KTNA1_RAT
ID KTNA1_RAT Reviewed; 491 AA.
AC Q6E0V2; Q4V7G3;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=p60 katanin {ECO:0000255|HAMAP-Rule:MF_03023};
GN Name=Katna1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF LYS-255.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10209026; DOI=10.1083/jcb.145.2.305;
RA Ahmad F.J., Yu W., McNally F.J., Baas P.W.;
RT "An essential role for katanin in severing microtubules in the neuron.";
RL J. Cell Biol. 145:305-315(1999).
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. 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:10209026,
CC ECO:0000269|PubMed:15215300}.
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 (By similarity). 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 {ECO:0000250|UniProtKB:O75449, ECO:0000250|UniProtKB:Q9WV86,
CC ECO:0000255|HAMAP-Rule:MF_03023}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Midbody {ECO:0000255|HAMAP-
CC Rule:MF_03023}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome. Cytoplasm, cytoskeleton, spindle pole {ECO:0000255|HAMAP-
CC 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). Interacts with CAMSAP2 and
CC CAMSAP3; leading to regulate the length of CAMSAP-decorated microtubule
CC stretches (By similarity). {ECO:0000250|UniProtKB:O75449,
CC ECO:0000255|HAMAP-Rule:MF_03023}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY621629; AAT44333.1; -; mRNA.
DR EMBL; BC097929; AAH97929.1; -; mRNA.
DR RefSeq; NP_001004217.2; NM_001004217.4.
DR AlphaFoldDB; Q6E0V2; -.
DR SMR; Q6E0V2; -.
DR BioGRID; 253846; 16.
DR STRING; 10116.ENSRNOP00000020417; -.
DR jPOST; Q6E0V2; -.
DR PaxDb; Q6E0V2; -.
DR PRIDE; Q6E0V2; -.
DR GeneID; 292464; -.
DR KEGG; rno:292464; -.
DR UCSC; RGD:1303062; rat.
DR CTD; 11104; -.
DR RGD; 1303062; Katna1.
DR eggNOG; KOG0738; Eukaryota.
DR InParanoid; Q6E0V2; -.
DR OrthoDB; 717356at2759; -.
DR PhylomeDB; Q6E0V2; -.
DR TreeFam; TF323170; -.
DR BRENDA; 5.6.1.1; 5301.
DR PRO; PR:Q6E0V2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0005811; C:lipid droplet; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; TAS:RGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:RGD.
DR GO; GO:0070840; F:dynein complex binding; ISO:RGD.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0008568; F:microtubule severing ATPase activity; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISO:RGD.
DR GO; GO:0001578; P:microtubule bundle formation; ISO:RGD.
DR GO; GO:0051013; P:microtubule severing; IDA:RGD.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
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; 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; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Isomerase;
KW Microtubule; Mitosis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..491
FT /note="Katanin p60 ATPase-containing subunit A1"
FT /id="PRO_0000084596"
FT REGION 1..185
FT /note="Interaction with microtubules"
FT /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
FT REGION 87..183
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 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 255
FT /note="K->A: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:15215300"
SQ SEQUENCE 491 AA; 55844 MW; AE85B1B307A37AA4 CRC64;
MSLLMITENV KLAREYALLG NYDSAMVYYQ GVLDQINKYL YSVKDTHLHQ KWQQVWQEIN
VEAKHVKEIM KTLESFKLDS TSLKAAQHEL PSSEGEVWSL PVPVERRPLP GPRKRQSTQH
SDPKPHSNRP GAVVRAHRPS AQSLHSDRGK AVRSREKKEQ SKGREEKNKL PAAVTEPEAN
KFDSTGYDKD LVEALERDII SQNPNVRWYD IADLVEAKKL LQEAVVLPMW MPEFFKGIRR
PWKGVLMVGP PGTGKTLLAK AVATECKTTF FNVSSSTLTS KYRGESEKLV RLLFEMARFY
SPATIFIDEI DSICSRRGTS EEHEASRRVK AELLVQMDGV GGASENDDPS KMVMVLAATN
FPWDIDEALR RRLEKRIYIP LPSAKGREEL LRISLRELEL ADDVNLASIA ENMEGYSGAD
ITNVCRDASL MAMRRRIEGL TPEEIRNLSR EEMHMPTTME DFEMALKKVS KSVSAADIER
YEKWIVEFGS C
