GGT1_RAT
ID GGT1_RAT Reviewed; 568 AA.
AC P07314; Q63217; Q63218; Q6AZ32;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 4.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Glutathione hydrolase 1 proenzyme;
DE EC=3.4.19.13 {ECO:0000269|PubMed:6122208};
DE AltName: Full=Gamma-glutamyltransferase 1;
DE AltName: Full=Gamma-glutamyltranspeptidase 1;
DE Short=GGT 1;
DE EC=2.3.2.2 {ECO:0000269|PubMed:6122208};
DE AltName: Full=Leukotriene-C4 hydrolase;
DE EC=3.4.19.14 {ECO:0000269|PubMed:6122208};
DE AltName: CD_antigen=CD224;
DE Contains:
DE RecName: Full=Glutathione hydrolase 1 heavy chain;
DE Contains:
DE RecName: Full=Glutathione hydrolase 1 light chain;
DE Flags: Precursor;
GN Name=Ggt1; Synonyms=Ggt;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2567622; DOI=10.1016/0304-3835(89)90217-6;
RA Griffiths S.A., Manson M.M.;
RT "Rat liver gamma glutamyl transpeptidase mRNA differs in the 5'
RT untranslated sequence from the corresponding kidney mRNA.";
RL Cancer Lett. 46:69-74(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-43 AND 380-388, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=2869484; DOI=10.1073/pnas.83.4.937;
RA Laperche Y., Bulle F., Aissani T., Chobert M.-N., Aggerbeck M., Hanoune J.,
RA Guellaen G.;
RT "Molecular cloning and nucleotide sequence of rat kidney gamma-glutamyl
RT transpeptidase cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:937-941(1986).
RN [3]
RP ERRATUM OF PUBMED:2869484, AND SEQUENCE REVISION TO 66-135.
RA Laperche Y., Bulle F., Aissani T., Chobert M.-N., Aggerbeck M., Hanoune J.,
RA Guellaen G.;
RL Proc. Natl. Acad. Sci. U.S.A. 86:3159-3159(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 PROTEIN SEQUENCE OF 1-21, AND TOPOLOGY.
RX PubMed=6136502; DOI=10.1093/oxfordjournals.jbchem.a134278;
RA Matsuda Y., Tsuji A., Katunuma N.;
RT "Studies on the structure of gamma-glutamyltranspeptidase. III. Evidence
RT that the amino terminus of the heavy subunit is the membrane binding
RT segment.";
RL J. Biochem. 93:1427-1433(1983).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-18.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=7910821; DOI=10.1016/s0021-9258(17)36547-x;
RA Brouillet A., Darbouy M., Okamoto T., Chobert M.-N., Lahuna O.,
RA Garlatti M., Goodspeed D.C., Laperche Y.;
RT "Functional characterization of the rat gamma-glutamyl transpeptidase
RT promoter that is expressed and regulated in the liver and hepatoma cells.";
RL J. Biol. Chem. 269:14878-14884(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RC TISSUE=Kidney;
RX PubMed=1671556; DOI=10.1021/bi00220a025;
RA Kurauchi O., Lahuna O., Darbouy M., Aggerbeck M., Chobert M.-N.,
RA Laperche Y.;
RT "Organization of the 5' end of the rat gamma-glutamyl transpeptidase gene:
RT structure of a promoter active in the kidney.";
RL Biochemistry 30:1618-1623(1991).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-568.
RC TISSUE=Kidney;
RX PubMed=2869471; DOI=10.1093/nar/14.3.1393;
RA Coloma J., Pitot H.C.;
RT "Characterization and sequence of a cDNA clone of gamma-
RT glutamyltranspeptidase.";
RL Nucleic Acids Res. 14:1393-1403(1986).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 64-136.
RX PubMed=2907498; DOI=10.1016/0378-1119(88)90307-1;
RA Sakamuro D., Yamazoe M., Matsuda Y., Kangawa K., Taniguchi N., Matsuo H.,
RA Yoshikawa H., Ogasawara N.;
RT "The primary structure of human gamma-glutamyl transpeptidase.";
RL Gene 73:1-9(1988).
RN [10]
RP PROTEIN SEQUENCE OF 30-47 AND 380-402.
