KTNA1_CAEEL
ID KTNA1_CAEEL Reviewed; 472 AA.
AC P34808; Q8I4G6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Meiotic spindle formation protein mei-1 {ECO:0000255|HAMAP-Rule:MF_03023};
DE EC=5.6.1.1 {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:28783150};
DE AltName: Full=Katanin p60 ATPase-containing subunit A1 {ECO:0000255|HAMAP-Rule:MF_03023};
DE Short=Katanin p60 subunit A1 {ECO:0000255|HAMAP-Rule:MF_03023};
DE AltName: Full=p60 katanin {ECO:0000255|HAMAP-Rule:MF_03023};
GN Name=mei-1 {ECO:0000255|HAMAP-Rule:MF_03023}; ORFNames=T01G9.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS A AND B),
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-36; GLU-66; PRO-99; GLY-126;
RP ARG-128; ILE-195; PRO-225; LEU-231; PRO-235; GLU-308; PRO-360; ARG-414 AND
RP GLY-470.
RC STRAIN=Bristol N2;
RX PubMed=8150281; DOI=10.1093/genetics/136.2.533;
RA Clark-Maguire S., Mains P.E.;
RT "mei-1, a gene required for meiotic spindle formation in Caenorhabditis
RT elegans, is a member of a family of ATPases.";
RL Genetics 136:533-546(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=8027178; DOI=10.1083/jcb.126.1.199;
RA Clark-Maguire S., Mains P.E.;
RT "Localization of the mei-1 gene product of Caenorhaditis elegans, a
RT meiotic-specific spindle component.";
RL J. Cell Biol. 126:199-209(1994).
RN [4]
RP FUNCTION, INTERACTION WITH MEI-2, AND SUBCELLULAR LOCATION.
RX PubMed=10809666;
RA Srayko M., Buster D.W., Bazirgan O.A., McNally F.J., Mains P.E.;
RT "MEI-1/MEI-2 katanin-like microtubule severing activity is required for
RT Caenorhabditis elegans meiosis.";
RL Genes Dev. 14:1072-1084(2000).
RN [5]
RP REGULATION BY UBIQUITIN MEDIATED PROTEOLYSIS.
RX PubMed=11847342; DOI=10.1126/science.1067765;
RA Kurz T., Pintard L., Willis J.H., Hamill D.R., Goenczy P., Peter M.,
RA Bowerman B.;
RT "Cytoskeletal regulation by the Nedd8 ubiquitin-like protein modification
RT pathway.";
RL Science 295:1294-1298(2002).
RN [6]
RP REGULATION BY UBIQUITIN MEDIATED PROTEOLYSIS, AND SUBCELLULAR LOCATION.
RX PubMed=12781129; DOI=10.1016/s0960-9822(03)00336-1;
RA Pintard L., Kurz T., Glaser S., Willis J.H., Peter M., Bowerman B.;
RT "Neddylation and deneddylation of CUL-3 is required to target MEI-1/katanin
RT for degradation at the meiosis-to-mitosis transition in C. elegans.";
RL Curr. Biol. 13:911-921(2003).
RN [7]
RP FUNCTION.
RX PubMed=12885567; DOI=10.1016/s0012-1606(03)00216-1;
RA Yang H.-Y., McNally K., McNally F.J.;
RT "MEI-1/katanin is required for translocation of the meiosis I spindle to
RT the oocyte cortex in C elegans.";
RL Dev. Biol. 260:245-259(2003).
RN [8]
RP INTERACTION WITH MEL-26, AND REGULATION BY UBIQUITIN MEDIATED PROTEOLYSIS.
RX PubMed=13679921; DOI=10.1038/nature01959;
RA Pintard L., Willis J.H., Willems A., Johnson J.-L.F., Srayko M., Kurz T.,
RA Glaser S., Mains P.E., Tyers M., Bowerman B., Peter M.;
RT "The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3
RT ubiquitin-ligase.";
RL Nature 425:311-316(2003).
