ID M3Z302_MUSPF Unreviewed; 491 AA.
AC M3Z302;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Katanin p60 ATPase-containing subunit A1 {ECO:0000256|HAMAP-Rule:MF_03023};
DE Short=Katanin p60 subunit A1 {ECO:0000256|HAMAP-Rule:MF_03023};
DE EC=5.6.1.1 {ECO:0000256|HAMAP-Rule:MF_03023};
DE AltName: Full=p60 katanin {ECO:0000256|HAMAP-Rule:MF_03023};
GN Name=KATNA1 {ECO:0000256|HAMAP-Rule:MF_03023,
GN ECO:0000313|Ensembl:ENSMPUP00000017964.1,
GN ECO:0000313|RefSeq:XP_004752832.1, ECO:0000313|RefSeq:XP_012911718.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000017964.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000017964.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004752832.1, ECO:0000313|RefSeq:XP_012911718.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004752832.1,
RC ECO:0000313|RefSeq:XP_012911718.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalytic subunit of a complex which severs microtubules in
CC an ATP-dependent manner. Microtubule severing may promote rapid
CC reorganization of cellular microtubule arrays and the release of
CC microtubules from the centrosome following nucleation. Microtubule
CC release from the mitotic spindle poles may allow depolymerization of
CC the microtubule end proximal to the spindle pole, leading to poleward
CC microtubule flux and poleward motion of chromosome. Microtubule release
CC within the cell body of neurons may be required for their transport
CC into neuronal processes by microtubule-dependent motor proteins. This
CC transport is required for axonal growth. {ECO:0000256|HAMAP-
CC Rule:MF_03023}.
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_03023};
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by microtubules,
CC which promote homooligomerization. ATP-dependent microtubule severing
CC is stimulated by interaction with KATNB1. {ECO:0000256|HAMAP-
CC Rule:MF_03023}.
CC -!- SUBUNIT: Can homooligomerize into hexameric rings, which may be
CC promoted by interaction with microtubules. Interacts with KATNB1, which
CC may serve as a targeting subunit. Interacts with ASPM; the katanin
CC complex formation KATNA1:KATNB1 is required for the association of
CC ASPM. Interacts with dynein and NDEL1. Associates with the E3 ligase
CC complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1 proteins (EDVP
CC complex). Interacts with KLHL42 (via the kelch domains). Interacts with
CC CUL3; the interaction is enhanced by KLHL42. Interacts with KATNB1 and
CC KATNBL1. Interacts with CAMSAP2 and CAMSAP3; leading to regulate the
CC length of CAMSAP-decorated microtubule stretches. {ECO:0000256|HAMAP-
CC Rule:MF_03023}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|ARBA:ARBA00004186, ECO:0000256|HAMAP-Rule:MF_03023}.
CC Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03023}. Midbody
CC {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03023}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|HAMAP-
CC Rule:MF_03023}. Note=Predominantly cytoplasmic. Localized diffusely in
CC the cytoplasm during the interphase. During metaphase is localized
CC throughout the cell and more widely dispersed than the microtubules. In
CC anaphase and telophase is localized at the midbody region. Also
CC localized to the interphase centrosome and the mitotic spindle poles.
CC Enhanced recruitment to the mitotic spindle poles requires microtubules
CC and interaction with KATNB1. Localizes within the cytoplasm, partially
CC overlapping with microtubules, in interphase and to the mitotic spindle
CC and spindle poles during mitosis. {ECO:0000256|HAMAP-Rule:MF_03023}.
CC -!- DOMAIN: The N-terminus is sufficient for interaction with microtubules,
CC although high affinity binding to microtubules also requires an intact
CC C-terminal domain and ATP, which promotes oligomerization.
CC {ECO:0000256|HAMAP-Rule:MF_03023}.
CC -!- PTM: Phosphorylation by DYRK2 triggers ubiquitination and subsequent
CC degradation. {ECO:0000256|HAMAP-Rule:MF_03023}.
CC -!- PTM: Ubiquitinated by the BCR(KLHL42) E3 ubiquitin ligase complex,
CC leading to its proteasomal degradation. Ubiquitinated by the EDVP E3
CC ligase complex and subsequently targeted for proteasomal degradation.
CC {ECO:0000256|HAMAP-Rule:MF_03023}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03023}.
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DR EMBL; AEYP01032464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01032465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01032466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01032467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01032468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004752832.1; XM_004752775.3.
DR RefSeq; XP_012911718.1; XM_013056264.2.
DR STRING; 9669.ENSMPUP00000017964; -.
DR Ensembl; ENSMPUT00000018226.1; ENSMPUP00000017964.1; ENSMPUG00000018075.1.
DR GeneID; 101691127; -.
DR KEGG; mpuf:101691127; -.
DR CTD; 11104; -.
DR eggNOG; KOG0738; Eukaryota.
DR GeneTree; ENSGT00940000156638; -.
DR HOGENOM; CLU_000688_21_1_1; -.
DR OMA; PRDEMHM; -.
DR OrthoDB; 276256at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008352; C:katanin complex; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0097431; C:mitotic spindle pole; IEA:Ensembl.
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:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:Ensembl.
DR GO; GO:0051013; P:microtubule severing; IEA:UniProtKB-UniRule.
DR CDD; cd21748; Kp60-NTD; 1.
DR CDD; cd19522; RecA-like_KTNA1; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR HAMAP; MF_03023; Katanin_p60_A1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR028596; KATNA1.
DR InterPro; IPR048611; KATNA1_MIT.
DR InterPro; IPR048612; KTNA1_AAA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Spast_Vps4_C.
DR PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23074:SF71; KATANIN P60 ATPASE-CONTAINING SUBUNIT A1; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF21126; KATNA1_MIT; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03023}; Cell cycle {ECO:0000256|HAMAP-Rule:MF_03023};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_03023};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03023};
KW Cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03023};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_03023};
KW Microtubule {ECO:0000256|HAMAP-Rule:MF_03023};
KW Mitosis {ECO:0000256|HAMAP-Rule:MF_03023};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03023}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03023};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Ubl conjugation {ECO:0000256|HAMAP-Rule:MF_03023}.
FT DOMAIN 241..383
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 97..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 249..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03023"
FT MOD_RES 42
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03023"
FT MOD_RES 109
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03023"
FT MOD_RES 133
FT /note="Phosphothreonine; by DYRK2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03023"
SQ SEQUENCE 491 AA; 55945 MW; C06669C43B7B4071 CRC64;
MSLLMISENV KLAREYALLG NYDSAMVYYQ GVLDQMNKYL YSVKDTYLQQ KWQQVWQEIN
VEAKHVKDIM KTLESFKLDN TPLKAAQHEL PASEGEVWSL PVPVERRPSP GPRKRQSPQY
SDPKPHGNRP GTTVRVHRSS AHNLHNDRGK AVRCREKKEQ SKGREEKNKS PAAVTEPETS
KFDSTGYDKD LVEALERDII SQNPNVRWDD IADLVEAKKL LKEAVVLPMW MPEFFKGIRR
PWKGVLMVGP PGTGKTLLAK AVATECKTTF FNVSSSTLTS KYRGESEKLV RLLFEMARFY
SPATIFIDEI DSICSRRGTS EEHEASRRVK AELLVQMDGV GGASENDDPS KMVMVLAATN
FPWDIDEALR RRLEKRIYIP LPSAKGREEL LRISLRELEL ADDVDLASIA ENMEGYSGAD
ITNVCRDASL MAMRRRIEGL TPEEIRNLSR EEMHMPTTME DFEMALKKVS KSVSAADIER
YEKWIFEFGS C
//
