KTNA1_MACFA
ID KTNA1_MACFA Reviewed; 491 AA.
AC Q4R407;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 {ECO:0000255|HAMAP-Rule:MF_03023}; ORFNames=QtsA-12977;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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 Interacts with CAMSAP2 and CAMSAP3; leading to regulate the length of
CC CAMSAP-decorated microtubule stretches (By similarity).
CC {ECO:0000250|UniProtKB:O75449, ECO:0000250|UniProtKB:Q9WV86,
CC ECO:0000255|HAMAP-Rule:MF_03023}.
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 -!- 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; AB179108; BAE02159.1; -; mRNA.
DR RefSeq; NP_001272255.1; NM_001285326.1.
DR AlphaFoldDB; Q4R407; -.
DR SMR; Q4R407; -.
DR STRING; 9541.XP_005552153.1; -.
DR Ensembl; ENSMFAT00000033496; ENSMFAP00000025348; ENSMFAG00000044145.
DR GeneID; 101864950; -.
DR CTD; 11104; -.
DR eggNOG; KOG0738; Eukaryota.
DR GeneTree; ENSGT00940000156638; -.
DR OrthoDB; 717356at2759; -.
DR Proteomes; UP000233100; Chromosome 4.
DR Bgee; ENSMFAG00000044145; Expressed in lymph node and 13 other tissues.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0008352; C:katanin complex; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
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; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008568; F:microtubule severing ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0051013; P:microtubule severing; IEA:UniProtKB-UniRule.
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; 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 2: Evidence at transcript 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_0000357490"
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..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..140
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 MOD_RES 109
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0000250|UniProtKB:O75449, ECO:0000255|HAMAP-
FT Rule:MF_03023"
FT MOD_RES 133
FT /note="Phosphothreonine; by DYRK2"
FT /evidence="ECO:0000250|UniProtKB:O75449, ECO:0000255|HAMAP-
FT Rule:MF_03023"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75449"
SQ SEQUENCE 491 AA; 55909 MW; F0BCAEFC5A9DC256 CRC64;
MSLLMISENV KLAREYALLG NYDSAMVYYQ GVLDQMNKYL YSVKDTYLQQ KWQQVWQEIN
VEAKHVKDIM KTLESFKLDS TPLKAAQHDL PASEGEVWSM PVPVERRPSP GPRKRQSSQY
SDSKSHGNRP GTTVRVHRSS AQNLHNDRGK AVRCREKKEQ NKGREEKNKS PAAVTEPETN
KFDSTGYDKD LVEALERDII SQNPNVRWDD IADLVEAKKL LKEAVVLPMW MPEFFKGIRR
PWKGVLMVGP PGTGKTLLAK AVATECKTTF FNVSSSTLTS KYRGESEKLV RLLFEMARFY
SPATIFIDEI DSICSRRGTS EEHEASRRVK AELLVQMDGV GGASENDDPS KMVMVLAATN
FPWDIDEALR RRLEKRIYIP LPSAKGREEL LRISLRELEL ADDVDLASIA ENMEGYSGAD
ITNVCRDASL MAMRRRIEGL TPEEIRNLSK EEMHMPTTME DFEMALKKVS KSVSAADIER
YEKWIFEFGS C
