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 01-MAY-2013, entry version 182.
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. Initiator Met-1 is removed. Acetylated at Ala-2;
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 IPI; IPI00016862; -.
DR IPI; IPI00759575; -.
DR IPI; IPI00953236; -.
DR IPI; IPI00953696; -.
DR IPI; IPI00978634; -.
DR PIR; S08979; RDHUU.
DR RefSeq; NP_000628.2; NM_000637.3.
DR RefSeq; NP_001182031.1; NM_001195102.1.
DR RefSeq; NP_001182032.1; NM_001195103.1.
DR RefSeq; NP_001182033.1; NM_001195104.1.
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=62-522.
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=62-522.
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 IntAct; P00390; 4.
DR MINT; MINT-5000460; -.
DR STRING; 9606.ENSP00000221130; -.
DR PhosphoSite; P00390; -.
DR DMDM; 14916998; -.
DR REPRODUCTION-2DPAGE; IPI00759575; -.
DR PaxDb; P00390; -.
DR PRIDE; P00390; -.
DR Ensembl; ENST00000221130; ENSP00000221130; ENSG00000104687.
DR Ensembl; ENST00000414019; ENSP00000390065; ENSG00000104687.
DR Ensembl; ENST00000537535; ENSP00000438845; ENSG00000104687.
DR Ensembl; ENST00000541648; ENSP00000444559; ENSG00000104687.
DR Ensembl; ENST00000546342; ENSP00000445516; ENSG00000104687.
DR GeneID; 2936; -.
DR KEGG; hsa:2936; -.
DR UCSC; uc003xih.2; human.
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; PHESQIP; -.
DR OrthoDB; EOG42BX8H; -.
DR PhylomeDB; P00390; -.
DR BioCyc; MetaCyc:HS02602-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P00390; -.
DR BindingDB; P00390; -.
DR ChEMBL; CHEMBL2755; -.
DR DrugBank; DB00262; Carmustine.
DR DrugBank; DB00143; Glutathione.
DR DrugBank; DB00157; NADH.
DR EvolutionaryTrace; P00390; -.
DR GenomeRNAi; 2936; -.
DR NextBio; 11635; -.
DR ArrayExpress; P00390; -.
DR Bgee; P00390; -.
DR CleanEx; HS_GSR; -.
DR Genevestigator; P00390; -.
DR GermOnline; ENSG00000104687; Homo sapiens.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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 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; FAD/NAD-linked_reductase_dimer; 1.
DR TIGRFAMs; TIGR01421; gluta_reduc_1; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative splicing;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; FAD; Flavoprotein; Mitochondrion; NADP;
KW Oxidoreductase; Polymorphism; Redox-active center; Reference proteome;
KW 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 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
//
