Detail Information for IndEnz0005000276
IED ID IndEnz0005000276
Enzyme Type ID lipase000276
Protein Name Katanin p60 ATPase-containing subunit A1
Katanin p60 subunit A1
EC 5.6.1.1
Lipotransin
p60 katanin
Gene Name Katna1
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MSLQMIVENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTHLRQKWQQVWQEINVEAKQVKDIMKTLESFKLDITSLQAAQHELPAAEGEVWSLPVPVERRPLPGPRKRQSSQHSDPKPHSNRPSTVVRAHRPSPQNLHNDRGKAVRSREKKEQSKGREEKNKLPAAVTEPEANKFDGTGYDKDLVEALERDIISQNPNVRWYDIADLVEAKKLLQEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRMKAELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPSAKGREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRNLSREAMHMPTTMEDFEMALKKISKSVSAADIERYEKWIVEFGSC
Enzyme Length 491
Uniprot Accession Number Q9WV86
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: ATPase activity is stimulated by microtubules, which promote homooligomerization. ATP-dependent microtubule severing is stimulated by interaction with KATNB1. {ECO:0000255|HAMAP-Rule:MF_03023}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=n ATP + n H(2)O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03023};
DNA Binding
EC Number 5.6.1.1
Enzyme Function FUNCTION: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. The function in regulating microtubule dynamics at spindle poles seems to depend on the association of the katanin KATNA1:KATNB1 complex with ASPM which recruits it to microtubules. Reversely KATNA1:KATNB1 can enhance ASPM blocking activity on microtubule minus-end growth. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:28436967}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 249..256; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_03023
Features Chain (1); Compositional bias (3); Helix (3); Modified residue (1); Mutagenesis (2); Nucleotide binding (1); Region (4)
Keywords 3D-structure;ATP-binding;Cell cycle;Cell division;Cytoplasm;Cytoskeleton;Isomerase;Microtubule;Mitosis;Nucleotide-binding;Phosphoprotein;Reference proteome;Ubl conjugation
Interact With Q8BG40
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03023}. Midbody {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O75449}. Note=Predominantly cytoplasmic. Localized diffusely in the cytoplasm during the interphase. During metaphase is localized throughout the cell and more widely dispersed than the microtubules. In anaphase and telophase is localized at the midbody region. Also localized to the interphase centrosome and the mitotic spindle poles. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1 (By similarity). Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis (By similarity). {ECO:0000250|UniProtKB:O75449, ECO:0000255|HAMAP-Rule:MF_03023}.
Modified Residue MOD_RES 42; /note="Phosphoserine; by DYRK2"; /evidence="ECO:0000250|UniProtKB:O75449, ECO:0000255|HAMAP-Rule:MF_03023"
Post Translational Modification PTM: Phosphorylation by DYRK2 triggers ubiquitination and subsequent degradation. {ECO:0000255|HAMAP-Rule:MF_03023}.; PTM: Ubiquitinated by the BCR(KLHL42) E3 ubiquitin ligase complex, leading to its proteasomal degradation. Ubiquitinated by the EDVP E3 ligase complex and subsequently targeted for proteasomal degradation. {ECO:0000255|HAMAP-Rule:MF_03023}.
Signal Peptide
Structure 3D X-ray crystallography (3); NMR spectroscopy (1)
Cross Reference PDB 2RPA; 5LB7; 5NBT; 6GZC;
Mapped Pubmed ID 10893253; 11217851; 12466851; 12520002; 14610273; 15944385; 16203747; 18799693; 20339000; 20463617; 20530212; 21267068; 21677750; 22325007; 23126280; 25521379; 25535916; 29097679; 31353241; 31685876; 34059773; 34608154;
Motif
Gene Encoded By
Mass 55,949
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 5.6.1.1;