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   07-APR-2021, entry version 166.
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;
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;
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;
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 and other gamma-glutamyl
CC       compounds, such as leukotriene C4 (LTC4). The metabolism of glutathione
CC       by GGT1 releases free glutamate and the dipeptide cysteinyl-glycine,
CC       which is hydrolyzed to cysteine and glycine by dipeptidases. In the
CC       presence of high concentrations of dipeptides and some amino acids, can
CC       also catalyze a transpeptidation reaction, transferring the gamma-
CC       glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl
CC       compound. Contributes to cysteine homeostasis, glutathione homeostasis
CC       and in the conversion of the leukotriene LTC4 to LTD4.
CC       {ECO:0000250|UniProtKB:P19440}.
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   -!- 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:0000250|UniProtKB:P19440};
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:0000269|PubMed:6122208};
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: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:0000250|UniProtKB:P19440}.
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   SMR; P07314; -.
DR   BindingDB; P07314; -.
DR   ChEMBL; CHEMBL2943; -.
DR   DrugCentral; P07314; -.
DR   GlyConnect; 170; 1 O-Linked glycan.
DR   GlyGen; P07314; 7 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; P07314; -.
DR   PhosphoSitePlus; P07314; -.
DR   PRIDE; P07314; -.
DR   GeneID; 116568; -.
DR   KEGG; rno:116568; -.
DR   CTD; 2678; -.
DR   RGD; 2683; Ggt1.
DR   InParanoid; P07314; -.
DR   OMA; GILWNNE; -.
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   UniPathway; UPA00204; -.
DR   PRO; PR:P07314; -.
DR   Proteomes; UP000002494; Unplaced.
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: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:0016755; F:transferase activity, transferring amino-acyl groups; IDA: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   REGION          398..400
FT                   /note="Glutamate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P19440"
FT   REGION          450..451
FT                   /note="Glutamate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P19440"
FT   ACT_SITE        380
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P19440"
FT   BINDING         106
FT                   /note="Glutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P19440"
FT   BINDING         419
FT                   /note="Glutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P19440"
FT   BINDING         422
FT                   /note="Glutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P19440"
FT   BINDING         473
FT                   /note="Glutamate; via amide nitrogen"
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
//