ID A0A4W4HS28_ELEEL Unreviewed; 679 AA. AC A0A4W4HS28; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 24-JUL-2024, entry version 19. 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 Name=tgm2b {ECO:0000313|Ensembl:ENSEEEP00000051738.1}; OS Electrophorus electricus (Electric eel) (Gymnotus electricus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gymnotiformes; OC Gymnotoidei; Gymnotidae; Electrophorus. OX NCBI_TaxID=8005 {ECO:0000313|Ensembl:ENSEEEP00000051738.1, ECO:0000313|Proteomes:UP000314983}; RN [1] {ECO:0000313|Proteomes:UP000314983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24970089; RA Gallant J.R., Traeger L.L., Volkening J.D., Moffett H., Chen P.H., RA Novina C.D., Phillips G.N.Jr., Anand R., Wells G.B., Pinch M., Guth R., RA Unguez G.A., Albert J.S., Zakon H.H., Samanta M.P., Sussman M.R.; RT "Nonhuman genetics. Genomic basis for the convergent evolution of electric RT organs."; RL Science 344:1522-1525(2014). RN [2] {ECO:0000313|Proteomes:UP000314983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=28695212; RA Traeger L.L., Sabat G., Barrett-Wilt G.A., Wells G.B., Sussman M.R.; RT "A tail of two voltages: Proteomic comparison of the three electric organs RT of the electric eel."; RL Sci. Adv. 3:e1700523-e1700523(2017). RN [3] {ECO:0000313|Ensembl:ENSEEEP00000051738.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2023) to UniProtKB. 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 AlphaFoldDB; A0A4W4HS28; -. DR Ensembl; ENSEEET00000052296.1; ENSEEEP00000051738.1; ENSEEEG00000024292.1. DR GeneTree; ENSGT01050000244866; -. DR Proteomes; UP000314983; 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:0007399; P:nervous system development; IEA:UniProt. 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; 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 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:UP000314983}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 266..358 FT /note="Transglutaminase-like" FT /evidence="ECO:0000259|SMART:SM00460" FT ACT_SITE 274 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT ACT_SITE 332 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT ACT_SITE 355 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT BINDING 395 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 397 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 443 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 448 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" SQ SEQUENCE 679 AA; 76360 MW; A2BB0E25A0B193B3 CRC64; LVQNLIVLTY IGSWDLACEF NNMDHHTELN GTDRLIVRRG QPFTVSLSLR SGSYQPGTHQ LRITADTGIA PMEEYGTRAV FGLSDVIDNT HWSAVVTSPP ADTITLSICS APDAPIGRYI LTLDSQIQFE LILLFNPWCP RDAVYMDSKD KLEEYVLAQD GIIYRGDAKY PVPLPWYFGQ FEDSILDICL RILDVNPKYQ RNPGKDCSGR RNPVYVTRVL SAMVNSNDRD NGVLVGCWKN SFEDGISPMS WKGSVNILRN WNSTSCMSVR YGQCWVFAAV ACTVSRALGI PCRVVTNYLS AHDTNTNLVI ERYYDEKGQL LNSTRDMIWN YHCWVESWMT RPDLKAGFDG WQASDPTPQE KSEGVYCCGP VPLQAIKEGE LTLKYDAPFV FAEVNADLET YLKYKDGSMK RLYDKSKVGQ KISTKSVGSD QREDITHLYK YAEGSDEERE VFQKANHQNK LLKQQDNTGL HITIKVSAEM RKGCDFDVFA LVTNSTSVDK KCRLVFASRA VAYDGTIGQE CGFKDLLNVE LPPGGERKVP LRLNYSKYCN AITQDNLIRL GALLIDYSTR DAILDMRTIV LENPEICIRI LGEPKVNRRL AAEVTLQNPL SEPLEACCFS IEGANLTGNK IPTRVEPGQE VKAKIYFTPT HCGVRKLLVD FNSDKLGHVK GFRNVIIGK //