RC TISSUE=Kidney;
RX PubMed=2896486; DOI=10.1016/0003-9861(88)90390-6;
RA Tate S.S., Khadse V., Wellner D.;
RT "Renal gamma-glutamyl transpeptidases: structural and immunological
RT studies.";
RL Arch. Biochem. Biophys. 262:397-408(1988).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Kidney;
RX PubMed=6122208; DOI=10.1073/pnas.79.4.1088;
RA Anderson M.E., Allison R.D., Meister A.;
RT "Interconversion of leukotrienes catalyzed by purified gamma-glutamyl
RT transpeptidase: concomitant formation of leukotriene D4 and gamma-glutamyl
RT amino acids.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:1088-1091(1982).
RN [12]
RP GENE ORGANIZATION, AND ALTERNATIVE PROMOTER USAGE.
RX PubMed=10392451; DOI=10.1016/s0305-0491(99)00013-9;
RA Chikhi N., Holic N., Guellaen G., Laperche Y.;
RT "Gamma-glutamyl transpeptidase gene organization and expression: a
RT comparative analysis in rat, mouse, pig and human species.";
RL Comp. Biochem. Physiol. 122B:367-380(1999).
RN [13]
RP GLYCOSYLATION, AND SIALIC ACID CONTENT.
RX PubMed=8776; DOI=10.1073/pnas.73.8.2599;
RA Tate S.S., Meister A.;
RT "Subunit structure and isozymic forms of gamma-glutamyl transpeptidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 73:2599-2603(1976).
RN [14]
RP GLYCOSYLATION.
RX PubMed=6142889; DOI=10.1016/s0021-9258(17)43715-x;
RA Nash B., Tate S.S.;
RT "In vitro translation and processing of rat kidney gamma-glutamyl
RT transpeptidase.";
RL J. Biol. Chem. 259:678-685(1984).
RN [15]
RP GLYCOSYLATION.
RX PubMed=2573604; DOI=10.1016/s0021-9258(19)47122-6;
RA Blochberger T.C., Sabatine J.M., Lee Y.C., Hughey R.P.;
RT "O-linked glycosylation of rat renal gamma-glutamyltranspeptidase adjacent
RT to its membrane anchor domain.";
RL J. Biol. Chem. 264:20718-20722(1989).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-510, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Cleaves the gamma-glutamyl bond of extracellular glutathione
CC (gamma-Glu-Cys-Gly), glutathione conjugates (such as maresin conjugate
CC (13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-
CC docosahexaenoate, MCTR1) and other gamma-glutamyl compounds (such as
CC leukotriene C4, LTC4) (PubMed:6122208) (By similarity). The metabolism
CC of glutathione by GGT1 releases free glutamate and the dipeptide
CC cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by
CC dipeptidases (PubMed:6122208). In the presence of high concentrations
CC of dipeptides and some amino acids, can also catalyze a
CC transpeptidation reaction, transferring the gamma-glutamyl moiety to an
CC acceptor amino acid to form a new gamma-glutamyl compound
CC (PubMed:6122208). Contributes to cysteine homeostasis, glutathione
CC homeostasis and in the conversion of the leukotriene LTC4 to LTD4
CC (PubMed:6122208). {ECO:0000250|UniProtKB:P19440,
CC ECO:0000269|PubMed:6122208}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] =
CC 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide];
CC Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795,
CC ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599,
CC ChEBI:CHEBI:78608; EC=2.3.2.2; Evidence={ECO:0000269|PubMed:6122208};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23905;
CC Evidence={ECO:0000305|PubMed:6122208};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23906;
CC Evidence={ECO:0000305|PubMed:6122208};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate;
CC Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13;
CC Evidence={ECO:0000269|PubMed:6122208};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28808;
CC Evidence={ECO:0000305|PubMed:6122208};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione + H2O = an S-substituted L-
CC cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:143103; EC=3.4.19.13;
CC Evidence={ECO:0000250|UniProtKB:P19440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59469;
CC Evidence={ECO:0000250|UniProtKB:P19440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + leukotriene C4 = L-glutamate + leukotriene D4;
CC Xref=Rhea:RHEA:31563, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:63166; EC=3.4.19.14;
CC Evidence={ECO:0000269|PubMed:6122208};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31564;
CC Evidence={ECO:0000305|PubMed:6122208};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-
CC docosahexaenoate + H2O = (13R)-S-cysteinylglycyl-(14S)-hydroxy-
CC (4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate + L-glutamate;
CC Xref=Rhea:RHEA:53512, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:137407, ChEBI:CHEBI:137408;
CC Evidence={ECO:0000250|UniProtKB:P19440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53513;
CC Evidence={ECO:0000250|UniProtKB:P19440};
CC -!- ACTIVITY REGULATION: Activated by autocatalytic cleavage.
