TGM2_CAVCU
ID TGM2_CAVCU Reviewed; 690 AA.
AC P08587;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase 2 {ECO:0000305};
DE EC=2.3.2.13 {ECO:0000269|PubMed:16385579, ECO:0000269|PubMed:29618516};
DE AltName: Full=Guinea pig liver transglutaminase {ECO:0000303|PubMed:2900023, ECO:0000303|PubMed:5543674};
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:0000269|PubMed:16385579};
DE AltName: Full=Protein-glutamine dopaminyltransferase TGM2 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:22858378};
DE AltName: Full=Protein-glutamine histaminyltransferase TGM2 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:23022564};
DE AltName: Full=Protein-glutamine noradrenalinyltransferase TGM2 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:22858378};
DE AltName: Full=Protein-glutamine serotonyltransferase TGM2 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:14697203, ECO:0000269|PubMed:22858378};
DE AltName: Full=Tissue transglutaminase {ECO:0000303|PubMed:16385579};
DE Short=tTG {ECO:0000303|PubMed:16385579};
DE Short=tTgase {ECO:0000303|PubMed:22858378};
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 Cavia cutleri (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10144;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2900023; DOI=10.1021/bi00408a035;
RA Ikura K., Nasu T.-A., Yokota H., Tsuchiya Y., Sasaki R., Chiba H.;
RT "Amino acid sequence of guinea pig liver transglutaminase from its cDNA
RT sequence.";
RL Biochemistry 27:2898-2905(1988).
RN [2]
RP PROTEIN SEQUENCE OF 2-5.
RC TISSUE=Liver;
RX PubMed=5543674; DOI=10.1016/s0021-9258(18)62435-4;
RA Connellan J.M., Chung S.I., Whetzel N.K., Bradley L.M., Folk J.E.;
RT "Structural properties of guinea pig liver transglutaminase.";
RL J. Biol. Chem. 246:1093-1098(1971).
RN [3]
RP PROTEIN SEQUENCE OF 2-8 AND 684-690, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=2566328; DOI=10.1021/bi00431a054;
RA Ikura K., Yokota H., Sasaki R., Chiba H.;
RT "Determination of amino- and carboxyl-terminal sequences of guinea pig
RT liver transglutaminase: evidence for amino-terminal processing.";
RL Biochemistry 28:2344-2348(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 189-632.
RC TISSUE=Liver;
RA Ikura K., Nasu T.-A., Yokota H., Sasaki R., Chiba H.;
RT "Cloning of cDNA coding for guinea pig liver transglutaminase.";
RL Agric. Biol. Chem. 51:957-961(1987).
RN [5]
RP ACTIVITY REGULATION.
RX PubMed=2879844; DOI=10.1016/s0021-9258(19)75724-x;
RA Achyuthan K.E., Greenberg C.S.;
RT "Identification of a guanosine triphosphate-binding site on guinea pig
RT liver transglutaminase. Role of GTP and calcium ions in modulating
RT activity.";
RL J. Biol. Chem. 262:1901-1906(1987).
RN [6]
RP FUNCTION.
RX DOI=10.1111/j.1745-4514.1993.tb00472.x;
RA Larre C., Chiarello M., Blanloeil Y., Chenu M., Gueguen J.;
RT "Gliadin modifications catalyzed by guinea pig liver transglutaminase.";
RL J. Food Biochem. 17:267-282(1993).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14697203; DOI=10.1016/s0092-8674(03)01014-6;
RA Walther D.J., Peter J.U., Winter S., Hoeltje M., Paulmann N., Grohmann M.,
RA Vowinckel J., Alamo-Bethencourt V., Wilhelm C.S., Ahnert-Hilger G.,
RA Bader M.;
RT "Serotonylation of small GTPases is a signal transduction pathway that
RT triggers platelet alpha-granule release.";
RL Cell 115:851-862(2003).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16385579; DOI=10.1002/prot.20837;
RA Boros S., Ahrman E., Wunderink L., Kamps B., de Jong W.W., Boelens W.C.,
RA Emanuelsson C.S.;
RT "Site-specific transamidation and deamidation of the small heat-shock
RT protein Hsp20 by tissue transglutaminase.";
RL Proteins 62:1044-1052(2006).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22858378; DOI=10.1016/j.febslet.2012.07.062;
RA Hummerich R., Thumfart J.O., Findeisen P., Bartsch D., Schloss P.;
RT "Transglutaminase-mediated transamidation of serotonin, dopamine and
RT noradrenaline to fibronectin: evidence for a general mechanism of
RT monoaminylation.";
RL FEBS Lett. 586:3421-3428(2012).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23022564; DOI=10.1016/j.febslet.2012.09.027;
RA Vowinckel J., Stahlberg S., Paulmann N., Bluemlein K., Grohmann M.,
RA Ralser M., Walther D.J.;
RT "Histaminylation of glutamine residues is a novel posttranslational
RT modification implicated in G-protein signaling.";
RL FEBS Lett. 586:3819-3824(2012).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND TRANSGLUTAMINATION AT GLN-636.
