FIGL1_CAEEL
ID FIGL1_CAEEL Reviewed; 594 AA.
AC O16299;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Fidgetin-like protein 1;
DE EC=3.6.4.-;
DE AltName: Full=Fidgetin homolog;
GN Name=figl-1; ORFNames=F32D1.1;
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 [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 [2]
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF THR-360; CYS-368; CYS-373 AND CYS-527.
RX PubMed=15581640; DOI=10.1016/j.febslet.2004.11.009;
RA Yakushiji Y., Yamanaka K., Ogura T.;
RT "Identification of a cysteine residue important for the ATPase activity of
RT C. elegans fidgetin homologue.";
RL FEBS Lett. 578:191-197(2004).
RN [3]
RP SUBUNIT, AND MUTAGENESIS OF LYS-362; GLU-416; ASN-461; ARG-471; ARG-472 AND
RP ARG-473.
RX PubMed=16621600; DOI=10.1016/j.jsb.2006.03.001;
RA Yakushiji Y., Nishikori S., Yamanaka K., Ogura T.;
RT "Mutational analysis of the functional motifs in the ATPase domain of
RT Caenorhabditis elegans fidgetin homologue FIGL-1: firm evidence for an
RT intersubunit catalysis mechanism of ATP hydrolysis by AAA ATPases.";
RL J. Struct. Biol. 156:93-100(2006).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17878235; DOI=10.1242/jcs.015883;
RA Luke-Glaser S., Pintard L., Tyers M., Peter M.;
RT "The AAA-ATPase FIGL-1 controls mitotic progression, and its levels are
RT regulated by the CUL-3MEL-26 E3 ligase in the C. elegans germ line.";
RL J. Cell Sci. 120:3179-3187(2007).
CC -!- FUNCTION: Has a role in spindle assembly which acts in the progression
CC through mitosis during embryogenesis. Required for fertility.
CC {ECO:0000269|PubMed:17878235}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:15581640};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15581640};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.44 mM for ATP {ECO:0000269|PubMed:15581640};
CC Vmax=225 nmol/min/mg enzyme {ECO:0000269|PubMed:15581640};
CC Note=At 25 degrees Celsius and pH 8.0.;
CC pH dependence:
CC Optimum pH is 8.0-8.8. {ECO:0000269|PubMed:15581640};
CC Temperature dependence:
CC Optimum temperature is 25-30 degrees Celsius.
CC {ECO:0000269|PubMed:15581640};
CC -!- SUBUNIT: Hexamer. {ECO:0000269|PubMed:16621600}.
CC -!- INTERACTION:
CC O16299; Q7K7J0: gei-18; NbExp=4; IntAct=EBI-320880, EBI-2315822;
CC O16299; Q9U2T9: itsn-1; NbExp=3; IntAct=EBI-320880, EBI-2414252;
CC O16299; G5EC32: sorb-1; NbExp=8; IntAct=EBI-320880, EBI-325337;
CC O16299; Q8MPT2: T04C9.1; NbExp=5; IntAct=EBI-320880, EBI-2315635;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17878235}.
CC -!- TISSUE SPECIFICITY: Expressed in germ cells.
CC {ECO:0000269|PubMed:17878235}.
CC -!- DISRUPTION PHENOTYPE: Sterility owing to depletion of germ cells.
CC {ECO:0000269|PubMed:17878235}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; FO081012; CCD68481.1; -; Genomic_DNA.
DR PIR; T03922; T03922.
DR RefSeq; NP_504197.1; NM_071796.3.
DR PDB; 4L15; X-ray; 2.60 A; A=261-594.
DR PDB; 4L16; X-ray; 2.80 A; A=261-594.
DR PDBsum; 4L15; -.
DR PDBsum; 4L16; -.
DR AlphaFoldDB; O16299; -.
DR SMR; O16299; -.
DR BioGRID; 43882; 23.
DR DIP; DIP-25869N; -.
DR IntAct; O16299; 18.
DR MINT; O16299; -.
DR STRING; 6239.F32D1.1; -.
DR EPD; O16299; -.
DR PaxDb; O16299; -.
DR PeptideAtlas; O16299; -.
DR PRIDE; O16299; -.
DR EnsemblMetazoa; F32D1.1a.1; F32D1.1a.1; WBGene00017981.
DR GeneID; 178829; -.
DR KEGG; cel:CELE_F32D1.1; -.
DR UCSC; F32D1.1; c. elegans.
DR CTD; 178829; -.
DR WormBase; F32D1.1a; CE09865; WBGene00017981; figl-1.