RN [9]
RP INTERACTION WITH MEL-26, AND REGULATION BY UBIQUITIN MEDIATED PROTEOLYSIS.
RX PubMed=14528312; DOI=10.1038/ncb1056;
RA Furukawa M., He Y.J., Borchers C., Xiong Y.;
RT "Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin
RT ligases.";
RL Nat. Cell Biol. 5:1001-1007(2003).
RN [10]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-92, AND
RP MUTAGENESIS OF ARG-36 AND SER-92.
RX PubMed=16338136; DOI=10.1016/j.cub.2005.11.063;
RA Stitzel M.L., Pellettieri J., Seydoux G.;
RT "The C. elegans DYRK Kinase MBK-2 marks oocyte proteins for degradation in
RT response to meiotic maturation.";
RL Curr. Biol. 16:56-62(2006).
RN [11]
RP FUNCTION, INTERACTION WITH PPH-4.1, AND MUTAGENESIS OF PRO-99 AND GLU-308.
RX PubMed=19087961; DOI=10.1534/genetics.108.096016;
RA Han X., Gomes J.E., Birmingham C.L., Pintard L., Sugimoto A., Mains P.E.;
RT "The role of protein phosphatase 4 in regulating microtubule severing in
RT the Caenorhabditis elegans embryo.";
RL Genetics 181:933-943(2009).
RN [12]
RP FUNCTION, INTERACTION WITH MEL-26, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP PRO-99 AND GLU-308.
RX PubMed=22621901; DOI=10.1091/mbc.e12-01-0055;
RA Wilson K.J., Qadota H., Mains P.E., Benian G.M.;
RT "UNC-89 (obscurin) binds to MEL-26, a BTB-domain protein, and affects the
RT function of MEI-1 (katanin) in striated muscle of Caenorhabditis elegans.";
RL Mol. Biol. Cell 23:2623-2634(2012).
RN [13]
RP FUNCTION, INTERACTION WITH MEL-26, PHOSPHORYLATION, AND MUTAGENESIS OF
RP PRO-235.
RX PubMed=23918937; DOI=10.1083/jcb.201304174;
RA Gomes J.E., Tavernier N., Richaudeau B., Formstecher E., Boulin T.,
RA Mains P.E., Dumont J., Pintard L.;
RT "Microtubule severing by the katanin complex is activated by PPFR-1-
RT dependent MEI-1 dephosphorylation.";
RL J. Cell Biol. 202:431-439(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) IN COMPLEX WITH ATP, FUNCTION,
RP CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF ASP-322; ARG-351; ARG-352
RP AND PHE-469.
RX PubMed=28783150; DOI=10.1038/nsmb.3448;
RA Zehr E., Szyk A., Piszczek G., Szczesna E., Zuo X., Roll-Mecak A.;
RT "Katanin spiral and ring structures shed light on power stroke for
RT microtubule severing.";
RL Nat. Struct. Mol. Biol. 24:717-725(2017).
CC -!- FUNCTION: Catalytic subunit of a complex which severs microtubules in
CC an ATP-dependent manner (PubMed:28783150). Microtubule severing may
CC promote rapid reorganization of cellular microtubule arrays. Required
CC specifically for meiotic spindle formation in the female germline; the
CC presence of this protein is inimical to the formation of mitotic
CC spindles (PubMed:8027178, PubMed:10809666, PubMed:12885567,
CC PubMed:19087961, PubMed:23918937). In body wall muscles, regulates
CC organization of myosin thick filaments (PubMed:22621901).
CC {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:10809666,
CC ECO:0000269|PubMed:12885567, ECO:0000269|PubMed:19087961,
CC ECO:0000269|PubMed:22621901, ECO:0000269|PubMed:28783150,
CC ECO:0000269|PubMed:8027178}.
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_03023,
CC ECO:0000269|PubMed:28783150};
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by microtubules,
CC which promote homooligomerization. ATP-dependent microtubule severing
CC is stimulated by interaction with mei-2. {ECO:0000255|HAMAP-
CC Rule:MF_03023}.
