(data stored in ACNUC27125 zone)

SWISSPROT: AK1C4_HUMAN

ID   AK1C4_HUMAN             Reviewed;         323 AA.
AC   P17516; Q5T6A3; Q8WW84; Q9NS54;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   11-DEC-2019, entry version 204.
DE   RecName: Full=Aldo-keto reductase family 1 member C4;
DE            EC=1.1.1.-;
DE   AltName: Full=3-alpha-HSD1;
DE   AltName: Full=3-alpha-hydroxysteroid dehydrogenase type I;
DE            EC=1.1.1.357;
DE   AltName: Full=Chlordecone reductase;
DE            Short=CDR;
DE            EC=1.1.1.225;
DE   AltName: Full=Dihydrodiol dehydrogenase 4;
DE            Short=DD-4;
DE            Short=DD4;
DE   AltName: Full=HAKRA;
GN   Name=AKR1C4; Synonyms=CHDR;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-250.
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 structurally
RT   related to 3 alpha-hydroxysteroid dehydrogenase.";
RL   J. Steroid Biochem. Mol. Biol. 46:673-679(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND VARIANT ARG-250.
RX   PubMed=7650035; DOI=10.1074/jbc.270.34.20162;
RA   Khanna M., Qin K.-N., Wang R.W., Cheng K.-C.;
RT   "Substrate specificity, gene structure, and tissue-specific distribution of
RT   multiple human 3 alpha-hydroxysteroid dehydrogenases.";
RL   J. Biol. Chem. 270:20162-20168(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-250.
RX   PubMed=7626489; DOI=10.1016/0960-0760(95)00019-v;
RA   Khanna M., Qin K.-N., Cheng K.-C.;
RT   "Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and
RT   molecular cloning of multiple cDNAs encoding structurally related proteins
RT   in humans.";
RL   J. Steroid Biochem. Mol. Biol. 53:41-46(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS CYS-145; ARG-250 AND VAL-311.
RC   TISSUE=Liver;
RX   PubMed=10634139;
RA   Kume T., Iwasa H., Shiraishi H., Yokoi T., Nagashima K., Otsuka M.,
RA   Terada T., Takagi T., Hara A., Kamataki T.;
RT   "Characterization of a novel variant (S145C/L311V) of 3alpha-
RT   hydroxysteroid/dihydrodiol dehydrogenase in human liver.";
RL   Pharmacogenetics 9:763-771(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT ARG-250.
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., Watanabe K.,
RA   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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION OF 3-ALPHA-HSD ACTIVITY,
RP   TISSUE SPECIFICITY, AND VARIANT ARG-250.
RC   TISSUE=Liver;
RX   PubMed=11158055; DOI=10.1210/jcem.86.2.7216;
RA   Dufort I., Labrie F., Luu-The V.;
RT   "Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases: differential
RT   lability and tissue distribution.";
RL   J. Clin. Endocrinol. Metab. 86:841-846(2001).
RN   [7]
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., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., 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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TYR-170 AND ARG-250.
RC   TISSUE=Liver;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-323, AND VARIANT ARG-250.
RC   TISSUE=Liver;
RX   PubMed=2187532; DOI=10.1021/bi00456a034;
RA   Winters C.J., Molowa D.T., Guzelian P.S.;
RT   "Isolation and characterization of cloned cDNAs encoding human liver
RT   chlordecone reductase.";
RL   Biochemistry 29:1080-1087(1990).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-323, PROTEIN SEQUENCE OF 5-29; 76-131;
RP   184-201 AND 271-294, AND VARIANT ARG-250.
RC   TISSUE=Liver;
RX   PubMed=8172617; DOI=10.1042/bj2990545;
RA   Deyashiki Y., Ogasawara A., Nakayama T., Nakanishi M., Miyabe Y., Sato K.,
RA   Hara A.;
RT   "Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol
RT   dehydrogenase isoenzymes that are identical with chlordecone reductase and
RT   bile-acid binder.";
RL   Biochem. J. 299:545-552(1994).
RN   [11]
RP   PROTEIN SEQUENCE OF 40-54; 105-121; 162-175; 184-196; 277-291 AND 307-321,
RP   AND CHARACTERIZATION AS 3-ALPHA-HSD.
RX   PubMed=1530633; DOI=10.1016/0006-291x(92)91260-w;
RA   Binstock J.M., Iyer R.B., Hamby C.V., Fried V.A., Schwartz I.S.,
RA   Weinstein B.I., Southren A.L.;
RT   "Human hepatic 3 alpha-hydroxysteroid dehydrogenase: possible identity with
RT   human hepatic chlordecone reductase.";
RL   Biochem. Biophys. Res. Commun. 187:760-766(1992).
RN   [12]
RP   INVOLVEMENT IN SRXY8.
