SYTL1

SYTL1
Identifiers
Aliases	SYTL1, JFC1, SLP1, synaptotagmin like 1
External IDs	OMIM: 608042 MGI: 1933365 HomoloGene: 12853 GeneCards: SYTL1
Gene location (Human)
Chr.	Chromosome 1 (human)[1]
End	27,353,937 bp[1]
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)[2]
End	133,263,113 bp[2]
Gene ontology
Molecular function	• calcium-dependent phospholipid binding; • clathrin binding; • calcium ion binding; • neurexin family protein binding; • Rab GTPase binding; • syntaxin binding; • GO:0001948 protein binding;
Cellular component	• melanosome; • cell membrane; • extrinsic component of plasma membrane; • extracellular exosome; • exocytic vesicle; • membrane; • presynapse; • microvillus membrane;
Biological process	• intracellular protein transport; • exocytosis; • calcium ion-regulated exocytosis of neurotransmitter; • vesicle fusion; • regulation of calcium ion-dependent exocytosis;
	Sources:Amigo / QuickGO
Orthologs
	84958
	269589
	ENSG00000142765
	ENSMUSG00000028860
	Q8IYJ3
	Q99N80
	NM_001193308; NM_032872
	NM_031393
	NP_001180237; NP_116261
	n/a
	Wikidata
View/Edit Human	View/Edit Mouse

Synaptotagmin-like protein 1 is a protein that in humans is encoded by the SYTL1 gene.[5][6]

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[7]
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Abnormal[8]
Plasma immunoglobulins	Abnormal
Haematology	Abnormal[9]
Peripheral blood lymphocytes	Abnormal[10]
Micronucleus test	Normal
Heart weight	Normal
Brain histopathology	Normal
Salmonella infection	Normal[11]
Citrobacter infection	Normal[12]
All tests and analysis from[13][14]

Model organisms have been used in the study of SYTL1 function. A conditional knockout mouse line, called Sytl1^{tm1a(KOMP)Wtsi}[15][16] 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.[17][18][19]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[13][20] Twenty four tests were carried out on homozygous mutant mice and six significant abnormalities were observed.[13] 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.[13]

Interactions

SYTL1 has been shown to interact with RAB27A.[21][22][23]

References

GRCh38: Ensembl release 89: ENSG00000142765 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000028860 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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.
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.

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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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000142765 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000028860 - 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.

[pmid12137562-5] 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-6] "Entrez Gene: SYTL1 synaptotagmin-like 1".

[Radiography-7] "Radiography data for Sytl1". Wellcome Trust Sanger Institute.

[Clinical_chemistry-8] "Clinical chemistry data for Sytl1". Wellcome Trust Sanger Institute.

[Haematology-9] "Haematology data for Sytl1". Wellcome Trust Sanger Institute.

[Peripheral_blood_lymphocytes-10] "Peripheral blood lymphocytes data for Sytl1". Wellcome Trust Sanger Institute.

[''Salmonella''_infection-11] "Salmonella infection data for Sytl1". Wellcome Trust Sanger Institute.

[''Citrobacter''_infection-12] "Citrobacter infection data for Sytl1". Wellcome Trust Sanger Institute.

[mgp_reference-13] 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.

[14] Mouse Resources Portal, Wellcome Trust Sanger Institute.

[allele_ref-15] "International Knockout Mouse Consortium".

[mgi_allele_ref-16] "Mouse Genome Informatics".

[pmid21677750-17] 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.

[mouse_library-18] Dolgin E (June 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.

[mouse_for_all_reasons-19] 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.

[pmid21722353-20] 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.

[pmid12590134-21] 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.

[pmid11980908-22] 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.

[pmid11773082-23] 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.

SYTL1

Model organisms

Interactions

References

Further reading