TGM2_BOVIN
ID TGM2_BOVIN Reviewed; 687 AA.
AC P51176; Q3ZBH7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase 2 {ECO:0000305};
DE EC=2.3.2.13 {ECO:0000305|PubMed:9880554};
DE AltName: Full=Isopeptidase TGM2 {ECO:0000305};
DE EC=3.4.-.- {ECO:0000250|UniProtKB:P21980};
DE AltName: Full=Protein-glutamine deamidase TGM2 {ECO:0000305};
DE EC=3.5.1.44 {ECO:0000250|UniProtKB:P21980};
DE AltName: Full=Protein-glutamine dopaminyltransferase TGM2 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:P21980};
DE AltName: Full=Protein-glutamine histaminyltransferase TGM2 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:P21980};
DE AltName: Full=Protein-glutamine noradrenalinyltransferase TGM2 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:P08587};
DE AltName: Full=Protein-glutamine serotonyltransferase TGM2 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:25128524};
DE AltName: Full=Tissue transglutaminase {ECO:0000303|PubMed:9880554};
DE Short=TG {ECO:0000303|PubMed:9880554};
DE AltName: Full=Transglutaminase-2 {ECO:0000250|UniProtKB:P21980};
DE Short=TGase-2 {ECO:0000250|UniProtKB:P21980};
GN Name=TGM2 {ECO:0000250|UniProtKB:P21980};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 79-95; 157-166; 242-251 AND
RP 581-587, AND TISSUE SPECIFICITY.
RC TISSUE=Artery;
RX PubMed=1682150; DOI=10.1111/j.1432-1033.1991.tb16338.x;
RA Nakanishi K., Nara K., Hagiwara H., Aoyama Y., Ueno H., Hirose S.;
RT "Cloning and sequence analysis of cDNA clones for bovine aortic-
RT endothelial-cell transglutaminase.";
RL Eur. J. Biochem. 202:15-21(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 79-95; 157-166 AND 242-251, AND INDUCTION.
RX PubMed=2572599; DOI=10.1016/s0021-9258(19)47302-x;
RA Nara K., Nakanishi K., Hagiwara H., Wakita K., Kojima S., Hirose S.;
RT "Retinol-induced morphological changes of cultured bovine endothelial cells
RT are accompanied by a marked increase in transglutaminase.";
RL J. Biol. Chem. 264:19308-19312(1989).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9880554; DOI=10.1074/jbc.274.3.1729;
RA Kaartinen M.T., Pirhonen A., Linnala-Kankkunen A., Maeenpaeae P.H.;
RT "Cross-linking of osteopontin by tissue transglutaminase increases its
RT collagen binding properties.";
RL J. Biol. Chem. 274:1729-1735(1999).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25128524; DOI=10.1152/ajplung.00162.2014;
RA Penumatsa K.C., Toksoz D., Warburton R.R., Hilmer A.J., Liu T., Khosla C.,
RA Comhair S.A., Fanburg B.L.;
RT "Role of hypoxia-induced transglutaminase 2 in pulmonary artery smooth
RT muscle cell proliferation.";
RL Am. J. Physiol. 307:L576-L585(2014).
CC -!- FUNCTION: Calcium-dependent acyltransferase that catalyzes the
CC formation of covalent bonds between peptide-bound glutamine and various
CC primary amines, such as gamma-amino group of peptide-bound lysine, or
CC mono- and polyamines, thereby producing cross-linked or aminated
CC proteins, respectively (By similarity). Involved in many biological
CC processes, such as bone development, angiogenesis, wound healing,
CC cellular differentiation, chromatin modification and apoptosis
CC (PubMed:9880554). Acts as a protein-glutamine gamma-glutamyltransferase
CC by mediating the cross-linking of proteins, such as ACO2, HSPB6, FN1,
CC HMGB1, RAP1GDS1, SLC25A4/ANT1, SPP1 and WDR54 (PubMed:9880554). Under
CC physiological conditions, the protein cross-linking activity is
CC inhibited by GTP; inhibition is relieved by Ca(2+) in response to
CC various stresses (By similarity). When secreted, catalyzes cross-
CC linking of proteins of the extracellular matrix, such as FN1 and SPP1
CC resulting in the formation of scaffolds (By similarity). Plays a key
CC role during apoptosis, both by (1) promoting the cross-linking of
CC cytoskeletal proteins resulting in condensation of the cytoplasm, and
CC by (2) mediating cross-linking proteins of the extracellular matrix,
CC resulting in the irreversible formation of scaffolds that stabilize the
CC integrity of the dying cells before their clearance by phagocytosis,
CC thereby preventing the leakage of harmful intracellular components (By
CC similarity). In addition to protein cross-linking, can use different
CC monoamine substrates to catalyze a vast array of protein post-
CC translational modifications: mediates aminylation of serotonin,
CC dopamine, noradrenaline or histamine into glutamine residues of target
CC proteins to generate protein serotonylation, dopaminylation,
CC noradrenalinylation or histaminylation, respectively (PubMed:25128524).