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   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NADP.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of human 3-alpha hydroxysteroid/dihydrodiol
RT   dehydrogenase (AKR1C4) complexed with NADP+.";
RL   Submitted (FEB-2006) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the transformation of the potent androgen
CC       dihydrotestosterone (DHT) into the less active form, 5-alpha-androstan-
CC       3-alpha,17-beta-diol (3-alpha-diol). Also has some 20-alpha-
CC       hydroxysteroid dehydrogenase activity. The biotransformation of the
CC       pesticide chlordecone (kepone) to its corresponding alcohol leads to
CC       increased biliary excretion of the pesticide and concomitant reduction
CC       of its neurotoxicity since bile is the major excretory route.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chlordecone alcohol + NADP(+) = chlordecone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:14401, ChEBI:CHEBI:15378, ChEBI:CHEBI:16548,
CC         ChEBI:CHEBI:17184, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.225;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3alpha-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) +
CC         NADPH; Xref=Rhea:RHEA:34783, ChEBI:CHEBI:15378, ChEBI:CHEBI:36835,
CC         ChEBI:CHEBI:47788, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.357;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3alpha-hydroxysteroid + NAD(+) = a 3-oxosteroid + H(+) +
CC         NADH; Xref=Rhea:RHEA:34779, ChEBI:CHEBI:15378, ChEBI:CHEBI:36835,
CC         ChEBI:CHEBI:47788, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.357;
CC   -!- SUBUNIT: Monomer. {ECO:0000269|Ref.14}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Liver specific. {ECO:0000269|PubMed:11158055,
CC       ECO:0000269|PubMed:7650035}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- POLYMORPHISM: The allele with Cys-145/Val-311 shows a three- to five-
CC       fold decrease in catalytic efficiency for xenobiotic and steroidal
CC       substrates compared to the Ser-145/Leu-311 allele.
CC   -!- DISEASE: 46,XY sex reversal 8 (SRXY8) [MIM:614279]: A disorder of sex
CC       development. Affected individuals have a 46,XY karyotype but present as
CC       phenotypically normal females. {ECO:0000269|PubMed:21802064}. Note=The
CC       gene represented in this entry may act as a disease modifier. A
CC       splicing mutation resulting in loss of AKR1C4 exon 2 has been found in
CC       affected individuals carrying a causative mutation in AKR1C2
CC       (PubMed:21802064). These patients manifest a more severe disease
CC       phenotype than individuals only carrying mutations in AKR1C2.
CC       {ECO:0000269|PubMed:21802064}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA35658.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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   CCDS; CCDS7064.1; -.
DR   PIR; A57407; A57407.
DR   PIR; S59620; S59620.
DR   RefSeq; NP_001809.3; NM_001818.3.
DR   PDB; 2FVL; X-ray; 2.40 A; A/B/C=1-323.
DR   PDBsum; 2FVL; -.
DR   SMR; P17516; -.
DR   BioGrid; 107534; 5.
DR   IntAct; P17516; 3.
DR   STRING; 9606.ENSP00000369814; -.
DR   BindingDB; P17516; -.
DR   ChEMBL; CHEMBL4999; -.
DR   DrugBank; DB13751; Glycyrrhizic acid.
DR   DrugBank; DB00461; Nabumetone.
DR   DrugBank; DB00157; NADH.
DR   DrugCentral; P17516; -.
DR   SwissLipids; SLP:000000805; -.
DR   iPTMnet; P17516; -.
DR   PhosphoSitePlus; P17516; -.
DR   SwissPalm; P17516; -.
DR   BioMuta; AKR1C4; -.
DR   DMDM; 308153631; -.
DR   jPOST; P17516; -.
DR   MassIVE; P17516; -.
DR   MaxQB; P17516; -.
DR   PaxDb; P17516; -.
DR   PeptideAtlas; P17516; -.
DR   PRIDE; P17516; -.
DR   ProteomicsDB; 53480; -.
DR   DNASU; 1109; -.
DR   Ensembl; ENST00000263126; ENSP00000263126; ENSG00000198610.
DR   Ensembl; ENST00000380448; ENSP00000369814; ENSG00000198610.
DR   GeneID; 1109; -.
DR   KEGG; hsa:1109; -.
DR   UCSC; uc001ihw.2; human.
DR   CTD; 1109; -.
DR   DisGeNET; 1109; -.
DR   EuPathDB; HostDB:ENSG00000198610.10; -.
DR   GeneCards; AKR1C4; -.
DR   HGNC; HGNC:387; AKR1C4.
DR   HPA; HPA044720; -.
DR   HPA; HPA068265; -.
DR   MalaCards; AKR1C4; -.
DR   MIM; 600451; gene.
DR   MIM; 614279; phenotype.
DR   neXtProt; NX_P17516; -.
DR   OpenTargets; ENSG00000198610; -.
DR   Orphanet; 443087; 46,XY disorder of sex development due to testicular 17,20-desmolase deficiency.
DR   PharmGKB; PA24680; -.
DR   eggNOG; KOG1577; Eukaryota.
DR   eggNOG; COG0656; LUCA.
DR   GeneTree; ENSGT00940000163771; -.
DR   HOGENOM; HOG000250272; -.
DR   InParanoid; P17516; -.
