ID M7BAE1_CHEMY Unreviewed; 667 AA. AC M7BAE1; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 29-MAY-2024, entry version 40. DE RecName: Full=Protein-glutamine gamma-glutamyltransferase 2 {ECO:0000256|ARBA:ARBA00040561}; DE EC=2.3.2.13 {ECO:0000256|ARBA:ARBA00024222}; DE EC=3.5.1.44 {ECO:0000256|ARBA:ARBA00039019}; DE AltName: Full=Isopeptidase TGM2 {ECO:0000256|ARBA:ARBA00042099}; DE AltName: Full=Protein-glutamine deamidase TGM2 {ECO:0000256|ARBA:ARBA00042239}; DE AltName: Full=Protein-glutamine dopaminyltransferase TGM2 {ECO:0000256|ARBA:ARBA00042105}; DE AltName: Full=Protein-glutamine histaminyltransferase TGM2 {ECO:0000256|ARBA:ARBA00043104}; DE AltName: Full=Protein-glutamine noradrenalinyltransferase TGM2 {ECO:0000256|ARBA:ARBA00043138}; DE AltName: Full=Protein-glutamine serotonyltransferase TGM2 {ECO:0000256|ARBA:ARBA00042912}; DE AltName: Full=Tissue transglutaminase {ECO:0000256|ARBA:ARBA00041677}; DE AltName: Full=Transglutaminase-2 {ECO:0000256|ARBA:ARBA00041650}; GN ORFNames=UY3_17738 {ECO:0000313|EMBL:EMP25192.1}; OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira; OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia. OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP25192.1, ECO:0000313|Proteomes:UP000031443}; RN [1] {ECO:0000313|Proteomes:UP000031443} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23624526; DOI=10.1038/ng.2615; RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C., RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y., RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J., RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S., RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.; RT "The draft genomes of soft-shell turtle and green sea turtle yield insights RT into the development and evolution of the turtle-specific body plan."; RL Nat. Genet. 45:701-706(2013). 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:0000256|ARBA:ARBA00036051}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66561; CC Evidence={ECO:0000256|ARBA:ARBA00036051}; 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:0000256|ARBA:ARBA00036025}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16442; CC Evidence={ECO:0000256|ARBA:ARBA00036025}; 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] + 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 -!- 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:0000256|ARBA:ARBA00036119}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66557; CC Evidence={ECO:0000256|ARBA:ARBA00036119}; 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:0000256|ARBA:ARBA00036107}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66565; CC Evidence={ECO:0000256|ARBA:ARBA00036107}; 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}. Membrane CC {ECO:0000256|ARBA:ARBA00004370}. 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; KB593659; EMP25192.1; -; Genomic_DNA. DR AlphaFoldDB; M7BAE1; -. DR STRING; 8469.M7BAE1; -. DR eggNOG; ENOG502QUSX; Eukaryota. DR Proteomes; UP000031443; Unassembled WGS sequence. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:TreeGrafter. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. 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; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 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; 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 3: Inferred from homology; 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 Extracellular matrix {ECO:0000256|ARBA:ARBA00022530}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022670}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {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 Reference proteome {ECO:0000313|Proteomes:UP000031443}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMP25192.1}. FT DOMAIN 248..340 FT /note="Transglutaminase-like" FT /evidence="ECO:0000259|SMART:SM00460" FT ACT_SITE 256 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT ACT_SITE 314 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT ACT_SITE 337 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT BINDING 377 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 379 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 425 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 430 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" SQ SEQUENCE 667 AA; 74983 MW; 266918C117A1BAEC CRC64; MTADMGNQQL VVRRGQSFII TLLFTGRGYE EGVDKLALNV ETGPCPIESS GTKSHFPVSD ALQASEWSAV VDHRDGTSLS LLIYSPPDAR IGRYTLTLEA SMGYQGTSFR LGEFILLFNP WCPDDSVFLE FEDQRCEFVL TQQGLIYQGS LKFIVPIPWN FGQFEDDIVN ICLQLLDTNP KFLRDQNRDC SRRNDPVYIG RVVSAMVNCN DDQGVLAGRW DNKYEDGMSP MSWIGSVDIL RRWRKYGCQP VRYGQCWVFA AVACTVLRCL GIPTRVVTNY NSAHDTNSNL VIDRYLDEMG NLQKTSKDTI WNFHCWVESW MTRPDLPPGC DGWQALDPTP QEKSEGAYCC GPAPVKAIKE GELRLNYDIP FVFAEVNADV VYWVLQKDGS RKKTIHSSTV GKNMSTKSVG KDTREDITHN YKYPEGSDQE REVFAKAELQ KSHLTEEEKG VSIKIKVSEG MNNGCDFDVY AVISNNTEAE RLYRLMFCAR TTSYNGVMGP ECGMKDLLNV ILLPHAEKTV PLRILYEKYG SCLTQDNMIK LMALLIEYQT GDIILGVRDI YIKNPDIKIR ILGEPMQKRK LVADLTLTNP LSTPLSGCVF TLEGAGLTDG QKIQELASPI EPEQEAKVRV DLAPQQSGLH KLVVNFESDK LKGVKGYRNV IVAPLPK //