SYTL1
| SYTL1 | ||||||
|---|---|---|---|---|---|---|
| Identifiers | ||||||
| Aliases | SYTL1, JFC1, SLP1, synaptotagmin like 1 | |||||
| External IDs | MGI: 1933365 HomoloGene: 12853 GeneCards: SYTL1 | |||||
| Orthologs | ||||||
| Species | Human | Mouse | ||||
| Entrez | ||||||
| Ensembl | ||||||
| UniProt | ||||||
| RefSeq (mRNA) | ||||||
| RefSeq (protein) |
| |||||
| Location (UCSC) | Chr 1: 27.34 – 27.35 Mb | Chr 4: 133.25 – 133.26 Mb | ||||
| PubMed search | [1] | [2] | ||||
| Wikidata | ||||||
| View/Edit Human | View/Edit Mouse |
Synaptotagmin-like protein 1 is a protein that in humans is encoded by the SYTL1 gene.[3][4]
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[5] |
| Body temperature | Normal |
| Eye morphology | Normal |
| Clinical chemistry | Abnormal[6] |
| Plasma immunoglobulins | Abnormal |
| Haematology | Abnormal[7] |
| Peripheral blood lymphocytes | Abnormal[8] |
| Micronucleus test | Normal |
| Heart weight | Normal |
| Brain histopathology | Normal |
| Salmonella infection | Normal[9] |
| Citrobacter infection | Normal[10] |
| All tests and analysis from[11][12] |
Model organisms have been used in the study of SYTL1 function. A conditional knockout mouse line, called Sytl1tm1a(KOMP)Wtsi[13][14] 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.[15][16][17]
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[11][18] Twenty four tests were carried out on homozygous mutant mice and six significant abnormalities were observed.[11] 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.[11]
Interactions
SYTL1 has been shown to interact with RAB27A.[19][20][21]
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ Catz SD, Babior BM, Johnson JL (November 2002). "JFC1 is transcriptionally activated by nuclear factor-kappaB and up-regulated by tumour necrosis factor alpha in prostate carcinoma cells". The Biochemical Journal. 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.
- 1 2 3 4 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 WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (June 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
- ↑ Dolgin E (June 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
- ↑ Collins FS, Rossant J, Wurst W (January 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 Biology. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
- ↑ Fukuda M (April 2003). "Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through interaction with the GDP-bound form of Rab27A in PC12 cells". The Journal of Biological Chemistry. 278 (17): 15390–6. doi:10.1074/jbc.M213090200. PMID 12590134.
- ↑ Strom M, Hume AN, Tarafder AK, Barkagianni E, Seabra MC (July 2002). "A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport". The Journal of Biological Chemistry. 277 (28): 25423–30. doi:10.1074/jbc.M202574200. PMID 11980908.
- ↑ Kuroda TS, Fukuda M, Ariga H, Mikoshiba K (March 2002). "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain". The Journal of Biological Chemistry. 277 (11): 9212–8. doi:10.1074/jbc.M112414200. PMID 11773082.
Further reading
- Fukuda M, Mikoshiba K (March 2001). "Synaptotagmin-like protein 1-3: a novel family of C-terminal-type tandem C2 proteins". Biochemical and Biophysical Research Communications. 281 (5): 1226–33. doi:10.1006/bbrc.2001.4512. PMID 11243866.
- McAdara Berkowitz JK, Catz SD, Johnson JL, Ruedi JM, Thon V, Babior BM (June 2001). "JFC1, a novel tandem C2 domain-containing protein associated with the leukocyte NADPH oxidase". The Journal of Biological Chemistry. 276 (22): 18855–62. doi:10.1074/jbc.M011167200. PMID 11278853.
- Kuroda TS, Fukuda M, Ariga H, Mikoshiba K (March 2002). "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain". The Journal of Biological Chemistry. 277 (11): 9212–8. doi:10.1074/jbc.M112414200. PMID 11773082.
- Strom M, Hume AN, Tarafder AK, Barkagianni E, Seabra MC (July 2002). "A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport". The Journal of Biological Chemistry. 277 (28): 25423–30. doi:10.1074/jbc.M202574200. PMID 11980908.
- Fukuda M (April 2003). "Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through interaction with the GDP-bound form of Rab27A in PC12 cells". The Journal of Biological Chemistry. 278 (17): 15390–6. doi:10.1074/jbc.M213090200. PMID 12590134.
- Johnson JL, Ellis BA, Noack D, Seabra MC, Catz SD (November 2005). "The Rab27a-binding protein, JFC1, regulates androgen-dependent secretion of prostate-specific antigen and prostatic-specific acid phosphatase". The Biochemical Journal. 391 (Pt 3): 699–710. doi:10.1042/BJ20050380. PMC 1276972. PMID 16004602.
- Schmid M, Fellermann K, Fritz P, Wiedow O, Stange EF, Wehkamp J (April 2007). "Attenuated induction of epithelial and leukocyte serine antiproteases elafin and secretory leukocyte protease inhibitor in Crohn's disease". Journal of Leukocyte Biology. 81 (4): 907–15. doi:10.1189/jlb.0906581. PMID 17200145.
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