KTNA1_XENLA
ID KTNA1_XENLA Reviewed; 486 AA.
AC Q9PUL2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 99.
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};
DE Flags: Fragment;
GN Name=katna1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RA McNally K.P., Buster D.W., McNally F.J.;
RT "Katanin is regulated by inhibitors that are inactivated by cyclinB/cdk1
RT during mitosis.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9658175; DOI=10.1091/mbc.9.7.1847;
RA McNally F.J., Thomas S.;
RT "Katanin is responsible for the M-phase microtubule-severing activity in
RT Xenopus eggs.";
RL Mol. Biol. Cell 9:1847-1861(1998).
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. In mitotic
CC spindles this could allow depolymerization of the microtubule end
CC proximal to the centrosome, and subsequent poleward microtubule flux.
CC {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:9658175}.
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. {ECO:0000255|HAMAP-Rule:MF_03023}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03023}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle
CC pole {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:9658175}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O75449}.
CC Note=Predominantly cytoplasmic. Also localized to the interphase
CC centrosome and the mitotic spindle poles. Enhanced recruitment to the
CC mitotic spindle poles requires microtubules and interaction with
CC katnb1. {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; AF177942; AAD53310.1; -; mRNA.
DR AlphaFoldDB; Q9PUL2; -.
DR SMR; Q9PUL2; -.
DR IntAct; Q9PUL2; 2.
DR BRENDA; 5.6.1.1; 6725.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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:InterPro.
DR GO; GO:0008568; F:microtubule severing ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051013; P:microtubule severing; IEA:InterPro.
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 Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 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; Reference proteome.
FT CHAIN 1..>486
FT /note="Katanin p60 ATPase-containing subunit A1"
FT /id="PRO_0000084597"
FT REGION 84..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03023"
FT NON_TER 486
SQ SEQUENCE 486 AA; 55430 MW; 32952B49D1B2FDC4 CRC64;
MSLLMISENV KLAREYALLG NYDSAMVYYQ GVLDQMNKYL YSVKDTFLQQ KWQQVWQEIN
MECKHVKDIM STLEGFKLDS SPVKTTQHEF PSHDGEVWSL PVPVERRPSP GPRKRQSVQC
NDNKSHNNRF SAAAKGPNLP SARNANNVKM KPVRAREKKD ALIKNKSSAD VSETEVKRFD
GSGYDKDLIE ALERDIISQN PNIRWDDIAD LEEAKKLLKE AVVLPMWMPE FFKGIRRPWK
GVLMVGPPGT GKTLLAKAVA TECKTTFFNI SSSTLTSKYR GESEKLVRLL FEMARFYAPT
TIFIDEIDSI CSRRGTSEEH EASRRVKAEL LVQMDGVGGA SENEDPSKMV MVLAATNFPW
DIDEALRRRL EKRIYIPLPS AKGREELLRI NLKELELADD VNIECIAENM DGYSGADITN
VCRDASLMAM RRRIEGLTPE EIRNLSRDDM HMPTTMEDFE MALKKVSKSV SASDIEKYEK
WIFEFG
