ID B3DM72_XENTR Unreviewed; 691 AA. AC B3DM72; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 02-SEP-2026, entry version 87. DE RecName: Full=Protein-glutamine gamma-glutamyltransferase {ECO:0000256|PROSITE-ProRule:PRU10024}; DE EC=2.3.2.13 {ECO:0000256|PROSITE-ProRule:PRU10024}; GN Name=tgm2 {ECO:0000313|Xenbase:XB-GENE-5940894}; GN Synonyms=LOC100170618 {ECO:0000313|EMBL:AAI67727.1}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana. OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI67727.1}; RN [1] {ECO:0000313|EMBL:AAI67727.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testes {ECO:0000313|EMBL:AAI67727.1}; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutaminyl-[protein] + (R)-noradrenaline = 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:0000256|ARBA:ARBA00048230}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66561; CC Evidence={ECO:0000256|ARBA:ARBA00048230}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutaminyl-[protein] + H2O = 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:0000256|ARBA:ARBA00047868}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16442; CC Evidence={ECO:0000256|ARBA:ARBA00047868}; 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; CC Evidence={ECO:0000256|ARBA:ARBA00036876}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54817; CC Evidence={ECO:0000256|ARBA:ARBA00036876}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutaminyl-[protein] + dopamine = 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:0000256|ARBA:ARBA00048365}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66557; CC Evidence={ECO:0000256|ARBA:ARBA00048365}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutaminyl-[protein] + histamine = 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:0000256|ARBA:ARBA00047876}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66565; CC Evidence={ECO:0000256|ARBA:ARBA00047876}; 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:0000256|ARBA:ARBA00036377}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66553; CC Evidence={ECO:0000256|ARBA:ARBA00036377}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|PIRSR:PIRSR000459-2}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000459-2}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. CC Chromosome {ECO:0000256|ARBA:ARBA00004286}. Cytoplasm, cytosol CC {ECO:0000256|ARBA:ARBA00004514}. Mitochondrion CC {ECO:0000256|ARBA:ARBA00004173}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. Secreted, extracellular space, CC extracellular matrix {ECO:0000256|ARBA:ARBA00004498}. CC -!- SIMILARITY: Belongs to the transglutaminase superfamily. CC Transglutaminase family. {ECO:0000256|ARBA:ARBA00005968}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC167727; AAI67727.1; -; mRNA. DR RefSeq; NP_001123852.1; NM_001130380.1. DR AlphaFoldDB; B3DM72; -. DR GeneID; 100170618; -. DR KEGG; xtr:100170618; -. DR AGR; Xenbase:XB-GENE-5940894; -. DR CTD; 7052; -. DR Xenbase; XB-GENE-5940894; tgm2. DR OMA; CTVGPGE; -. DR OrthoDB; 437511at2759; -. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IBA:GO_Central. DR GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-EC. DR GO; GO:0060348; P:bone development; IBA:GO_Central. DR GO; GO:0018149; P:peptide cross-linking; IBA:GO_Central. DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central. DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; IBA:GO_Central. DR GO; GO:2000425; P:regulation of apoptotic cell clearance; IBA:GO_Central. DR FunFam; 2.60.40.10:FF:000090; Protein-glutamine gamma-glutamyltransferase 2; 1. DR FunFam; 2.60.40.10:FF:000278; Protein-glutamine gamma-glutamyltransferase 2; 1. DR FunFam; 2.60.40.10:FF:001042; Protein-glutamine gamma-glutamyltransferase 2; 1. DR FunFam; 3.90.260.10:FF:000001; Protein-glutamine gamma-glutamyltransferase 2; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 3. DR Gene3D; 3.90.260.10; Transglutaminase-like; 1. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR InterPro; IPR050779; Transglutaminase. 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 PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1. DR PANTHER; PTHR11590:SF6; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE 2; 1. 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; SSF54001; Cysteine proteinases; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF49309; Transglutaminase, two C-terminal domains; 2. DR PROSITE; PS00547; TRANSGLUTAMINASES; 1. PE 2: Evidence at transcript level; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315}; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR000459-2}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Chromosome {ECO:0000256|ARBA:ARBA00022454}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000459-2}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 269..361 FT /note="Transglutaminase-like" FT /evidence="ECO:0000259|SMART:SM00460" FT ACT_SITE 277 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1, FT ECO:0000256|PROSITE-ProRule:PRU10024" FT ACT_SITE 335 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT ACT_SITE 358 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT BINDING 398 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 400 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 446 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 451 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" SQ SEQUENCE 691 AA; 77879 MW; 7F03CB6BC0080527 CRC64; MAEELYLESF DLDCSGNNRS HRTAEATCER LIVRRGQPFQ ITLNFSPRGY EEGVDKLSLN AVTGPCPSEE SGTSNHIPVS DALQDGAWSA AITSTDGGTL ILSITSPPDA RIGYYNLSLE TSTEYQGSSF QLGSFTLLFN PWCPEDSVYL ETEEERKEYV LCQHGIIFQG TKDSVEHVPW NFGQFEDEIL DITLQVLDTS PKFLNDSNRD CSRRNDPVYI SRVISAMVNC NDDRGVLFGR WDNKYDDGIS PMFWMGSVAI LRRWRKFSCQ AVKYGQCWVY AAVACTVLRC LGIPARVITN YNSAHDTNSN LLIEQYLDEH GKRQPKQKEI IWNYHCWTEA WMTRPDLGEA YNGWQVVDPT PQEKSEGTYC CGPTPVKAVK EGDLNLKYDV PFVFAEVNAD VVYFVQQNDG SVKKTQFISL VGQKISTKAI GKDEREDITL NYKYPEGSED ERRVFEKANK QSEAEEERVE TPSDFTIKIK VSEGMNKGSD FDVFAVITNN REEEKQCRLM FCARTCSYTG EVGPECGMKD LLNLTLTPQE EKRVPLRILY EKYGPTMTEN NTIKLVAMLY DYSSKEIILA VRDIHVKNPS IKIKVLGEPK QKRKLVAEIS LKNPLAEPLT GCCFTVEGAG LTAEQLVKTL DCPVEPGQEA KVRVDLMPQL AGKLSLVVDF ESDLLKAVKG YRNIIIAPLP K //