ID A0A1L8I2W9_XENLA Unreviewed; 542 AA.
AC A0A1L8I2W9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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.L {ECO:0000313|RefSeq:XP_018106019.1,
GN ECO:0000313|Xenbase:XB-GENE-5827303};
GN Synonyms=KATNAL2 {ECO:0000256|HAMAP-Rule:MF_03025}, katnal2
GN {ECO:0000313|RefSeq:XP_018106019.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018106019.1};
RN [1] {ECO:0000313|RefSeq:XP_018106019.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018106019.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018106019.1};
RG RefSeq;
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 RefSeq; XP_018106019.1; XM_018250530.2.
DR AlphaFoldDB; A0A1L8I2W9; -.
DR STRING; 8355.A0A1L8I2W9; -.
DR PaxDb; 8355-A0A1L8I2W9; -.
DR GeneID; 734847; -.
DR AGR; Xenbase:XB-GENE-5827303; -.
DR CTD; 734847; -.
DR Xenbase; XB-GENE-5827303; katnal2.L.
DR OrthoDB; 276256at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 734847; Expressed in testis and 11 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:UP000186698}.
FT DOMAIN 290..428
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 94..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 298..305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03025"
SQ SEQUENCE 542 AA; 60966 MW; 23F05E64D18182DD CRC64;
MELSYQALRV ASQNREAEEL RTEARRKNLL ILIMHYLLQE GYVDSANSLE QETKISSRRF
EVCDNVDLET ILMEYESYYY IKFQKYPKIT KKALDHDSRV QPKPRSAGKL RRAGSNSTQG
LPRISQQQVI HRPVSSTYYR TNGHQKALSR ENSKQESGGN SPQEASEVGL NVSAISKASG
EGSHTRRRQV IDFRSMIQDT IKGASQEIAL NSLNCNPDPS ERLIKPVGAF IGGNSEMREL
AAVISRDIYL QNPNVRWDDI IGLDAAKRLV KEAVVYPIRY PQLFTGILSP WKGLLLYGPP
GTGKTLLAKA VATECNTTFF NISASTIVSK WRGDSEKLVR VLFELARYHA PSTIFLDELE
SVMSQRGTGP GGEHEGSRRM KTELLVQMDG LARSDDLVFV LAASNLPWEL DYAMLRRLEK
RILVDLPSKE ARQAMIQHWL PPISNSSGVE LRTDLDYSTL GEETDGYSGS DIRLVCKEAA
MRPVRKIFDA LENHHSEHKK LPVISLETVT TSDFSEVLAH TKPSAKSLAE KYSAWQNEFE
SV
//