KTNA1_SALSA
ID KTNA1_SALSA Reviewed; 486 AA.
AC B5X3X5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
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 Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
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}.
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; BT045744; ACI34006.1; -; mRNA.
DR RefSeq; NP_001133845.1; NM_001140373.1.
DR RefSeq; XP_014060201.1; XM_014204726.1.
DR AlphaFoldDB; B5X3X5; -.
DR SMR; B5X3X5; -.
DR STRING; 8030.ENSSSAP00000088260; -.
DR GeneID; 100195344; -.
DR KEGG; sasa:100195344; -.
DR CTD; 11104; -.
DR OMA; YSVRDTY; -.
DR OrthoDB; 717356at2759; -.
DR Proteomes; UP000087266; Chromosome ssa06.
DR Bgee; ENSSSAG00000070033; Expressed in ovary and 16 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: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; IEA:UniProtKB-UniRule.
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..486
FT /note="Katanin p60 ATPase-containing subunit A1"
FT /id="PRO_0000367128"
FT REGION 103..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 244..251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03023"
SQ SEQUENCE 486 AA; 55462 MW; CE761BF2A907FA47 CRC64;
MSLHEINENV KLAREYALLG NYSSAIVCYR GVLEQIKKYL FTVRDSSFQQ KWQQVWQEIN
EENNQVQEIM RTLESFQLET TPSKPPSNQD GINDIWPVQV ERRSSPLPVR RPPVPYKDSK
PHNNRLSVAG VRAQHRQSPR GANGDRAKPL KGKEKKEAKP KDDKNKAEVS EKEVKRFDGQ
GYDKDLIEAL ERDIISQNPN VKWDDIADLE EAKKLLKEAV VLPMWMPEFF KGIRRPWKGV
LMVGPPGTGK TLLAKAVATE CRTTFFNVSS STLTSKYRGE SEKLVRILFE MARFYAPTTI
FIDEIDSMCS RRGTSEEHEA SRRVKAELLV QMDGVGGASD NEDPSKMVMV LAATNFPWDI
DEALRRRLEK RIYIPLPSAK GRVELLRINL KELELANDVD MAKIAEQSEG YSGADITNVC
RDASLMAMRR RIEGLTPEEI RNISRAEMHM PTTMEDFESS LKKVSKSVSA SDLEKYEKWI
EEFGSC
