KTNA1_MOUSE
ID KTNA1_MOUSE Reviewed; 491 AA.
AC Q9WV86;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Katanin p60 ATPase-containing subunit A1 {ECO:0000255|HAMAP-Rule:MF_03023};
DE Short=Katanin p60 subunit A1 {ECO:0000255|HAMAP-Rule:MF_03023};
DE EC=5.6.1.1 {ECO:0000255|HAMAP-Rule:MF_03023};
DE AltName: Full=Lipotransin;
DE AltName: Full=p60 katanin {ECO:0000255|HAMAP-Rule:MF_03023};
GN Name=Katna1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10445032; DOI=10.1016/s1097-2765(00)80192-6;
RA Syu L.-J., Saltiel A.R.;
RT "Lipotransin: a novel docking protein for hormone-sensitive lipase.";
RL Mol. Cell 4:109-115(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=15215300; DOI=10.1523/jneurosci.1382-04.2004;
RA Karabay A., Yu W., Solowska J.M., Baird D.H., Baas P.W.;
RT "Axonal growth is sensitive to the levels of katanin, a protein that severs
RT microtubules.";
RL J. Neurosci. 24:5778-5788(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-78 IN COMPLEX WITH KATNB1,
RP FUNCTION, INTERACTION WITH ASPM, AND MUTAGENESIS OF LEU-18 AND LEU-19.
RX PubMed=28436967; DOI=10.1038/ncb3511;
RA Jiang K., Rezabkova L., Hua S., Liu Q., Capitani G., Maarten Altelaar A.F.,
RA Heck A.J.R., Kammerer R.A., Steinmetz M.O., Akhmanova A.;
RT "Microtubule minus-end regulation at spindle poles by an ASPM-katanin
RT complex.";
RL Nat. Cell Biol. 19:480-492(2017).
CC -!- FUNCTION: Catalytic subunit of a complex which severs microtubules in
CC an ATP-dependent manner. Microtubule severing may promote rapid
CC reorganization of cellular microtubule arrays and the release of
CC microtubules from the centrosome following nucleation. Microtubule
CC release from the mitotic spindle poles may allow depolymerization of
CC the microtubule end proximal to the spindle pole, leading to poleward
CC microtubule flux and poleward motion of chromosome. The function in
CC regulating microtubule dynamics at spindle poles seems to depend on the
CC association of the katanin KATNA1:KATNB1 complex with ASPM which
CC recruits it to microtubules. Reversely KATNA1:KATNB1 can enhance ASPM
CC blocking activity on microtubule minus-end growth. Microtubule release
CC within the cell body of neurons may be required for their transport
CC into neuronal processes by microtubule-dependent motor proteins. This
CC transport is required for axonal growth. {ECO:0000255|HAMAP-
CC Rule:MF_03023, ECO:0000269|PubMed:28436967}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1)
CC alpha/beta tubulin heterodimers.; EC=5.6.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03023};
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by microtubules,
CC which promote homooligomerization. ATP-dependent microtubule severing
CC is stimulated by interaction with KATNB1. {ECO:0000255|HAMAP-
CC Rule:MF_03023}.
CC -!- SUBUNIT: Can homooligomerize into hexameric rings, which may be
CC promoted by interaction with microtubules. Interacts with KATNB1, which
CC may serve as a targeting subunit (By similarity). Interacts with ASPM;
CC the katanin complex formation KATNA1:KATNB1 is required for the
CC association of ASPM (PubMed:28436967). Interacts with dynein and NDEL1.
CC Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1
CC and DCAF1 proteins (EDVP complex). Interacts with KLHL42 (via the kelch
CC domains). Interacts with CUL3; the interaction is enhanced by KLHL42
CC (By similarity). Interacts with KATNB1 and KATNBL1 (By similarity).
CC Interacts with CAMSAP2 and CAMSAP3; leading to regulate the length of
CC CAMSAP-decorated microtubule stretches (By similarity).
CC {ECO:0000250|UniProtKB:O75449, ECO:0000255|HAMAP-Rule:MF_03023,
CC ECO:0000269|PubMed:28436967}.
CC -!- INTERACTION:
CC Q9WV86; Q8BG40: Katnb1; NbExp=8; IntAct=EBI-7692898, EBI-7692933;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03023}.
CC Midbody {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000255|HAMAP-
CC Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:O75449}. Note=Predominantly cytoplasmic.
CC Localized diffusely in the cytoplasm during the interphase. During
CC metaphase is localized throughout the cell and more widely dispersed
CC than the microtubules. In anaphase and telophase is localized at the
CC midbody region. Also localized to the interphase centrosome and the
CC mitotic spindle poles. Enhanced recruitment to the mitotic spindle
CC poles requires microtubules and interaction with KATNB1 (By
CC similarity). Localizes within the cytoplasm, partially overlapping with
CC microtubules, in interphase and to the mitotic spindle and spindle
CC poles during mitosis (By similarity). {ECO:0000250|UniProtKB:O75449,
CC ECO:0000255|HAMAP-Rule:MF_03023}.
CC -!- DEVELOPMENTAL STAGE: Elevated during early neuronal development.
CC Expressed in dorsal root ganglia and peripheral and central processes
CC of sensory neurons at 13 dpc. Also expressed in neurons and axons of
CC the embryonic tectum at 13 dpc, and in the cerebral cortex at 16 dpc.
CC Highly expressed in layers containing hippocampal neurons at P1, with
CC expression becoming undetectable by P8. {ECO:0000269|PubMed:15215300}.
