ID   Q1ECX3_DANRE            Unreviewed;       679 AA.
AC   Q1ECX3; A0A8M1PHE7; F1R7N2;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   04-NOV-2026, entry version 135.
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|EMBL:AAI17636.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-030131-2576};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI17636.1};
RN   [1] {ECO:0000313|EMBL:AAI17636.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Whole {ECO:0000313|EMBL:AAI17636.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2006) 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}.
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DR   EMBL; BC117635; AAI17636.1; -; mRNA.
DR   RefSeq; NP_997821.2; NM_212656.2.
DR   SMR; Q1ECX3; -.
DR   PeptideAtlas; Q1ECX3; -.
DR   GeneID; 323856; -.
DR   KEGG; dre:323856; -.
DR   CTD; 323856; -.
DR   AGR; ZFIN:ZDB-GENE-030131-2576; -.
DR   ZFIN; ZDB-GENE-030131-2576; tgm2b.
DR   eggNOG; ENOG502QUSX; Eukaryota.
DR   GeneTree; ENSGT01050000244866; -.
DR   HOGENOM; CLU_013435_1_0_1; -.
DR   OrthoDB; 437511at2759; -.
DR   BRENDA; 2.3.2.13; 928.
DR   Bgee; ENSDARG00000074094; Expressed in spleen and 23 other cell types or tissues.
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; 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   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:0007399; P:nervous system development; IEA:UniProtKB-ARBA.
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   AlphaFoldDB; Q1ECX3; -.
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          260..353
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   ACT_SITE        268
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        327
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        350
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         390
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         392
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         438
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"
SQ   SEQUENCE   679 AA;  75773 MW;  CA43F4888970F033 CRC64;
     MALDIGSWDL ACKFNNTDHH TELNGTDRLI VRRGQAFTIN LQLNSGSYQP GYSQINITAE
     TGPDPQQQYG TRAVFSLSSE VDSSCWSAAV SSPPGESVCL SICAAPDAPI GHYTLTLDER
     IQIQFILLFN PWCPLDVVYM DNEEKLAEYV LAQDGIIFRG DAGYPVPLAW NFGQFEEGIL
     DACFRILDMN PKHRRNPAKD CSGRRNVIYV TRVLSAMINS NDQDSGVLEG CWRDTFDGGV
     SPMSWGGSVQ ILRTWDRSSC LPVRYGQCWV FAAVACTVAR AVGIPCRVVT NYYSAHDTNS
     NLLIERYVNE KGEVDHSSTR DMIWNYHCWV ESWMGRSDLP PGFDGWQASD PTPQEKSEGV
     FCCGPVPVRA IKEGELTFKY DAPFVFAEVN ADLVYFLKSK DGSTRKINYD QKVGQKISTK
     SVGRDEREDI THLYKYPEGS ADERRVFEKA NHQNKLLQEK QNTGLNITIK LSSGVRKGCD
     FDVFAIVTNG TAEEKKCRLV FASRAVSYNG VIGRECGFKD LLNVELPPGG ERKVPLRLNY
     SKYCNNLTED NLIRLGALLI DYSTRDAIMA MRDIVLDDPE IKIRILGEPK ENRKLAAELT
     IQNPLPEALQ SCCFTIEGAN LTGGDSITHT LDSSIEPGQE AKAKIYFTPT QSGLRKLLVD
     FNSDKLGHVR GYRNVIIGK
//