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Database: UniProt
Entry: P00390
LinkDB: P00390
Original site: P00390 
ID   GSHR_HUMAN              Reviewed;         522 AA.
AC   P00390; C8KIL8; C8KIL9; C8KIM0; D3DSV3; Q7Z5C9; Q9NP63;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   03-SEP-2014, entry version 195.
DE   RecName: Full=Glutathione reductase, mitochondrial;
DE            Short=GR;
DE            Short=GRase;
DE            EC=1.8.1.7;
DE   Flags: Precursor;
GN   Name=GSR; Synonyms=GLUR, GRD1;
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 CYTOPLASMIC).
RC   TISSUE=Placenta;
RX   PubMed=2185014; DOI=10.1111/j.1432-1033.1990.tb15431.x;
RA   Tutic M., Lu X.A., Schirmer R.H., Werner D.;
RT   "Cloning and sequencing of mammalian glutathione reductase cDNA.";
RL   Eur. J. Biochem. 188:523-528(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM MITOCHONDRIAL), AND
RP   ALTERNATIVE INITIATION.
RX   PubMed=10708558; DOI=10.1006/bbrc.2000.2267;
RA   Kelner M.J., Montoya M.A.;
RT   "Structural organization of the human glutathione reductase (GSR)
RT   gene: determination of correct cDNA sequence and identification of a
RT   mitochondrial leader sequence.";
RL   Biochem. Biophys. Res. Commun. 269:366-368(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-153; SER-232;
RP   VAL-261 AND ASP-297.
RG   NIEHS SNPs program;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), ALTERNATIVE
RP   SPLICING, AND TISSUE SPECIFICITY.
RX   PubMed=20628807; DOI=10.1007/s10528-010-9362-z;
RA   Satoh N., Watanabe N., Kanda A., Sugaya-Fukazawa M., Hisatomi H.;
RT   "Expression of glutathione reductase splice variants in human
RT   tissues.";
RL   Biochem. Genet. 48:816-821(2010).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA   Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA   Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA   Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA   DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA   Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA   Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA   O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA   Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA   Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA   Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA   Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA   Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MITOCHONDRIAL).
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   [8]
RP   PROTEIN SEQUENCE OF 45-522.
RX   PubMed=7060551; DOI=10.1111/j.1432-1033.1982.tb05780.x;
RA   Krauth-Siegel R.L., Blatterspiel R., Saleh M., Schiltz E.,
RA   Schirmer R.H., Untucht-Grau R.;
RT   "Glutathione reductase from human erythrocytes. The sequences of the
RT   NADPH domain and of the interface domain.";
RL   Eur. J. Biochem. 121:259-267(1982).
RN   [9]
RP   PROTEIN SEQUENCE OF 98-110.
RC   TISSUE=Erythrocyte;
RX   PubMed=923580; DOI=10.1111/j.1432-1033.1977.tb11856.x;
RA   Krohne-Ehrich G., Schirmer R.H., Untucht-Grau R.;
RT   "Glutathione reductase from human erythrocytes. Isolation of the
RT   enzyme and sequence analysis of the redox-active peptide.";
RL   Eur. J. Biochem. 80:65-71(1977).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [11]
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).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS) OF 45-522.
RX   PubMed=7334521; DOI=10.1016/0022-2836(81)90126-1;
RA   Thieme R., Pai E.F., Schirmer R.H., Schulz G.E.;
RT   "Three-dimensional structure of glutathione reductase at 2-A
RT   resolution.";
RL   J. Mol. Biol. 152:763-782(1981).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 45-522.
RX   PubMed=3656429; DOI=10.1016/0022-2836(87)90191-4;
RA   Karplus P.A., Schulz G.E.;
RT   "Refined structure of glutathione reductase at 1.54-A resolution.";
RL   J. Mol. Biol. 195:701-729(1987).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 62-522, AND DISULFIDE BONDS.