DR eggNOG; KOG0740; Eukaryota.
DR GeneTree; ENSGT00940000171393; -.
DR HOGENOM; CLU_032424_0_0_1; -.
DR InParanoid; O16299; -.
DR OMA; AYAAWDK; -.
DR OrthoDB; 1176820at2759; -.
DR PhylomeDB; O16299; -.
DR SABIO-RK; O16299; -.
DR SignaLink; O16299; -.
DR PRO; PR:O16299; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00017981; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; O16299; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:WormBase.
DR GO; GO:0016787; F:hydrolase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:WormBase.
DR GO; GO:0008568; F:microtubule severing ATPase activity; IBA:GO_Central.
DR GO; GO:0046034; P:ATP metabolic process; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:WormBase.
DR Gene3D; 3.40.50.300; -; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09336; Vps4_C; 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; ATP-binding; Cell cycle; Cell division; Hydrolase; Magnesium;
KW Metal-binding; Mitosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..594
FT /note="Fidgetin-like protein 1"
FT /id="PRO_0000302729"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
FT BINDING 359..364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
FT MUTAGEN 360
FT /note="T->C: No effect on ATPase activity."
FT /evidence="ECO:0000269|PubMed:15581640"
FT MUTAGEN 362
FT /note="K->A: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:16621600"
FT MUTAGEN 368
FT /note="C->A: Strongly inhibits ATPase activity."
FT /evidence="ECO:0000269|PubMed:15581640"
FT MUTAGEN 373
FT /note="C->A: Slightly inhibits ATPase activity."
FT /evidence="ECO:0000269|PubMed:15581640"
FT MUTAGEN 416
FT /note="E->A: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:16621600"
FT MUTAGEN 461
FT /note="N->A: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:16621600"
FT MUTAGEN 471
FT /note="R->A: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:16621600"
FT MUTAGEN 472
FT /note="R->A: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:16621600"
FT MUTAGEN 473
FT /note="R->A: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:16621600"
FT MUTAGEN 527
FT /note="C->A: Slightly inhibits ATPase activity."
FT /evidence="ECO:0000269|PubMed:15581640"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:4L15"
FT TURN 314..317
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 333..337
FT /evidence="ECO:0007829|PDB:4L15"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:4L15"
FT STRAND 350..360
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 362..372
FT /evidence="ECO:0007829|PDB:4L15"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 382..386
FT /evidence="ECO:0007829|PDB:4L15"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 393..406
FT /evidence="ECO:0007829|PDB:4L15"
FT STRAND 407..415
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 417..421
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 430..446
FT /evidence="ECO:0007829|PDB:4L15"
FT STRAND 454..461
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:4L15"
FT TURN 468..473
FT /evidence="ECO:0007829|PDB:4L15"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 485..496
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 505..514
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 520..536
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 537..543
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 555..564
FT /evidence="ECO:0007829|PDB:4L15"
FT HELIX 571..584
FT /evidence="ECO:0007829|PDB:4L15"
SQ SEQUENCE 594 AA; 66187 MW; 59E0FFBA05B6712F CRC64;
MYSPKRVKLN VTSGMRKRPE TGENNDDLYP PTALARNGIS PYFIGKPRRK IVVETPSDSA
QQQPPFKSRS QQNGLDDELD GIIIDEDEDR TVDVSFSQKQ DTRKLKSRPF LGEKSSFKLG
EIPKPKEEKR REEPFTMRGF DFGSDDKVTK IRDKICDIVD PTNARRTDPN FIRQMHENTL
KGIEVASNPH FKKTRAPTKN RAAIQNTLGT LYPSFTTAAG QDPQNSKFQV PLDRQSSSQS
IGSLAGIPPA RRAPDIPKRC SNPLIRKAMG MDTEGGGKDE KMSGLRAEPT LKHFDENIIS
LIESEIMSVN NEIGWADVAG LEGAKKALRE IVVLPFKRPD VFTGIRAPPK GVLLFGPPGT
GKTMIGRCVA SQCKATFFNI SASSLTSKWV GEGEKLVRAL FSVARLKLPS VIFIDEIDSL
LSSRSESEHE SSRRIKTEFL VQLDGVNTAP DERLLVLGAT NRPQELDEAA RRRFQKRLYI
ALPEPESRTQ IVQNLLVGTR HDITNHNLER IRELTDGYSG ADMRQLCTEA AMGPIRDIGD
DIETIDKDDI RAVTVMDFAE AARVVRPTVD DSQLDAYAAW DKKFGCLPPP SISR
