SYTL1
| Synaptotagmin-like 1 | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||||
| Symbols | SYTL1 ; JFC1; SLP1 | ||||||||||||
| External IDs | OMIM: 608042 MGI: 1933365 HomoloGene: 12853 GeneCards: SYTL1 Gene | ||||||||||||
| |||||||||||||
| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 84958 | 269589 | |||||||||||
| Ensembl | ENSG00000142765 | ENSMUSG00000028860 | |||||||||||
| UniProt | Q8IYJ3 | A2AE94 | |||||||||||
| RefSeq (mRNA) | NM_001193308 | NM_031393 | |||||||||||
| RefSeq (protein) | NP_001180237 | NP_113570 | |||||||||||
| Location (UCSC) | Chr 1: 27.67 – 27.68 Mb | Chr 4: 133.25 – 133.26 Mb | |||||||||||
| PubMed search | |||||||||||||
Synaptotagmin-like protein 1 is a protein that in humans is encoded by the SYTL1 gene.[1][2]
Model organisms
| Characteristic | Phenotype |
|---|---|
| Homozygote viability | Normal |
| Fertility | Normal |
| Body weight | Normal |
| Anxiety | Normal |
| Neurological assessment | Abnormal |
| Grip strength | Normal |
| Hot plate | Normal |
| Dysmorphology | Normal |
| Indirect calorimetry | Normal |
| Glucose tolerance test | Normal |
| Auditory brainstem response | Normal |
| DEXA | Normal |
| Radiography | Abnormal[3] |
| Body temperature | Normal |
| Eye morphology | Normal |
| Clinical chemistry | Abnormal[4] |
| Plasma immunoglobulins | Abnormal |
| Haematology | Abnormal[5] |
| Peripheral blood lymphocytes | Abnormal[6] |
| Micronucleus test | Normal |
| Heart weight | Normal |
| Brain histopathology | Normal |
| Salmonella infection | Normal[7] |
| Citrobacter infection | Normal[8] |
| All tests and analysis from[9][10] |
Model organisms have been used in the study of SYTL1 function. A conditional knockout mouse line, called Sytl1tm1a(KOMP)Wtsi[11][12] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[13][14][15]
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[9][16] Twenty four tests were carried out on homozygous mutant mice and six significant abnormalities were observed.[9] Females had abnormal locomotor coordination, caudal vertebral transformation, decreased circulating amylase levels and increased mean platelet volume. Both sexes displayed decreased IgG2b levels and abnormal peripheral blood lymphocyte parameters.[9]
Interactions
SYTL1 has been shown to interact with RAB27A.[17][18][19]
References
- ↑ Catz SD, Babior BM, Johnson JL (Oct 2002). "JFC1 is transcriptionally activated by nuclear factor-kappaB and up-regulated by tumour necrosis factor alpha in prostate carcinoma cells". Biochem J 367 (Pt 3): 791–9. doi:10.1042/BJ20020345. PMC 1222920. PMID 12137562.
- ↑ "Entrez Gene: SYTL1 synaptotagmin-like 1".
- ↑ "Radiography data for Sytl1". Wellcome Trust Sanger Institute.
- ↑ "Clinical chemistry data for Sytl1". Wellcome Trust Sanger Institute.
- ↑ "Haematology data for Sytl1". Wellcome Trust Sanger Institute.
- ↑ "Peripheral blood lymphocytes data for Sytl1". Wellcome Trust Sanger Institute.
- ↑ "Salmonella infection data for Sytl1". Wellcome Trust Sanger Institute.
- ↑ "Citrobacter infection data for Sytl1". Wellcome Trust Sanger Institute.
- ↑ 9.0 9.1 9.2 9.3 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
- ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
- ↑ "International Knockout Mouse Consortium".
- ↑ "Mouse Genome Informatics".
- ↑ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
- ↑ Dolgin E (2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
- ↑ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
- ↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
- ↑ Fukuda, Mitsunori (Apr 2003). "Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through interaction with the GDP-bound form of Rab27A in PC12 cells". J. Biol. Chem. (United States) 278 (17): 15390–6. doi:10.1074/jbc.M213090200. ISSN 0021-9258. PMID 12590134.
- ↑ Strom, Molly; Hume Alistair N; Tarafder Abul K; Barkagianni Eleni; Seabra Miguel C (Jul 2002). "A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport". J. Biol. Chem. (United States) 277 (28): 25423–30. doi:10.1074/jbc.M202574200. ISSN 0021-9258. PMID 11980908.
- ↑ Kuroda, Taruho S; Fukuda Mitsunori; Ariga Hiroyoshi; Mikoshiba Katsuhiko (Mar 2002). "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain". J. Biol. Chem. (United States) 277 (11): 9212–8. doi:10.1074/jbc.M112414200. ISSN 0021-9258. PMID 11773082.
Further reading
- Fukuda M, Mikoshiba K (2001). "Synaptotagmin-like protein 1-3: a novel family of C-terminal-type tandem C2 proteins". Biochem. Biophys. Res. Commun. 281 (5): 1226–33. doi:10.1006/bbrc.2001.4512. PMID 11243866.
- McAdara Berkowitz JK, Catz SD, Johnson JL et al. (2001). "JFC1, a novel tandem C2 domain-containing protein associated with the leukocyte NADPH oxidase". J. Biol. Chem. 276 (22): 18855–62. doi:10.1074/jbc.M011167200. PMID 11278853.
- Kuroda TS, Fukuda M, Ariga H, Mikoshiba K (2002). "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain". J. Biol. Chem. 277 (11): 9212–8. doi:10.1074/jbc.M112414200. PMID 11773082.
- Strom M, Hume AN, Tarafder AK et al. (2002). "A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport". J. Biol. Chem. 277 (28): 25423–30. doi:10.1074/jbc.M202574200. PMID 11980908.
- 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Fukuda M (2003). "Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through interaction with the GDP-bound form of Rab27A in PC12 cells". J. Biol. Chem. 278 (17): 15390–6. doi:10.1074/jbc.M213090200. PMID 12590134.
- 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.
- 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.
- Johnson JL, Ellis BA, Noack D et al. (2006). "The Rab27a-binding protein, JFC1, regulates androgen-dependent secretion of prostate-specific antigen and prostatic-specific acid phosphatase". Biochem. J. 391 (Pt 3): 699–710. doi:10.1042/BJ20050380. PMC 1276972. PMID 16004602.
- Schmid M, Fellermann K, Fritz P et al. (2007). "Attenuated induction of epithelial and leukocyte serine antiproteases elafin and secretory leukocyte protease inhibitor in Crohn's disease". J. Leukoc. Biol. 81 (4): 907–15. doi:10.1189/jlb.0906581. PMID 17200145.