ID   KATL2_XENLA             Reviewed;         505 AA.
AC   Q3B8D5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Katanin p60 ATPase-containing subunit A-like 2 {ECO:0000255|HAMAP-Rule:MF_03025};
DE            Short=Katanin p60 subunit A-like 2 {ECO:0000255|HAMAP-Rule:MF_03025};
DE            EC=5.6.1.1 {ECO:0000255|HAMAP-Rule:MF_03025};
DE   AltName: Full=p60 katanin-like 2 {ECO:0000255|HAMAP-Rule:MF_03025};
GN   Name=katnal2;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Severs microtubules in vitro in an ATP-dependent manner. This
CC       activity may promote rapid reorganization of cellular microtubule
CC       arrays. {ECO:0000255|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:0000255|HAMAP-Rule:MF_03025};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC       Rule:MF_03025}. Cytoplasm {ECO:0000250|UniProtKB:Q8IYT4}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8IYT4}. Cytoplasm,
CC       cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q8IYT4}.
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:0000250|UniProtKB:Q8IYT4}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1
CC       subfamily. A-like 2 sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03025}.
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DR   EMBL; BC106552; AAI06553.1; -; mRNA.
DR   RefSeq; NP_001089782.1; NM_001096313.1.
DR   AlphaFoldDB; Q3B8D5; -.
DR   SMR; Q3B8D5; -.
DR   MaxQB; Q3B8D5; -.
DR   DNASU; 734847; -.
DR   GeneID; 734847; -.
DR   KEGG; xla:734847; -.
DR   CTD; 734847; -.
DR   Xenbase; XB-GENE-5827303; katnal2.L.
DR   OrthoDB; 787710at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 734847; Expressed in testis and 11 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; 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:0051013; P:microtubule severing; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 2.
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   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; SSF52540; 1.
DR   PROSITE; PS50896; LISH; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Isomerase; Microtubule;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..505
FT                   /note="Katanin p60 ATPase-containing subunit A-like 2"
FT                   /id="PRO_0000333794"
FT   DOMAIN          25..57
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03025"
FT   REGION          94..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..127
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:0000255|HAMAP-Rule:MF_03025"
SQ   SEQUENCE   505 AA;  56827 MW;  91F7F9D6BCACD13B CRC64;
     MELSYQALRV ASQNREAEEL RTEARRKNLL ILIMHYLLQE GYVDSANSLE QETKISSRRF
     EVCDNVDLET ILMEYESYYY IKFQKYPKIT KKALDHDSRV QPKPRSAGKL RRAGSNSTQG
     LPRIGQQQVI HRPVSSSYYR TNGHQKALSR ENSKQESGGN SPQEASEVGL NVSAISKASG
     EGSHTRRRQV IDFRSMIQDT IKGASQEIAL NSLNCNPDPS ERLIKPVGAF IGGNSEMREL
     AAVISRDIYL QNPNVRWDDI IGLDAAKRLV KEAVVYPIRY PQLFTGILSP WKGLLLYGPP
     GTGKTLLAKA VATECNTTFF NISASTIVSK WRGDSEKLVR VLFELARYHA PSTIFLDELE
     SVMSQRGTGP GELDYAMLRR LEKRILVDLP SKEARQAMIQ HWLPPISNSS GVELRMDLDY
     STLGEETDGY SGSDIRLVCK EAAMRPVRKI FDALENHHSE HKKLPVISLE TVTTSDFSEV
     LAHTKPSAKS LAEKYSAWQN EFESV