CC Mediates protein serotonylation of small GTPases during activation and
CC aggregation of platelets, leading to constitutive activation of these
CC GTPases (By similarity). Plays a key role in chromatin organization by
CC mediating serotonylation and dopaminylation of histone H3 (By
CC similarity). Catalyzes serotonylation of 'Gln-5' of histone H3
CC (H3Q5ser) during serotonergic neuron differentiation, thereby
CC facilitating transcription (By similarity). Acts as a mediator of
CC neurotransmission-independent role of nuclear dopamine in ventral
CC tegmental area (VTA) neurons: catalyzes dopaminylation of 'Gln-5' of
CC histone H3 (H3Q5dop), thereby regulating relapse-related
CC transcriptional plasticity in the reward system (By similarity).
CC Regulates vein remodeling by mediating serotonylation and subsequent
CC inactivation of ATP2A2/SERCA2 (By similarity). Also acts as a protein
CC deamidase by mediating the side chain deamidation of specific glutamine
CC residues of proteins to glutamate (By similarity). Catalyzes specific
CC deamidation of protein gliadin, a component of wheat gluten in the diet
CC (By similarity). May also act as an isopeptidase cleaving the
CC previously formed cross-links (By similarity). Also able to participate
CC in signaling pathways independently of its acyltransferase activity:
CC acts as a signal transducer in alpha-1 adrenergic receptor-mediated
CC stimulation of phospholipase C-delta (PLCD) activity and is required
CC for coupling alpha-1 adrenergic agonists to the stimulation of
CC phosphoinositide lipid metabolism (By similarity).
CC {ECO:0000250|UniProtKB:P08587, ECO:0000250|UniProtKB:P21980,
CC ECO:0000250|UniProtKB:P21981, ECO:0000269|PubMed:25128524,
CC ECO:0000269|PubMed:9880554}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-
CC lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011,
CC ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10024, ECO:0000305|PubMed:9880554};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54817;
CC Evidence={ECO:0000305|PubMed:9880554};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[protein] + serotonin = 5-serotonyl-L-glutamyl-
CC [protein] + NH4(+); Xref=Rhea:RHEA:66552, Rhea:RHEA-COMP:10207,
CC Rhea:RHEA-COMP:17052, ChEBI:CHEBI:28938, ChEBI:CHEBI:30011,
CC ChEBI:CHEBI:167174, ChEBI:CHEBI:350546;
CC Evidence={ECO:0000269|PubMed:25128524};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66553;
CC Evidence={ECO:0000269|PubMed:25128524};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dopamine + L-glutaminyl-[protein] = 5-dopaminyl-L-glutamyl-
CC [protein] + NH4(+); Xref=Rhea:RHEA:66556, Rhea:RHEA-COMP:10207,
CC Rhea:RHEA-COMP:17053, ChEBI:CHEBI:28938, ChEBI:CHEBI:30011,
CC ChEBI:CHEBI:59905, ChEBI:CHEBI:167175;
CC Evidence={ECO:0000250|UniProtKB:P21980};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66557;
CC Evidence={ECO:0000250|UniProtKB:P21980};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=histamine + L-glutaminyl-[protein] = 5-histaminyl-L-glutamyl-
CC [protein] + NH4(+); Xref=Rhea:RHEA:66564, Rhea:RHEA-COMP:10207,
CC Rhea:RHEA-COMP:17056, ChEBI:CHEBI:28938, ChEBI:CHEBI:30011,
CC ChEBI:CHEBI:58432, ChEBI:CHEBI:167179;
CC Evidence={ECO:0000250|UniProtKB:P21980};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66565;
CC Evidence={ECO:0000250|UniProtKB:P21980};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-noradrenaline + L-glutaminyl-[protein] = 5-(R)-
CC noradrenalinyl-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:66560,
CC Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:17054, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30011, ChEBI:CHEBI:72587, ChEBI:CHEBI:167178;
CC Evidence={ECO:0000250|UniProtKB:P08587};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66561;
CC Evidence={ECO:0000250|UniProtKB:P08587};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+);
CC Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973,
CC ChEBI:CHEBI:30011; EC=3.5.1.44;
CC Evidence={ECO:0000250|UniProtKB:P21980};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16442;
CC Evidence={ECO:0000250|UniProtKB:P21980};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P21980};
CC -!- ACTIVITY REGULATION: Acyltransferase activity is regulated by the
CC binding of GTP and Ca(2+): inactivated by GTP, which stabilizes its
CC closed structure, thereby obstructing the accessibility of substrates
CC to the active sites. In contrast, Ca(2+) acts as a cofactor by inducing
CC conformational change to the active open form. In absence of Ca(2+),
CC Mg(2+) may bind Ca(2+)-binding sites, promoting GTP-binding and
CC subsequent inhibition of the acyltransferase activity.
