Serine–tRNA ligase, mitochondrial

"SARS2" redirects here. For the COVID-19 virus, see Severe acute respiratory syndrome coronavirus 2.

SARS2
Identifiers
Aliases	SARS2, SARS, SARSM, SERS, SYS, SerRS, SerRSmt, mtSerRS, seryl-tRNA synthetase 2, mitochondrial
External IDs	OMIM: 612804; MGI: 1919234; GeneCards: SARS2
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 6.1.1.11 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 19 (human) Band 19q13.2 Start 38,915,266 bp End 38,930,763 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7 B1|7 16.91 cM Start 28,441,417 bp End 28,453,296 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in apex of heart right lobe of thyroid gland right adrenal cortex left lobe of thyroid gland right lobe of liver mucosa of transverse colon left adrenal gland left adrenal cortex pituitary gland primary visual cortex Top expressed in epiblast soleus muscle Gonadal ridge yolk sac embryo muscle of thigh embryo maxillary prominence thoracic diaphragm intercostal muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function aminoacyl-tRNA ligase activity nucleotide binding ligase activity ATP binding serine-tRNA ligase activity RNA binding Cellular component cytoplasm mitochondrial matrix mitochondrion Biological process tRNA aminoacylation for protein translation protein biosynthesis seryl-tRNA aminoacylation selenocysteinyl-tRNA(Sec) biosynthetic process Sources:Amigo / QuickGO
Orthologs Databases NCBI: entry; OMA: entry Species Human Mouse Entrez 54938 71984 Ensembl ENSG00000104835 ENSG00000283104 ENSMUSG00000070699 UniProt Q9NP81 Q9JJL8 RefSeq (mRNA) NM_017827 NM_001145901 NM_023637 RefSeq (protein) NP_001139373 NP_060297 NP_076126 Location (UCSC) Chr 19: 38.92 – 38.93 Mb Chr 7: 28.44 – 28.45 Mb PubMed search
Wikidata
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Serine–tRNA ligase, mitochondrial, also called seryl-tRNA synthetase 2, mitochondrial, is an enzyme that in humans is encoded by the SARS2 gene. Like serine–tRNA ligase, cytoplasmic (SARS1), this enzyme functions as a serine–tRNA ligase, which means it participates in RNA-to-protein translation by attaching the amino acid serine to the corresponding serine transfer RNA (tRNA-Ser).

Medical significance

Pathogenic homozygous mutations in SARS2 are associated with symptoms including premature birth and infant onset kidney failure, called HUPRA syndrome (Hyperuricemia, pulmonary hypertension, renal failure, and alkalosis syndrome).

As with many mutations that affect protein translation, mutations in SARS2 have been shown to cause a collection of diseases, such as hyperuricemia, metabolic alkalosis, pulmonary hypertension, and progressive kidney failure in infancy; together, these conditions are known as HUPRA syndrome.

Some cases of missense mutations in SARS2 have been observed to result in a complete lack of acetylated seryl-tRNA synthetase and a severely reduced amount of non-acetylated enzyme. This results in the ineffective or complete inability of L-serine to be transferred to its cognate tRNA, resulting in incomplete protein translation and folding. The impacts appear to only reach a phenotypic pathology in certain high energy expenditure cells, such as renal cells and lung tissue. It has been suggested that the residual activity of the SARS2 gene allows most other tissues to avoid cytopathic symptoms, however, is unable to protect high-energy requirement cells from damage.

SARS2 mutations resulting in HUPRA syndrome are extremely rare, with less than 1 in 1,000,000 babies born with the condition. A Palestinian community in the Greater Jerusalem region appears to have a much higher incidence of the mutation, potentially due to a common ancestor.

Further reading

• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1) 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Müller T, Deschauer M, Neudecker S, Zierz S (2007). "Late-onset mitochondrial myopathy with dystrophic changes due to a G7497A mutation in the mitochondrial tRNA(Ser(UCN)) gene". Acta Neuropathol. 110 (4): 426–30. doi:10.1007/s00401-005-1063-z. PMID 16133542. S2CID 23568019.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Ihalamulla RL, Liyanage CP, Karunaweera ND (2004). "A simple device to maintain in vitro cultures of Leishmania in tropical countries". Trans. R. Soc. Trop. Med. Hyg. 98 (5): 315–7. doi:10.1016/j.trstmh.2003.10.004. PMID 15109557.
• Gibbons WJ, Yan Q, Li R, et al. (2004). "Genomic organization, expression, and subcellular localization of mouse mitochondrial seryl-tRNA synthetase". Biochem. Biophys. Res. Commun. 317 (3): 774–8. Bibcode:2004BBRC..317..774G. doi:10.1016/j.bbrc.2004.03.113. PMID 15081407.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Casas C, Ribera J, Esquerda JE (2001). "Antibodies against c-Jun N-terminal peptide cross-react with neo-epitopes emerging after caspase-mediated proteolysis during apoptosis". J. Neurochem. 77 (3): 904–15. doi:10.1046/j.1471-4159.2001.00314.x. PMID 11331419. S2CID 27427659.