SYTL1

Synaptotagmin-like 1
Identifiers
Symbols	SYTL1 ; JFC1; SLP1
External IDs	OMIM: 608042 MGI: 1933365 HomoloGene: 12853 GeneCards: SYTL1 Gene
Gene ontology Molecular function • calcium ion binding • protein binding • calcium-dependent phospholipid binding • Rab GTPase binding • syntaxin binding • clathrin binding • neurexin family protein binding Cellular component • plasma membrane • extrinsic component of plasma membrane • melanosome • extracellular exosome • exocytic vesicle Biological process • intracellular protein transport • exocytosis • synaptic vesicle exocytosis • regulation of calcium ion-dependent exocytosis • calcium ion-dependent exocytosis of neurotransmitter Sources: Amigo / QuickGO
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: 27.34 – 27.35 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

Sytl1 knockout mouse phenotype

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 Sytl1^{tm1a(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

1. 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.
2. "Entrez Gene: SYTL1 synaptotagmin-like 1".
3. "Radiography data for Sytl1". Wellcome Trust Sanger Institute.
4. "Clinical chemistry data for Sytl1". Wellcome Trust Sanger Institute.
5. "Haematology data for Sytl1". Wellcome Trust Sanger Institute.
6. "Peripheral blood lymphocytes data for Sytl1". Wellcome Trust Sanger Institute.
7. "Salmonella infection data for Sytl1". Wellcome Trust Sanger Institute.
8. "Citrobacter infection data for Sytl1". Wellcome Trust Sanger Institute.
9. 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.
10. Mouse Resources Portal, Wellcome Trust Sanger Institute.
11. "International Knockout Mouse Consortium".
12. "Mouse Genome Informatics".
13. 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.
14. Dolgin E (2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
15. 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.
16. 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.
17. 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.
18. 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.
19. 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.