CC -!- DOMAIN: The N-terminus is sufficient for interaction with microtubules,
CC although high affinity binding to microtubules also requires an intact
CC C-terminal domain and ATP, which promotes oligomerization.
CC {ECO:0000255|HAMAP-Rule:MF_03023}.
CC -!- PTM: Phosphorylation by DYRK2 triggers ubiquitination and subsequent
CC degradation. {ECO:0000255|HAMAP-Rule:MF_03023}.
CC -!- PTM: Ubiquitinated by the BCR(KLHL42) E3 ubiquitin ligase complex,
CC leading to its proteasomal degradation. Ubiquitinated by the EDVP E3
CC ligase complex and subsequently targeted for proteasomal degradation.
CC {ECO:0000255|HAMAP-Rule:MF_03023}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03023}.
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DR EMBL; AF153197; AAD42087.1; -; mRNA.
DR EMBL; BC009136; AAH09136.1; -; mRNA.
DR CCDS; CCDS23689.2; -.
DR PDB; 2RPA; NMR; -; A=1-72.
DR PDB; 5LB7; X-ray; 1.50 A; B=1-78.
DR PDB; 5NBT; X-ray; 2.40 A; B/D=1-78.
DR PDB; 6GZC; X-ray; 2.00 A; B/D=1-78.
DR PDBsum; 2RPA; -.
DR PDBsum; 5LB7; -.
DR PDBsum; 5NBT; -.
DR PDBsum; 6GZC; -.
DR AlphaFoldDB; Q9WV86; -.
DR BMRB; Q9WV86; -.
DR SMR; Q9WV86; -.
DR IntAct; Q9WV86; 2.
DR MINT; Q9WV86; -.
DR STRING; 10090.ENSMUSP00000132514; -.
DR iPTMnet; Q9WV86; -.
DR PhosphoSitePlus; Q9WV86; -.
DR EPD; Q9WV86; -.
DR MaxQB; Q9WV86; -.
DR PaxDb; Q9WV86; -.
DR PRIDE; Q9WV86; -.
DR ProteomicsDB; 264957; -.
DR MGI; MGI:1344353; Katna1.
DR eggNOG; KOG0738; Eukaryota.
DR InParanoid; Q9WV86; -.
DR PhylomeDB; Q9WV86; -.
DR BRENDA; 5.6.1.1; 3474.
DR ChiTaRS; Katna1; mouse.
DR EvolutionaryTrace; Q9WV86; -.
DR PRO; PR:Q9WV86; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9WV86; protein.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0008352; C:katanin complex; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; IDA:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MGI.
DR GO; GO:0070840; F:dynein complex binding; IDA:MGI.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0008568; F:microtubule severing ATPase activity; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IDA:MGI.
DR GO; GO:0001578; P:microtubule bundle formation; IGI:MGI.
DR GO; GO:0051013; P:microtubule severing; IGI:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IPI:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IEA:GOC.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03023; Katanin_p60_A1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR028596; KATNA1.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF116846; SSF116846; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Isomerase; Microtubule; Mitosis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..491
FT /note="Katanin p60 ATPase-containing subunit A1"
FT /id="PRO_0000084595"
FT REGION 1..185
FT /note="Interaction with microtubules; sufficient for
FT microtubule severing activity"
FT /evidence="ECO:0000269|PubMed:28436967"
FT REGION 1..75
FT /note="Interaction with dynein and NDEL1"
FT /evidence="ECO:0000250"
FT REGION 1..29
FT /note="Interaction with KATNB1"
FT REGION 101..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 249..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03023"
FT MOD_RES 42
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0000250|UniProtKB:O75449, ECO:0000255|HAMAP-
FT Rule:MF_03023"
FT MUTAGEN 18
FT /note="L->A: Disrupts KATNA1:KATNB1 interaction with ASPM."
FT /evidence="ECO:0000269|PubMed:28436967"
FT MUTAGEN 19
FT /note="L->A: Disrupts KATNA1:KATNB1 interaction with ASPM."
FT /evidence="ECO:0000269|PubMed:28436967"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:5LB7"
FT HELIX 22..42
FT /evidence="ECO:0007829|PDB:5LB7"
FT HELIX 46..74
FT /evidence="ECO:0007829|PDB:5LB7"
SQ SEQUENCE 491 AA; 55949 MW; 3F02C73FDE94DE42 CRC64;
MSLQMIVENV KLAREYALLG NYDSAMVYYQ GVLDQMNKYL YSVKDTHLRQ KWQQVWQEIN
VEAKQVKDIM KTLESFKLDI TSLQAAQHEL PAAEGEVWSL PVPVERRPLP GPRKRQSSQH
SDPKPHSNRP STVVRAHRPS PQNLHNDRGK AVRSREKKEQ SKGREEKNKL PAAVTEPEAN
KFDGTGYDKD LVEALERDII SQNPNVRWYD IADLVEAKKL LQEAVVLPMW MPEFFKGIRR
PWKGVLMVGP PGTGKTLLAK AVATECKTTF FNVSSSTLTS KYRGESEKLV RLLFEMARFY
SPATIFIDEI DSICSRRGTS EEHEASRRMK AELLVQMDGV GGASENDDPS KMVMVLAATN
FPWDIDEALR RRLEKRIYIP LPSAKGREEL LRISLRELEL ADDVNLASIA ENMEGYSGAD
ITNVCRDASL MAMRRRIEGL TPEEIRNLSR EAMHMPTTME DFEMALKKIS KSVSAADIER
YEKWIVEFGS C