RX PubMed=29618516; DOI=10.1074/jbc.ra117.001078;
RA Willis W.L., Wang L., Wada T.T., Gardner M., Abdouni O., Hampton J.,
RA Valiente G., Young N., Ardoin S., Agarwal S., Freitas M.A., Wu L.C.,
RA Jarjour W.N.;
RT "The proinflammatory protein HMGB1 is a substrate of transglutaminase-2 and
RT forms high-molecular weight complexes with autoantigens.";
RL J. Biol. Chem. 293:8394-8409(2018).
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 (PubMed:16385579, PubMed:14697203,
CC PubMed:22858378, PubMed:23022564). Involved in many biological
CC processes, such as bone development, angiogenesis, wound healing,
CC cellular differentiation, chromatin modification and apoptosis (By
CC similarity). Acts as a protein-glutamine gamma-glutamyltransferase by
CC mediating the cross-linking of proteins, such as ACO2, HSPB6, FN1,
CC HMGB1, RAP1GDS1, SLC25A4/ANT1, SPP1 and WDR54 (PubMed:16385579,
CC PubMed:29618516). Under physiological conditions, the protein cross-
CC linking activity is inhibited by GTP; inhibition is relieved by Ca(2+)
CC in response to various stresses (By similarity). When secreted,
CC catalyzes cross-linking of proteins of the extracellular matrix, such
CC as FN1 and SPP1 resulting in the formation of scaffolds (By
CC similarity). Plays a key role during apoptosis, both by (1) promoting
CC the cross-linking of cytoskeletal proteins resulting in condensation of
CC the cytoplasm, and by (2) mediating cross-linking proteins of the
CC extracellular matrix, resulting in the irreversible formation of
CC scaffolds that stabilize the integrity of the dying cells before their
CC clearance by phagocytosis, thereby preventing the leakage of harmful
CC intracellular components (By similarity). In addition to protein cross-
CC linking, can use different monoamine substrates to catalyze a vast
CC array of protein post-translational modifications: mediates aminylation
CC of serotonin, dopamine, noradrenaline or histamine into glutamine
CC residues of target proteins to generate protein serotonylation,
CC dopaminylation, noradrenalinylation or histaminylation, respectively
CC (PubMed:14697203, PubMed:22858378, PubMed:23022564). Mediates protein
CC serotonylation of small GTPases during activation and aggregation of
CC platelets, leading to constitutive activation of these GTPases
CC (PubMed:14697203). 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 (PubMed:16385579). Catalyzes specific
CC deamidation of protein gliadin, a component of wheat gluten in the diet
CC (Ref.6). May also act as an isopeptidase cleaving the previously formed
CC cross-links (By similarity). Also able to participate in signaling
CC pathways independently of its acyltransferase activity: acts as a
CC signal transducer in alpha-1 adrenergic receptor-mediated stimulation
CC of phospholipase C-delta (PLCD) activity and is required for coupling
CC alpha-1 adrenergic agonists to the stimulation of phosphoinositide
CC lipid metabolism (By similarity). {ECO:0000250|UniProtKB:P21980,
CC ECO:0000250|UniProtKB:P21981, ECO:0000269|PubMed:14697203,
CC ECO:0000269|PubMed:16385579, ECO:0000269|PubMed:22858378,
CC ECO:0000269|PubMed:23022564, ECO:0000269|PubMed:29618516,
CC ECO:0000269|Ref.6}.
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:0000269|PubMed:16385579,
CC ECO:0000269|PubMed:29618516};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54817;
CC Evidence={ECO:0000269|PubMed:16385579, ECO:0000269|PubMed:29618516};
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:14697203, ECO:0000269|PubMed:22858378};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66553;
CC Evidence={ECO:0000269|PubMed:14697203, ECO:0000269|PubMed:22858378};
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:0000269|PubMed:22858378};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66557;
CC Evidence={ECO:0000269|PubMed:22858378};
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:0000269|PubMed:23022564};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66565;
CC Evidence={ECO:0000269|PubMed:23022564};
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:0000269|PubMed:22858378};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66561;
CC Evidence={ECO:0000269|PubMed:22858378};
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:0000269|PubMed:16385579};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16442;
CC Evidence={ECO:0000269|PubMed:16385579};
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 (PubMed:2879844). In contrast, Ca(2+) acts as a
CC cofactor by inducing conformational change to the active open form
CC (PubMed:2879844). In absence of Ca(2+), Mg(2+) may bind Ca(2+)-binding
CC sites, promoting GTP-binding and subsequent inhibition of the
CC acyltransferase activity (By similarity).
