ID G1KDN8_ANOCA Unreviewed; 501 AA.
AC G1KDN8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_03023, ECO:0000256|HAMAP-Rule:MF_03024};
DE Includes:
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};
DE Includes:
DE RecName: Full=Katanin p60 ATPase-containing subunit A-like 1 {ECO:0000256|HAMAP-Rule:MF_03024};
DE Short=Katanin p60 subunit A-like 1 {ECO:0000256|HAMAP-Rule:MF_03024};
DE AltName: Full=p60 katanin-like 1 {ECO:0000256|HAMAP-Rule:MF_03024};
GN Name=KATNAL1 {ECO:0000256|HAMAP-Rule:MF_03024,
GN ECO:0000313|Ensembl:ENSACAP00000005040.3};
GN Synonyms=KATNA1 {ECO:0000256|HAMAP-Rule:MF_03023};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000005040.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000005040.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000005040.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000005040.3}
RP IDENTIFICATION.
RG Ensembl;
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.
CC {ECO:0000256|HAMAP-Rule:MF_03023}.
CC -!- FUNCTION: Regulates microtubule dynamics in Sertoli cells, a process
CC that is essential for spermiogenesis and male fertility. Severs
CC microtubules in an ATP-dependent manner, promoting rapid reorganization
CC of cellular microtubule arrays. {ECO:0000256|HAMAP-Rule:MF_03024}.
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. {ECO:0000256|HAMAP-Rule:MF_03023}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000256|ARBA:ARBA00004647, ECO:0000256|HAMAP-Rule:MF_03023,
CC ECO:0000256|HAMAP-Rule:MF_03024}. Cytoplasm, cytoskeleton
CC {ECO:0000256|HAMAP-Rule:MF_03024}. Cytoplasm {ECO:0000256|HAMAP-
CC Rule:MF_03023, ECO:0000256|HAMAP-Rule:MF_03024}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03023,
CC ECO:0000256|HAMAP-Rule:MF_03024}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03023}.
CC Note=Colocalizes with microtubules throughout the basal and adluminal
CC compartments of Sertoli cells. Localizes within the cytoplasm,
CC partially overlapping with microtubules, in interphase and to the
CC mitotic spindle and spindle poles during mitosis. {ECO:0000256|HAMAP-
CC Rule:MF_03024}. Predominantly cytoplasmic. Also localized to the
CC interphase centrosome and the mitotic spindle poles. Enhanced
CC recruitment to the mitotic spindle poles requires microtubules and
CC interaction with KATNB1. {ECO:0000256|HAMAP-Rule:MF_03023}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1
CC subfamily. A-like 1 sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_03024}.
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DR AlphaFoldDB; G1KDN8; -.
DR STRING; 28377.ENSACAP00000005040; -.
DR Ensembl; ENSACAT00000005153.3; ENSACAP00000005040.3; ENSACAG00000005119.3.
DR eggNOG; KOG0738; Eukaryota.
DR GeneTree; ENSGT00940000156630; -.
DR HOGENOM; CLU_000688_21_1_1; -.
DR InParanoid; G1KDN8; -.
DR TreeFam; TF323170; -.
DR Proteomes; UP000001646; Chromosome 3.
DR Bgee; ENSACAG00000005119; Expressed in testis and 13 other cell types or tissues.
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:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
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:0042802; F:identical protein binding; IEA:Ensembl.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051013; P:microtubule severing; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; 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 HAMAP; MF_03024; Katanin_p60_AL1; 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; IPR028594; Katnal1_chordates.
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:SF65; KATANIN P60 ATPASE-CONTAINING SUBUNIT A-LIKE 1; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001646}.
FT DOMAIN 251..393
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 101..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 259..266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03023"
SQ SEQUENCE 501 AA; 56761 MW; 10C07FBE295BC8F8 CRC64;
MNVCLIVDFS KKMNLAEICD NAKKGREYAL LGNYDSSMVY YQGVIQQIQR HCQSIRDPAL
KSKWQQVRQE LLEEYEQVKS IVNTLESFKI DRPTDIPVSY QDDHFRDPAV WPPPVPAEHR
APPQIKRPNR EVKPLRRESP GLQRGPVGRA QPISKNEKSA SSRERESKGK GKDEKGKKIP
QDGAGDSEIQ KFDGAGYDKD LVEALERDIV SRNLSIHWDD IADLEEAKKL LREAVVLPMW
MPDFFKGIRR PWKGVLMVGP PGTGKTMLAK AVATECGTTF FNVSSSTLTS KYRGESEKLV
RLLFEMARFY APTTIFIDEI DSICSRRGTS DEHEASRRVK SELLVQMDGV GGALENDDPS
RMVMVLAATN FPWDIDEALR RRLEKRIYIP LPTAKGRAEL LKINLREVEL DPDIRLEEIA
EKIEGYSGAD ITNVCRDASL MAMRRRINGL SPEEIRALSK EELLMPVTKG DFELALKKIS
KSVSAADLEK YEKWMSEFGS A
//