DR   KO; K00037; -.
DR   OMA; ECGEGVA; -.
DR   OrthoDB; 1016440at2759; -.
DR   PhylomeDB; P17516; -.
DR   TreeFam; TF106492; -.
DR   BioCyc; MetaCyc:HS10739-MONOMER; -.
DR   BRENDA; 1.1.1.357; 2681.
DR   Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR   Reactome; R-HSA-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
DR   Reactome; R-HSA-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR   Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR   SABIO-RK; P17516; -.
DR   SIGNOR; P17516; -.
DR   ChiTaRS; AKR1C4; human.
DR   EvolutionaryTrace; P17516; -.
DR   GeneWiki; 3-alpha-HSD; -.
DR   GenomeRNAi; 1109; -.
DR   Pharos; P17516; Tbio.
DR   PRO; PR:P17516; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; P17516; protein.
DR   Bgee; ENSG00000198610; Expressed in 41 organ(s), highest expression level in right lobe of liver.
DR   Genevisible; P17516; HS.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IBA:GO_Central.
DR   GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0004033; F:aldo-keto reductase (NADP) activity; TAS:ProtInc.
DR   GO; GO:0047023; F:androsterone dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0032052; F:bile acid binding; IBA:GO_Central.
DR   GO; GO:0015125; F:bile acid transmembrane transporter activity; TAS:ProtInc.
DR   GO; GO:0047743; F:chlordecone reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR   GO; GO:0047086; F:ketosteroid monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:UniProtKB.
DR   GO; GO:0001758; F:retinal dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0016229; F:steroid dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0008209; P:androgen metabolic process; TAS:ProtInc.
DR   GO; GO:0015721; P:bile acid and bile salt transport; TAS:ProtInc.
DR   GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
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:0044598; P:doxorubicin metabolic process; IMP:UniProtKB.
DR   GO; GO:0042448; P:progesterone metabolic process; IBA:GO_Central.
DR   GO; GO:0006693; P:prostaglandin metabolic process; IBA:GO_Central.
DR   GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
DR   GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
DR   CDD; cd06660; Aldo_ket_red; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR020471; Aldo/keto_reductase.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
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; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P17516.
DR   SWISS-2DPAGE; P17516.
KW   3D-structure; Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase;
KW   Polymorphism; Reference proteome.
FT   CHAIN           1..323
FT                   /note="Aldo-keto reductase family 1 member C4"
FT                   /id="PRO_0000124640"
FT   NP_BIND         20..24
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|Ref.14"
FT   NP_BIND         166..167
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|Ref.14"
FT   NP_BIND         216..221
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|Ref.14"
FT   NP_BIND         270..280
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|Ref.14"
FT   ACT_SITE        55
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         50
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|Ref.14"
FT   BINDING         117
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|Ref.14"
FT   SITE            54
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000250"
FT   SITE            84
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
FT   VARIANT         135
FT                   /note="G -> E (in dbSNP:rs11253043)"
FT                   /id="VAR_028240"
FT   VARIANT         145
FT                   /note="S -> C (in dbSNP:rs3829125)"
FT                   /evidence="ECO:0000269|PubMed:10634139"
FT                   /id="VAR_013290"
FT   VARIANT         170
FT                   /note="C -> Y (in dbSNP:rs17851824)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_028241"
FT   VARIANT         250
FT                   /note="Q -> R (in dbSNP:rs4880718)"
FT                   /evidence="ECO:0000269|PubMed:10634139,
FT                   ECO:0000269|PubMed:10672042, ECO:0000269|PubMed:11158055,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2187532,
FT                   ECO:0000269|PubMed:7626489, ECO:0000269|PubMed:7650035,
FT                   ECO:0000269|PubMed:8172617, ECO:0000269|PubMed:8274401"
FT                   /id="VAR_028242"
FT   VARIANT         311
FT                   /note="L -> V (in dbSNP:rs17134592)"
FT                   /evidence="ECO:0000269|PubMed:10634139"
FT                   /id="VAR_013291"
FT   HELIX           3..5
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   STRAND          7..9
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   STRAND          15..22
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   HELIX           33..44
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   STRAND          48..50
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   HELIX           53..55
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   HELIX           58..71
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   HELIX           76..78
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   STRAND          80..85
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   HELIX           87..89
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   HELIX           92..106
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   STRAND          111..117
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   STRAND          124..126
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   HELIX           144..156
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   STRAND          159..167
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   HELIX           170..177
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   STRAND          187..192
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   HELIX           200..208
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   STRAND          212..217
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   TURN            225..227
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   HELIX           235..237
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   HELIX           239..247
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   HELIX           252..262
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   STRAND          266..270
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   HELIX           274..280
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   HELIX           281..285
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   HELIX           290..297
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   HELIX           309..311
FT                   /evidence="ECO:0000244|PDB:2FVL"
FT   STRAND          318..321
FT                   /evidence="ECO:0000244|PDB:2FVL"
SQ   SEQUENCE   323 AA;  37067 MW;  E728CE4B420E8C58 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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