1.1.1.-;AltName:
DE   Full=3-alpha-HSD1;AltName: Full=3-alpha-hydroxysteroid dehydrogenase type
DE   I; EC=1.1.1.50;AltName: Full=Chlordecone reductase; Short=CDR; EC=1.1.1
DE   225;AltName: Full=Dihydrodiol dehydrogenase 4; Short=DD-4;
DE   Short=DD4;AltName: Full=HAKRA; (HS10.PE101).
GN   Name=AKR1C4; Synonyms=CHDR;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS10.PE101.
CC       Homo sapiens chromosome 10 GRCh37  sequence 1..135524747 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:AK1C4_HUMAN
CC   -!- FUNCTION: Catalyzes the transformation of the potent androgen
CC       dihydrotestosterone (DHT) into the less active form, 5-alpha-
CC       androstan-3-alpha,17-beta-diol (3-alpha-diol). Also has some 20-
CC       alpha-hydroxysteroid dehydrogenase activity. The biotransformation
CC       of the pesticide chlordecone (kepone) to its corresponding alcohol
CC       leads to increased biliary excretion of the pesticide and
CC       concomitant reduction of its neurotoxicity since bile is the major
CC       excretory route.
CC   -!- CATALYTIC ACTIVITY: Chlordecone alcohol + NADP(+) = chlordecone +
CC       NADPH.
CC   -!- CATALYTIC ACTIVITY: Androsterone + NAD(P)(+) = 5-alpha-androstane-
CC       3,17-dione + NAD(P)H.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Liver specific.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- POLYMORPHISM: The allele with Cys-145/Val-311 shows a three- to
CC       five-fold decrease in catalytic efficiency for xenobiotic and
CC       steroidal substrates compared to the Ser-145/Leu-311 allele.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA35658.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC   -!- GENE_FAMILY: HOG000250272 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000198610;ENST00000263126;ENSP00000263126.
DR   EMBL; AB031085; - ;
DR   EMBL; AB032163; - ;
DR   EMBL; AB045829; - ;
DR   EMBL; AL355303; - ;
DR   EMBL; BC020744; - ;
DR   EMBL; D26125; - ;
DR   EMBL; D89962; - ;
DR   EMBL; M33375; - ;
DR   EMBL; S68287; - ;
DR   UniProtKB/Swiss-Prot; P17516; Q5T6A3; Q8WW84; Q9NS54; -.
DR   EMBL; S68287; AAD14010.1; -; mRNA.
DR   EMBL; AB045829; BAA99542.1; -; mRNA.
DR   EMBL; AB031085; BAA92885.1; -; mRNA.
DR   EMBL; AB032163; BAA92893.1; -; Genomic_DNA.
DR   EMBL; AL355303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC020744; AAH20744.1; -; mRNA.
DR   EMBL; M33375; AAA35658.1; ALT_INIT; mRNA.
DR   EMBL; D26125; BAA05122.1; -; mRNA.
DR   IPI; IPI00289524; -.
DR   PIR; A57407; A57407.
DR   PIR; S59620; S59620.
DR   RefSeq; NP_001809.3; NM_001818.3.
DR   UniGene; Hs.567245; -.
DR   PDB; 2FVL; X-ray; 2.40 A; A/B/C=1-323.
DR   PDBsum; 2FVL; -.
DR   ProteinModelPortal; P17516; -.
DR   SMR; P17516; 1-323.
DR   STRING; P17516; -.
DR   PhosphoSite; P17516; -.
DR   PRIDE; P17516; -.
DR   Ensembl; ENST00000263126; ENSP00000263126; ENSG00000198610.
DR   Ensembl; ENST00000380448; ENSP00000369814; ENSG00000198610.
DR   GeneID; 1109; -.
DR   KEGG; hsa:1109; -.
DR   UCSC; uc001ihw.1; human.
DR   CTD; 1109; -.
DR   GeneCards; GC10P005228; -.
DR   H-InvDB; HIX0008607; -.
DR   HGNC; HGNC:387; AKR1C4.
DR   HPA; CAB006258; -.
DR   MIM; 600451; gene.
DR   neXtProt; NX_P17516; -.
DR   PharmGKB; PA24680; -.
DR   eggNOG; prNOG19511; -.
DR   InParanoid; P17516; -.
DR   OMA; KYQRVEL; -.
DR   OrthoDB; EOG4Q2DG2; -.
DR   PhylomeDB; P17516; -.
DR   Reactome; REACT_22258; Metabolism of lipids and lipoproteins.
DR   DrugBank; DB00157; NADH.
DR   NextBio; 4602; -.
DR   ArrayExpress; P17516; -.
DR   Bgee; P17516; -.
DR   CleanEx; HS_AKR1C4; -.
DR   Genevestigator; P17516; -.
DR   GermOnline; ENSG00000198610; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0004033; F:aldo-keto reductase (NADP) activity; EXP:Reactome.
DR   GO; GO:0047042; F:androsterone dehydrogenase (B-specific) activity; IEA:EC.
DR   GO; GO:0015125; F:bile acid transmembrane transporter activity; TAS:ProtInc.
DR   GO; GO:0047743; F:chlordecone reductase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; TAS:UniProtKB.
DR   GO; GO:0008209; P:androgen metabolic process; TAS:ProtInc.
DR   GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
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   Gene3D; G3DSA:3.20.20.100; Aldo/ket_red; 1.
DR   PANTHER; PTHR11732; Aldo/ket_red; 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; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
DR   HOGENOMDNA; HS10.PE101; -.
KW   ENSG000001986101755old_1320000031; ENSP000002631267901old_1320000031;
KW   Q96SD9_HUMAN; AB031085; AB032163; AB045829; AL355303; BC020744; D26125;
KW   M33375; S68287;
KW   3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; NADP; Oxidoreductase; Phosphoprotein;
KW   Polymorphism; Reference proteome.
SQ   SEQUENCE   323 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDPKYQRVEL NDGHFMPVLG FGTYAPPEVP RNRAVEVTKL AIEAGFRHID SAYLYNNEEQ
     VGLAIRSKIA DGSVKREDIF YTSKLWCTFF QPQMVQPALE SSLKKLQLDY VDLYLLHFPM
     ALKPGETPLP KDENGKVIFD TVDLSATWEV MEKCKDAGLA KSIGVSNFNC RQLEMILNKP
     GLKYKPVCNQ VECHPYLNQS KLLDFCKSKD IVLVAHSALG TQRHKLWVDP NSPVLLEDPV
     LCALAKKHKQ TPALIALRYQ LQRGVVVLAK SYNEQRIREN IQVFEFQLTS EDMKVLDGLN
     RNYRYVVMDF LMDHPDYPFS DEY
//

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