SNAP29

SNAP29
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4WY4
Identifiers
Aliases	SNAP29 , CEDNIK, SNAP-29, synaptosome associated protein 29kDa, synaptosome associated protein 29
External IDs	OMIM: 604202 MGI: 1914724 HomoloGene: 3512 GeneCards: SNAP29
Gene location (Human) Chr. Chromosome 22 (human) [1] Band 22q11.21 Start 20,859,007 bp [1] End 20,891,214 bp [1]
Gene location (Mouse) Chr. Chromosome 16 (mouse) [2] Band 16|16 A3 Start 17,223,850 bp [2] End 17,248,691 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte islet of Langerhans gastrocnemius muscle stromal cell of endometrium liver right ventricle right lobe of liver smooth muscle tissue vastus lateralis muscle parotid gland Top expressed in spermatocyte secondary oocyte spermatid esophagus yolk sac blood jejunum seminiferous tubule spleen intestinal villus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function SNAP receptor activity protein binding syntaxin binding Cellular component cytoplasm centrosome Golgi apparatus cell projection membrane plasma membrane cilium autophagosome membrane SNARE complex ciliary membrane ciliary pocket membrane cytoplasmic vesicle presynapse Golgi membrane nucleoplasm autophagosome cytosol azurophil granule membrane synapse Biological process vesicle targeting synaptic vesicle fusion to presynaptic active zone membrane membrane fusion autophagy autophagosome maturation cell projection organization synaptic vesicle priming protein transport exocytosis autophagosome membrane docking neutrophil degranulation cilium assembly vesicle fusion Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9342 67474 Ensembl ENSG00000099940 ENSMUSG00000022765 UniProt O95721 Q9ERB0 RefSeq (mRNA) NM_004782 NM_023348 RefSeq (protein) NP_004773 NP_075837 Location (UCSC) Chr 22: 20.86 – 20.89 Mb Chr 16: 17.22 – 17.25 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Synaptosomal-associated protein 29 is a protein that in humans is encoded by the SNAP29 gene. ^{[5] [6] [7]}

Function

This gene, a member of the SNAP25 gene family, encodes a protein involved in multiple membrane trafficking steps. Two other members of this gene family, SNAP23 and SNAP25, encode proteins that bind a syntaxin protein and mediate synaptic vesicle membrane docking and fusion to the plasma membrane. The protein encoded by this gene binds tightly to multiple syntaxins and is localized to intracellular membrane structures rather than to the plasma membrane. While the protein is mostly membrane-bound, a significant fraction of it is found free in the cytoplasm. Use of multiple polyadenylation sites has been noted for this gene. ^[7]

Model organisms

Snap29 knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Abnormal
Recessive lethal study	Abnormal
Fertility	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology	Normal
Peripheral blood lymphocytes	Normal
Micronucleus test	Normal
Heart weight	Normal
Brain histopathology	Normal
Eye Histopathology	Normal
Salmonella infection	Normal [8]
Citrobacter infection	Normal [9]
All tests and analysis from [10] [11]

Model organisms have been used in the study of SNAP29 function. A conditional knockout mouse line, called Snap29^{tm1a(EUCOMM)Wtsi [12] [13]} 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. ^{[14] [15] [16]}

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. ^{[10] [17]} Twenty five tests were carried out on mutant mice and two significant abnormalities were observed. ^[10] No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice; no significant abnormalities were observed in these animals. ^[10]

Interactions

SNAP29 has been shown to interact with Syntaxin 3 ^[5] and EHD1. ^[18]

SNAP29 was shown to interact with CVB3 and EV-D68 viral protease 3C. ^{[19] [20]}

See also

• CEDNIK Syndrome

References

1. GRCh38: Ensembl release 89: ENSG00000099940 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022765 - 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. Steegmaier M, Yang B, Yoo JS, Huang B, Shen M, Yu S, Luo Y, Scheller RH (January 1999). "Three novel proteins of the syntaxin/SNAP-25 family". J Biol Chem. 273 (51): 34171–9. doi: 10.1074/jbc.273.51.34171 . PMID   9852078.
6. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP (Dec 1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi: 10.1038/990031 . PMID   10591208.
7. "Entrez Gene: SNAP29 synaptosomal-associated protein, 29kDa".
8. "Salmonella infection data for Snap29". Wellcome Trust Sanger Institute.
9. "Citrobacter infection data for Snap29". Wellcome Trust Sanger Institute.
10. 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. S2CID   85911512.
11. Mouse Resources Portal, Wellcome Trust Sanger Institute.
12. "International Knockout Mouse Consortium".
13. "Mouse Genome Informatics".
14. 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 (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.
15. Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi: 10.1038/474262a . PMID   21677718.
16. 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. S2CID   18872015.
17. 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.
18. Rotem-Yehudar R, Galperin E, Horowitz M (August 2001). "Association of insulin-like growth factor 1 receptor with EHD1 and SNAP29". J. Biol. Chem. 276 (35): 33054–60. doi: 10.1074/jbc.M009913200 . PMID   11423532.
19. Mohamud, Yasir; Shi, Junyan; Qu, Junyan; Poon, Tak; Xue, Yuan Chao; Deng, Haoyu; Zhang, Jingchun; Luo, Honglin (2018-03-20). "Enteroviral Infection Inhibits Autophagic Flux via Disruption of the SNARE Complex to Enhance Viral Replication". Cell Reports. 22 (12): 3292–3303. doi:10.1016/j.celrep.2018.02.090. ISSN   2211-1247. PMID   29562184.
20. Corona, Abigail K.; Saulsbery, Holly M.; Corona Velazquez, Angel F.; Jackson, William T. (2018-03-20). "Enteroviruses Remodel Autophagic Trafficking through Regulation of Host SNARE Proteins to Promote Virus Replication and Cell Exit". Cell Reports. 22 (12): 3304–3314. doi:10.1016/j.celrep.2018.03.003. ISSN   2211-1247. PMC   5894509 . PMID   29562185.

