UniProt functional annotation for Q9FHN8



	UniProt functional annotation for Q9FHN8

UniProt code: Q9FHN8.

Organism: Arabidopsis thaliana (Mouse-ear cress).

Taxonomy: Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.

Function: Minus-end microtubule-dependent motor protein involved in the regulation of cell division and trichome morphogenesis through microtubules bundling. Possesses basal and microtubule-stimulated ATPase activities. Acts as a hub that brings together microtubules and actin filaments to modulate the cytoskeleton during trichome formation and morphogenesis (PubMed:26287478). Could be involved in the negative regulation of root growth (PubMed:25262228). {ECO:0000269|PubMed:10623599, ECO:0000269|PubMed:14688294, ECO:0000269|PubMed:17951708, ECO:0000269|PubMed:25262228, ECO:0000269|PubMed:26287478, ECO:0000269|PubMed:8636137, ECO:0000269|PubMed:8990207, ECO:0000269|PubMed:9177205, ECO:0000269|PubMed:9418053, ECO:0000269|PubMed:9634584, ECO:0000269|PubMed:9712269}.

Subunit: Homodimer (via C-terminus) (PubMed:23805258). Binds microtubules via its N-terminus containing the MyTH4 domain and binds F-actin via its FERM domain (PubMed:26287478). Interacts with KIPK1 (PubMed:10788494, PubMed:25262228). Interacts with KIPK2 (PubMed:25262228). Interacts with AN (PubMed:11889034). Interacts with AIR9 (PubMed:25908862). Interacts (via C-terminus) with KIC, CAM2, CAM4 and CAM6. KIC and calmodulin show competitive binding to KCBP. Binding to calmodulin inhibits microtubule binding activity. Binding to KIC inhibits microtubule binding activity and microtubule-stimulated ATPase activity. {ECO:0000269|PubMed:10531384, ECO:0000269|PubMed:10623599, ECO:0000269|PubMed:10788494, ECO:0000269|PubMed:11889034, ECO:0000269|PubMed:14688294, ECO:0000269|PubMed:17951708, ECO:0000269|PubMed:19416847, ECO:0000269|PubMed:23805258, ECO:0000269|PubMed:25262228, ECO:0000269|PubMed:25908862, ECO:0000269|PubMed:26287478, ECO:0000269|PubMed:8990207, ECO:0000269|PubMed:9418053, ECO:0000269|PubMed:9634584, ECO:0000269|PubMed:9712269}.

Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:25908862}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:25908862, ECO:0000269|PubMed:9450347}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:25908862, ECO:0000269|PubMed:9450347}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26287478}. Note=Colocalizes with microtubules during preprophase and cytokinesis. In M-phase, locates to the preprophase band then remained in the cotical division site throughout mitotis and cytokinesis. Also detected towards the poles of the anaphase spindle and on the phragmoplast but absent from the metaphase spindle (PubMed:9450347, PubMed:25908862). Colocalizes with microtubules along the trichome branch and colocalizes with F-actin at the branch apex (PubMed:26287478). {ECO:0000269|PubMed:25908862, ECO:0000269|PubMed:26287478, ECO:0000269|PubMed:9450347}.

Tissue specificity: Widely expressed with the highest levels in flowers (PubMed:8636137). Strongly expressed in the root tip (PubMed:25908862). Highly detected in the branch apex of the trichome (PubMed:26287478). {ECO:0000269|PubMed:25908862, ECO:0000269|PubMed:26287478, ECO:0000269|PubMed:8636137}.

Disruption phenotype: Trichomes with reduced branch number (PubMed:9177205, PubMed:25262228, PubMed:26287478). Impairment of trichomes branch tip sharpening due to disrupted transverse cortical F- actin cap (PubMed:26287478). {ECO:0000269|PubMed:25262228, ECO:0000269|PubMed:26287478, ECO:0000269|PubMed:9177205}.

Similarity: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. KIN-14 subfamily. {ECO:0000303|PubMed:16448571}.

Annotations taken from UniProtKB at the EBI.


Organism:		Arabidopsis thaliana (Mouse-ear cress).
Taxonomy:		Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.