CC -!- SUBUNIT: Homohexamer; ATP hydrolysis initiates a cycle between an open
CC spiral and a closed ring conformation which is probably involved in
CC pulling tubulin dimers out from microtubules (PubMed:28783150).
CC Interacts with mei-2, which may serve as a targeting subunit
CC (PubMed:10809666). Interacts with mel-26, which targets mei-1 for
CC ubiquitin mediated proteolysis (PubMed:13679921, PubMed:14528312,
CC PubMed:23918937). Interacts with phosphatase pph-4.1 (PubMed:19087961).
CC {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:10809666,
CC ECO:0000269|PubMed:13679921, ECO:0000269|PubMed:14528312,
CC ECO:0000269|PubMed:19087961, ECO:0000269|PubMed:22621901,
CC ECO:0000269|PubMed:23918937, ECO:0000269|PubMed:28783150}.
CC -!- INTERACTION:
CC P34808; Q9XTS1: CELE_F47G4.4; NbExp=3; IntAct=EBI-323248, EBI-312192;
CC P34808; Q9XTS3: CELE_F47G4.5; NbExp=4; IntAct=EBI-323248, EBI-2417913;
CC P34808; Q9XTF3-2: mbk-2; NbExp=2; IntAct=EBI-323248, EBI-2565597;
CC P34808; P34808: mei-1; NbExp=6; IntAct=EBI-323248, EBI-323248;
CC P34808; O44740: mei-2; NbExp=3; IntAct=EBI-323248, EBI-323243;
CC P34808; Q94420: mel-26; NbExp=6; IntAct=EBI-323248, EBI-320790;
CC P34808-2; Q94420: mel-26; NbExp=3; IntAct=EBI-521381, EBI-320790;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:10809666,
CC ECO:0000269|PubMed:12781129, ECO:0000269|PubMed:8027178}. Chromosome
CC {ECO:0000269|PubMed:12781129, ECO:0000269|PubMed:16338136}. Cytoplasm
CC {ECO:0000269|PubMed:16338136}. Note=Localizes to the spindle poles and
CC condensed chromatin during female meiosis (PubMed:10809666,
CC PubMed:12781129, PubMed:8027178, PubMed:16338136). This localization
CC requires mei-2 (PubMed:10809666). Also localizes to the polar body
CC (PubMed:12781129). Ser-92 phosphorylated mei-1 is first detected on the
CC maternal chromatin in anaphase of meiosis I, then localizes to the
CC cytoplasm during meiosis II and quickly disappears between pronuclear
CC formation and the first cell division, except in the polar bodies
CC (PubMed:16338136). {ECO:0000269|PubMed:10809666,
CC ECO:0000269|PubMed:12781129, ECO:0000269|PubMed:16338136,
CC ECO:0000269|PubMed:8027178}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P34808-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P34808-2; Sequence=VSP_012951;
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the female germline.
CC Degradation at the meiosis-mitosis transition reduces cytoplasmic
CC microtubule severing activity, thereby allowing the formation of larger
CC mitotic spindles. {ECO:0000269|PubMed:8027178}.
CC -!- PTM: Phosphorylated (PubMed:16338136, PubMed:23918937). Phosphorylation
CC by mbk-2 is required for its rapid degradation following meiosis II
CC (PubMed:16338136). Likely dephosphorylated by the PP4 complex composed
CC of catalytic subunit pph-4.1 and regulatory subunit ppfr-1
CC (PubMed:23918937). {ECO:0000269|PubMed:16338136,
CC ECO:0000269|PubMed:23918937}.
CC -!- PTM: Polyubiquitination targets the protein for rapid degradation via
CC the ubiquitin system at the end of meiosis. The BTB domain protein mel-
CC 26 may serve to specifically target mei-1 for ubiquitination by cul-3
CC containing complexes. The cul-3 protein is in turn regulated by
CC neddylation by ned-8.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at the L1 larval stage
CC results in the disorganization of myosin thick filaments in adult body
CC wall muscles characterized by the formation of abnormal myosin heavy
CC chain myo-3 aggregates and V-shaped crossing of A-bands. In addition,
CC body wall muscle cells appear shorter and broader.
