KTNA1_XENTR
ID KTNA1_XENTR Reviewed; 492 AA.
AC Q0IIR9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Oviduct;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) 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.
CC {ECO:0000255|HAMAP-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. {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}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250|UniProtKB:O75449}. Note=Predominantly cytoplasmic.
CC Also localized to the interphase centrosome and the mitotic spindle
CC poles. Enhanced recruitment to the mitotic spindle poles requires
CC microtubules and interaction with katnb1. {ECO:0000255|HAMAP-
CC 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; BC121679; AAI21680.1; -; mRNA.
DR RefSeq; NP_001072433.1; NM_001078965.1.
DR AlphaFoldDB; Q0IIR9; -.
DR SMR; Q0IIR9; -.
DR STRING; 8364.ENSXETP00000046241; -.
DR Ensembl; ENSXETT00000046241; ENSXETP00000046241; ENSXETG00000021382.
DR GeneID; 779887; -.
DR KEGG; xtr:779887; -.
DR CTD; 11104; -.
DR Xenbase; XB-GENE-995720; katna1.
DR eggNOG; KOG0738; Eukaryota.
DR InParanoid; Q0IIR9; -.
DR OrthoDB; 717356at2759; -.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000021382; Expressed in testis and 12 other tissues.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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: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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051013; P:microtubule severing; IBA:GO_Central.
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..492
FT /note="Katanin p60 ATPase-containing subunit A1"
FT /id="PRO_0000367129"
FT REGION 91..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 250..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03023"
SQ SEQUENCE 492 AA; 56162 MW; 9DA129246BF0EBD7 CRC64;
MSLLMISENV KLAREYALLG NYDSAMVYYQ GVLDQMNKYL YSVKDTFLQQ KWQQVWQEIN
MEAKHVKDIM STLEGFKLDN SPVKTTQHEF PAHDGEVWSL PVPVERRPSP GPRKRQSVQC
NDNKSHNNRF GAGKGPNLPS SKNTNNVKMK PVRAREKKDT FLKVKDEKNK SSVDVSETEV
KKFDGTGYDK DLIEALERDI ISQNPNIRWD DIADLEEAKK LLKEAVVLPM WMPEFFKGIR
RPWKGVLMVG PPGTGKTLLA KAVATECKTT FFNISSSTLT SKYRGESEKL VRLLFEMARF
YAPTTIFIDE IDSICSRRGT SEEHEASRRV KAELLVQMDG VGGASENEDP SKMVMVLAAT
NFPWDIDEAL RRRLEKRIYI PLPSAKGREE LLRINLKELE LADDVNIECI AENMDGYSGA
DITNVCRDAS LMAMRRRIEG LTPEEIRNLS RDDMHMPTTM EDFEMALKKV SKSVSASDIE
KYEKWIEEFG SC
