A0A091IWI6 · A0A091IWI6_CALAN
- ProteinProtein-glutamine gamma-glutamyltransferase 2
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids685 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
Catalytic activity
- L-glutaminyl-[protein] + (R)-noradrenaline = 5-(R)-noradrenalinyl-L-glutamyl-[protein] + NH4+This reaction proceeds in the forward direction.
- L-glutaminyl-[protein] + serotonin = 5-serotonyl-L-glutamyl-[protein] + NH4+This reaction proceeds in the forward direction.
- L-glutaminyl-[protein] + dopamine = 5-dopaminyl-L-glutamyl-[protein] + NH4+This reaction proceeds in the forward direction.
- L-glutaminyl-[protein] + histamine = 5-histaminyl-L-glutamyl-[protein] + NH4+This reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 Ca2+ ion per subunit.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 275 | |||||
Sequence: C | ||||||
Active site | 333 | |||||
Sequence: H | ||||||
Active site | 356 | |||||
Sequence: D | ||||||
Binding site | 396 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 398 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 444 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 449 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | cytosol | |
Cellular Component | extracellular region | |
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Molecular Function | GTP binding | |
Molecular Function | metal ion binding | |
Molecular Function | peptidase activity | |
Molecular Function | protein-glutamine gamma-glutamyltransferase activity | |
Biological Process | peptide cross-linking | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein-glutamine gamma-glutamyltransferase 2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Strisores > Apodiformes > Trochilidae > Calypte
Accessions
- Primary accessionA0A091IWI6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 267-359 | Transglutaminase-like | ||||
Sequence: CQPVKYGQCWVFAAVACTVMRCLGIPSRVVTNYNSAHDTNGNLIIDRYLSETGEEDRRSRDMIWNFHCWVESWMARPDLAPGYDGWQALDPTP |
Sequence similarities
Belongs to the transglutaminase superfamily. Transglutaminase family.
Family and domain databases
Sequence
- Sequence statusFragment
- Length685
- Mass (Da)77,215
- Last updated2014-11-26 v1
- Checksum1467D3CB6F1E162B
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: E | ||||||
Non-terminal residue | 685 | |||||
Sequence: P |
Keywords
- Technical term