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O16299 (FIGL1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fidgetin-like protein 1

EC=3.6.4.-
Alternative name(s):
Fidgetin homolog
Gene names
Name:figl-1
ORF Names:F32D1.1
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length594 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has a role in spindle assembly which acts in the progression through mitosis during embryogenesis. Required for fertility. Ref.4

Catalytic activity

ATP + H2O = ADP + phosphate. Ref.2

Cofactor

Magnesium. Ref.2

Subunit structure

Hexamer. Ref.3

Subcellular location

Nucleus Ref.4.

Tissue specificity

Expressed in germ cells. Ref.4

Disruption phenotype

Sterility owing to depletion of germ cells. Ref.4

Sequence similarities

Belongs to the AAA ATPase family.

Biophysicochemical properties

Kinetic parameters:

At 25 degrees Celsius and pH 8.0.

KM=0.44 mM for ATP Ref.2

Vmax=225 nmol/min/mg enzyme

pH dependence:

Optimum pH is 8.0-8.8.

Temperature dependence:

Optimum temperature is 25-30 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 594594Fidgetin-like protein 1
PRO_0000302729

Regions

Nucleotide binding359 – 3646ATP By similarity

Sites

Binding site3191ATP; via amide nitrogen and carbonyl oxygen By similarity

Experimental info

Mutagenesis3601T → C: No effect on ATPase activity. Ref.2
Mutagenesis3621K → A: Abolishes ATPase activity. Ref.3
Mutagenesis3681C → A: Strongly inhibits ATPase activity. Ref.2
Mutagenesis3731C → A: Slightly inhibits ATPase activity. Ref.2
Mutagenesis4161E → A: Abolishes ATPase activity. Ref.3
Mutagenesis4611N → A: Abolishes ATPase activity. Ref.3
Mutagenesis4711R → A: Abolishes ATPase activity. Ref.3
Mutagenesis4721R → A: Abolishes ATPase activity. Ref.3
Mutagenesis4731R → A: Abolishes ATPase activity. Ref.3
Mutagenesis5271C → A: Slightly inhibits ATPase activity. Ref.2

Secondary structure

................................................... 594
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O16299 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 59E0FFBA05B6712F

FASTA59466,187
        10         20         30         40         50         60 
MYSPKRVKLN VTSGMRKRPE TGENNDDLYP PTALARNGIS PYFIGKPRRK IVVETPSDSA 

        70         80         90        100        110        120 
QQQPPFKSRS QQNGLDDELD GIIIDEDEDR TVDVSFSQKQ DTRKLKSRPF LGEKSSFKLG 

       130        140        150        160        170        180 
EIPKPKEEKR REEPFTMRGF DFGSDDKVTK IRDKICDIVD PTNARRTDPN FIRQMHENTL 

       190        200        210        220        230        240 
KGIEVASNPH FKKTRAPTKN RAAIQNTLGT LYPSFTTAAG QDPQNSKFQV PLDRQSSSQS 

       250        260        270        280        290        300 
IGSLAGIPPA RRAPDIPKRC SNPLIRKAMG MDTEGGGKDE KMSGLRAEPT LKHFDENIIS 

       310        320        330        340        350        360 
LIESEIMSVN NEIGWADVAG LEGAKKALRE IVVLPFKRPD VFTGIRAPPK GVLLFGPPGT 

       370        380        390        400        410        420 
GKTMIGRCVA SQCKATFFNI SASSLTSKWV GEGEKLVRAL FSVARLKLPS VIFIDEIDSL 

       430        440        450        460        470        480 
LSSRSESEHE SSRRIKTEFL VQLDGVNTAP DERLLVLGAT NRPQELDEAA RRRFQKRLYI 

       490        500        510        520        530        540 
ALPEPESRTQ IVQNLLVGTR HDITNHNLER IRELTDGYSG ADMRQLCTEA AMGPIRDIGD 

       550        560        570        580        590 
DIETIDKDDI RAVTVMDFAE AARVVRPTVD DSQLDAYAAW DKKFGCLPPP SISR 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[2]"Identification of a cysteine residue important for the ATPase activity of C. elegans fidgetin homologue."
Yakushiji Y., Yamanaka K., Ogura T.
FEBS Lett. 578:191-197(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF THR-360; CYS-368; CYS-373 AND CYS-527.
[3]"Mutational analysis of the functional motifs in the ATPase domain of Caenorhabditis elegans fidgetin homologue FIGL-1: firm evidence for an intersubunit catalysis mechanism of ATP hydrolysis by AAA ATPases."
Yakushiji Y., Nishikori S., Yamanaka K., Ogura T.
J. Struct. Biol. 156:93-100(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, MUTAGENESIS OF LYS-362; GLU-416; ASN-461; ARG-471; ARG-472 AND ARG-473.
[4]"The AAA-ATPase FIGL-1 controls mitotic progression, and its levels are regulated by the CUL-3MEL-26 E3 ligase in the C. elegans germ line."
Luke-Glaser S., Pintard L., Tyers M., Peter M.
J. Cell Sci. 120:3179-3187(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FO081012 Genomic DNA. Translation: CCD68481.1.
PIRT03922.
RefSeqNP_504197.1. NM_071796.3.
UniGeneCel.6491.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4L15X-ray2.60A261-594[»]
4L16X-ray2.80A261-594[»]
ProteinModelPortalO16299.
SMRO16299. Positions 286-588.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid43882. 9 interactions.
DIPDIP-25869N.
IntActO16299. 18 interactions.
MINTMINT-117972.
STRING6239.F32D1.1.

Proteomic databases

PaxDbO16299.
PRIDEO16299.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaF32D1.1; F32D1.1; WBGene00017981.
GeneID178829.
KEGGcel:CELE_F32D1.1.
UCSCF32D1.1. c. elegans.

Organism-specific databases

CTD178829.
WormBaseF32D1.1; CE09865; WBGene00017981; figl-1.

Phylogenomic databases

eggNOGCOG0464.
GeneTreeENSGT00570000078874.
HOGENOMHOG000112588.
InParanoidO16299.
OMAHFDENII.
OrthoDBEOG7GXPCR.
PhylomeDBO16299.

Enzyme and pathway databases

SABIO-RKO16299.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00004. AAA. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio902732.
PROO16299.

Entry information

Entry nameFIGL1_CAEEL
AccessionPrimary (citable) accession number: O16299
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase