Reviewed,
UniProtKB/Swiss-Prot P51176 (TGM2_BOVIN)
Last modified
January 19, 2010.
Version 83.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Protein-glutamine gamma-glutamyltransferase 2 EC=2.3.2.13 Alternative name(s): Tissue transglutaminase TGase C Short name=TGC Short name=TG(C) Transglutaminase-2 | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 687 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. |
| Catalytic activity | Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3. |
| Cofactor | Binds 1 calcium ion per subunit By similarity. |
| Subunit structure | Monomer By similarity. |
| Tissue specificity | Highest levels are detected in the lung. Lower levels are found in the liver, spleen and heart, but not in the brain. |
| Induction | By retinoic acid. |
| Sequence similarities | Belongs to the transglutaminase superfamily. Transglutaminase family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Calcium Metal-binding |
| Molecular function | Acyltransferase Transferase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | peptide cross-linking Inferred from electronic annotation. Source: InterPro |
| Molecular function | acyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW calcium ion bindingInferred from electronic annotation. Source: UniProtKB-KW protein-glutamine gamma-glutamyltransferase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 687 | 686 | Protein-glutamine gamma-glutamyltransferase 2 | PRO_0000213705 | |||||
Sites | |||||||||
| Active site | 277 | 1 | By similarity | ||||||
| Active site | 335 | 1 | By similarity | ||||||
| Active site | 358 | 1 | By similarity | ||||||
| Metal binding | 398 | 1 | Calcium By similarity | ||||||
| Metal binding | 400 | 1 | Calcium By similarity | ||||||
| Metal binding | 447 | 1 | Calcium By similarity | ||||||
| Metal binding | 452 | 1 | Calcium By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Modified residue | 219 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 369 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 427 | 1 | Phosphoserine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 638 | 1 | V → I in AAI03291. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and sequence analysis of cDNA clones for bovine aortic-endothelial-cell transglutaminase." Nakanishi K., Nara K., Hagiwara H., Aoyama Y., Ueno H., Hirose S. Eur. J. Biochem. 202:15-21(1991) [PubMed: 1682150] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 79-95; 157-166; 242-251 AND 581-587. Tissue: Artery. |
| [2] | NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Uterus. |
| [3] | "Retinol-induced morphological changes of cultured bovine endothelial cells are accompanied by a marked increase in transglutaminase." Nara K., Nakanishi K., Hagiwara H., Wakita K., Kojima S., Hirose S. J. Biol. Chem. 264:19308-19312(1989) [PubMed: 2572599] [Abstract] Cited for: PROTEIN SEQUENCE OF 79-95; 157-166 AND 242-251. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X60686 mRNA. Translation: CAA43097.1. BC103290 mRNA. Translation: AAI03291.1. |
| IPI | IPI00703915. |
| PIR | S19680. |
| RefSeq | NP_803473.1. |
| UniGene | Bt.5401 |
3D structure databases | |
| SMR | P51176. Positions 15-687. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P51176. |
Genome annotation databases | |
| Ensembl | ENSBTAT00000021569; ENSBTAP00000021569; ENSBTAG00000016208; Bos taurus. [Genome view] |
| GeneID | 281528. |
| KEGG | bta:281528. |
Organism-specific databases | |
| CTD | 281528. |
Phylogenomic databases | |
| eggNOG | maNOG06398. |
| HOVERGEN | P51176. |
| InParanoid | P51176. |
Enzyme and pathway databases | |
| BRENDA | 2.3.2.13. 251. |
Family and domain databases | |
| InterPro | IPR008957. Fibronectin_typ-III-like_fold. IPR013783. Ig-like_fold. IPR014756. Ig_E-set. IPR002931. Transglutaminase-like. IPR008958. Transglutaminase_C. IPR013808. Transglutaminase_CS. IPR001102. Transglutaminase_N. [Graphical view] |
| Gene3D | G3DSA:2.60.40.30. FN_III-like. 1 hit. G3DSA:2.60.40.10. Ig-like_fold. 1 hit. |
| Pfam | PF00927. Transglut_C. 2 hits. PF01841. Transglut_core. 1 hit. PF00868. Transglut_N. 1 hit. [Graphical view] |
| SMART | SM00460. TGc. 1 hit. [Graphical view] |
| PROSITE | PS00547. TRANSGLUTAMINASES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TGM2_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P51176 Secondary accession number(s): Q3ZBH7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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