CC {ECO:0000269|PubMed:22621901}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03023}.
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DR EMBL; L25423; AAA28109.1; -; Genomic_DNA.
DR EMBL; Z75713; CAB00052.1; -; Genomic_DNA.
DR EMBL; Z75713; CAD56596.1; -; Genomic_DNA.
DR PIR; S47861; S47861.
DR PIR; T24316; T24316.
DR RefSeq; NP_492257.1; NM_059856.6. [P34808-1]
DR RefSeq; NP_871793.1; NM_181993.5.
DR PDB; 5WC0; EM; 4.40 A; A/B/C/D/E/F=1-472.
DR PDB; 5WC1; X-ray; 3.30 A; A=1-472.
DR PDB; 5WCB; EM; 6.00 A; A/B/C/D/E/F=1-472.
DR PDB; 6B5D; X-ray; 3.10 A; A=164-471.
DR PDB; 6UGD; EM; 3.50 A; A/B/C/D/E/F=1-472.
DR PDB; 6UGE; EM; 3.60 A; A/B/C/D/E/F=1-472.
DR PDB; 6UGF; EM; 4.20 A; A/B/C/D/E/F=1-472.
DR PDBsum; 5WC0; -.
DR PDBsum; 5WC1; -.
DR PDBsum; 5WCB; -.
DR PDBsum; 6B5D; -.
DR PDBsum; 6UGD; -.
DR PDBsum; 6UGE; -.
DR PDBsum; 6UGF; -.
DR AlphaFoldDB; P34808; -.
DR SMR; P34808; -.
DR BioGRID; 38046; 14.
DR ComplexPortal; CPX-3889; Katanin complex.
DR DIP; DIP-25343N; -.
DR IntAct; P34808; 7.
DR MINT; P34808; -.
DR STRING; 6239.T01G9.5b; -.
DR iPTMnet; P34808; -.
DR EPD; P34808; -.
DR PaxDb; P34808; -.
DR PeptideAtlas; P34808; -.
DR PRIDE; P34808; -.
DR EnsemblMetazoa; T01G9.5a.1; T01G9.5a.1; WBGene00003183. [P34808-1]
DR EnsemblMetazoa; T01G9.5b.1; T01G9.5b.1; WBGene00003183. [P34808-2]
DR GeneID; 172612; -.
DR UCSC; T01G9.5a.1; c. elegans. [P34808-1]
DR CTD; 249838; -.
DR WormBase; T01G9.5a; CE06342; WBGene00003183; mei-1. [P34808-1]
DR WormBase; T01G9.5b; CE32479; WBGene00003183; mei-1. [P34808-2]
DR eggNOG; KOG0738; Eukaryota.
DR GeneTree; ENSGT00940000169739; -.
DR HOGENOM; CLU_000688_21_1_1; -.
DR InParanoid; P34808; -.
DR OMA; EVCWEDI; -.
DR OrthoDB; 714481at2759; -.
DR PhylomeDB; P34808; -.
DR BRENDA; 5.6.1.1; 1045.
DR SignaLink; P34808; -.
DR PRO; PR:P34808; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003183; Expressed in embryo and 4 other tissues.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR GO; GO:0000785; C:chromatin; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008352; C:katanin complex; IDA:UniProtKB.
DR GO; GO:0072687; C:meiotic spindle; IDA:WormBase.
DR GO; GO:0090619; C:meiotic spindle pole; IDA:WormBase.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005819; C:spindle; IDA:WormBase.
DR GO; GO:0000922; C:spindle pole; IDA:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0090736; F:MATH domain binding; IPI:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008568; F:microtubule severing ATPase activity; IDA:WormBase.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:WormBase.
DR GO; GO:0051229; P:meiotic spindle disassembly; IMP:WormBase.
DR GO; GO:0000212; P:meiotic spindle organization; IMP:WormBase.