Function:		Minus-end microtubule-dependent motor protein involved in the regulation of cell division and trichome morphogenesis through microtubules bundling. Possesses basal and microtubule-stimulated ATPase activities. Acts as a hub that brings together microtubules and actin filaments to modulate the cytoskeleton during trichome formation and morphogenesis (PubMed:26287478). Could be involved in the negative regulation of root growth (PubMed:25262228). {ECO:0000269\|PubMed:10623599, ECO:0000269\|PubMed:14688294, ECO:0000269\|PubMed:17951708, ECO:0000269\|PubMed:25262228, ECO:0000269\|PubMed:26287478, ECO:0000269\|PubMed:8636137, ECO:0000269\|PubMed:8990207, ECO:0000269\|PubMed:9177205, ECO:0000269\|PubMed:9418053, ECO:0000269\|PubMed:9634584, ECO:0000269\|PubMed:9712269}.


Subunit:		Homodimer (via C-terminus) (PubMed:23805258). Binds microtubules via its N-terminus containing the MyTH4 domain and binds F-actin via its FERM domain (PubMed:26287478). Interacts with KIPK1 (PubMed:10788494, PubMed:25262228). Interacts with KIPK2 (PubMed:25262228). Interacts with AN (PubMed:11889034). Interacts with AIR9 (PubMed:25908862). Interacts (via C-terminus) with KIC, CAM2, CAM4 and CAM6. KIC and calmodulin show competitive binding to KCBP. Binding to calmodulin inhibits microtubule binding activity. Binding to KIC inhibits microtubule binding activity and microtubule-stimulated ATPase activity. {ECO:0000269\|PubMed:10531384, ECO:0000269\|PubMed:10623599, ECO:0000269\|PubMed:10788494, ECO:0000269\|PubMed:11889034, ECO:0000269\|PubMed:14688294, ECO:0000269\|PubMed:17951708, ECO:0000269\|PubMed:19416847, ECO:0000269\|PubMed:23805258, ECO:0000269\|PubMed:25262228, ECO:0000269\|PubMed:25908862, ECO:0000269\|PubMed:26287478, ECO:0000269\|PubMed:8990207, ECO:0000269\|PubMed:9418053, ECO:0000269\|PubMed:9634584, ECO:0000269\|PubMed:9712269}.
Subcellular location:		Cytoplasm, cell cortex {ECO:0000269\|PubMed:25908862}. Cytoplasm, cytoskeleton, spindle {ECO:0000269\|PubMed:25908862, ECO:0000269\|PubMed:9450347}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269\|PubMed:25908862, ECO:0000269\|PubMed:9450347}. Cytoplasm, cytoskeleton {ECO:0000269\|PubMed:26287478}. Note=Colocalizes with microtubules during preprophase and cytokinesis. In M-phase, locates to the preprophase band then remained in the cotical division site throughout mitotis and cytokinesis. Also detected towards the poles of the anaphase spindle and on the phragmoplast but absent from the metaphase spindle (PubMed:9450347, PubMed:25908862). Colocalizes with microtubules along the trichome branch and colocalizes with F-actin at the branch apex (PubMed:26287478). {ECO:0000269\|PubMed:25908862, ECO:0000269\|PubMed:26287478, ECO:0000269\|PubMed:9450347}.
Tissue specificity:		Widely expressed with the highest levels in flowers (PubMed:8636137). Strongly expressed in the root tip (PubMed:25908862). Highly detected in the branch apex of the trichome (PubMed:26287478). {ECO:0000269\|PubMed:25908862, ECO:0000269\|PubMed:26287478, ECO:0000269\|PubMed:8636137}.
Disruption phenotype:		Trichomes with reduced branch number (PubMed:9177205, PubMed:25262228, PubMed:26287478). Impairment of trichomes branch tip sharpening due to disrupted transverse cortical F- actin cap (PubMed:26287478). {ECO:0000269\|PubMed:25262228, ECO:0000269\|PubMed:26287478, ECO:0000269\|PubMed:9177205}.
Similarity:		Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. KIN-14 subfamily. {ECO:0000303\|PubMed:16448571}.