CC {ECO:0000250|UniProtKB:P19440}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.9 uM for leukotriene C(4) {ECO:0000269|PubMed:6122208};
CC KM=5.7 uM for glutathione {ECO:0000269|PubMed:6122208};
CC KM=5.8 uM for gamma-glutamyl-p-anilide {ECO:0000269|PubMed:6122208};
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC {ECO:0000305|PubMed:6122208}.
CC -!- PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis.
CC {ECO:0000305|PubMed:6122208}.
CC -!- SUBUNIT: Heterodimer composed of the light and heavy chains. The active
CC site is located in the light chain. {ECO:0000250|UniProtKB:P19440}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P19440};
CC Single-pass type II membrane protein {ECO:0000305|PubMed:6136502}.
CC -!- TISSUE SPECIFICITY: Detected in adult kidney and mammary gland, and in
CC fetal liver. {ECO:0000269|PubMed:2869484}.
CC -!- PTM: N-glycosylated on both chains; contains sialic acid residues. It
CC is not known if the sialic acid residues are present on N-linked or on
CC O-linked glycans. {ECO:0000269|PubMed:6142889}.
CC -!- PTM: O-glycosylated; close to the membrane anchor on the heavy chain
CC and on the light chain. The sugar moieties are localized to the stretch
CC Thr-28 to Ser-30. Contains sialic acid residues. It is not known if the
CC sialic acid residues are present on N-linked or on O-linked glycans.
CC {ECO:0000269|PubMed:2573604}.
CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit and the
CC autocatalytic cleavage is essential to the functional activation of the
CC enzyme. {ECO:0000250|UniProtKB:P19440}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA27224.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X15443; CAA33483.1; -; mRNA.
DR EMBL; M33821; AAA57295.1; ALT_SEQ; mRNA.
DR EMBL; M33822; AAB59698.1; -; mRNA.
DR EMBL; BC078768; AAH78768.1; -; mRNA.
DR EMBL; L29167; AAA41218.1; -; mRNA.
DR EMBL; M57672; AAA41217.1; -; Genomic_DNA.
DR EMBL; X03518; CAA27224.1; ALT_FRAME; mRNA.
DR PIR; A05225; A05225.
DR RefSeq; NP_446292.2; NM_053840.2.
DR AlphaFoldDB; P07314; -.
DR SMR; P07314; -.
DR BindingDB; P07314; -.
DR ChEMBL; CHEMBL2943; -.
DR DrugCentral; P07314; -.
DR GlyConnect; 170; 1 O-Linked glycan.
DR GlyGen; P07314; 8 sites, 2 N-linked glycans (1 site), 2 O-linked glycans (1 site).
DR iPTMnet; P07314; -.
DR PhosphoSitePlus; P07314; -.
DR PRIDE; P07314; -.
DR Ensembl; ENSRNOT00000074533; ENSRNOP00000065923; ENSRNOG00000047697.
DR GeneID; 116568; -.
DR KEGG; rno:116568; -.
DR CTD; 2678; -.
DR RGD; 2683; Ggt1.
DR GeneTree; ENSGT00940000154601; -.
DR InParanoid; P07314; -.
DR OrthoDB; 1419292at2759; -.
DR PhylomeDB; P07314; -.
DR BRENDA; 2.3.2.2; 5301.
DR Reactome; R-RNO-174403; Glutathione synthesis and recycling.
DR Reactome; R-RNO-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR Reactome; R-RNO-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR UniPathway; UPA00204; -.
DR UniPathway; UPA00880; -.
DR PRO; PR:P07314; -.
DR Proteomes; UP000002494; Chromosome 20.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0016755; F:aminoacyltransferase activity; IDA:RGD.