CC {ECO:0000250|UniProtKB:P21980, ECO:0000269|PubMed:2879844}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=794.1 nM for serotonin (for protein-glutamine serotonyltransferase
CC activity) {ECO:0000269|PubMed:22858378};
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 -!- 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-636 and the epsilon-amino group of a
CC lysine residue of itself or HMGB1, forming homopolymers and
CC heteropolymers, respectively. {ECO:0000269|PubMed:29618516}.
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; M19646; AAA37056.1; -; mRNA.
DR EMBL; D00114; BAA00068.1; -; mRNA.
DR PIR; A29996; A29996.
DR AlphaFoldDB; P08587; -.
DR SMR; P08587; -.
DR IntAct; P08587; 6.
DR MINT; P08587; -.
DR BindingDB; P08587; -.
DR ChEMBL; CHEMBL3988613; -.
DR iPTMnet; P08587; -.
DR PRIDE; P08587; -.
DR BRENDA; 2.3.2.13; 14541.
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; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA: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:0120296; F:peptide dopaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0120299; F:peptide histaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0120298; F:peptide noradrenalinyltransferase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0008483; F:transaminase activity; IDA:MGI.
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; IDA:UniProtKB.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IDA:UniProtKB.
DR GO; GO:0018277; P:protein deamination; IDA: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 GO; GO:1900046; P:regulation of hemostasis; IDA: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; S-nitrosylation;
KW Secreted; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2566328,
FT ECO:0000269|PubMed:5543674"
FT CHAIN 2..690
FT /note="Protein-glutamine gamma-glutamyltransferase 2"
FT /id="PRO_0000213706"
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 436
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P21980"
FT BINDING 446
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00488"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00488"
FT BINDING 479..486
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P21980"
FT BINDING 542
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P21980"
FT BINDING 583..586
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P21980"
FT SITE 519
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P52181"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2566328"
FT MOD_RES 467
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 636
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000269|PubMed:29618516"
FT CONFLICT 2..3
FT /note="AE -> EA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="G -> A (in Ref. 4; BAA00068)"
FT /evidence="ECO:0000305"
FT CONFLICT 336..354
FT /note="CWVESWMTRPDLEPGYEGW -> SLLGGVVDDQAGPGAWVRGV (in Ref.
FT 4; BAA00068)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 690 AA; 77141 MW; 047223D38DBEA4A4 CRC64;
MAEDLILERC DLQLEVNGRD HRTADLCRER LVLRRGQPFW LTLHFEGRGY EAGVDTLTFN
AVTGPDPSEE AGTMARFSLS SAVEGGTWSA SAVDQQDSTV SLLLSTPADA PIGLYRLSLE
ASTGYQGSSF VLGHFILLYN PRCPADAVYM DSDQERQEYV LTQQGFIYQG SAKFINGIPW
NFGQFEDGIL DICLMLLDTN PKFLKNAGQD CSRRSRPVYV GRVVSAMVNC NDDQGVLQGR
WDNNYSDGVS PMSWIGSVDI LRRWKDYGCQ RVKYGQCWVF AAVACTVLRC LGIPTRVVTN
FNSAHDQNSN LLIEYFRNES GEIEGNKSEM IWNFHCWVES WMTRPDLEPG YEGWQALDPT
PQEKSEGTYC CGPVPVRAIK EGHLNVKYDA PFVFAEVNAD VVNWIRQKDG SLRKSINHLV
VGLKISTKSV GRDEREDITH TYKYPEGSEE EREAFVRANH LNKLATKEEA QEETGVAMRI
RVGQNMTMGS DFDIFAYITN GTAESHECQL LLCARIVSYN GVLGPVCSTN DLLNLTLDPF
SENSIPLHIL YEKYGDYLTE SNLIKVRGLL IEPAANSYVL AERDIYLENP EIKIRVLGEP
KQNRKLIAEV SLKNPLPVPL LGCIFTVEGA GLTKDQKSVE VPDPVEAGEQ AKVRVDLLPT
EVGLHKLVVN FECDKLKAVK GYRNVIIGPA
