ID   Q6INH7_XENLA            Unreviewed;       691 AA.
AC   Q6INH7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 101.
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.L {ECO:0000313|RefSeq:NP_001085410.1,
GN   ECO:0000313|Xenbase:XB-GENE-982477};
GN   Synonyms=g-alpha-h {ECO:0000313|RefSeq:NP_001085410.1}, gnah
GN   {ECO:0000313|RefSeq:NP_001085410.1}, MGC82568
GN   {ECO:0000313|EMBL:AAH72304.1}, tg2
GN   {ECO:0000313|RefSeq:NP_001085410.1}, tgc
GN   {ECO:0000313|RefSeq:NP_001085410.1}, tgm2
GN   {ECO:0000313|RefSeq:NP_001085410.1}, tgm2-a
GN   {ECO:0000313|RefSeq:NP_001085410.1}, tgm2-b
GN   {ECO:0000313|RefSeq:NP_001085410.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH72304.1};
RN   [1] {ECO:0000313|RefSeq:NP_001085410.1}
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:AAH72304.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen {ECO:0000313|EMBL:AAH72304.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001085410.1}
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; BC072304; AAH72304.1; -; mRNA.
DR   RefSeq; NP_001085410.1; NM_001091941.1.
DR   DNASU; 443836; -.
DR   GeneID; 443836; -.
DR   KEGG; xla:443836; -.
DR   AGR; Xenbase:XB-GENE-982477; -.
DR   CTD; 443836; -.
DR   Xenbase; XB-GENE-982477; tgm2.L.
DR   OrthoDB; 5344745at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 443836; Expressed in spleen and 17 other cell types or tissues.
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:UP000186698};
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;  77728 MW;  3C11DA1D157B031A CRC64;
     MAEELFLESF DLDCSGNNRS HRTAEASCER LIVRRGQPFQ ITLNFAPRGY EEGVDRLSLN
     AITGPCPSEE SGTSNNFPVS DALQDGAWSA AINSTDGGTV ILSITSPPNA RIGYYNLSLE
     TSTEYQGSSF QLGSFTLLFN PWCPEDSVYL EKKDERKEYV LCQHGIIFQG TKNSTDHVPW
     NFGQFEDGIL EIALQILDTS PKFLNDSNRD CSRRNDPVYI SRVISAMVNC NDDKGVLYGR
     WDNKYDDGVS PMFWMGSVAI LRRWKKFGCQ AVKYGQCWVF AAVACTVLRC LGIPARVITN
     YNSAHDTNSN LLIEQYLDEH GKRQSKQKDL IWNYHCWVEV WMARPDLGED YNGWQVVDPT
     PQEKSEGTYC CGPAPVNAVK EGDLNVKYDV PFVFAEVNAD VMYYVQQNDG SVKKTHSISL
     VGQNISTKAI GKDEREDITH NYKYPEGSQD ERRVFEKANK QFVEAEEEEE KPLDVTIKIK
     VSEGMNIGSD FDVFAVITNN TEDEKKCRLM FCARTTSYNG EVGPECGMKD LLNLTLPPQE
     EKRVPLHIQY EKYGPTITEN NMIKLVAMLY DYSSKDIILA MRDIHIKNPS IKIKILGEPK
     QKRKLVAEIS LKNPLAEPLT GCCFTVEGAG LTAEQLVQTL DCPIEPGQEA KVRVDLMPQL
     PGKLSLVVDF ESDLLKAVKG YRNIIIAPLP K
//