GSH1_HUMAN
ID GSH1_HUMAN Reviewed; 637 AA.
AC P48506; Q14399;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Glutamate--cysteine ligase catalytic subunit {ECO:0000305};
DE EC=6.3.2.2 {ECO:0000269|PubMed:12663448, ECO:0000269|PubMed:9675072};
DE AltName: Full=GCS heavy chain;
DE AltName: Full=Gamma-ECS;
DE AltName: Full=Gamma-glutamylcysteine synthetase;
GN Name=GCLC {ECO:0000312|HGNC:HGNC:4311}; Synonyms=GLCL, GLCLC;
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].
RC TISSUE=Liver;
RX PubMed=1350904; DOI=10.1080/02500169208537777;
RA Gipp J.J., Chang C., Mulcahy R.T.;
RT "Cloning and nucleotide sequence of a full-length cDNA for human liver
RT gamma-glutamylcysteine synthetase.";
RL Biochem. Biophys. Res. Commun. 185:29-35(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-462.
RG NIEHS SNPs program;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RC TISSUE=Foreskin fibroblast;
RX PubMed=7726839; DOI=10.1006/bbrc.1995.1493;
RA Mulcahy R.T., Gipp J.J.;
RT "Identification of a putative antioxidant response element in the 5'-
RT flanking region of the human gamma-glutamylcysteine synthetase heavy
RT subunit gene.";
RL Biochem. Biophys. Res. Commun. 209:227-233(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 341-440, AND VARIANT HAGGSD LEU-370.
RX PubMed=10515893;
RA Beutler E., Gelbart T., Kondo T., Matsunaga A.T.;
RT "The molecular basis of a case of gamma-glutamylcysteine synthetase
RT deficiency.";
RL Blood 94:2890-2894(1999).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=9675072; DOI=10.1006/prep.1998.0897;
RA Misra I., Griffith O.W.;
RT "Expression and purification of human gamma-glutamylcysteine synthetase.";
RL Protein Expr. Purif. 13:268-276(1998).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-5 AND SER-8, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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., Buerckstuemmer T.,
RA 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
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 [12]
RP VARIANT HAGGSD LEU-158.
RX PubMed=10733484;
RA Ristoff E., Augustson C., Geissler J., de Rijk T., Carlsson K., Luo J.-L.,
RA Andersson K., Weening R.S., van Zwieten R., Larsson A., Roos D.;
RT "A missense mutation in the heavy subunit of gamma-glutamylcysteine
RT synthetase gene causes hemolytic anemia.";
RL Blood 95:2193-2196(2000).
RN [13]
RP VARIANT HAGGSD CYS-127, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY,
RP AND CHARACTERIZATION OF VARIANT HAGGSD CYS-127.
RX PubMed=12663448; DOI=10.1182/blood-2002-11-3622;
RA Hamilton D., Wu J.H., Alaoui-Jamali M., Batist G.;
RT "A novel missense mutation in the gamma-glutamylcysteine synthetase
RT catalytic subunit gene causes both decreased enzymatic activity and
RT glutathione production.";
RL Blood 102:725-730(2003).
CC -!- FUNCTION: Catalyzes the ATP-dependent ligation of L-glutamate and L-
CC cysteine and participates in the first and rate-limiting step in
CC glutathione biosynthesis. {ECO:0000269|PubMed:9675072}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC Evidence={ECO:0000269|PubMed:12663448, ECO:0000269|PubMed:9675072};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13286;
CC Evidence={ECO:0000305|PubMed:12663448, ECO:0000305|PubMed:9675072};
CC -!- ACTIVITY REGULATION: Feedback inhibition by glutathione.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 mM for L-glutamate {ECO:0000269|PubMed:9675072};
CC KM=7.16 mM for L-glutamate {ECO:0000269|PubMed:12663448};
CC KM=0.1 mM for L-cysteine {ECO:0000269|PubMed:9675072};
CC KM=1.3 mM for L-aminobutyrate {ECO:0000269|PubMed:9675072};
CC KM=2.39 mM for L-aminobutyrate {ECO:0000269|PubMed:12663448};
CC KM=0.4 mM for ATP {ECO:0000269|PubMed:9675072};
CC Vmax=1650 umol/h/mg enzyme {ECO:0000269|PubMed:9675072};
CC Vmax=531.75 umol/h/mg enzyme {ECO:0000269|PubMed:12663448};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2. {ECO:0000305|PubMed:9675072}.
