Gars1
entrez
353172
canonical
uniprot
Q9CZD3
canonical
ensembl
ENSMUSG00000029777
resolver
ensp
ENSMUSP00000003572
resolver
enst
ENSMUST00000003572
resolver
genesymbol
Gars1
resolver
genesymbol_syn
Gars
resolver
uniprot
Q3TMM4
resolver
uniprot
Q3UK01
resolver
uniprot
Q8VC67
resolver
uniprot_entry
GARS_MOUSE
resolver
uniprot_sec
Q3TMM4
resolver
uniprot_sec
Q3UK01
resolver
uniprot_sec
Q8VC67
resolver
amino_acid_sequence
MPCLLPSLLRATRAALPLLSPPRVVAASASQRLLSAPAQPAASRSSMDSAEELLAPLRLAVRQQGDFVRKLKEDKAPQVDVDRAVAELKARKRVLEAKELALQPKDDIVDRAKMEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQAWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKFADFMVKDVKNGECFRADHLLKAHLQKLMSDKKCSAEKKSEMESVLAQLDNYGQQELADLFVNYNVKSPTTGNDLSPPVPFNLMFQTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPTEKDHPKFQSVADLCLYLYSAKAQVTGQSARKMRLGDAVEQGVINNSVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPNKGAVGKAYKKDAKLVLEYLSACDECYISEMELLLSEKGEFTIETEGKTFQLTKDMVSVKRFQKTLHVEEVVPSVIEPSFGLGRIMYTILEHTFHVREGDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRNGVSHKVDDSSGSIGRRYARTDEIGVAFGITIDFDTVNKTPHTATLRDRDSMRQIRAEVSELPNVVRDLANGNITWADVEARYPLFEGQETGKKETVEE
uniprot
proteins
disease_involvement
DISEASE: Note=Mice (Nmf249) heterozygous for the P278YK variant are used a model for human Charcot-Marie-Tooth 2D (CMT2D), which is caused by dominant GARS mutations. They exhibit reduced amplitudes of muscle compound action potentials and a large reduction in sciatic nerve conduction velocity in the absence of demyelination or remyelination, resulting from an age-related decrease in the number of large myelinated motor and sensory axons. The loss of myelinated axons is length-dependent, and there is a length- and time-dependent decrease in motor innervation of distal versus proximal muscles. Most of the axonal loss occurs by 1 month of age and mice that survive this period can be long-lived. At the molecular level, the P278YK mutation creates a neomorphic binding activity leading to the interaction of the variant with NRP1. This interaction competes out VEGFA binding and inhibits VEGFA-NRP1 signaling which is essential for motor neuron survival. VEGFA, but not GDNF treatment significantly ameliorates the loss of motor function in mutant mice. {ECO:0000269|PubMed:16982418}.
uniprot
proteins
ec_number
2.7.7.-
uniprot
proteins
ec_number
6.1.1.14
uniprot
proteins
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. {ECO:0000250|UniProtKB:P41250}.
uniprot
proteins
mass_dalton
81878
uniprot
proteins
protein_family
Class-II aminoacyl-tRNA synthetase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16982418
uniprot
proteins
pubmed
17947660
uniprot
proteins
pubmed
18614015
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
26503042
uniprot
proteins
pubmed
26789244
uniprot
proteins
sequence_length
729
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41250}. Mitochondrion {ECO:0000269|PubMed:18614015}. Cell projection, axon {ECO:0000250|UniProtKB:P41250}. Secreted {ECO:0000269|PubMed:26503042}. Secreted, extracellular exosome {ECO:0000305|PubMed:26503042}. 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). {ECO:0000250|UniProtKB:P41250, ECO:0000269|PubMed:26503042}.
uniprot
proteins