DR GO; GO:0007019; P:microtubule depolymerization; IDA:WormBase.
DR GO; GO:0051013; P:microtubule severing; IMP:UniProtKB.
DR GO; GO:1902120; P:negative regulation of meiotic spindle elongation; IMP:WormBase.
DR GO; GO:0071688; P:striated muscle myosin thick filament assembly; IMP:UniProtKB.
DR DisProt; DP02999; -.
DR Gene3D; 3.40.50.300; -; 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; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Chromosome; Cytoplasm; Cytoskeleton; Isomerase; Meiosis; Microtubule;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..472
FT /note="Meiotic spindle formation protein mei-1"
FT /id="PRO_0000084599"
FT REGION 83..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 233..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03023,
FT ECO:0000269|PubMed:28783150, ECO:0007744|PDB:5WC0,
FT ECO:0007744|PDB:5WCB"
FT BINDING 351..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:28783150,
FT ECO:0007744|PDB:5WC0, ECO:0007744|PDB:5WCB"
FT MOD_RES 92
FT /note="Phosphoserine; by mbk-2"
FT /evidence="ECO:0000269|PubMed:16338136"
FT VAR_SEQ 416
FT /note="Y -> YFRY (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_012951"
FT MUTAGEN 36
FT /note="R->C: In ct46ct99; loss of function. Does not affect
FT mei-1 degradation. Prevents mei-1 degradation during the
FT transition from meiosis to mitosis; when associated with A-
FT 92."
FT /evidence="ECO:0000269|PubMed:16338136,
FT ECO:0000269|PubMed:8150281"
FT MUTAGEN 66
FT /note="E->K: In ct46sb18; gain of function."
FT /evidence="ECO:0000269|PubMed:8150281"
FT MUTAGEN 92
FT /note="S->A: Abolishes phosphorylation by mbk-2. Abolishes
FT interaction with mel-26. Prevents mei-1 degradation during
FT the transition from meiosis to mitosis; when associated
FT with C-36."
FT /evidence="ECO:0000269|PubMed:16338136,
FT ECO:0000269|PubMed:23918937"
FT MUTAGEN 92
FT /note="S->D: Phosphomimetic mutant. No effect on the
FT interaction with mel-26."
FT /evidence="ECO:0000269|PubMed:23918937"
FT MUTAGEN 99
FT /note="P->L: In ct46; gain of function. Embryonic lethal.
FT Abolishes interaction with mel-26 and probably mel-26-
FT mediated degradation. Simultaneous RNAi-mediated knockdown
FT of ppfr-1, pph-4.1 or ppfr-4, partially rescues embryonic
FT lethality. Myosin thick filaments are disorganized in body
FT wall muscles in an unc-29 (e1072) mutant background."
FT /evidence="ECO:0000269|PubMed:19087961,
FT ECO:0000269|PubMed:22621901, ECO:0000269|PubMed:8150281"
FT MUTAGEN 126
FT /note="G->S: In ct46sb9 and ct46sb17; gain of function."
FT /evidence="ECO:0000269|PubMed:8150281"
FT MUTAGEN 128
FT /note="R->C: In ct46sb22; gain of function."
FT /evidence="ECO:0000269|PubMed:8150281"
FT MUTAGEN 195
FT /note="I->K: In ct46sb3; dominant negative."
FT /evidence="ECO:0000269|PubMed:8150281"
FT MUTAGEN 225
FT /note="P->L: In b284; dominant negative."
FT /evidence="ECO:0000269|PubMed:8150281"
FT MUTAGEN 231
FT /note="L->P: In ct81; dominant negative."
FT /evidence="ECO:0000269|PubMed:8150281"
FT MUTAGEN 235
FT /note="P->L: In ct93; dominant negative."
FT /evidence="ECO:0000269|PubMed:8150281"
FT MUTAGEN 235
FT /note="P->S: In ct46ct103; dominant negative. Formation of
FT an abnormally large polar body during oocyte meiosis II.
