LRRC16A

Leucine rich repeat containing 16A
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3LK2, 3LK3
Identifiers
Symbols	LRRC16A ; CARMIL; CARMIL1; CARMIL1a; LRRC16; dJ501N12.1; dJ501N12.5
External IDs	OMIM: 609593 HomoloGene: 9757 GeneCards: LRRC16A Gene
Gene ontology Molecular function • protein complex binding Cellular component • nucleus • cytoplasm • cytosol • lamellipodium • filamentous actin • extracellular exosome Biological process • actin filament organization • blood coagulation • cell migration • lamellipodium assembly • positive regulation of cell migration • positive regulation of actin filament polymerization • ruffle organization • urate metabolic process • positive regulation of stress fiber assembly • barbed-end actin filament uncapping • positive regulation of substrate adhesion-dependent cell spreading • positive regulation of lamellipodium organization • negative regulation of barbed-end actin filament capping Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	55604	68732
Ensembl	ENSG00000079691	ENSMUSG00000021338
UniProt	Q5VZK9	Q6EDY6
RefSeq (mRNA)	NM_001173977	NM_026825
RefSeq (protein)	NP_001167448	NP_081101
Location (UCSC)	Chr 6: 25.28 – 25.62 Mb	Chr 13: 24.01 – 24.28 Mb
PubMed search

Leucine rich repeat containing 16A is a protein that in humans is encoded by the LRRC16A gene.^[1] The gene is also known as LRRC16, CARMIL, CARMIL1 or CARMIL1a.^[1]

Model organisms

Lrrc16a knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Normal
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
Micronucleus test	Normal
Heart weight	Normal
Brain histopathology	Normal
Salmonella infection	Normal[2]
Citrobacter infection	Normal[3]
All tests and analysis from[4][5]

Model organisms have been used in the study of LRRC16A function. A conditional knockout mouse line, called Lrrc16a^{tm1a(KOMP)Wtsi[6][7]} 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 — at the Wellcome Trust Sanger Institute.^[8][9][10]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.^[4][11] Twenty two tests were carried out on mutant mice but no significant abnormalities were observed.^[4]

References

1. "leucine rich repeat containing 16A". Retrieved 2011-12-04.
2. "Salmonella infection data for Lrrc16a". Wellcome Trust Sanger Institute.
3. "Citrobacter infection data for Lrrc16a". Wellcome Trust Sanger Institute.
4. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica 88 (S248). doi:10.1111/j.1755-3768.2010.4142.x.
5. Mouse Resources Portal, Wellcome Trust Sanger Institute.
6. "International Knockout Mouse Consortium".
7. "Mouse Genome Informatics".
8. Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; 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.
9. Dolgin E (June 2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
10. 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.
11. 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.

Further reading

• Yang, C.; Pring, M.; Wear, M. A.; Huang, M.; Cooper, J. A.; Svitkina, T. M.; Zigmond, S. H. (2005). "Mammalian CARMIL Inhibits Actin Filament Capping by Capping Protein". Developmental Cell 9 (2): 209–221. doi:10.1016/j.devcel.2005.06.008. PMC 2628720. PMID 16054028.
• Liang, Y.; Niederstrasser, H.; Edwards, M.; Jackson, C. E.; Cooper, J. A. (2009). "Distinct Roles for CARMIL Isoforms in Cell Migration". Molecular Biology of the Cell 20 (24): 5290–5305. doi:10.1091/mbc.E08-10-1071. PMC 2793302. PMID 19846667.
• Gunjaca, G.; Boban, M.; Pehlić, M.; Zemunik, T.; Budimir, D.; Kolcić, I.; Lauc, G.; Rudan, I.; Polasek, O. (2010). "Predictive Value of 8 Genetic Loci for Serum Uric Acid Concentration". Croatian medical journal 51 (1): 23–31. doi:10.3325/cmj.2010.51.23. PMC 2829178. PMID 20162742.