Q9CZD3 · GARS_MOUSE
- ProteinGlycine--tRNA ligase
- GeneGars1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids729 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP). Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis.
Catalytic activity
- ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)This reaction proceeds in the forward direction.
- 2 ATP + H+ = diphosphate + P1,P4-bis(5'-adenosyl) tetraphosphateThis reaction proceeds in the forward direction.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 289 | glycine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 321-323 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RNE | ||||||
Binding site | 332-333 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RV | ||||||
Binding site | 340 | glycine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 447-448 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EI | ||||||
Binding site | 566-568 | glycine (UniProtKB | ChEBI) | ||||
Sequence: EPS | ||||||
Binding site | 573 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | mitochondrion | |
Cellular Component | secretory granule | |
Molecular Function | ATP binding | |
Molecular Function | ATP:ATP adenylyltransferase activity | |
Molecular Function | bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity | |
Molecular Function | glycine-tRNA ligase activity | |
Molecular Function | identical protein binding | |
Molecular Function | protein dimerization activity | |
Biological Process | diadenosine tetraphosphate biosynthetic process | |
Biological Process | glycyl-tRNA aminoacylation | |
Biological Process | mitochondrial glycyl-tRNA aminoacylation | |
Biological Process | tRNA aminoacylation for protein translation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGlycine--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9CZD3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with granules in cultured neuron cells (By similarity).
Secreted by motor neuron and differentiated myotube cell lines, but not by undifferentiated myoblasts, possibly through the exosome pathway (PubMed:26503042).
Secreted by motor neuron and differentiated myotube cell lines, but not by undifferentiated myoblasts, possibly through the exosome pathway (PubMed:26503042).
Keywords
- Cellular component
Phenotypes & Variants
Involvement in disease
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 278 | found in Nmf249 mice, a Charcot-Marie-Tooth 2D model; involved in neuromuscular dysfunction; contrary to the wild-type protein, strongly interacts with NRP1 and competes with VEGFA for NRP1-binding; no effect on subcellular location | ||||
Sequence: P → YK |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 41 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-33 | Mitochondrion | ||||
Sequence: MPCLLPSLLRATRAALPLLSPPRVVAASASQRL | ||||||
Chain | PRO_0000072999 | 34-729 | Glycine--tRNA ligase | |||
Sequence: LSAPAQPAASRSSMDSAEELLAPLRLAVRQQGDFVRKLKEDKAPQVDVDRAVAELKARKRVLEAKELALQPKDDIVDRAKMEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQAWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKFADFMVKDVKNGECFRADHLLKAHLQKLMSDKKCSAEKKSEMESVLAQLDNYGQQELADLFVNYNVKSPTTGNDLSPPVPFNLMFQTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPTEKDHPKFQSVADLCLYLYSAKAQVTGQSARKMRLGDAVEQGVINNSVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPNKGAVGKAYKKDAKLVLEYLSACDECYISEMELLLSEKGEFTIETEGKTFQLTKDMVSVKRFQKTLHVEEVVPSVIEPSFGLGRIMYTILEHTFHVREGDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRNGVSHKVDDSSGSIGRRYARTDEIGVAFGITIDFDTVNKTPHTATLRDRDSMRQIRAEVSELPNVVRDLANGNITWADVEARYPLFEGQETGKKETVEE | ||||||
Modified residue | 194 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 443 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 491 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 690 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 726 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q9CZD3 | GARS1 P41250 | 2 | EBI-8321941, EBI-724143 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 53-109 | WHEP-TRS | ||||
Sequence: LLAPLRLAVRQQGDFVRKLKEDKAPQVDVDRAVAELKARKRVLEAKELALQPKDDIV |
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length729
- Mass (Da)81,878
- Last updated2001-06-01 v1
- Checksum596613F746B9C7D0
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 5 | in Ref. 1; BAE38417 | ||||
Sequence: L → V | ||||||
Sequence conflict | 584 | in Ref. 1; BAE27003 | ||||
Sequence: H → N | ||||||
Sequence conflict | 597 | in Ref. 1; BAE27003 | ||||
Sequence: F → L | ||||||
Sequence conflict | 694 | in Ref. 2; AAH21747 | ||||
Sequence: N → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK146238 EMBL· GenBank· DDBJ | BAE27003.1 EMBL· GenBank· DDBJ | mRNA | ||
AK165857 EMBL· GenBank· DDBJ | BAE38417.1 EMBL· GenBank· DDBJ | mRNA | ||
BC021747 EMBL· GenBank· DDBJ | AAH21747.1 EMBL· GenBank· DDBJ | mRNA |