CC {ECO:0000250|UniProtKB:P21980}.
CC -!- SUBUNIT: Monomer. Interacts with phospholipase C; promoting alpha-1
CC adrenergic receptor signaling (By similarity). Interacts with PLCD1 (By
CC similarity). {ECO:0000250|UniProtKB:P21980,
CC ECO:0000250|UniProtKB:Q9WVJ6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P21980}. Nucleus {ECO:0000250|UniProtKB:P21980}.
CC Chromosome {ECO:0000250|UniProtKB:P21980}. Secreted, extracellular
CC space, extracellular matrix {ECO:0000250|UniProtKB:P21980}. Cell
CC membrane {ECO:0000250|UniProtKB:Q9WVJ6}. Mitochondrion
CC {ECO:0000250|UniProtKB:P21980}. Note=Mainly localizes to the cytosol.
CC Present at much lower level in the nucleus and chromatin. Also secreted
CC via a non-classical secretion pathway to the extracellular matrix.
CC {ECO:0000250|UniProtKB:P21980}.
CC -!- TISSUE SPECIFICITY: Highest levels are detected in the lung. Lower
CC levels are found in the liver, spleen and heart, but not in the brain.
CC {ECO:0000269|PubMed:1682150}.
CC -!- INDUCTION: By retinoic acid. {ECO:0000269|PubMed:2572599}.
CC -!- PTM: Disulfide bond formation inactivates the calcium-dependent
CC acyltransferase activity. Cys-370 can form disulfide bonds with both
CC Cys-230 and Cys-371: formation of a disulfide bond between Cys-230 and
CC Cys-370 facilitates formation of the disulfide between Cys-370 and Cys-
CC 371, which promotes inactivation of the acyltransferase activity. May
CC also form interchain disulfids between Cys-230 and Cys-370. Ca(2+)
CC protects against disulfide bond formation and inactivation.
CC {ECO:0000250|UniProtKB:P21980}.
CC -!- PTM: Auto-transglutaminated: Forms covalent cross-links mediated by
CC transglutaminase between Gln-633 and the epsilon-amino group of a
CC lysine residue of itself or HMGB1, forming homopolymers and
CC heteropolymers, respectively. {ECO:0000250|UniProtKB:P08587}.
CC -!- PTM: S-nitrosylated, leading to inactivation of the acyltransferase
CC activity. {ECO:0000250|UniProtKB:P21981}.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000305}.
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DR EMBL; X60686; CAA43097.1; -; mRNA.
DR EMBL; BC103290; AAI03291.1; -; mRNA.
DR PIR; S19680; S19680.
DR RefSeq; NP_803473.1; NM_177507.2.
DR AlphaFoldDB; P51176; -.
DR SMR; P51176; -.
DR STRING; 9913.ENSBTAP00000021569; -.
DR PaxDb; P51176; -.
DR PeptideAtlas; P51176; -.
DR PRIDE; P51176; -.
DR GeneID; 281528; -.
DR KEGG; bta:281528; -.
DR CTD; 7052; -.
DR eggNOG; ENOG502QUSX; Eukaryota.
DR HOGENOM; CLU_013435_1_0_1; -.
DR InParanoid; P51176; -.
