KTNA1_STRPU
ID KTNA1_STRPU Reviewed; 516 AA.
AC O61577;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
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 Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 77-100; 136-152;
RP 214-261; 355-373; 402-412; 445-458 AND 462-466.
RX PubMed=9568719; DOI=10.1016/s0092-8674(00)81578-0;
RA Hartman J.J., Mahr J., McNally K., Okawa K., Iwamatsu A., Thomas S.,
RA Cheesman S., Heuser J., Vale R.D., McNally F.J.;
RT "Katanin, a microtubule-severing protein, is a novel AAA ATPase that
RT targets to the centrosome using a WD40-containing subunit.";
RL Cell 93:277-287(1998).
RN [2]
RP FUNCTION, AND INTERACTION WITH KATNB1.
RX PubMed=8221885; DOI=10.1016/0092-8674(93)90377-3;
RA McNally F.J., Vale R.D.;
RT "Identification of katanin, an ATPase that severs and disassembles stable
RT microtubules.";
RL Cell 75:419-429(1993).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=8907702; DOI=10.1242/jcs.109.3.561;
RA McNally F.J., Okawa K., Iwamatsu A., Vale R.D.;
RT "Katanin, the microtubule-severing ATPase, is concentrated at
RT centrosomes.";
RL J. Cell Sci. 109:561-567(1996).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF GLU-334.
RX PubMed=10531065; DOI=10.1126/science.286.5440.782;
RA Hartman J.J., Vale R.D.;
RT "Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme
RT katanin.";
RL Science 286:782-785(1999).
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:10531065,
CC ECO:0000269|PubMed:8221885}.
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.
CC -!- SUBUNIT: Can homooligomerize into hexameric rings, which may be
CC promoted by interaction with microtubules (By similarity). Interacts
CC with KATNB1, which may serve as a targeting subunit (PubMed:8221885).
CC {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:8221885}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03023}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:8907702}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000255|HAMAP-Rule:MF_03023,
CC ECO:0000269|PubMed:8907702}. Note=Predominantly cytoplasmic (By
CC similarity). Also localized to the interphase centrosome and the
CC mitotic spindle poles (PubMed:8907702). Enhanced recruitment to the
CC mitotic spindle poles requires microtubules and interaction with KATNB1
CC (By similarity). {ECO:0000255|HAMAP-Rule:MF_03023,
CC ECO:0000269|PubMed:8907702}.
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; AF052191; AAC15706.1; -; mRNA.
DR RefSeq; NP_999733.1; NM_214568.1.
DR RefSeq; XP_011684098.1; XM_011685796.1.
DR RefSeq; XP_011684100.1; XM_011685798.1.
DR AlphaFoldDB; O61577; -.
DR SMR; O61577; -.
DR STRING; 7668.SPU_008417-tr; -.
DR PRIDE; O61577; -.
DR EnsemblMetazoa; NM_214568; NP_999733; GeneID_373368.
DR EnsemblMetazoa; XM_011685796; XP_011684098; GeneID_373368.
DR EnsemblMetazoa; XM_011685798; XP_011684100; GeneID_373368.
DR GeneID; 373368; -.
DR KEGG; spu:373368; -.
DR CTD; 11104; -.
DR InParanoid; O61577; -.
DR OMA; YEKWMSE; -.
DR OrthoDB; 717356at2759; -.
DR PhylomeDB; O61577; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Isomerase; Microtubule; Mitosis;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..516
FT /note="Katanin p60 ATPase-containing subunit A1"
FT /id="PRO_0000084598"
FT REGION 75..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..125
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 274..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03023"
FT MUTAGEN 334
FT /note="E->Q: Abolishes ATPase and microtubule severing
FT activity; promotes formation of stable oligomers."
FT /evidence="ECO:0000269|PubMed:10531065"
SQ SEQUENCE 516 AA; 57593 MW; A4E573AA643EF57F CRC64;
MSVDEICENT KMGREYALLG NYETSLVYYQ GVLQQIQKLL TSVHEPQRKH QWQTIRQELS
QEYEHVKNIT KTLNGFKSEP AAPEPAPNHR AAPFSHHQHA AKPAAAEPAR DPDVWPPPTP
VDHRPSPPYQ RAARKDPPRR SEPSKPANRA PGNDRGGRGP SDRRGDARSG GGGRGGARGS
DKDKNRGGKS DKDKKAPSGE EGDEKKFDPA GYDKDLVENL ERDIVQRNPN VHWADIAGLT
EAKRLLEEAV VLPLWMPDYF KGIRRPWKGV LMVGPPGTGK TMLAKAVATE CGTTFFNVSS
ASLTSKYHGE SEKLVRLLFE MARFYAPSTI FIDEIDSICS KRGTGSEHEA SRRVKSELLI
QMDGVSGPSA GEESSKMVMV LAATNFPWDI DEALRRRLEK RIYIPLPEID GREQLLRINL
KEVPLADDID LKSIAEKMDG YSGADITNVC RDASMMAMRR RIQGLRPEEI RHIPKEELNQ
PSTPADFLLA LQKVSKSVGK EDLVKYMAWM EEFGSV
