P08587 (TGM2_CAVCU) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 102.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Protein-glutamine gamma-glutamyltransferase 2 EC=2.3.2.13 Alternative name(s): Tissue transglutaminase Transglutaminase C Short name=TG(C) Short name=TGC Short name=TGase C Transglutaminase-2 Short name=TGase-2 | ||
| Gene names |
| ||
| Organism | Cavia cutleri (Guinea pig) | ||
| Taxonomic identifier | 10144 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia![]() |
Protein attributes
| Sequence length | 690 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. |
| Sequence similarities | Belongs to the transglutaminase superfamily. Transglutaminase family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Calcium Metal-binding |
| Molecular function | Acyltransferase Transferase |
| PTM | Acetylation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | peptide cross-linking Inferred from electronic annotation. Source: InterPro |
| Molecular_function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein-glutamine gamma-glutamyltransferase activityInferred from electronic annotation. Source: EC transaminase activityInferred from direct assay PubMed 11723121. Source: MGI |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 Ref.3 | ||||||
| Chain | 2 – 690 | 689 | Protein-glutamine gamma-glutamyltransferase 2 | PRO_0000213706 | |||||
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 | 446 | 1 | Calcium By similarity | ||||||
| Metal binding | 451 | 1 | Calcium By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.3 | ||||||
Experimental info | |||||||||
| Sequence conflict | 2 – 3 | 2 | AE → EA AA sequence Ref.2 | ||||||
| Sequence conflict | 292 | 1 | G → A in BAA00068. Ref.4 | ||||||
| Sequence conflict | 336 – 354 | 19 | CWVES…GYEGW → SLLGGVVDDQAGPGAWVRGV in BAA00068. Ref.4 | ||||||
Sequences
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References
| [1] | "Amino acid sequence of guinea pig liver transglutaminase from its cDNA sequence." Ikura K., Nasu T.-A., Yokota H., Tsuchiya Y., Sasaki R., Chiba H. Biochemistry 27:2898-2905(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | "Structural properties of guinea pig liver transglutaminase." Connellan J.M., Chung S.I., Whetzel N.K., Bradley L.M., Folk J.E. J. Biol. Chem. 246:1093-1098(1971) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5. Tissue: Liver. |
| [3] | "Determination of amino- and carboxyl-terminal sequences of guinea pig liver transglutaminase: evidence for amino-terminal processing." Ikura K., Yokota H., Sasaki R., Chiba H. Biochemistry 28:2344-2348(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8 AND 684-690, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Liver. |
| [4] | "Cloning of cDNA coding for guinea pig liver transglutaminase." Ikura K., Nasu T.-A., Yokota H., Sasaki R., Chiba H. Agric. Biol. Chem. 51:957-961(1987) Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 189-632. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M19646 mRNA. Translation: AAA37056.1. D00114 mRNA. Translation: BAA00068.1. |
| PIR | A29996. |
3D structure databases | |
| ProteinModelPortal | P08587. |
| SMR | P08587. Positions 15-690. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P08587. 2 interactions. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG004342. |
Family and domain databases | |
| Gene3D | 2.60.40.10. 3 hits. |
| InterPro | IPR023608. Gln_gamma-glutamylTfrase_euk. IPR013783. Ig-like_fold. IPR014756. Ig_E-set. IPR002931. Transglutaminase-like. IPR008958. Transglutaminase_C. IPR013808. Transglutaminase_CS. IPR001102. Transglutaminase_N. [Graphical view] |
| PANTHER | PTHR11590. PTHR11590. 1 hit. |
| Pfam | PF00927. Transglut_C. 2 hits. PF01841. Transglut_core. 1 hit. PF00868. Transglut_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000459. TGM_EBP42. 1 hit. |
| SMART | SM00460. TGc. 1 hit. [Graphical view] |
| SUPFAM | SSF81296. Ig_E-set. 1 hit. SSF49309. Transglut_C. 2 hits. |
| PROSITE | PS00547. TRANSGLUTAMINASES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TGM2_CAVCU | ||||||||
| Accession | Primary (citable) accession number: P08587 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