DR GO; GO:0036374; F:glutathione hydrolase activity; ISS:UniProtKB.
DR GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0002951; F:leukotriene-C(4) hydrolase; ISO:RGD.
DR GO; GO:0000048; F:peptidyltransferase activity; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0006520; P:cellular amino acid metabolic process; ISO:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEP:RGD.
DR GO; GO:0019344; P:cysteine biosynthetic process; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; ISO:RGD.
DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:0006750; P:glutathione biosynthetic process; ISO:RGD.
DR GO; GO:0006751; P:glutathione catabolic process; ISS:UniProtKB.
DR GO; GO:0061017; P:hepatoblast differentiation; IEP:RGD.
DR GO; GO:0070365; P:hepatocyte differentiation; IEP:RGD.
DR GO; GO:1901750; P:leukotriene D4 biosynthetic process; ISO:RGD.
DR GO; GO:0006691; P:leukotriene metabolic process; ISO:RGD.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0031179; P:peptide modification; IDA:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0002682; P:regulation of immune system process; ISO:RGD.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
DR GO; GO:0097305; P:response to alcohol; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0034612; P:response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR GO; GO:0031638; P:zymogen activation; ISS:UniProtKB.
DR Gene3D; 1.10.246.130; -; 1.
DR Gene3D; 3.60.20.40; -; 1.
DR InterPro; IPR043138; GGT_lsub_C.
DR InterPro; IPR000101; GGT_peptidase.
DR InterPro; IPR043137; GGT_ssub.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR11686; PTHR11686; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR00066; g_glut_trans; 1.
DR PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glutathione biosynthesis; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Sialic acid; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix; Zymogen.
FT CHAIN 1..379
FT /note="Glutathione hydrolase 1 heavy chain"
FT /id="PRO_0000011064"
FT CHAIN 380..568
FT /note="Glutathione hydrolase 1 light chain"
FT /evidence="ECO:0000269|PubMed:2869484"
FT /id="PRO_0000011065"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:6136502"
FT TRANSMEM 5..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305|PubMed:6136502"
FT TOPO_DOM 27..568
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:6136502"
FT ACT_SITE 380
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 106
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 398..400
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 419
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 422
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 450..451
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 473
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT DISULFID 49..73
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT DISULFID 191..195
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT CONFLICT 9
FT /note="G -> A (in Ref. 7; AAA41217)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="R -> K (in Ref. 2; AAA57295/AAB59698)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="R -> K (in Ref. 2; AAB59698)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="P -> A (in Ref. 2; AAA57295/AAB59698 and 8;
FT CAA27224)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="S -> M (in Ref. 8; CAA27224)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="F -> V (in Ref. 8; CAA27224)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="P -> L (in Ref. 2; AAA57295/AAB59698)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 568 AA; 61610 MW; 24DC62A1DEEEA38C CRC64;
MKNRFLVLGL VAVVLVFVII GLCIWLPTTS GKPDHVYSRA AVATDAKRCS EIGRDMLQEG
GSVVDAAIAS LLCMGLINAH SMGIGGGLFF TIYNSTTRKA EVINAREMAP RLANTSMFNN
SKDSEEGGLS VAVPGEIRGY ELAHQRHGRL PWARLFQPSI QLARHGFPVG KGLARALDKK
RDIIEKTPAL CEVFCRQGKV LQEGETVTMP KLADTLQILA QEGARAFYNG SLTAQIVKDI
QEAGGIMTVE DLNNYRAEVI EHPMSIGLGD STLYVPSAPL SGPVLILILN ILKGYNFSPK
SVATPEQKAL TYHRIVEAFR FAYAKRTMLG DPKFVDVSQV IRNMSSEFYA TQLRARITDE
TTHPTAYYEP EFYLPDDGGT AHLSVVSEDG SAVAATSTIN LYFGSKVLSR VSGILFNDEM
DDFSSPNFTN QFGVAPSPAN FIKPGKQPLS SMCPSIIVDK DGKVRMVVGA SGGTQITTSV
ALAIINSLWF GYDVKRAVEE PRLHNQLLPN TTTVEKNIDQ VVTAGLKTRH HHTEVTPDFI
AVVQAVVRTS GGWAAASDSR KGGEPAGY
