CNTNAP1

Contactin associated protein 1
Identifiers
Symbols	CNTNAP1 ; CASPR; CNTNAP; NRXN4; P190
External IDs	OMIM: 602346 HomoloGene: 2693 GeneCards: CNTNAP1 Gene
Gene ontology Molecular function • receptor activity • SH3/SH2 adaptor activity • protein binding • SH3 domain binding Cellular component • integral component of plasma membrane • voltage-gated potassium channel complex • integral component of membrane • paranode region of axon • myelin sheath Biological process • protein localization to paranode region of axon • cytoskeleton organization • cell adhesion • signal transduction • axon guidance • positive regulation of signal transduction • neuronal action potential propagation • paranodal junction assembly • neuron projection morphogenesis • neuromuscular process controlling posture • neuromuscular process controlling balance Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8506	53321
Ensembl	ENSG00000108797	ENSMUSG00000017167
UniProt	P78357	O54991
RefSeq (mRNA)	NM_003632	NM_016782
RefSeq (protein)	NP_003623	NP_058062
Location (UCSC)	Chr 17: 42.68 – 42.7 Mb	Chr 11: 101.17 – 101.19 Mb
PubMed search

Contactin associated protein 1 is a protein that in humans is encoded by the CNTNAP1 gene. ^[1]

Function

The gene product was initially identified as a 190-kD protein associated with the contactin-PTPRZ1 complex. The 1,384-amino acid protein, also designated p190 or CASPR for 'contactin-associated protein,' includes an extracellular domain with several putative protein-protein interaction domains, a putative transmembrane domain, and a 74-amino acid cytoplasmic domain. Northern blot analysis showed that the gene is transcribed predominantly in brain as a transcript of 6.2 kb, with weak expression in several other tissues tested. The architecture of its extracellular domain is similar to that of neurexins, and this protein may be the signaling subunit of contactin, enabling recruitment and activation of intracellular signaling pathways in neurons. [provided by RefSeq, Jan 2009].

Mutations in CNTNAP1 cause arthrogryposis multiplex congenita .^[2]

References

1. "Entrez Gene: Contactin associated protein 1". Retrieved 2014-04-30.
2. Laquérriere, A; Maluenda, J; Camus, A; Fontenas, L; Dieterich, K; Nolent, F; Zhou, J; Monnier, N; Latour, P; Gentil, D; Héron, D; Desguerres, I; Landrieu, P; Beneteau, C; Delaporte, B; Bellesme, C; Baumann, C; Capri, Y; Goldenberg, A; Lyonnet, S; Bonneau, D; Estournet, B; Quijano-Roy, S; Francannet, C; Odent, S; Saint-Frison, M. H.; Sigaudy, S; Figarella-Branger, D; Gelot, A; et al. (2014). "Mutations in CNTNAP1 and ADCY6 are responsible for severe arthrogryposis multiplex congenita with axoglial defects". Human Molecular Genetics 23 (9): 2279–89. doi:10.1093/hmg/ddt618. PMID 24319099.

Further reading

• Martins-De-Souza, D; Guest, P. C.; Mann, D. M.; Roeber, S; Rahmoune, H; Bauder, C; Kretzschmar, H; Volk, B; Baborie, A; Bahn, S (2012). "Proteomic analysis identifies dysfunction in cellular transport, energy, and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration". Journal of Proteome Research 11 (4): 2533–43. doi:10.1021/pr2012279. PMID 22360420.
• Velez Edwards, D. R.; Naj, A. C.; Monda, K; North, K. E.; Neuhouser, M; Magvanjav, O; Kusimo, I; Vitolins, M. Z.; Manson, J. E.; O'Sullivan, M. J.; Rampersaud, E; Edwards, T. L. (2013). "Gene-environment interactions and obesity traits among postmenopausal African-American and Hispanic women in the Women's Health Initiative SHARe Study". Human Genetics 132 (3): 323–36. doi:10.1007/s00439-012-1246-3. PMC 3704217. PMID 23192594.
• Li, R; Zhang, B; Zheng, Y (1997). "Structural determinants required for the interaction between Rho GTPase and the GTPase-activating domain of p190". The Journal of Biological Chemistry 272 (52): 32830–5. doi:10.1074/jbc.272.52.32830. PMID 9407060.
• Lee, J. Y.; Park, A. K.; Lee, K. M.; Park, S. K.; Han, S; Han, W; Noh, D. Y.; Yoo, K. Y.; Kim, H; Chanock, S. J.; Rothman, N; Kang, D (2009). "Candidate gene approach evaluates association between innate immunity genes and breast cancer risk in Korean women". Carcinogenesis 30 (9): 1528–31. doi:10.1093/carcin/bgp084. PMID 19372141.
• Peles, E; Nativ, M; Lustig, M; Grumet, M; Schilling, J; Martinez, R; Plowman, G. D.; Schlessinger, J (1997). "Identification of a novel contactin-associated transmembrane receptor with multiple domains implicated in protein-protein interactions". The EMBO Journal 16 (5): 978–88. doi:10.1093/emboj/16.5.978. PMC 1169698. PMID 9118959.
• Hur, J. Y.; Teranishi, Y; Kihara, T; Yamamoto, N. G.; Inoue, M; Hosia, W; Hashimoto, M; Winblad, B; Frykman, S; Tjernberg, L. O. (2012). "Identification of novel γ-secretase-associated proteins in detergent-resistant membranes from brain". Journal of Biological Chemistry 287 (15): 11991–2005. doi:10.1074/jbc.M111.246074. PMC 3320946. PMID 22315232.
• Venken, K; Meuleman, J; Irobi, J; Ceuterick, C; Martini, R; De Jonghe, P; Timmerman, V (2001). "Caspr1/Paranodin/Neurexin IV is most likely not a common disease-causing gene for inherited peripheral neuropathies". NeuroReport 12 (11): 2609–14. doi:10.1097/00001756-200108080-00063. PMID 11496158.
• Charles, P; Tait, S; Faivre-Sarrailh, C; Barbin, G; Gunn-Moore, F; Denisenko-Nehrbass, N; Guennoc, A. M.; Girault, J. A.; Brophy, P. J.; Lubetzki, C (2002). "Neurofascin is a glial receptor for the paranodin/Caspr-contactin axonal complex at the axoglial junction". Current Biology 12 (3): 217–20. doi:10.1016/S0960-9822(01)00680-7. PMID 11839274.
• Nie, D. -Y.; Zhou, Z. H.; Ang, B. T.; Teng, F. Y.; Xu, G.; Xiang, T.; Wang, C. Y.; Zeng, L.; Takeda, Y.; Xu, T. L.; Ng, Y. K.; Faivre-Sarrailh, C.; Popko, B.; Ling, E. A.; Schachner, M.; Watanabe, K.; Pallen, C. J.; Tang, B. L.; Xiao, Z. C. (2003). "Nogo-A at CNS paranodes is a ligand of Caspr: Possible regulation of K+ channel localization". The EMBO Journal 22 (21): 5666–5678. doi:10.1093/emboj/cdg570. PMC 275427. PMID 14592966.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.