RX   PubMed=8626496; DOI=10.1074/jbc.271.14.8101;
RA   Savvides S.N., Karplus P.A.;
RT   "Kinetics and crystallographic analysis of human glutathione reductase
RT   in complex with a xanthene inhibitor.";
RL   J. Biol. Chem. 271:8101-8107(1996).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 62-522.
RX   PubMed=9174360; DOI=10.1021/bi963074p;
RA   Stoll V.S., Simpson S.J., Krauth-Siegel R.L., Walsh C.T., Pai E.F.;
RT   "Glutathione reductase turned into trypanothione reductase: structural
RT   analysis of an engineered change in substrate specificity.";
RL   Biochemistry 36:6437-6447(1997).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 62-522.
RX   PubMed=9546215; DOI=10.1038/nsb0498-267;
RA   Becker K., Savvides S.N., Keese M., Schirmer R.H., Karplus P.A.;
RT   "Enzyme inactivation through sulfhydryl oxidation by physiologic NO-
RT   carriers.";
RL   Nat. Struct. Biol. 5:267-271(1998).
CC   -!- FUNCTION: Maintains high levels of reduced glutathione in the
CC       cytosol.
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + NADP(+) = glutathione
CC       disulfide + NADPH.
CC   -!- COFACTOR: Binds 1 FAD per subunit.
CC   -!- SUBUNIT: Homodimer; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion.
CC   -!- SUBCELLULAR LOCATION: Isoform Cytoplasmic: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=5;
CC       Name=Mitochondrial;
CC         IsoId=P00390-1; Sequence=Displayed;
CC       Name=Cytoplasmic;
CC         IsoId=P00390-2; Sequence=VSP_018972;
CC         Note=Produced by alternative initiation of isoform
CC         Mitochondrial;
CC       Name=2; Synonyms=delta8;
CC         IsoId=P00390-3; Sequence=VSP_042908;
CC       Name=3; Synonyms=delta9;
CC         IsoId=P00390-4; Sequence=VSP_042909;
CC         Note=Expressed at very high levels in peripheral blood;
CC       Name=4; Synonyms=delta8+9;
CC         IsoId=P00390-5; Sequence=VSP_042908, VSP_042909;
CC   -!- DOMAIN: Each subunit can be divided into 4 domains that are
CC       consecutive along the polypeptide chain. Domains 1 and 2 bind FAD
CC       and NADPH, respectively. Domain 4 forms the interface.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP88037.1; Type=Erroneous initiation;
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/gsr/";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Glutathione reductase entry;
CC       URL="http://en.wikipedia.org/wiki/Glutathione_reductase";
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DR   EMBL; X15722; CAA33744.1; -; mRNA.
DR   EMBL; AF228703; AAF37572.1; -; Genomic_DNA.
DR   EMBL; AF228703; AAF37573.1; -; Genomic_DNA.
DR   EMBL; AF228704; AAF37574.1; -; mRNA.
DR   EMBL; AY338490; AAP88037.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AB519179; BAI43437.1; -; mRNA.
DR   EMBL; AB519180; BAI43438.1; -; mRNA.
DR   EMBL; AB519181; BAI43439.1; -; mRNA.
DR   EMBL; AC009314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC103959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF215848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471080; EAW63443.1; -; Genomic_DNA.
DR   EMBL; CH471080; EAW63445.1; -; Genomic_DNA.
DR   EMBL; BC069244; AAH69244.1; -; mRNA.
DR   CCDS; CCDS34877.1; -. [P00390-1]
DR   CCDS; CCDS56530.1; -. [P00390-5]
DR   CCDS; CCDS56531.1; -. [P00390-3]
DR   CCDS; CCDS56532.1; -. [P00390-4]
DR   PIR; S08979; RDHUU.
DR   RefSeq; NP_000628.2; NM_000637.3. [P00390-1]
DR   RefSeq; NP_001182031.1; NM_001195102.1. [P00390-3]
DR   RefSeq; NP_001182032.1; NM_001195103.1. [P00390-4]
DR   RefSeq; NP_001182033.1; NM_001195104.1. [P00390-5]
DR   UniGene; Hs.271510; -.
