ID L5JYM2_PTEAL Unreviewed; 687 AA.
AC L5JYM2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 ORFNames=PAL_GLEAN10024319 {ECO:0000313|EMBL:ELK04177.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK04177.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB031072; ELK04177.1; -; Genomic_DNA.
DR RefSeq; XP_006921867.1; XM_006921805.2.
DR AlphaFoldDB; L5JYM2; -.
DR STRING; 9402.L5JYM2; -.
DR GeneID; 102892954; -.
DR KEGG; pale:102892954; -.
DR CTD; 7052; -.
DR eggNOG; ENOG502QUSX; Eukaryota.
DR InParanoid; L5JYM2; -.
DR OrthoDB; 5344745at2759; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
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 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:UP000010552};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ELK04177.1}.
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; 77378 MW; 42D66C434084DEC7 CRC64;
MAEDLVLERC DLELEANGRD HHTADLCRER LVVRRGQPFR LTLYFEGRNY EAGVDSLTFS
VVTGPAPSKE AGTKARFPLS DAVEEGAWTA SVVDQQDNAL SLQLSTPAHA PIGLYRLSLE
ASTGYQGSSF VLGHFTLLFN TWCPEDAVYL DSDEERREYV LTQQGFIYQG SSKFINSIPW
NFGQFEDGIL DICLMLLDIN PKFLKDSGRD CSRRSSPVYV GRVVSGMVNC NDDQGVLMGR
WDNNYKDGIS PMFWIGSVDI LRRWKNYGCQ NVKYGQCWVF AAVACTVLRC LGIPTRVVTN
YNSAHDQNSN LLIEYFRNEF GEIQGDKSEM IWNFHCWVES WMTRPDLQPG YEGWQALDPT
PQEKSEGTYC CGPVPVRAIK EGDLSTKYDA PFVYAEVNAD VVDWIRQDDG SMHKSINHSL
VVGLKISTKS VGRDEREDIT HTYKYPEGSS EEREAFKRAN HMNKLADKEE TGVAMRIRVG
ESMKMGSDFD VFAHITNNTA EDHTCRLLLR ACTVSYNGIL GPQCGTKELL DLPMEPFSEK
SIPFRILYEK YCDCLTESNL IKVRGLLVEP AANSYLLAER DIYLENPEIK IRILGEPKQN
RKLVAEVSLR NPLTVPLEGC IFTVEGAGLT EEQKTVEIPD PVEVGQEAKA RVDLLPLLVG
RHKLVVDFES DKLKAVKGYR NVIIGPP
//