CC -!- SUBUNIT: Heterodimer of a catalytic heavy chain and a regulatory light
CC chain.
CC -!- INTERACTION:
CC P48506; P48507: GCLM; NbExp=2; IntAct=EBI-2832840, EBI-1051387;
CC -!- DISEASE: Hemolytic anemia due to gamma-glutamylcysteine synthetase
CC deficiency (HAGGSD) [MIM:230450]: A disease characterized by hemolytic
CC anemia, glutathione deficiency, myopathy, late-onset spinocerebellar
CC degeneration, and peripheral neuropathy. {ECO:0000269|PubMed:10515893,
CC ECO:0000269|PubMed:10733484, ECO:0000269|PubMed:12663448}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 3 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/gclc/";
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DR EMBL; M90656; AAA58499.1; -; mRNA.
DR EMBL; AY780794; AAV31778.1; -; Genomic_DNA.
DR EMBL; AL033397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022487; AAH22487.1; -; mRNA.
DR EMBL; BC039894; AAH39894.1; -; mRNA.
DR EMBL; L39773; AAC41751.1; -; Genomic_DNA.
DR EMBL; AF118846; AAD18031.1; -; Genomic_DNA.
DR CCDS; CCDS4952.1; -.
DR PIR; JH0611; JH0611.
DR RefSeq; NP_001184044.1; NM_001197115.1.
DR RefSeq; NP_001489.1; NM_001498.3.
DR AlphaFoldDB; P48506; -.
DR SMR; P48506; -.
DR BioGRID; 108991; 28.
DR CORUM; P48506; -.
DR IntAct; P48506; 6.
DR STRING; 9606.ENSP00000229416; -.
DR BindingDB; P48506; -.
DR ChEMBL; CHEMBL4055; -.
DR DrugBank; DB14001; alpha-Tocopherol succinate.
DR DrugBank; DB00151; Cysteine.
DR DrugBank; DB14002; D-alpha-Tocopherol acetate.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00163; Vitamin E.
DR iPTMnet; P48506; -.
DR PhosphoSitePlus; P48506; -.
DR BioMuta; GCLC; -.
DR DMDM; 1346190; -.
DR EPD; P48506; -.
DR jPOST; P48506; -.
DR MassIVE; P48506; -.
DR PaxDb; P48506; -.
DR PeptideAtlas; P48506; -.
DR PRIDE; P48506; -.
DR ProteomicsDB; 55896; -.
DR Antibodypedia; 4035; 430 antibodies from 35 providers.
DR DNASU; 2729; -.
DR Ensembl; ENST00000650454.1; ENSP00000497574.1; ENSG00000001084.13.
DR GeneID; 2729; -.
DR KEGG; hsa:2729; -.
DR MANE-Select; ENST00000650454.1; ENSP00000497574.1; NM_001498.4; NP_001489.1.
DR UCSC; uc003pbx.5; human.
DR CTD; 2729; -.
DR DisGeNET; 2729; -.
DR GeneCards; GCLC; -.
DR HGNC; HGNC:4311; GCLC.
DR HPA; ENSG00000001084; Tissue enhanced (liver).
DR MalaCards; GCLC; -.
DR MIM; 230450; phenotype.
DR MIM; 606857; gene+phenotype.
DR neXtProt; NX_P48506; -.
DR OpenTargets; ENSG00000001084; -.
DR Orphanet; 586; Cystic fibrosis.
DR Orphanet; 33574; Glutamate-cysteine ligase deficiency.
DR PharmGKB; PA28612; -.
DR VEuPathDB; HostDB:ENSG00000001084; -.
DR eggNOG; KOG3754; Eukaryota.
DR GeneTree; ENSGT00390000011908; -.
DR HOGENOM; CLU_010467_0_0_1; -.
DR InParanoid; P48506; -.
DR OMA; YISQDPR; -.
DR OrthoDB; 575052at2759; -.
DR PhylomeDB; P48506; -.
DR TreeFam; TF105644; -.
DR BioCyc; MetaCyc:ENSG00000001084-MON; -.
DR BRENDA; 6.3.2.2; 2681.
DR PathwayCommons; P48506; -.
DR Reactome; R-HSA-174403; Glutathione synthesis and recycling.
DR Reactome; R-HSA-5578999; Defective GCLC causes HAGGSD.
DR Reactome; R-HSA-9759194; Nuclear events mediated by NFE2L2.
DR SignaLink; P48506; -.