DR   PDB; 1ALG; NMR; -; A=480-503.
DR   PDB; 1BWC; X-ray; 2.10 A; A=45-522.
DR   PDB; 1DNC; X-ray; 1.70 A; A=45-522.
DR   PDB; 1GRA; X-ray; 2.00 A; A=45-522.
DR   PDB; 1GRB; X-ray; 1.85 A; A=45-522.
DR   PDB; 1GRE; X-ray; 2.00 A; A=45-522.
DR   PDB; 1GRF; X-ray; 2.00 A; A=45-522.
DR   PDB; 1GRG; X-ray; 2.00 A; A=45-522.
DR   PDB; 1GRH; X-ray; 3.00 A; A=45-522.
DR   PDB; 1GRT; X-ray; 2.30 A; A=45-522.
DR   PDB; 1GSN; X-ray; 1.70 A; A=45-522.
DR   PDB; 1K4Q; X-ray; 1.90 A; A=62-522.
DR   PDB; 1XAN; X-ray; 2.00 A; A=62-522.
DR   PDB; 2AAQ; X-ray; 2.60 A; A=44-522.
DR   PDB; 2GH5; X-ray; 1.70 A; A/B=45-522.
DR   PDB; 2GRT; X-ray; 2.70 A; A=62-522.
DR   PDB; 3DJG; X-ray; 1.80 A; X=59-522.
DR   PDB; 3DJJ; X-ray; 1.10 A; A=45-522.
DR   PDB; 3DK4; X-ray; 1.20 A; A=45-522.
DR   PDB; 3DK8; X-ray; 1.10 A; A=45-522.
DR   PDB; 3DK9; X-ray; 0.95 A; A=45-522.
DR   PDB; 3GRS; X-ray; 1.54 A; A=45-522.
DR   PDB; 3GRT; X-ray; 2.50 A; A=62-522.
DR   PDB; 3SQP; X-ray; 2.21 A; A/B=45-522.
DR   PDB; 4GR1; X-ray; 2.40 A; A=45-522.
DR   PDB; 4GRT; X-ray; 2.80 A; A=62-522.
DR   PDB; 5GRT; X-ray; 2.40 A; A=62-522.
DR   PDBsum; 1ALG; -.
DR   PDBsum; 1BWC; -.
DR   PDBsum; 1DNC; -.
DR   PDBsum; 1GRA; -.
DR   PDBsum; 1GRB; -.
DR   PDBsum; 1GRE; -.
DR   PDBsum; 1GRF; -.
DR   PDBsum; 1GRG; -.
DR   PDBsum; 1GRH; -.
DR   PDBsum; 1GRT; -.
DR   PDBsum; 1GSN; -.
DR   PDBsum; 1K4Q; -.
DR   PDBsum; 1XAN; -.
DR   PDBsum; 2AAQ; -.
DR   PDBsum; 2GH5; -.
DR   PDBsum; 2GRT; -.
DR   PDBsum; 3DJG; -.
DR   PDBsum; 3DJJ; -.
DR   PDBsum; 3DK4; -.
DR   PDBsum; 3DK8; -.
DR   PDBsum; 3DK9; -.
DR   PDBsum; 3GRS; -.
DR   PDBsum; 3GRT; -.
DR   PDBsum; 3SQP; -.
DR   PDBsum; 4GR1; -.
DR   PDBsum; 4GRT; -.
DR   PDBsum; 5GRT; -.
DR   ProteinModelPortal; P00390; -.
DR   SMR; P00390; 61-522.
DR   BioGrid; 109191; 27.
DR   IntAct; P00390; 4.
DR   MINT; MINT-5000460; -.
DR   STRING; 9606.ENSP00000221130; -.
DR   BindingDB; P00390; -.
DR   ChEMBL; CHEMBL2755; -.
