Reviewed,
UniProtKB/Swiss-Prot P22758 (TGM1_RABIT)
Last modified
June 16, 2009.
Version 75.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Protein-glutamine gamma-glutamyltransferase K EC=2.3.2.13 Alternative name(s): Transglutaminase K Short name=TGase K Short name=TGK Short name=TG(K) Transglutaminase-1 Epidermal TGase | ||
| Gene names |
| ||
| Organism | Oryctolagus cuniculus (Rabbit) | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 836 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Responsible for cross-linking epidermal proteins during formation of the stratum corneum. |
| Catalytic activity | Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3. |
| Cofactor | Binds 1 calcium ion per subunit By similarity. |
| Enzyme regulation | Inhibited by retinoic acid, but phorbol ester treatment activates it. |
| Subcellular location | |
| Sequence similarities | Belongs to the transglutaminase superfamily. Transglutaminase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Keratinization |
| Cellular component | Membrane |
| Ligand | Calcium Metal-binding |
| Molecular function | Acyltransferase Transferase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | keratinization Inferred from electronic annotation. Source: UniProtKB-KW peptide cross-linkingInferred from electronic annotation. Source: InterPro |
| Cellular component | membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 836 | 836 | Protein-glutamine gamma-glutamyltransferase K | PRO_0000213703 | |||||
Sites | |||||||||
| Active site | 397 | 1 | By similarity | ||||||
| Active site | 456 | 1 | By similarity | ||||||
| Active site | 479 | 1 | By similarity | ||||||
| Metal binding | 519 | 1 | Calcium By similarity | ||||||
| Metal binding | 521 | 1 | Calcium By similarity | ||||||
| Metal binding | 568 | 1 | Calcium By similarity | ||||||
| Metal binding | 573 | 1 | Calcium By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 98 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 112 | 1 | Phosphoserine By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Regulation of transglutaminase type I expression in squamous differentiating rabbit tracheal epithelial cells and human epidermal keratinocytes: effects of retinoic acid and phorbol esters." Saunders N.A., Bernacki S.H., Vollberg T.M., Jetten A.M. Mol. Endocrinol. 7:387-398(1993) [PubMed: 8097865] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: New Zealand white. Tissue: Tracheobronchial epithelium. |
| [2] | "Regulation of type I (epidermal) transglutaminase mRNA levels during squamous differentiation: down regulation by retinoids." Floyd E.E., Jetten A.M. Mol. Cell. Biol. 9:4846-4851(1989) [PubMed: 2574824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 368-749. |
| [3] | "The complete amino acid sequence of the human transglutaminase K enzyme deduced from the nucleic acid sequences of cDNA clones." Kim H.C., Idler W.W., Kim I.-G., Han J.H., Chung S.-I., Steinert P.M. J. Biol. Chem. 266:536-539(1991) [PubMed: 1670769] [Abstract] Cited for: SEQUENCE REVISION. |
Cross-references
Sequence databases | |
|---|---|
| L10714 mRNA. No translation available. M30468 mRNA. Translation: AAA31475.1. | |
| PIR | A33477. A54269. |
| UniGene | Ocu.1972 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1KV3 based on UniProtKB P21980. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P22758. |
Enzyme and pathway databases | |
| BRENDA | 2.3.2.13. 255. |
Family and domain databases | |
| InterPro | IPR008957. Fibronectin_typ-III-like_fold. IPR013783. Ig-like_fold. 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 | TGM1_RABIT | ||||||||
| Accession | Primary (citable) accession number: P22758 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


