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Protein

Katanin p60 ATPase-containing subunit A1

Gene

Katna1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation

Enzyme regulationi

ATPase activity is stimulated by microtubules, which promote homooligomerization. ATP-dependent microtubule severing is stimulated by interaction with KATNB1.UniRule annotation

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi249 – 256ATPUniRule annotation8

GO - Molecular functioni

  • ATPase activity Source: MGI
  • ATP binding Source: UniProtKB-KW
  • dynein complex binding Source: MGI
  • microtubule binding Source: MGI
  • microtubule-severing ATPase activity Source: UniProtKB-EC
  • protein heterodimerization activity Source: MGI

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cytoplasmic microtubule organization Source: MGI
  • microtubule bundle formation Source: MGI
  • microtubule severing Source: MGI
  • neuron migration Source: MGI
  • protein localization Source: MGI
  • protein ubiquitination Source: GOC

Keywordsi

Molecular functionHydrolase
Biological processCell cycle, Cell division, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.4.3. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Katanin p60 ATPase-containing subunit A1UniRule annotation (EC:3.6.4.3UniRule annotation)
Short name:
Katanin p60 subunit A1UniRule annotation
Alternative name(s):
Lipotransin
p60 kataninUniRule annotation
Gene namesi
Name:Katna1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1344353. Katna1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi18L → A: Disrupts KATNA1:KATNB1 interaction with ASPM. 1 Publication1
Mutagenesisi19L → A: Disrupts KATNA1:KATNB1 interaction with ASPM. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000845951 – 491Katanin p60 ATPase-containing subunit A1Add BLAST491

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei42Phosphoserine; by DYRK2UniRule annotationBy similarity1

Post-translational modificationi

Phosphorylation by DYRK2 triggers ubiquitination and subsequent degradation.UniRule annotation
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.UniRule annotation

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9WV86.
MaxQBiQ9WV86.
PaxDbiQ9WV86.
PRIDEiQ9WV86.

PTM databases

iPTMnetiQ9WV86.
PhosphoSitePlusiQ9WV86.

Expressioni

Developmental stagei

Elevated during early neuronal development. Expressed in dorsal root ganglia and peripheral and central processes of sensory neurons at E13. Also expressed in neurons and axons of the embryonic tectum at E13, and in the cerebral cortex at E16. Highly expressed in layers containing hippocampal neurons at P1, with expression becoming undetectable by P8.1 Publication

Gene expression databases

CleanExiMM_KATNA1.

Interactioni

Subunit structurei

Can homooligomerize into hexameric rings, which may be promoted by interaction with microtubules. Interacts with KATNB1, which may serve as a targeting subunit (By similarity). Interacts with ASPM; the katanin complex formation KATNA1:KATNB1 is required for the association of ASPM (PubMed:28436967). Interacts with dynein and NDEL1. Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1 proteins (EDVP complex). Interacts with KLHL42 (via the kelch domains). Interacts with CUL3; the interaction is enhanced by KLHL42 (By similarity). Interacts with KATNB1 and KATNBL1 (By similarity). Interacts with CAMSAP2 and CAMSAP3; leading to regulate the length of CAMSAP-decorated microtubule stretches (By similarity).UniRule annotationBy similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Katnb1Q8BG408EBI-7692898,EBI-7692933

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9WV86. 2 interactors.
MINTiMINT-8307998.
STRINGi10090.ENSMUSP00000132514.

Structurei

Secondary structure

1491
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 18Combined sources16
Helixi22 – 42Combined sources21
Helixi46 – 74Combined sources29

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RPANMR-A1-72[»]
5LB7X-ray1.50B1-78[»]
5NBTX-ray2.40B/D1-78[»]
ProteinModelPortaliQ9WV86.
SMRiQ9WV86.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WV86.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 185Interaction with microtubules; sufficient for microtubule severing activity1 PublicationAdd BLAST185
Regioni1 – 75Interaction with dynein and NDEL1By similarityAdd BLAST75
Regioni1 – 29Interaction with KATNB1Add BLAST29

Domaini

The N-terminus is sufficient for interaction with microtubules, although high affinity binding to microtubules also requires an intact C-terminal domain and ATP, which promotes oligomerization.UniRule annotation

Sequence similaritiesi

Belongs to the AAA ATPase family. Katanin p60 subunit A1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG0738. Eukaryota.
ENOG410XPN7. LUCA.
HOGENOMiHOG000225142.
HOVERGENiHBG057074.
InParanoidiQ9WV86.
PhylomeDBiQ9WV86.

Family and domain databases

HAMAPiMF_03023. Katanin_p60_A1. 1 hit.
InterProiView protein in InterPro
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR028596. KATNA1.
IPR036181. MIT_dom_sf.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
PfamiView protein in Pfam
PF00004. AAA. 1 hit.
PF09336. Vps4_C. 1 hit.
SMARTiView protein in SMART
SM00382. AAA. 1 hit.
SUPFAMiSSF116846. SSF116846. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiView protein in PROSITE
PS00674. AAA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9WV86-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLQMIVENV KLAREYALLG NYDSAMVYYQ GVLDQMNKYL YSVKDTHLRQ
60 70 80 90 100
KWQQVWQEIN VEAKQVKDIM KTLESFKLDI TSLQAAQHEL PAAEGEVWSL
110 120 130 140 150
PVPVERRPLP GPRKRQSSQH SDPKPHSNRP STVVRAHRPS PQNLHNDRGK
160 170 180 190 200
AVRSREKKEQ SKGREEKNKL PAAVTEPEAN KFDGTGYDKD LVEALERDII
210 220 230 240 250
SQNPNVRWYD IADLVEAKKL LQEAVVLPMW MPEFFKGIRR PWKGVLMVGP
260 270 280 290 300
PGTGKTLLAK AVATECKTTF FNVSSSTLTS KYRGESEKLV RLLFEMARFY
310 320 330 340 350
SPATIFIDEI DSICSRRGTS EEHEASRRMK AELLVQMDGV GGASENDDPS
360 370 380 390 400
KMVMVLAATN FPWDIDEALR RRLEKRIYIP LPSAKGREEL LRISLRELEL
410 420 430 440 450
ADDVNLASIA ENMEGYSGAD ITNVCRDASL MAMRRRIEGL TPEEIRNLSR
460 470 480 490
EAMHMPTTME DFEMALKKIS KSVSAADIER YEKWIVEFGS C
Length:491
Mass (Da):55,949
Last modified:November 1, 1999 - v1
Checksum:i3F02C73FDE94DE42
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF153197 mRNA. Translation: AAD42087.1.
BC009136 mRNA. Translation: AAH09136.1.
UniGeneiMm.28127.
Mm.421297.

Similar proteinsi

Entry informationi

Entry nameiKTNA1_MOUSE
AccessioniPrimary (citable) accession number: Q9WV86
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: November 1, 1999
Last modified: November 22, 2017
This is version 121 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families