DR   DrugBank; DB00262; Carmustine.
DR   DrugBank; DB00143; Glutathione.
DR   DrugBank; DB00157; NADH.
DR   GuidetoPHARMACOLOGY; 2613; -.
DR   PhosphoSite; P00390; -.
DR   DMDM; 14916998; -.
DR   REPRODUCTION-2DPAGE; IPI00759575; -.
DR   MaxQB; P00390; -.
DR   PaxDb; P00390; -.
DR   PRIDE; P00390; -.
DR   Ensembl; ENST00000221130; ENSP00000221130; ENSG00000104687. [P00390-1]
DR   Ensembl; ENST00000414019; ENSP00000390065; ENSG00000104687. [P00390-2]
DR   Ensembl; ENST00000537535; ENSP00000438845; ENSG00000104687. [P00390-5]
DR   Ensembl; ENST00000541648; ENSP00000444559; ENSG00000104687. [P00390-4]
DR   Ensembl; ENST00000546342; ENSP00000445516; ENSG00000104687. [P00390-3]
DR   GeneID; 2936; -.
DR   KEGG; hsa:2936; -.
DR   UCSC; uc003xih.2; human. [P00390-1]
DR   UCSC; uc022ato.1; human. [P00390-4]
DR   UCSC; uc022atp.1; human. [P00390-3]
DR   UCSC; uc022atq.1; human. [P00390-5]
DR   CTD; 2936; -.
DR   GeneCards; GC08M030535; -.
DR   HGNC; HGNC:4623; GSR.
DR   HPA; CAB008632; -.
DR   HPA; HPA001538; -.
DR   MIM; 138300; gene+phenotype.
DR   neXtProt; NX_P00390; -.
DR   Orphanet; 90030; Hemolytic anemia due to glutathione reductase deficiency.
DR   PharmGKB; PA29014; -.
DR   eggNOG; COG1249; -.
DR   HOGENOM; HOG000276712; -.
DR   HOVERGEN; HBG004959; -.
DR   InParanoid; P00390; -.
DR   KO; K00383; -.
DR   OMA; GTNSDGF; -.
DR   OrthoDB; EOG7HHWS0; -.
DR   PhylomeDB; P00390; -.
DR   TreeFam; TF105353; -.
DR   BioCyc; MetaCyc:HS02602-MONOMER; -.
DR   Reactome; REACT_172715; Detoxification of Reactive Oxygen Species.
DR   Reactome; REACT_21330; Synthesis and interconversion of nucleotide di- and triphosphates.
DR   SABIO-RK; P00390; -.
DR   EvolutionaryTrace; P00390; -.
DR   GeneWiki; Glutathione_reductase; -.
DR   GenomeRNAi; 2936; -.
DR   NextBio; 11635; -.
DR   PRO; PR:P00390; -.
DR   ArrayExpress; P00390; -.
DR   Bgee; P00390; -.
DR   CleanEx; HS_GSR; -.
DR   Genevestigator; P00390; -.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0009055; F:electron carrier activity; TAS:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase activity; TAS:Reactome.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR   GO; GO:0055086; P:nucleobase-containing small molecule metabolic process; TAS:Reactome.
DR   GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR   Gene3D; 3.30.390.30; -; 1.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR006322; Glutathione_Rdtase_euk/bac.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   TIGRFAMs; TIGR01421; gluta_reduc_1; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative initiation;
KW   Alternative splicing; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW   Mitochondrion; NADP; Oxidoreductase; Polymorphism;
KW   Redox-active center; Reference proteome; Transit peptide.
FT   TRANSIT       1     43       Mitochondrion (Potential).
FT   CHAIN        44    522       Glutathione reductase, mitochondrial.
FT                                /FTId=PRO_0000030276.
FT   NP_BIND      94    102       FAD.
FT   ACT_SITE    511    511       Proton acceptor.
FT   MOD_RES      97     97       N6-acetyllysine (By similarity).
