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SYTL2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3BC1
Identifiers
Aliases	SYTL2, CHR11SYT, EXO4, PPP1R151, SGA72M, SLP2, SLP2A, synaptotagmin like 2
External IDs	OMIM: 612880; MGI: 1933366; HomoloGene: 131343; GeneCards: SYTL2; OMA:SYTL2 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11q14.1 Start 85,694,224 bp End 85,811,159 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7|7 E1 Start 89,951,460 bp End 90,059,927 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in saphenous vein rectum mucosa of sigmoid colon bronchial epithelial cell endothelial cell urethra vena cava right coronary artery tibial arteries mucosa of transverse colon Top expressed in iris epithelium of stomach pyloric antrum transitional epithelium of urinary bladder motor neuron mucous cell of stomach facial motor nucleus zygote hair follicle secondary oocyte More reference expression data BioGPS More reference expression data
Gene ontology Molecular function calcium ion binding phosphatase binding clathrin binding phosphatidylserine binding neurexin family protein binding protein binding calcium-dependent phospholipid binding phosphatidylinositol-4,5-bisphosphate binding syntaxin binding Cellular component cytoplasm exocytic vesicle membrane melanosome plasma membrane extrinsic component of plasma membrane synapse presynapse Biological process negative regulation of phosphatase activity vesicle docking involved in exocytosis protein localization to plasma membrane intracellular protein transport positive regulation of mucus secretion vesicle-mediated transport exocytosis regulation of calcium ion-dependent exocytosis calcium ion-regulated exocytosis of neurotransmitter vesicle fusion Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 54843 83671 Ensembl ENSG00000137501 ENSMUSG00000030616 UniProt Q9HCH5 Q99N50 RefSeq (mRNA) NM_001162951 NM_001162952 NM_001162953 NM_001289608 NM_001289609 NM_001289610 NM_032379 NM_032943 NM_206927 NM_206928 NM_206929 NM_206930 NM_001365826 NM_001365827 NM_001365828 NM_001365829 NM_001365830 NM_001365831 NM_001365832 NM_001365833 NM_001365834 NM_001365835 NM_001040085 NM_001040086 NM_001040087 NM_001040088 NM_001289583 NM_001289584 NM_001289585 NM_001289586 NM_031394 NM_001368878 RefSeq (protein) NP_001156423 NP_001156424 NP_001156425 NP_001276537 NP_001276538 NP_001276539 NP_116561 NP_996812 NP_996813 NP_001352755 NP_001352756 NP_001352757 NP_001352758 NP_001352759 NP_001352760 NP_001352761 NP_001352762 NP_001352763 NP_001352764 NP_996810 NP_996811 NP_001035174 NP_001035176 NP_001035177 NP_001276512 NP_001276513 NP_001276514 NP_001276515 NP_113571 NP_001355807 Location (UCSC) Chr 11: 85.69 – 85.81 Mb Chr 7: 89.95 – 90.06 Mb PubMed search
Wikidata
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Synaptotagmin-like 2, also known as SYTL2, is a human gene.

Function

The protein encoded by this gene is a synaptotagmin-like protein (SLP) that belongs to a C2 domain-containing protein family. The SLP homology domain (SHD) of this protein has been shown to specifically bind the GTP-bound form of Ras-related protein Rab-27A (RAB27A), which suggests a role in vesicle trafficking. Multiple alternatively spiced transcript variants encoding distinct isoforms have been observed.

Interactions

SYTL2 has been shown to interact with RAB27A.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000137501 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000030616 – 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: SYTL2 synaptotagmin-like 2".
6. 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.
7. 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.
8. 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

• Nalefski EA, Falke JJ (December 1996). "The C2 domain calcium-binding motif: structural and functional diversity". Protein Science. 5 (12): 2375–90. doi:10.1002/pro.5560051201. PMC 2143302. PMID 8976547.
• Duncan RR, Shipston MJ, Chow RH (May 2000). "Double C2 protein. A review". Biochimie. 82 (5): 421–6. doi:10.1016/S0300-9084(00)00214-5. PMID 10865129.
• Maruyama K, Sugano S (January 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.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 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.
• Dias Neto E, Correa RG, Verjovski-Almeida S, Briones MR, Nagai MA, da Silva W, Zago MA, Bordin S, Costa FF, Goldman GH, Carvalho AF, Matsukuma A, Baia GS, Simpson DH, Brunstein A, de Oliveira PS, Bucher P, Jongeneel CV, O'Hare MJ, Soares F, Brentani RR, Reis LF, de Souza SJ, Simpson AJ (March 2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proceedings of the National Academy of Sciences of the United States of America. 97 (7): 3491–6. Bibcode:2000PNAS...97.3491D. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800.
• Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O (August 2000). "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 7 (4): 273–81. doi:10.1093/dnares/7.4.271. PMID 10997877.
• 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.
• Fukuda M, Saegusa C, Mikoshiba K (May 2001). "Novel splicing isoforms of synaptotagmin-like proteins 2 and 3: identification of the Slp homology domain". Biochemical and Biophysical Research Communications. 283 (2): 513–9. doi:10.1006/bbrc.2001.4803. PMID 11327731.
• Craxton M (September 2001). "Genomic analysis of synaptotagmin genes". Genomics. 77 (1–2): 43–9. doi:10.1006/geno.2001.6619. PMID 11543631.
• 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.
• Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA (December 2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• 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.
• Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (July 2004). "Functional proteomics mapping of a human signaling pathway". Genome Research. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Research. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.
• Yu M, Kasai K, Nagashima K, Torii S, Yokota-Hashimoto H, Okamoto K, Takeuchi T, Gomi H, Izumi T (February 2007). "Exophilin4/Slp2-a targets glucagon granules to the plasma membrane through unique Ca2+-inhibitory phospholipid-binding activity of the C2A domain". Molecular Biology of the Cell. 18 (2): 688–96. doi:10.1091/mbc.E06-10-0914. PMC 1783794. PMID 17182843.

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