KTNA1_CHICK
ID KTNA1_CHICK Reviewed; 492 AA.
AC Q1HGK7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
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};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Korulu S., Yildiz A., Baas P.W., Karabay A.;
RT "Chicken p60-katanin expression during embryonal development.";
RL Submitted (APR-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; DQ486889; ABF21049.1; -; mRNA.
DR RefSeq; NP_001038113.1; NM_001044648.1.
DR AlphaFoldDB; Q1HGK7; -.
DR SMR; Q1HGK7; -.
DR STRING; 9031.ENSGALP00000041928; -.
DR PaxDb; Q1HGK7; -.
DR GeneID; 421626; -.
DR KEGG; gga:421626; -.
DR CTD; 11104; -.
DR VEuPathDB; HostDB:geneid_421626; -.
DR eggNOG; KOG0738; Eukaryota.
DR HOGENOM; CLU_000688_21_1_1; -.
DR InParanoid; Q1HGK7; -.
DR OrthoDB; 717356at2759; -.
DR PhylomeDB; Q1HGK7; -.
DR TreeFam; TF323170; -.
DR PRO; PR:Q1HGK7; -.
DR Proteomes; UP000000539; Unplaced.
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 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; Reference proteome.
FT CHAIN 1..492
FT /note="Katanin p60 ATPase-containing subunit A1"
FT /id="PRO_0000367127"
FT REGION 80..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..186
FT /note="Basic and acidic 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; 56039 MW; 7B2193884DD627CE CRC64;
MSLVMISENV KLAREYALLG NYDSAMVYYQ GVLDQMNKYL YSLRDTYLQQ KWQQVWQEIS
VEAKHVKDIM KMLESFKIDS TPPKASQQEL PAHDAEVWSL PVPAERRPSP GPRKRQSAQY
SDCRGHNNRI SAAVRGPHRP SSRNPNDKGK AVRGREKKDQ QNKGKEEKSK STSEISESEP
KKFDSTGYDK DLVEALERDI ISQNPNIRWD DIADLVEAKK LLKEAVVLPM WMPEFFKGIR
RPWKGVLMVG PPGTGKTLLA KAVATECKTT FFNVSSSTLT SKYRGESEKL VRLLFEMARF
YAPTTIFIDE IDSICSRRGT SEEHEASRRV KAELLVQMDG VGGATENDDP SKMVMVLAAT
NFPWDIDEAL RRRLEKRIYI PLPSAKGREE LLRINLRELE LADDVDLANI AEKMEGYSGA
DITNVCRDAS LMAMRRRIEG LTPEEIRNLS RDEMHMPTTM EDFEIALKKV SKSVSAADIE
KYEKWIVEFG SC
