ID A0A0D9RZH6_CHLSB Unreviewed; 535 AA.
AC A0A0D9RZH6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Katanin p60 ATPase-containing subunit A-like 2 {ECO:0000256|HAMAP-Rule:MF_03025};
DE Short=Katanin p60 subunit A-like 2 {ECO:0000256|HAMAP-Rule:MF_03025};
DE EC=5.6.1.1 {ECO:0000256|HAMAP-Rule:MF_03025};
DE AltName: Full=p60 katanin-like 2 {ECO:0000256|HAMAP-Rule:MF_03025};
GN Name=KATNAL2 {ECO:0000256|HAMAP-Rule:MF_03025,
GN ECO:0000313|Ensembl:ENSCSAP00000014015.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000014015.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000014015.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000014015.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Severs microtubules in vitro in an ATP-dependent manner. This
CC activity may promote rapid reorganization of cellular microtubule
CC arrays. {ECO:0000256|HAMAP-Rule:MF_03025}.
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:0000256|HAMAP-Rule:MF_03025};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-
CC Rule:MF_03025}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03025}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03025}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000256|HAMAP-Rule:MF_03025}.
CC Note=Localizes within the cytoplasm, partially overlapping with
CC microtubules in interphase and to the mitotic spindle and spindle poles
CC during mitosis. {ECO:0000256|HAMAP-Rule:MF_03025}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1
CC subfamily. A-like 2 sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_03025}.
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DR EMBL; AQIB01128024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0D9RZH6; -.
DR STRING; 60711.ENSCSAP00000014015; -.
DR Ensembl; ENSCSAT00000016093.1; ENSCSAP00000014015.1; ENSCSAG00000018001.1.
DR eggNOG; KOG0738; Eukaryota.
DR GeneTree; ENSGT00940000157302; -.
DR OMA; MKTQGKY; -.
DR Proteomes; UP000029965; Chromosome 18.
DR Bgee; ENSCSAG00000018001; Expressed in pituitary gland and 2 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
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:0051013; P:microtubule severing; IEA:UniProtKB-UniRule.
DR CDD; cd19509; RecA-like_VPS4-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_03025; Katanin_p60_AL2; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027497; Katanin_p60_AL2.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23074:SF78; KATANIN P60 ATPASE-CONTAINING SUBUNIT A-LIKE 2; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF08513; LisH; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00667; LisH; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50896; LISH; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03025};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03025};
KW Cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03025};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_03025};
KW Microtubule {ECO:0000256|HAMAP-Rule:MF_03025};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03025};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965}.
FT DOMAIN 283..421
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 92..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 291..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03025"
SQ SEQUENCE 535 AA; 60425 MW; 98734C1E27D3B332 CRC64;
FKSLSLKFTI EKAACEMRTE ARRKNLLILI SHYLTQEGYI DTANALEQET KLGLRRFEVC
DNIDLETILM EYESYYFVKF QKYPKIVKKS SDTAENNLPQ RSGGKTRRVM NDSCQNLPKI
NQQRPRSKTT VGKTGDTKSL NKEHPNQEVV NNTRLESANF GLNISRIGKD SGEENAHPRR
GQIVDFRGLL TDAIKGATSE LALNTFDHNP DPSERLLKPL SAFIGMNSEM RELAAVVSRD
IYLHNPNIKW NDIIGLDAAK QLVKEAVVYP IRYPQLFTGI LSPWKGLLLY GPPGTGKTLL
AKAVATECKT TFFNISASTI VSKWRGDSEK LVRVLFELAR YHAPSTIFLD ELESVMSQRG
TAPGGEHEGS LRMKTELLVQ MDGLAHSEDL VFVLAASNLP WELDCAMLRR LEKRILVDLP
SREARQAMIY HWLPPVSKSR ALELRTELEY SVLSQETEGY SGSDIKLVCR EAAMRPVRKI
FDALENHQSE SSDLPGIQLD TVTTADFLDV LTHTKPSAKN LAQRYSAWQR EFESV
//
