| IED ID | IndEnz0002012472 |
| Enzyme Type ID | protease012472 |
| Protein Name |
Protein-glutamine gamma-glutamyltransferase E EC 2.3.2.13 Transglutaminase E TG E TGE TGase E Transglutaminase-3 TGase-3 Cleaved into: Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain; Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain |
| Gene Name | Tgm3 Tgase3 |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MSALEVQNINWQMPMNRRAHHTDKFSSQDFIVRRGQPWEVILLCNRSLESGDNLNFIVSTGPQPSESARTKAVFSISGRNTSGWSAALKASNGNNLFIAIASPVSAPIGLYTLNVEVSSKGRVSSVKLGTFTVLFNPWQQGDDVFMSNHAERQEYVEEDSGIIYVGSTNRIGMVGWNFGQFEEDILSISLSILDRSLNFRRDPATDVARRNDPKYVCRVLSAMINANDDSGVLSGNWSGNYSGGVDPRTWNGSVEILKNWKKSGFRPVQFGQCWVFAGTLNTVLRCLGVPSRVITNFNSAHDTDRNLSVDVYYDAMGNPLEKGSDSVWNFHVWNEGWFVRTDLGPSYNGWQVLDATPQERSQGVFQCGPASVNAIKDGEVDQNFDMIFIFAEVNADRITWIYNNRDGSQKQNSVDTYSIGKYISTKAVGSNSRMDVTIKYKHPEGSKEERQVQQKAMNKLKPNASFGATSSRGPQGEEKEPSISGKFKVTGVLAVGKEVSLALILKNTTSDRKTVTTNMTAWTIVYNGTLVHEVWKDSATISLDPEEEIQYPVKIAYSQYDRYLKADNMIRITAVCKVPDEAEVVVERDVILDNPTLTLEVLDQAQLRKPVVVQMLFSNPLDEPVKNCVLMVEGSGLLRGSLKIDVPALRPKEKSRVRFEIFPTRIGIKQLLADFSCNKFPAIKAMLVIEVSE |
| Enzyme Length | 693 |
| Uniprot Accession Number | D4A5U3 |
| Absorption | |
| Active Site | ACT_SITE 273; /evidence=ECO:0000255|PROSITE-ProRule:PRU10024; ACT_SITE 331; /evidence=ECO:0000255|PROSITE-ProRule:PRU10024; ACT_SITE 354; /evidence=ECO:0000255|PROSITE-ProRule:PRU10024 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011, ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence={ECO:0000250|UniProtKB:Q08188, ECO:0000255|PROSITE-ProRule:PRU10024}; |
| DNA Binding | |
| EC Number | 2.3.2.13 |
| Enzyme Function | FUNCTION: Catalyzes the calcium-dependent formation of isopeptide cross-links between glutamine and lysine residues in various proteins, as well as the conjugation of polyamines to proteins. Involved in the formation of the cornified envelope (CE), a specialized component consisting of covalent cross-links of proteins beneath the plasma membrane of terminally differentiated keratinocytes. Catalyzes small proline-rich proteins and LOR cross-linking to form small interchain oligomers, which are further cross-linked by TGM1 onto the growing CE scaffold. In hair follicles, involved in cross-linking structural proteins to hardening the inner root sheath (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Compositional bias (1); Metal binding (13); Modified residue (2); Region (1); Site (1) |
| Keywords | Acyltransferase;Calcium;Cytoplasm;Keratinization;Metal-binding;Phosphoprotein;Reference proteome;Transferase;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q08188}. |
| Modified Residue | MOD_RES 111; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:Q08188; MOD_RES 112; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q08188 |
| Post Translational Modification | PTM: Activated by proteolytic processing. In vitro activation is commonly achieved by cleavage with dispase, a neutral bacterial protease. Physiological activation may be catalyzed by CTSL and, to a lesser extent, by CTSS (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 77,230 |
| Kinetics | |
| Metal Binding | METAL 222; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 225; /note=Calcium 1; /evidence=ECO:0000250; METAL 227; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 228; /note=Calcium 1; /evidence=ECO:0000250; METAL 302; /note=Calcium 2; /evidence=ECO:0000250; METAL 304; /note=Calcium 2; /evidence=ECO:0000250; METAL 306; /note=Calcium 2; /evidence=ECO:0000250; METAL 308; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 325; /note=Calcium 2; /evidence=ECO:0000250; METAL 394; /note=Calcium 3; /evidence=ECO:0000250; METAL 416; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 444; /note=Calcium 3; /evidence=ECO:0000250; METAL 449; /note=Calcium 3; /evidence=ECO:0000250 |
| Rhea ID | RHEA:54816 |
| Cross Reference Brenda |