ID A0A455AH78_PHYMC Unreviewed; 537 AA.
AC A0A455AH78;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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_028335855.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028335855.1};
RN [1] {ECO:0000313|RefSeq:XP_028335855.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028335855.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_028335855.1; XM_028480054.2.
DR AlphaFoldDB; A0A455AH78; -.
DR Proteomes; UP000248484; Chromosome 19.
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:UP000248484}.
FT DOMAIN 285..423
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 96..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 293..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03025"
SQ SEQUENCE 537 AA; 60442 MW; D370587BE4A4387C CRC64;
MELSYQTLKF THQAREACEM RTEARRKNLL ILILHYLTQE GYIDAANALE QETKLGLRRF
EVCDNVDLET ILMEYESYYF VKFQKYPKIV KKASDTENNL PQRSGGKTRR VMSDSCQNLP
KISEQRPRSK TTVGKPGGTK PLHREHPKQE LVNHTHKESA DFGLSTSGIN KSSGEENVRP
PKGQIIDFRG LLTDAIKGAT SELGLNSFDC NPDPSERLLK PLSAFIGMNS EMRELAAVVS
RDIYLHNPNI KWNDIIGLDA AKQLVKEAVV YPIRYPQLFT GILSPWKGLL LYGPPGTGKT
LLAKAVATEC KTTFFNISAS TIVSKWRGDS EKLVRVLFEL ARYHAPSTIF LDELESVMSQ
RGTAPGGEHE GSLRMKTELL VQMDGLARSE DLVFVLAASN LPWELDCAML RRLEKRILVD
LPSQEARQAM IHHWLPPVCR SSALELRAEL EYSLLSRETE GYSGSDIKLV CREAAMRPVR
KIFSALENHQ SESSSLPGIQ LDTVTTADFL DVLVHTKPSA KNLTQRYSAW QSEFESV
//
