ID   G3RCE0_GORGO            Unreviewed;       687 AA.
AC   G3RCE0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 78.
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};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000013165.2, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000013165.2, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000013165.2, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000013165.2}
RP   IDENTIFICATION.
RG   Ensembl;
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; CABD030116762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_018872459.1; XM_019016914.1.
DR   RefSeq; XP_018872460.1; XM_019016915.1.
DR   RefSeq; XP_018872461.1; XM_019016916.1.
DR   AlphaFoldDB; G3RCE0; -.
DR   STRING; 9593.ENSGGOP00000013165; -.
DR   Ensembl; ENSGGOT00000013545.3; ENSGGOP00000013165.2; ENSGGOG00000013498.3.
DR   GeneID; 101154327; -.
DR   KEGG; ggo:101154327; -.
DR   CTD; 7052; -.
DR   eggNOG; ENOG502QUSX; Eukaryota.
DR   GeneTree; ENSGT01050000244866; -.
DR   HOGENOM; CLU_013435_1_0_1; -.
DR   InParanoid; G3RCE0; -.
DR   OMA; CTVGPGE; -.
DR   OrthoDB; 5344745at2759; -.
DR   TreeFam; TF324278; -.
DR   Proteomes; UP000001519; Chromosome 20.
DR   Bgee; ENSGGOG00000013498; Expressed in heart and 6 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:GOC.
DR   GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0000786; C:nucleosome; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0120297; F:histone dopaminyltransferase activity; IEA:Ensembl.
DR   GO; GO:0120295; F:histone serotonyltransferase activity; IEA:Ensembl.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0120299; F:peptide histaminyltransferase activity; IEA:Ensembl.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IBA:GO_Central.
DR   GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:Ensembl.
DR   GO; GO:0043277; P:apoptotic cell clearance; IEA:Ensembl.
DR   GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl.
DR   GO; GO:0071314; P:cellular response to cocaine; IEA:Ensembl.
DR   GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
DR   GO; GO:1904015; P:cellular response to serotonin; IEA:Ensembl.
DR   GO; GO:0014046; P:dopamine secretion; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
DR   GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:2000425; P:regulation of apoptotic cell clearance; IEA:Ensembl.
DR   GO; GO:0060662; P:salivary gland cavitation; IEA:Ensembl.
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   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:UP000001519};
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         447
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         452
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   687 AA;  77383 MW;  82AC9733BDA0EEA3 CRC64;
     MAEELVLERC DLELETNGRD HHTADLCREK LVVRRGQPFW LTLHFEGRNY EASVDSLTFS
     VVTGPAPSQE AGTKARFPLR DAVEEGDWTA TVVDQQDCTL SLQLTTPANA PIGLYRLSLE
     ASTGYQGSSF VLGHFILLFN AWCPADAVYL DLEEERQEYV LTQQGFIYQG SAKFIKNIPW
     NFGQFEDGIL DICLILLDVN PKFLKNAGRD CSRRSSPVYV GRVVSGMVNC NDDQGVLLGR
     WDNNYGDGIS PMSWIGSVDI LRRWKNHGCQ RVKYGQCWVF AAVACTVLRC LGIPTRVVTN
     YNSAHDQNSN LLIEYFRNEF GEIQGDKSEM IWNFHCWVES WMTRPDLQPG YEGWQALDPT
     PQEKSEGTYC CGPVPVRAIK EGDLSTKYDA PFVFAEVNAD VVDWIQQDDG SVHKSINRSL
     IVGLKISTKS VGRDEREDIT HTYKYPEGSS EEREAFTRAN HLNKLAEKEE TGMAMRIRVG
     QSMNMGSDFD VFAHITNNTA EEYVCRLLLC ARTVSYNGIL GPECGTKYLL NLNLEPFSEK
     SIPLCILYEK YRDCLTESNL IKVRALLVEP VINSYLLAER DLYLENPEIK IRILGEPKQK
     RKLVAEVSLQ NPLPVALEGC TFTVEGAGLT EEQKTVEIPD PVEAGEEVKV RMDLLPLHMG
     LHKLVVNFES DKLKAVKGFR NVIIGPA
//