P23606 · TGM1_RAT
- ProteinProtein-glutamine gamma-glutamyltransferase K
- GeneTgm1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids824 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
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. Involved in cell proliferation (By similarity).
Catalytic activity
- L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-lysyl-N6-5-L-glutamyl-[protein] + NH4+
Cofactor
Note: Binds 1 Ca2+ ion per subunit.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 385 | |||||
Sequence: C | ||||||
Active site | 444 | |||||
Sequence: H | ||||||
Active site | 467 | |||||
Sequence: D | ||||||
Binding site | 507 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 509 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 556 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 561 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | adherens junction | |
Cellular Component | membrane | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | protein-glutamine gamma-glutamyltransferase activity | |
Biological Process | animal organ morphogenesis | |
Biological Process | keratinization | |
Biological Process | keratinocyte differentiation | |
Biological Process | positive regulation of cell cycle | |
Biological Process | positive regulation of keratinocyte proliferation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein-glutamine gamma-glutamyltransferase K
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP23606
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000213704 | 1-824 | Protein-glutamine gamma-glutamyltransferase K | |||
Sequence: MEGPRSDVGRWGRSPWQPTTPSPEPEPEPEPDRSSRSRRGGGRSFWARCCGCCSCGNRADDDWGPEPSGSRSRGTSSRGGGSRGGDSRGRDSRGGRRPESRGSGVNAAGDGTIREGMLVVNGVDLLCSRSDQNRREHHTDEFEYDELILRRGQPFHIILFLNREYESSDRIALELLIGNNPEVGKGTHVIIPVGKGGSGGWKAQVTKTNGHNLTLRVHTSPNAIIGKFQFTVRTRSEAGEFQLPFDPRNEIYILFNPWCPEDIVYVDHEDWRQEYVLNESGRIYYGTEAQIGERTWNYGQFDHGVLDACLYILDRRGMPYGGRGDPVSVSRVVSAMVNSLDDNGVLIGNWTGDYSRGTNPSAWVGSVEILLSYLRTGYSVPYGQCWVFAGVTTTVLRCLGLATRTVTNFNSAHDTDTSLTMDIYFDENMKPLEHLNHDSVWNFHVWNDCWMKRPDLPSGFDGWQVVDATPQETSSGIFCCGPCSVESIKNGLVYMKYDTPFIFAEVNSDKVYWQRQDDGSFKIVYVEEKAIGTLIVTKAINSNMREDITHIYKHPEGSEAERKAVEKAAAHGSKPNVYATRDSAEDVAMQVEAQDAVMGQDLTVSVVLTNRGSSRRTVKLHLYLCVTYYTGVSGPTFKETKKEVVLAPGASDTVAMPVAYKEYKPHLVDQGAMLLNVSGHVKESGQVLAKQHTFRLRTPDLSLTLLGAAVVGQECEVQIVFKNPLPITLTNVVFRLEGSGLQRPKVLNVGDIGGNETVTLRQTFVPVRPGPRQLIASLDSPQLSQVHGVIQVDVAPSSGGRGFSEAVGDSRSGENIPMAFRGGA | ||||||
Modified residue | 20 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 22 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 70 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 92 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 100 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 103 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 812 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Palmitoylated.
The membrane anchorage region possesses a cluster of five cysteines within which fatty acid(s) may become thioester-linked. It is subject to phorbol ester-stimulated phosphorylation and is hypersensitive to proteolysis, which releases the enzyme in a soluble form.
Tyrosine-phosphorylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-44 | Disordered | ||||
Sequence: MEGPRSDVGRWGRSPWQPTTPSPEPEPEPEPDRSSRSRRGGGRS | ||||||
Region | 61-110 | Disordered | ||||
Sequence: DDWGPEPSGSRSRGTSSRGGGSRGGDSRGRDSRGGRRPESRGSGVNAAGD | ||||||
Compositional bias | 84-98 | Basic and acidic residues | ||||
Sequence: GGDSRGRDSRGGRRP | ||||||
Region | 801-824 | Disordered | ||||
Sequence: RGFSEAVGDSRSGENIPMAFRGGA |
Sequence similarities
Belongs to the transglutaminase superfamily. Transglutaminase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length824
- Mass (Da)90,770
- Last updated1991-11-01 v1
- ChecksumA7D81C148CEFD938
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I5ZX14 | A0A8I5ZX14_RAT | Tgm1 | 835 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 84-98 | Basic and acidic residues | ||||
Sequence: GGDSRGRDSRGGRRP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M57263 EMBL· GenBank· DDBJ | AAA63495.1 EMBL· GenBank· DDBJ | mRNA | ||
BC097305 EMBL· GenBank· DDBJ | AAH97305.1 EMBL· GenBank· DDBJ | mRNA |