Further reading

• Wong SH, Xu Y, Zhang T, Griffiths G, Lowe SL, Subramaniam VN, Seow KT, Hong W (1999). "GS32, a novel Golgi SNARE of 32 kDa, interacts preferentially with syntaxin 6". Mol. Biol. Cell. 10 (1): 119–34. doi:10.1091/mbc.10.1.119. PMC   25158 . PMID   9880331.
• Scales SJ, Chen YA, Yoo BY, Patel SM, Doung YC, Scheller RH (2000). "SNAREs contribute to the specificity of membrane fusion". Neuron. 26 (2): 457–64. doi: 10.1016/S0896-6273(00)81177-0 . PMID   10839363.
• Rotem-Yehudar R, Galperin E, Horowitz M (2001). "Association of insulin-like growth factor 1 receptor with EHD1 and SNAP29". J. Biol. Chem. 276 (35): 33054–60. doi: 10.1074/jbc.M009913200 . PMID   11423532.
• Hohenstein AC, Roche PA (2001). "SNAP-29 is a promiscuous syntaxin-binding SNARE". Biochem. Biophys. Res. Commun. 285 (2): 167–71. doi:10.1006/bbrc.2001.5141. PMID   11444821.
• Su Q, Mochida S, Tian JH, Mehta R, Sheng ZH (2002). "SNAP-29: a general SNARE protein that inhibits SNARE disassembly and is implicated in synaptic transmission". Proc. Natl. Acad. Sci. U.S.A. 98 (24): 14038–43. doi: 10.1073/pnas.251532398 . PMC   61163 . PMID   11707603.
• Martinez-Arca S, Rudge R, Vacca M, Raposo G, Camonis J, Proux-Gillardeaux V, Daviet L, Formstecher E, Hamburger A, Filippini F, D'Esposito M, Galli T (2003). "A dual mechanism controlling the localization and function of exocytic v-SNAREs". Proc. Natl. Acad. Sci. U.S.A. 100 (15): 9011–6. Bibcode:2003PNAS..100.9011M. doi: 10.1073/pnas.1431910100 . PMC   166429 . PMID   12853575.
• Xu Y, Shi H, Wei S, Wong SH, Hong W (2005). "Mutually exclusive interactions of EHD1 with GS32 and syndapin II". Mol. Membr. Biol. 21 (4): 269–77. doi:10.1080/09687680410001716871. PMID   15371016. S2CID   22820496.
• Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC   545604 . PMID   15461802.
• Pan PY, Cai Q, Lin L, Lu PH, Duan S, Sheng ZH (2005). "SNAP-29-mediated modulation of synaptic transmission in cultured hippocampal neurons". J. Biol. Chem. 280 (27): 25769–79. doi: 10.1074/jbc.M502356200 . PMC   1864940 . PMID   15890653.
• Sprecher E, Ishida-Yamamoto A, Mizrahi-Koren M, Rapaport D, Goldsher D, Indelman M, Topaz O, Chefetz I, Keren H, O'brien TJ, Bercovich D, Shalev S, Geiger D, Bergman R, Horowitz M, Mandel H (2005). "A mutation in SNAP29, coding for a SNARE protein involved in intracellular trafficking, causes a novel neurocutaneous syndrome characterized by cerebral dysgenesis, neuropathy, ichthyosis, and palmoplantar keratoderma". Am. J. Hum. Genet. 77 (2): 242–51. doi:10.1086/432556. PMC   1224527 . PMID   15968592.
• Carroll JS, Liu XS, Brodsky AS, Li W, Meyer CA, Szary AJ, Eeckhoute J, Shao W, Hestermann EV, Geistlinger TR, Fox EA, Silver PA, Brown M (2005). "Chromosome-wide mapping of estrogen receptor binding reveals long-range regulation requiring the forkhead protein FoxA1". Cell. 122 (1): 33–43. doi: 10.1016/j.cell.2005.05.008 . PMID   16009131. S2CID   16841542.
• 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 (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.

External links

• Overview of all the structural information available in the PDB for UniProt : O95721 (Synaptosomal-associated protein 29) at the PDBe-KB .