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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. 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 annotation

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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi249 – 2568ATPUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • cytoplasmic microtubule organization Source: MGI
  • microtubule bundle formation Source: MGI
  • microtubule severing Source: MGI
  • mitotic nuclear division Source: UniProtKB-KW
  • neuron migration Source: MGI
  • protein localization Source: MGI
  • protein ubiquitination Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1344353. Katna1.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Midbody UniRule annotation
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome UniRule annotation
  • Cytoplasmcytoskeletonspindle pole UniRule annotation

  • 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.UniRule annotation

GO - Cellular componenti

  • axon Source: MGI
  • centrosome Source: MGI
  • cytoplasm Source: UniProtKB
  • lipid particle Source: MGI
  • microtubule Source: UniProtKB-KW
  • microtubule organizing center Source: MGI
  • midbody Source: UniProtKB
  • nucleus Source: MGI
  • plasma membrane Source: MGI
  • spindle Source: UniProtKB
  • spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491Katanin p60 ATPase-containing subunit A1PRO_0000084595Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421Phosphoserine; by DYRK2UniRule annotationBy similarity

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.
PhosphoSiteiQ9WV86.

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. Interacts with dynein and NDEL1. Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and VPRBP proteins (EDVP complex). Interacts with KLHL42 (via the kelch domains). Interacts with CUL3; the interaction is enhanced by KLHL42.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
Katnb1Q8BG402EBI-7692898,EBI-7692933

GO - Molecular functioni

  • dynein binding Source: MGI
  • microtubule binding Source: MGI
  • protein heterodimerization activity Source: MGI

Protein-protein interaction databases

IntActiQ9WV86. 1 interaction.
MINTiMINT-8307998.
STRINGi10090.ENSMUSP00000132514.

Structurei

Secondary structure

491
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 33Combined sources
Helixi4 – 1916Combined sources
Helixi23 – 4119Combined sources
Helixi46 – 6924Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RPANMR-A1-72[»]
ProteinModelPortaliQ9WV86.
SMRiQ9WV86. Positions 1-72, 199-488.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WV86.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 185185Interaction with microtubulesAdd
BLAST
Regioni1 – 7575Interaction with dynein and NDEL1By similarityAdd
BLAST
Regioni1 – 2929Interaction with KATNB1Add
BLAST

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

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_03023. Katanin_p60_A1.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR028596. KATNA1.
IPR007330. MIT.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF116846. SSF116846. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RPANMR-A1-72[»]
ProteinModelPortaliQ9WV86.
SMRiQ9WV86. Positions 1-72, 199-488.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9WV86. 1 interaction.
MINTiMINT-8307998.
STRINGi10090.ENSMUSP00000132514.

PTM databases

iPTMnetiQ9WV86.
PhosphoSiteiQ9WV86.

Proteomic databases

EPDiQ9WV86.
MaxQBiQ9WV86.
PaxDbiQ9WV86.
PRIDEiQ9WV86.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1344353. Katna1.

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi3.6.4.3. 3474.

Miscellaneous databases

EvolutionaryTraceiQ9WV86.
PROiQ9WV86.
SOURCEiSearch...

Gene expression databases

CleanExiMM_KATNA1.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_03023. Katanin_p60_A1.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR028596. KATNA1.
IPR007330. MIT.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF116846. SSF116846. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Lipotransin: a novel docking protein for hormone-sensitive lipase."
    Syu L.-J., Saltiel A.R.
    Mol. Cell 4:109-115(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "Axonal growth is sensitive to the levels of katanin, a protein that severs microtubules."
    Karabay A., Yu W., Solowska J.M., Baird D.H., Baas P.W.
    J. Neurosci. 24:5778-5788(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiKTNA1_MOUSE
AccessioniPrimary (citable) accession number: Q9WV86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: November 1, 1999
Last modified: July 6, 2016
This is version 110 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.