DR SIGNOR; P48506; -.
DR UniPathway; UPA00142; UER00209.
DR BioGRID-ORCS; 2729; 67 hits in 1087 CRISPR screens.
DR ChiTaRS; GCLC; human.
DR GeneWiki; GCLC; -.
DR GenomeRNAi; 2729; -.
DR Pharos; P48506; Tchem.
DR PRO; PR:P48506; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P48506; protein.
DR Bgee; ENSG00000001084; Expressed in bronchial epithelial cell and 209 other tissues.
DR ExpressionAtlas; P48506; baseline and differential.
DR Genevisible; P48506; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0017109; C:glutamate-cysteine ligase complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016595; F:glutamate binding; IDA:UniProtKB.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IMP:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:UniProtKB.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0097069; P:cellular response to thyroxine stimulus; IEA:Ensembl.
DR GO; GO:0006534; P:cysteine metabolic process; IDA:UniProtKB.
DR GO; GO:0006536; P:glutamate metabolic process; IDA:UniProtKB.
DR GO; GO:0006750; P:glutathione biosynthetic process; IDA:UniProtKB.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:2000490; P:negative regulation of hepatic stellate cell activation; IEA:Ensembl.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0051900; P:regulation of mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0046685; P:response to arsenic-containing substance; IEA:Ensembl.
DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IDA:UniProtKB.
DR GO; GO:0009725; P:response to hormone; IDA:UniProtKB.
DR GO; GO:0044752; P:response to human chorionic gonadotropin; IEA:Ensembl.
DR GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
DR GO; GO:0051409; P:response to nitrosative stress; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR InterPro; IPR004308; GCS.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11164; PTHR11164; 1.
DR Pfam; PF03074; GCS; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Disease variant; Glutathione biosynthesis;
KW Hereditary hemolytic anemia; Ligase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..637
FT /note="Glutamate--cysteine ligase catalytic subunit"
FT /id="PRO_0000192563"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 55
FT /note="L -> S (in dbSNP:rs2066512)"
FT /id="VAR_014884"
FT VARIANT 127
FT /note="R -> C (in HAGGSD; strongly decreased glutamate-
FT cysteine ligase activity; dbSNP:rs760031222)"
FT /evidence="ECO:0000269|PubMed:12663448"
FT /id="VAR_021110"
FT VARIANT 158
FT /note="P -> L (in HAGGSD)"
FT /evidence="ECO:0000269|PubMed:10733484"
FT /id="VAR_015403"
FT VARIANT 370
FT /note="H -> L (in HAGGSD; dbSNP:rs121907946)"
FT /evidence="ECO:0000269|PubMed:10515893"
FT /id="VAR_013514"
FT VARIANT 462
FT /note="P -> S (in dbSNP:rs17883718)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_021100"
SQ SEQUENCE 637 AA; 72766 MW; 511F33F106A15504 CRC64;
MGLLSQGSPL SWEETKRHAD HVRRHGILQF LHIYHAVKDR HKDVLKWGDE VEYMLVSFDH
ENKKVRLVLS GEKVLETLQE KGERTNPNHP TLWRPEYGSY MIEGTPGQPY GGTMSEFNTV
EANMRKRRKE ATSILEENQA LCTITSFPRL GCPGFTLPEV KPNPVEGGAS KSLFFPDEAI
NKHPRFSTLT RNIRHRRGEK VVINVPIFKD KNTPSPFIET FTEDDEASRA SKPDHIYMDA
MGFGMGNCCL QVTFQACSIS EARYLYDQLA TICPIVMALS AASPFYRGYV SDIDCRWGVI
SASVDDRTRE ERGLEPLKNN NYRISKSRYD SIDSYLSKCG EKYNDIDLTI DKEIYEQLLQ
EGIDHLLAQH VAHLFIRDPL TLFEEKIHLD DANESDHFEN IQSTNWQTMR FKPPPPNSDI
GWRVEFRPME VQLTDFENSA YVVFVVLLTR VILSYKLDFL IPLSKVDENM KVAQKRDAVL
QGMFYFRKDI CKGGNAVVDG CGKAQNSTEL AAEEYTLMSI DTIINGKEGV FPGLIPILNS
YLENMEVDVD TRCSILNYLK LIKKRASGEL MTVARWMREF IANHPDYKQD SVITDEMNYS
LILKCNQIAN ELCECPELLG SAFRKVKYSG SKTDSSN
