KIF1C

Kinesin-like protein KIF1C is a protein that in humans is encoded by the KIF1C gene.[5][6] Kif1C is a fast, plus-end directed microtubule motor.[7] Kif1C transports α5β1-integrins in human cells.[8] Kif1C has been shown to be non-essential in mouse with other proteins able to perform the same function.[9] However, mutations in KIF1C lead to spastic paraplegia and cerebellar dysfunction in humans.[10][11][12][13]

KIF1C
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2G1L
Identifiers
Aliases	KIF1C, LTXS1, SATX2, SAX2, SPAX2, SPG58, kinesin family member 1C
External IDs	OMIM: 603060 MGI: 1098260 HomoloGene: 4821 GeneCards: KIF1C
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17p13.2 Start 4,997,950 bp[1] End 5,028,401 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 B3 Start 70,700,548 bp[2] End 70,731,964 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • microtubule binding • microtubule motor activity • nucleotide binding • ATPase activity • cellular motor activity • GO:0001948 protein binding • ATP binding • RNA binding • ATP-dependent microtubule motor activity, plus-end-directed Cellular component • cytoplasm • Golgi apparatus • microtubules • cytoskeleton • endoplasmic reticulum • kinesin complex • axon • dendrite • neuron projection • axon cytoplasm Biological process • cytoskeleton-dependent intracellular transport • microtubule-based movement • retrograde vesicle-mediated transport, Golgi to ER • vesicle-mediated transport • anterograde neuronal dense core vesicle transport • retrograde neuronal dense core vesicle transport Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10749	16562
Ensembl	ENSG00000129250	ENSMUSG00000020821
UniProt	O43896	O35071
RefSeq (mRNA)	NM_006612	NM_153103
RefSeq (protein)	NP_006603	NP_694743
Location (UCSC)	Chr 17: 5 – 5.03 Mb	Chr 11: 70.7 – 70.73 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

KIF1C has been shown to interact with PTPN21[5] and YWHAG.[14] KIF1C is a dimeric molecule that is held in an autoinhibited state by interaction of its stalk with the microtubule binding interface of the motor domain. Upon binding of PTPN21 or the cargo adapter HOOK3 to the KIF1C stalk, the motor domain is released, engages with microtubules and commences transport.[15]

References

1. GRCh38: Ensembl release 89: ENSG00000129250 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020821 - 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. Dorner C, Ciossek T, Müller S, Møller PH, Ullrich A, Lammers R (August 1998). "Characterization of KIF1C, a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum". The Journal of Biological Chemistry. 273 (32): 20267–75. doi:10.1074/jbc.273.32.20267. PMID 9685376.
6. "Entrez Gene: KIF1C kinesin family member 1C".
7. Rogers KR, Weiss S, Crevel I, Brophy PJ, Geeves M, Cross R (September 2001). "KIF1D is a fast non-processive kinesin that demonstrates novel K-loop-dependent mechanochemistry". The EMBO Journal. 20 (18): 5101–13. doi:10.1093/emboj/20.18.5101. PMC 125638. PMID 11566875.
8. Theisen U, Straube E, Straube A (December 2012). "Directional persistence of migrating cells requires Kif1C-mediated stabilization of trailing adhesions". Developmental Cell. 23 (6): 1153–66. doi:10.1016/j.devcel.2012.11.005. PMID 23237952.
9. Nakajima K, Takei Y, Tanaka Y, Nakagawa T, Nakata T, Noda Y, et al. (February 2002). "Molecular motor KIF1C is not essential for mouse survival and motor-dependent retrograde Golgi apparatus-to-endoplasmic reticulum transport". Molecular and Cellular Biology. 22 (3): 866–73. doi:10.1128/MCB.22.3.866-873.2002. PMC 133549. PMID 11784862.
10. Caballero Oteyza A, Battaloğlu E, Ocek L, Lindig T, Reichbauer J, Rebelo AP, et al. (June 2014). "Motor protein mutations cause a new form of hereditary spastic paraplegia". Neurology. 82 (22): 2007–16. doi:10.1212/WNL.0000000000000479. PMC 4105256. PMID 24808017.
11. Dor T, Cinnamon Y, Raymond L, Shaag A, Bouslam N, Bouhouche A, et al. (February 2014). "KIF1C mutations in two families with hereditary spastic paraparesis and cerebellar dysfunction". Journal of Medical Genetics. 51 (2): 137–42. doi:10.1136/jmedgenet-2013-102012. PMID 24319291. S2CID 24214406.
12. Yücel-Yılmaz D, Yücesan E, Yalnızoğlu D, Oğuz KK, Sağıroğlu MŞ, Özbek U, et al. (June 2018). "Clinical phenotype of hereditary spastic paraplegia due to KIF1C gene mutations across life span". Brain & Development. 40 (6): 458–464. doi:10.1016/j.braindev.2018.02.013. PMID 29544888. S2CID 3892411.
13. Marchionni E, Méneret A, Keren B, Melki J, Denier C, Durr A, et al. (2019). "KIF1C Variants Are Associated with Hypomyelination, Ataxia, Tremor, and Dystonia in Fraternal Twins". Tremor and Other Hyperkinetic Movements. 9. doi:10.7916/tohm.v0.641. PMC 6692767. PMID 31413903.
14. Dorner C, Ullrich A, Häring HU, Lammers R (November 1999). "The kinesin-like motor protein KIF1C occurs in intact cells as a dimer and associates with proteins of the 14-3-3 family". The Journal of Biological Chemistry. 274 (47): 33654–60. doi:10.1074/jbc.274.47.33654. PMID 10559254.
15. Siddiqui N, Zwetsloot AJ, Bachmann A, Roth D, Hussain H, Brandt J, et al. (June 2019). "PTPN21 and Hook3 relieve KIF1C autoinhibition and activate intracellular transport". Nature Communications. 10 (1): 2693. Bibcode:2019NatCo..10.2693S. doi:10.1038/s41467-019-10644-9. PMC 6584639. PMID 31217419.

Further reading

• Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, et al. (June 1998). "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Research. 5 (3): 169–76. doi:10.1093/dnares/5.3.169. PMID 9734811.
• Dorner C, Ullrich A, Häring HU, Lammers R (November 1999). "The kinesin-like motor protein KIF1C occurs in intact cells as a dimer and associates with proteins of the 14-3-3 family". The Journal of Biological Chemistry. 274 (47): 33654–60. doi:10.1074/jbc.274.47.33654. PMID 10559254.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, et al. (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.
• Kopp P, Lammers R, Aepfelbacher M, Woehlke G, Rudel T, Machuy N, et al. (June 2006). "The kinesin KIF1C and microtubule plus ends regulate podosome dynamics in macrophages". Molecular Biology of the Cell. 17 (6): 2811–23. doi:10.1091/mbc.E05-11-1010. PMC 1474789. PMID 16554367.
• Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (October 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243. S2CID 14294292.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.

External links

• Overview of all the structural information available in the PDB for UniProt: O43896 (Kinesin-like protein KIF1C) at the PDBe-KB.