ASRGL1

ASRGL1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3TKJ, 4ET0, 4O0C, 4O0D, 4O0E, 4O0F, 4O0G, 4O0H, 4OSX, 4OSY, 4PVP, 4PVQ, 4PVR, 4PVS, 4ZM9
Identifiers
Aliases	ASRGL1 , ALP, ALP1, CRASH, asparaginase like 1, asparaginase and isoaspartyl peptidase 1
External IDs	OMIM: 609212; MGI: 1913764; HomoloGene: 11825; GeneCards: ASRGL1; OMA:ASRGL1 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) [1] Band 11q12.3 Start 62,337,448 bp [1] End 62,393,412 bp [1]
Gene location (Mouse) Chr. Chromosome 19 (mouse) [2] Band 19|19 A Start 9,087,232 bp [2] End 9,113,000 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sperm putamen right uterine tube pars reticulata left testis nasal epithelium ventral tegmental area right testis amygdala cerebellar vermis Top expressed in seminiferous tubule spermatocyte neural layer of retina spermatid motor neuron substantia nigra supraoptic nucleus dentate gyrus of hippocampal formation granule cell suprachiasmatic nucleus deep cerebellar nuclei More reference expression data BioGPS More reference expression data
Gene ontology Molecular function peptidase activity beta-aspartyl-peptidase activity hydrolase activity N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity asparaginase activity Cellular component cytoplasm cytosol nucleus photoreceptor inner segment Biological process asparagine catabolic process via L-aspartate L-phenylalanine catabolic process proteolysis protein maturation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 80150 66514 Ensembl ENSG00000162174 ENSMUSG00000024654 UniProt Q7L266 Q8C0M9 RefSeq (mRNA) NM_001083926 NM_025080 NM_025610 RefSeq (protein) NP_001077395 NP_079356 NP_079886 Location (UCSC) Chr 11: 62.34 – 62.39 Mb Chr 19: 9.09 – 9.11 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

L-asparaginase is an enzyme that in humans is encoded by the ASRGL1 gene. ^[5]

Function

The ASRGL1 protein consists of 308 amino acids and is activated by autocleavage at amino acid 168 to form an alpha- and a beta-chain, which can dimerize into a heterodimer. ^[6] The ASRGL1 enzyme has both L-asparaginase and beta-aspartyl peptidase activity and may be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions.

According to antibody-based profiling and transcriptomics analysis, ASRGL1 protein is present in all analysed human tissues, with highest expression in brain, in female tissues such as the uterine cervix and fallopian tube, and in male tissues as testis. ^[7] Based on confocal microscopy ASRGL1 is mainly localized to the microtubules. ^[8]

Clinical significance

ASRGL1 is highly expressed in the normal endometrium and differentially expressed in endometrial cancer. Loss of ASRGL1 expression is an unfavorable prognostic feature for patients with endometrial cancer. ^{[9] [10]}

References

1. GRCh38: Ensembl release 89: ENSG00000162174 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000024654 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: ASRGL1 asparaginase like 1".
6. Li, Wenzong; Cantor, Jason R.; Yogesha, S. D.; Yang, Shirley; Chantranupong, Lynne; Liu, June Qingxia; Agnello, Giulia; Georgiou, George; Stone, Everett M. (2012-11-16). "Uncoupling Intramolecular Processing and Substrate Hydrolysis in the N-Terminal Nucleophile Hydrolase hASRGL1 by Circular Permutation". ACS Chemical Biology. 7 (11): 1840–1847. doi:10.1021/cb300232n. ISSN   1554-8929. PMC   3514461 . PMID   22891768.
7. "Tissue expression of ASRGL1 - Summary - The Human Protein Atlas". www.proteinatlas.org. Retrieved 2017-10-03.
8. "Cell atlas - ASRGL1 - The Human Protein Atlas". www.proteinatlas.org. Archived from the original on 2019-01-03. Retrieved 2017-10-03.
9. "Expression of ASRGL1 in endometrial cancer - The Human Protein Atlas". www.proteinatlas.org. Retrieved 2017-10-03.
10. Edqvist, Per-Henrik D.; Huvila, Jutta; Forsström, Björn; Talve, Lauri; Carpén, Olli; Salvesen, Helga B.; Krakstad, Camilla; Grénman, Seija; Johannesson, Henrik (2015). "Loss of ASRGL1 expression is an independent biomarker for disease-specific survival in endometrioid endometrial carcinoma". Gynecologic Oncology. 137 (3): 529–537. doi:10.1016/j.ygyno.2015.03.055. PMID   25858696.

External links

• ASRGL1 expression in the Human Protein Atlas
• Human ASRGL1 genome location and ASRGL1 gene details page in the UCSC Genome Browser .

Further reading

• Kim JM, Lee KH, Jeon YJ, Oh JH, Jeong SY, Song IS, Kim JM, Lee DS, Kim NS (2006). "Identification of genes related to Parkinson's disease using expressed sequence tags". DNA Res. 13 (6): 275–86. doi: 10.1093/dnares/dsl016 . PMID   17213182.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC   1356129 . PMID   16344560.
• Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC   515316 . PMID   15342556.
• Bush LA, Herr JC, Wolkowicz M, Sherman NE, Shore A, Flickinger CJ (2002). "A novel asparaginase-like protein is a sperm autoantigen in rats". Mol. Reprod. Dev. 62 (2): 233–47. doi: 10.1002/mrd.10092 . PMID   11984834. S2CID   32206911.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.