DR OrthoDB; 297055at2759; -.
DR TreeFam; TF324278; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0120297; F:histone dopaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0120295; F:histone serotonyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0120299; F:peptide histaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0120298; F:peptide noradrenalinyltransferase activity; IEA:RHEA.
DR GO; GO:0120294; F:peptide serotonyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IDA:UniProtKB.
DR GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0060348; P:bone development; IDA:UniProtKB.
DR GO; GO:1903351; P:cellular response to dopamine; ISS:UniProtKB.
DR GO; GO:1904015; P:cellular response to serotonin; ISS:UniProtKB.
DR GO; GO:0018149; P:peptide cross-linking; IDA:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; ISS:UniProtKB.
DR GO; GO:0018277; P:protein deamination; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:2000425; P:regulation of apoptotic cell clearance; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.90.260.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002931; Transglutaminase-like.
DR InterPro; IPR036985; Transglutaminase-like_sf.
DR InterPro; IPR023608; Transglutaminase_animal.
DR InterPro; IPR013808; Transglutaminase_AS.
DR InterPro; IPR008958; Transglutaminase_C.
DR InterPro; IPR036238; Transglutaminase_C_sf.
DR InterPro; IPR001102; Transglutaminase_N.
DR Pfam; PF00927; Transglut_C; 2.
DR Pfam; PF01841; Transglut_core; 1.
DR Pfam; PF00868; Transglut_N; 1.
DR PIRSF; PIRSF000459; TGM_EBP42; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF49309; SSF49309; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Calcium; Cell membrane; Chromosome;
KW Cytoplasm; Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW GTP-binding; Hydrolase; Isopeptide bond; Membrane; Metal-binding;
KW Mitochondrion; Nucleotide-binding; Nucleus; Protease; Reference proteome;
KW S-nitrosylation; Secreted; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P08587"
FT CHAIN 2..687
FT /note="Protein-glutamine gamma-glutamyltransferase 2"
FT /id="PRO_0000213705"
FT ACT_SITE 277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00488"
FT BINDING 400
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00488"
FT BINDING 437
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P21980"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00488"
FT BINDING 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00488"
FT BINDING 476..483
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P21980"
FT BINDING 539
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P21980"
FT BINDING 580..583
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P21980"
FT SITE 516
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P52181"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P08587"
FT MOD_RES 468
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P21981"
FT DISULFID 230..370
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:P21980"
FT DISULFID 370..371
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:P21980"
FT CROSSLNK 633
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000250|UniProtKB:P08587"
FT CONFLICT 638
FT /note="V -> I (in Ref. 2; AAI03291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 77112 MW; 7BBA00F15E779944 CRC64;
MAEELVLERC DLELEANGRD HHTADLCRER LVVRRGQPFW LTLHFEGRNY EASVDSLTFC
AVTGPDPSEE AGTKALFRLS DATEEGAWAA VAADQRDSTL SLHLSTPANA PVGHYRLSLE
ASTGYQGSSF MLGQFTLLFN SWCPADAVYL DSDEERQEYV LTQQGFIYQG SAKFIKNIPW
NFGQFEEGIL DICLMLLDVN PKFLRNAGRD CSRRSSPVYV GRVVSGMVNC NDDQGVLLGR
WDNNYADGIS PMSWIGSVDI LRRWKRDGCQ RVKYGQCWVF AAVACTVLRC LGIPTRVVTN
YNSAHDQNSN LLIEYFRNEF GEIQSDKSEM IWNFHCWVES WMTRPDLQPG YEGWQALDPT
PQEKSEGTYC CGPVPVRAIK EGDLSTKYDA PFVFAEVNAD VVDWIRQDDG SLHKSINHSL
VVGLKISTKC VGRDDREDIT HSYKYPEGSP EEREAFTRAN HLNKLVNKEE TGVAMRIRVG
EGMNRGCDFD VFAHITNSTP EEHTGRLLLC ARTVSYNGIL GPECGTKDLL SLSLEPYSEK
SIPLRILYEK YCDCLTESNL IKVRGLLIEP AANSYLLAER DIYLENPEIK IRILGEPKQN
RKLVAEISLQ NPLTVALSGC TFTVEGAGLI EEQKTVDVPD PVEAGEEVKV RVDLLPLYVG
RHKLVVNFES DRLKAVKGFR NVIVGPS
