Primary Information |
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| BoMiProt ID | Bomi6679 |
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| Protein Name | KN motif and ankyrin repeat domain-containing protein 2/Ankyrin repeat domain-containing protein 25 |
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| Organism | Bos taurus |
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| Uniprot ID | Q1LZH7 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001069999.1 |
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| Aminoacid Length | 858 |
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| Molecular Weight | 91957 |
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| FASTA Sequence |
Download |
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| Gene Name | KANK2/ANKRD25 |
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| Gene ID | 767586 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | KANK proteins are localised mainly to the plasma membrane in focal adhesions, indirectly affecting RhoA and Rac1 thus regulating actin cytoskeleton. In addition, Kank proteins are part of the cortical microtubule stabilisation complex regulating microtubules. |
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| Biochemical Properties | KN motif and ankyrin repeat domain-containing protein 1 (KANK1), a member of KANK family, recruits kinesin family member 21A (KIF21A) to the cell cortex to control microtubule growth via its C-terminal ankyrin domain.A stretch of ∼22 amino acids in KIF21A is sufficient for binding to KANK1 and its close homolog KANK2. Kank (Kank1)-associated members, Kank2, Kank3 and Kank4, which were found by domain and phylogenetic analyses. Besides the conserved ankyrin-repeat and coiled-coil domains, there was a conserved motif at the N-terminal (KN motif) containing potential motifs for nuclear localization and export signals. |
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| PTMs | Methy at Arg,Phosphorylation at Ser/Thr |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q1LZH7|KANK2_BOVIN KN motif and ankyrin repeat domain-containing protein 2 OS=Bos taurus OX=9913 GN=KANK2 PE=2 SV=1
MAQVLHVSAPFPGTPGPAS*19PPAFPSKEPDVPYSVETPYGYRLDLDFLKYVDDIEKGHTLR
RVAVQRRPRLGSLPRGPGSWWTS*83TES*86LCS*89NAS*92GDSRHSAYSYCGRGFYPQYGALETRGGF
NPRVERTLLDARRRLEDQAAAPAGLGSLTPSAAGSTSSLVGVGLPPPT*168PRGSGLSTPVPP
SAGHLAHVREQMAGALRKLRQLEEQVKLIPVLQVKLSVLQEEKRQLTVQLKSQKFLGHPA
GARGRGELCLDLPEAPEDPVTLETRSVGTWVRERDLGMPDGEAALAAKVAVLETQLKKAL
QELQAAQARQADLPPQAWPPPDS*323PVRVDT*329VRVVQGPREVEVAASTAAGAPAQRAQS*356LEPY
GAGLRALATSNGAES*375PPVFRSHEVMETVFPAPTASTSNVHQVKKISITERSCDGAAGHPQ
APAESSLSPPESEGATQAQPEKNTGQVPAHDDTTIKEPIRQAACHESEFEEAGGAGGAQA
GLRSIMKQKEEPTDPEAHRRSLQFVGVNGSISPRYESSSEDSSTAENFSDNESTENEAPE
PEERVPS*547VAEAPQLRPKET*559AKAKTSREESQLPQESLHTPTAEGASGSSAKDEIRMELSPD
LISACLALEKYLENPKALTERELKVAYTTVLQEWLRLACRSDAHPELVRRHLVTFRAMSA
RLLDYVVNIADSNGNTALHYSVSHANFPVVQQLLDSGVCQVDKQNRAGYSPIMLTALATL
KTQDDIQTILQLFRLGDVNAKASQAGQTALMLAVSHGRVDVVKALLACEADVNVQDDDGS
TALMCACEHGHKEITALLLAVPSCDISITDRDGSTALMVALDAGHSEIASMLYSRMNIKC
SFAPMSDDESPASSSAEE
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| Predicted Disorder Regions | 303-370, 414-474, 500-573, 842-850 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Additional Comments | The Kank (kidney or KN motif and ankyrin repeat domain-containing) family of proteins has been described as essential for crosstalk between actin and microtubules. |
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| Bibliography | 1.Guo Q, Liao S, Zhu Z, Li Y, Li F, Xu C. Structural basis for the recognition of kinesin family member 21A (KIF21A) by the ankyrin domains of KANK1 and KANK2 proteins. J Biol Chem. 2018 Jan 12;293(2):557-566. doi: 10.1074/jbc.M117.817494. Epub 2017 Nov 28. PMID: 29183992; PMCID: PMC5767861. 2.Zhu Y, Kakinuma N, Wang Y, Kiyama R. Kank proteins: a new family of ankyrin-repeat domain-containing proteins. Biochim Biophys Acta. 2008 Feb;1780(2):128-33. doi: 10.1016/j.bbagen.2007.09.017. Epub 2007 Oct 4. PMID: 17996375. 3.Tadijan A, Samaržija I, Humphries JD, Humphries MJ, Ambriović-Ristov A. KANK family proteins in cancer. Int J Biochem Cell Biol. 2021 Feb;131:105903. doi: 10.1016/j.biocel.2020.105903. Epub 2020 Dec 10. PMID: 33309958. |
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