FT Increased in metaphase and anaphase meiotic spindle length,
FT failure of chromosomes to align on the metaphase plate
FT persistence of spindle poles during anaphase resulting in
FT their mis-positioning and delay in anaphase meiotic spindle
FT disassembly."
FT /evidence="ECO:0000269|PubMed:23918937,
FT ECO:0000269|PubMed:8150281"
FT MUTAGEN 308
FT /note="E->D: In ct46ct101; null. Formation of an abnormally
FT large polar body during oocyte meiosis II. Myosin thick
FT filaments are disorganized in body wall muscles in an unc-
FT 29 (e1072) mutant background."
FT /evidence="ECO:0000269|PubMed:19087961,
FT ECO:0000269|PubMed:22621901, ECO:0000269|PubMed:8150281"
FT MUTAGEN 322
FT /note="D->R: Severe loss of ATPase activity and complete
FT loss of microtubule severing activity."
FT /evidence="ECO:0000269|PubMed:28783150"
FT MUTAGEN 351
FT /note="R->A: Severe loss of ATPase activity and complete
FT loss of microtubule severing activity."
FT /evidence="ECO:0000269|PubMed:28783150"
FT MUTAGEN 352
FT /note="R->A: Severe loss of ATPase activity and complete
FT loss of microtubule severing activity."
FT /evidence="ECO:0000269|PubMed:28783150"
FT MUTAGEN 360
FT /note="P->S: In ct46sb23; gain of function."
FT /evidence="ECO:0000269|PubMed:8150281"
FT MUTAGEN 414
FT /note="R->K: In ct46ct89; dominant negative."
FT /evidence="ECO:0000269|PubMed:8150281"
FT MUTAGEN 469
FT /note="F->A: Severe loss of ATPase activity and complete
FT loss of microtubule severing activity."
FT /evidence="ECO:0000269|PubMed:28783150"
FT MUTAGEN 470
FT /note="G->D: In ct46ct82; dominant negative."
FT /evidence="ECO:0000269|PubMed:8150281"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:6B5D"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 199..208
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:6B5D"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:6B5D"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:6B5D"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:6UGD"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:6B5D"
FT STRAND 284..292
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 316..324
FT /evidence="ECO:0007829|PDB:6B5D"
FT STRAND 333..340
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 347..352
FT /evidence="ECO:0007829|PDB:6B5D"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 364..374
FT /evidence="ECO:0007829|PDB:6B5D"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 386..392
FT /evidence="ECO:0007829|PDB:6B5D"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:5WC1"
FT HELIX 398..414
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:6B5D"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 428..435
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 440..449
FT /evidence="ECO:0007829|PDB:6B5D"
FT HELIX 456..465
FT /evidence="ECO:0007829|PDB:6B5D"
SQ SEQUENCE 472 AA; 51739 MW; 167A3929E573CD59 CRC64;
MNGDVQSVIR GYLERAQVAK TMSDAGRWNE AGDLLRQLMT DVKSCKISAS NRDEHDARNT
FLRALEANLK LVQQNVRDED DLHEAMTRQS GSPEPPADPD VWSKPSPPLP SSSKFGATKK
GVGAAGPRPR EISKSTSSMS TNPADVKPAN PTQGILPQNS AGDSFDASAY DAYIVQAVRG
TMATNTENTM SLDDIIGMHD VKQVLHEAVT LPLLVPEFFQ GLRSPWKAMV LAGPPGTGKT
LIARAIASES SSTFFTVSST DLSSKWRGDS EKIVRLLFEL ARFYAPSIIF IDEIDTLGGQ
RGNSGEHEAS RRVKSEFLVQ MDGSQNKFDS RRVFVLAATN IPWELDEALR RRFEKRIFIP
LPDIDARKKL IEKSMEGTPK SDEINYDDLA ARTEGFSGAD VVSLCRTAAI NVLRRYDTKS
LRGGELTAAM ESLKAELVRN IDFEAALQAV SPSAGPDTML KCKEWCDSFG AM