FT   DISULFID    102    107       Redox-active.
FT   DISULFID    134    134       Interchain.
FT   VAR_SEQ       1     43       Missing (in isoform Cytoplasmic).
FT                                /FTId=VSP_018972.
FT   VAR_SEQ     266    294       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_042908.
FT   VAR_SEQ     295    347       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_042909.
FT   VARIANT     153    153       R -> C (in dbSNP:rs8190955).
FT                                /FTId=VAR_019079.
FT   VARIANT     232    232       G -> R (in dbSNP:rs8190976).
FT                                /FTId=VAR_051775.
FT   VARIANT     232    232       G -> S (in dbSNP:rs8190976).
FT                                /FTId=VAR_019080.
FT   VARIANT     261    261       I -> V (in dbSNP:rs8190997).
FT                                /FTId=VAR_019081.
FT   VARIANT     297    297       E -> D (in dbSNP:rs8191004).
FT                                /FTId=VAR_019082.
FT   VARIANT     314    314       P -> H (in dbSNP:rs2020916).
FT                                /FTId=VAR_014554.
FT   STRAND       62     64
FT   STRAND       66     70
FT   HELIX        74     85
FT   STRAND       90     96
FT   HELIX       100    105
FT   HELIX       107    123
FT   TURN        124    130
FT   HELIX       140    164
FT   STRAND      168    172
FT   STRAND      174    176
FT   STRAND      183    186
FT   STRAND      189    192
FT   STRAND      196    198
FT   STRAND      202    204
FT   TURN        209    211
FT   HELIX       215    217
FT   HELIX       221    224
FT   STRAND      232    237
FT   HELIX       241    252
FT   STRAND      256    260
FT   STRAND      262    266
FT   HELIX       272    284
FT   STRAND      288    290
FT   STRAND      293    300
FT   STRAND      302    311
FT   STRAND      319    331
FT   STRAND      335    338
FT   TURN        340    343
FT   HELIX       344    347
FT   STRAND      370    372
FT   HELIX       374    377
FT   HELIX       383    398
FT   STRAND      413    415
FT   STRAND      417    419
FT   STRAND      421    425
FT   HELIX       428    435
FT   HELIX       437    439
FT   STRAND      440    447
FT   HELIX       450    454
FT   STRAND      461    468
FT   TURN        469    472
FT   STRAND      473    481
FT   HELIX       484    496
FT   HELIX       501    505
FT   STRAND      511    514
FT   HELIX       515    519
SQ   SEQUENCE   522 AA;  56257 MW;  DD8E2BA9D6E3757B CRC64;
     MALLPRALSA GAGPSWRRAA RAFRGFLLLL PEPAALTRAL SRAMACRQEP QPQGPPPAAG
     AVASYDYLVI GGGSGGLASA RRAAELGARA AVVESHKLGG TCVNVGCVPK KVMWNTAVHS
     EFMHDHADYG FPSCEGKFNW RVIKEKRDAY VSRLNAIYQN NLTKSHIEII RGHAAFTSDP
     KPTIEVSGKK YTAPHILIAT GGMPSTPHES QIPGASLGIT SDGFFQLEEL PGRSVIVGAG
     YIAVEMAGIL SALGSKTSLM IRHDKVLRSF DSMISTNCTE ELENAGVEVL KFSQVKEVKK
     TLSGLEVSMV TAVPGRLPVM TMIPDVDCLL WAIGRVPNTK DLSLNKLGIQ TDDKGHIIVD
     EFQNTNVKGI YAVGDVCGKA LLTPVAIAAG RKLAHRLFEY KEDSKLDYNN IPTVVFSHPP
     IGTVGLTEDE AIHKYGIENV KTYSTSFTPM YHAVTKRKTK CVMKMVCANK EEKVVGIHMQ
     GLGCDEMLQG FAVAVKMGAT KADFDNTVAI HPTSSEELVT LR
//
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