ID A0A1S3EPX5_DIPOR Unreviewed; 689 AA.
AC A0A1S3EPX5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:XP_012866443.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012866443.1};
RN [1] {ECO:0000313|RefSeq:XP_012866443.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012866443.1};
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 RefSeq; XP_012866443.1; XM_013010989.1.
DR AlphaFoldDB; A0A1S3EPX5; -.
DR STRING; 10020.ENSDORP00000010164; -.
DR GeneID; 105981707; -.
DR KEGG; dord:105981707; -.
DR CTD; 7052; -.
DR InParanoid; A0A1S3EPX5; -.
DR OrthoDB; 5344745at2759; -.
DR Proteomes; UP000081671; Unplaced.
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:UP000081671};
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 689 AA; 77215 MW; DDA6BE2472893EF3 CRC64;
MAQELILERC DLELEANGRD HHTADLCQDR LVVRRGQAFW LTLHFEGRGY EAGVDSLTFS
AVTGPAPSEE AGTKARFPLS DGVGEGGWAA SVADQQDNVL SLHLYTPAEA PIGLYRLSLE
TSTGYQGSSF VLGHFTLLFN AWCPADAVYL NAEAERQEYV LNQQGFIYQG SAKFIKSVPW
NFGQFEDRIL DTCLTLLDVN PKFLKDSSRD CARRSSPIYL GRVVSAMVNC NDDQGVLLGR
WDNNYGDGVS PMSWIGSVDI LRRWKDHGCQ HVKYGQCWVF AAVACTVLRC LGIPTRVVTN
YNSAHDQNSN LLIEYFRNEF GELESNKSEM IWNFHCWVES WMTRPDLEPG YEGWQAIDPT
PQEKSEGTYC CGPVPVRAIK EGDLSTKYDA PFVFAEVNAD VVDWIRQEDG SLHKSVNRSL
VVGLKISTKS VGRDDRQDIT HTYKYPEGSP EEREAFTKAN HLNRLEEKVE VQEGVDMRIR
VGQSMAVGSD FDVFAHITNN ASESRDTRLL LCARIVSYNG VLGPECGTMD PLDLTLEPFC
EKSIPLRILY EKYSDYLTES NLIKVRGLLI EPAANNYLLA ERDLYLENPE IKIRMLGEPK
QNRKLVAEVA LKNPLTVPLL GCIFTVEGAG LIKEQKIVEV PDPVEAGEEV KVRVDLIPFD
MGLHKLVVNF DCDKLKAVKG YRNVIIGPA
//
