ID   B3DM72_XENTR            Unreviewed;       691 AA.
AC   B3DM72;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=tgm2 {ECO:0000313|RefSeq:NP_001123852.1,
GN   ECO:0000313|Xenbase:XB-GENE-5940894};
GN   Synonyms=g-alpha-h {ECO:0000313|RefSeq:NP_001123852.1}, gnah
GN   {ECO:0000313|RefSeq:NP_001123852.1}, LOC100170618
GN   {ECO:0000313|EMBL:AAI67727.1}, tg2
GN   {ECO:0000313|RefSeq:NP_001123852.1}, tgc
GN   {ECO:0000313|RefSeq:NP_001123852.1}, tgm2-a
GN   {ECO:0000313|RefSeq:NP_001123852.1}, tgm2-b
GN   {ECO:0000313|RefSeq:NP_001123852.1};
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|RefSeq:NP_001123852.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {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.
RN   [3] {ECO:0000313|RefSeq:NP_001123852.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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}.
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DR   EMBL; BC167727; AAI67727.1; -; mRNA.
DR   RefSeq; NP_001123852.1; NM_001130380.1.
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; 5344745at2759; -.
DR   Proteomes; UP000008143; Chromosome 10.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000008143};
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   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
//