Kaptin (actin binding protein)

Kaptin is a protein that in humans is encoded by the KPTN gene.[5][6]

KPTN
Identifiers
Aliases	KPTN, 2E4, MRT41, kaptin (actin binding protein), kaptin, actin binding protein
External IDs	OMIM: 615620 MGI: 1890380 HomoloGene: 5127 GeneCards: KPTN
Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19q13.32 Start 47,475,150 bp[1] End 47,484,265 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7 A2|7 8.75 cM Start 16,119,895 bp[2] End 16,127,516 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • actin binding • actin filament binding Cellular component • cell projection • actin cytoskeleton • filamentous actin • postsynaptic actin cytoskeleton • stereocilium • KICSTOR complex • lysosome • lysosomal membrane • membrane • lamellipodium Biological process • actin filament organization • cellular response to glucose starvation • protein localization to lysosome • negative regulation of TORC1 signaling • cellular response to amino acid starvation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	11133	70394
Ensembl	ENSG00000118162	ENSMUSG00000006021
UniProt	Q9Y664	Q8VCX6
RefSeq (mRNA)	NM_001291296 NM_007059	NM_133727
RefSeq (protein)	NP_001278225 NP_008990	NP_598488
Location (UCSC)	Chr 19: 47.48 – 47.48 Mb	Chr 7: 16.12 – 16.13 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Model organisms

Kptn knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Normal
Fertility	Normal
Body weight	Abnormal[7]
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Abnormal[8]
Auditory brainstem response	Normal
DEXA	Abnormal[9]
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Abnormal[10]
Haematology	Normal
Peripheral blood lymphocytes	Abnormal[11]
Micronucleus test	Normal
Heart weight	Normal
Salmonella infection	Abnormal[12]
Citrobacter infection	Normal[13]
All tests and analysis from[14][15]

Model organisms have been used in the study of KPTN function. A conditional knockout mouse line, called Kptn^{tm1a(EUCOMM)Wtsi}[16][17] 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.[18][19][20]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[14][21] Twenty two tests were carried out on mutant mice and six significant abnormalities were observed.[14] Homozygous mutant mice had hyperalbuminemia, decreased mature B cell numbers and increased susceptibility to bacterial infection. Female mice also had increased body weight, body fat and impaired glucose tolerance.[14]

Clinical

Mutations in this gene have been associated with a syndrome of acrocephaly, muscular hypotonia, global development delay, dyspraxia and hand-mouth synkinesia.[22]

References

1. GRCh38: Ensembl release 89: ENSG00000118162 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000006021 - 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. Bearer EL, Abraham MT (February 1999). "2E4 (kaptin): a novel actin-associated protein from human blood platelets found in lamellipodia and the tips of the stereocilia of the inner ear". European Journal of Cell Biology. 78 (2): 117–26. doi:10.1016/s0171-9335(99)80013-2. PMC 3376092. PMID 10099934.
6. "Entrez Gene: KPTN kaptin (actin binding protein)".
7. "Body weight data for Kptn". Wellcome Trust Sanger Institute.
8. "Glucose tolerance test data for Kptn". Wellcome Trust Sanger Institute.
9. "DEXA data for Kptn". Wellcome Trust Sanger Institute.
10. "Clinical chemistry data for Kptn". Wellcome Trust Sanger Institute.
11. "Peripheral blood lymphocytes data for Kptn". Wellcome Trust Sanger Institute.
12. "Salmonella infection data for Kptn". Wellcome Trust Sanger Institute.
13. "Citrobacter infection data for Kptn". Wellcome Trust Sanger Institute.
14. 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.
15. Mouse Resources Portal, Wellcome Trust Sanger Institute.
16. "International Knockout Mouse Consortium".
17. "Mouse Genome Informatics".
18. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, et al. (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.
19. Dolgin E (June 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
20. 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.
21. van der Weyden L, White JK, Adams DJ, Logan DW (June 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.
22. Lucena PH, Armani-Franceschi G, Bispo-Torres AC, Bandeira ID, Lucena MF, Maldonado I, et al. (2020). "KPTN gene homozygous variant-related syndrome in the northeast of Brazil: A case report". Am J Med Genet A.

Further reading

• Bearer EL, Prakash JM, Li Z (2002). "Actin dynamics in platelets". International Review of Cytology. 217: 137–82. doi:10.1016/S0074-7696(02)17014-8. ISBN 9780123646217. PMC 3376087. PMID 12019562.
• Bearer EL (March 1992). "An actin-associated protein present in the microtubule organizing center and the growth cones of PC-12 cells". The Journal of Neuroscience. 12 (3): 750–61. doi:10.1523/jneurosci.12-03-00750.1992. PMC 3376081. PMID 1372044.
• 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.
• Bearer EL, Chen AF, Chen AH, Li Z, Mark HF, Smith RJ, Jackson CL (May 2000). "2E4/Kaptin (KPTN)--a candidate gene for the hearing loss locus, DFNA4". Annals of Human Genetics. 64 (Pt 3): 189–96. doi:10.1046/j.1469-1809.2000.6430189.x. PMC 3376086. PMID 11409409.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, et al. (January 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.