ID A0A2U3YAG1_LEPWE Unreviewed; 471 AA.
AC A0A2U3YAG1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 2.
DT 27-MAR-2024, entry version 26.
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|RefSeq:XP_006740709.2};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006740709.2};
RN [1] {ECO:0000313|RefSeq:XP_006740709.2}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006740709.2};
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03025}.
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DR RefSeq; XP_006740709.2; XM_006740646.2.
DR AlphaFoldDB; A0A2U3YAG1; -.
DR STRING; 9713.A0A2U3YAG1; -.
DR KEGG; lww:102740304; -.
DR OrthoDB; 276256at2759; -.
DR Proteomes; UP000245341; Unplaced.
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 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; 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; 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:UP000245341}.
FT DOMAIN 269..354
FT /note="ATPase AAA-type core"
FT /evidence="ECO:0000259|Pfam:PF00004"
FT DOMAIN 387..423
FT /note="AAA ATPase AAA+ lid"
FT /evidence="ECO:0000259|Pfam:PF17862"
FT REGION 123..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 53056 MW; D227E11AAC2F8E4C CRC64;
MRKMEQRKMS SPCLLAFNEH RSGVEGLMEL SYQTLKFTHQ AREACEMRTE ARRKNLLVLI
LHYLTQEGYI DAANALEQET KLGLRRFEVC DNIDLETILM EYESYYFVKF QKYPKIVKKA
SDTAENNLPP RSGGKTRRVM SDSCQNLPKI SQQRPRSRTT VGKSGDVKSL HKEHPKQEAV
TNSHAEGADF GLSISGINKG SGEENVRPQK GQIIDFRGLL TDAIKGATSE LGLNSFDCNP
DPSERLLKPL SALIGMNSEM RELAAVVSRV LFELARYHAP STIFLDELES VMSQRGTAPG
GEHEGSLRMK TELLVQMDGL ARSEDLVFVL AASNLPWELD CAMLRRLEKR ILVGLPSREA
RQAMIRHWLP PVSKSRALEL RTQLEYSMLS QETEGYSGSD IKLVCREAAM RPMRKIFSAL
ENHQSESSNL PGIQLDTVTT ADFLDVLAHT KPSAKNLTQR YSAWQSEFES V
//
