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   02-SEP-2026, entry version 208.
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=10.1016/s0006-291x(05)80950-7;
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 CNSHA7 LEU-370.
RX   PubMed=10515893; DOI=10.1182/blood.v94.8.2890.420k16_2890_2894;
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 CNSHA7 LEU-158.
RX   PubMed=10733484; DOI=10.1182/blood.v95.7.2193;
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 CNSHA7 CYS-127, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY,
RP   AND CHARACTERIZATION OF VARIANT CNSHA7 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=L-cysteine + L-glutamate + ATP = gamma-L-glutamyl-L-cysteine +
CC         ADP + phosphate + H(+); 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-2-aminobutanoate + L-glutamate + ATP = gamma-L-glutamyl-
CC         (2S)-2-aminobutanoate + ADP + phosphate + H(+); Xref=Rhea:RHEA:72067,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:74359, ChEBI:CHEBI:189406,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:9675072};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72068;
CC         Evidence={ECO:0000250|UniProtKB:P97494};
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=5; IntAct=EBI-2832840, EBI-1051387;
CC   -!- DISEASE: Anemia, congenital, non-spherocytic hemolytic, 7 (CNSHA7)
CC       [MIM:230450]: An autosomal recessive 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}.
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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_001197115.2.
DR   RefSeq; NP_001489.1; NM_001498.4.
DR   RefSeq; XP_054211163.1; XM_054355188.1.
DR   AlphaFoldDB; P48506; -.
DR   SMR; P48506; -.
DR   BioGRID; 108991; 44.
DR   ComplexPortal; CPX-2865; Glutamate-cysteine ligase complex.
DR   CORUM; P48506; -.
DR   FunCoup; P48506; 1002.
DR   IntAct; P48506; 10.
DR   NDEx; IQUERY-CP-GCLC; 15 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000497574; -.
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   jPOST; P48506; -.
DR   MassIVE; P48506; -.
DR   PaxDb; 9606-ENSP00000497574; -.
DR   PeptideAtlas; P48506; -.
DR   ProteomicsDB; 55896; -.
DR   Pumba; P48506; -.
DR   Antibodypedia; 4035; 443 antibodies from 38 providers.
DR   DNASU; 2729; -.
DR   Ensembl; ENST00000650454.1; ENSP00000497574.1; ENSG00000001084.14.
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   AGR; HGNC:4311; -.
DR   ClinPGx; PA28612; -.
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   OpenTargets; ENSG00000001084; -.
DR   Orphanet; 586; Cystic fibrosis.
DR   Orphanet; 33574; Glutamate-cysteine ligase deficiency.
DR   VEuPathDB; HostDB:ENSG00000001084; -.
DR   eggNOG; KOG3754; Eukaryota.
DR   GeneTree; ENSGT00390000011908; -.
DR   HOGENOM; CLU_010467_0_0_1; -.
DR   InParanoid; P48506; -.
DR   OMA; IAHMFIR; -.
DR   OrthoDB; 7939818at2759; -.
DR   PAN-GO; P48506; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; P48506; -.
DR   BioCyc; MetaCyc:ENSG00000001084-MONOMER; -.
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-9818027; NFE2L2 regulating anti-oxidant/detoxification enzymes.
DR   SignaLink; P48506; -.
DR   SIGNOR; P48506; -.
DR   UniPathway; UPA00142; UER00209.
DR   Agora; ENSG00000001084; -.
DR   BioGRID-ORCS; 2729; 72 hits in 1168 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 211 other cell types or tissues.
DR   ExpressionAtlas; P48506; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0017109; C:glutamate-cysteine ligase complex; IDA:UniProtKB.
DR   GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
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: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:0006536; P:glutamate metabolic process; IDA:UniProtKB.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:2000490; P:negative regulation of hepatic stellate cell activation; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0014823; P:response to activity; 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   FunFam; 1.10.8.960:FF:000001; Glutamate--cysteine ligase catalytic subunit; 1.
DR   FunFam; 3.30.590.50:FF:000002; Glutamate--cysteine ligase catalytic subunit; 1.
DR   FunFam; 3.30.590.50:FF:000003; Glutamate--cysteine ligase catalytic subunit; 1.
DR   Gene3D; 1.10.8.960; -; 1.
DR   Gene3D; 3.30.590.50; -; 2.
DR   InterPro; IPR004308; GCS.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   PANTHER; PTHR11164; GLUTAMATE CYSTEINE LIGASE; 1.
DR   PANTHER; PTHR11164:SF0; GLUTAMATE--CYSTEINE LIGASE CATALYTIC SUBUNIT; 1.
DR   Pfam; PF03074; GCS; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Disease variant; Glutathione biosynthesis;
KW   Hereditary hemolytic anemia; Ligase; Nucleotide-binding; Phosphoprotein;
KW   Proteomics identification; 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 CNSHA7; strongly decreased
FT                   glutamate-cysteine ligase activity; dbSNP:rs760031222)"
FT                   /evidence="ECO:0000269|PubMed:12663448"
FT                   /id="VAR_021110"
FT   VARIANT         158
FT                   /note="P -> L (in CNSHA7)"
FT                   /evidence="ECO:0000269|PubMed:10733484"
FT                   /id="VAR_015403"
FT   VARIANT         370
FT                   /note="H -> L (in CNSHA7; 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
//