Fidgetin-like protein 1 - Caenorhabditis elegans

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Reviewed, UniProtKB/Swiss-Prot O16299 (FIGL1_CAEEL)

Last modified June 16, 2009. Version 71. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Fidgetin-like protein 1
    EC=3.6.4.-
Alternative name(s):
    Fidgetin homolog

Gene names

Name:	figl-1
ORF Names:	F32D1.1

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

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Protein attributes

Sequence length	594 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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. K_M=0.44 mM for ATP V_max=225 nmol/min/mg enzyme pH dependence: Optimum pH is 8.0-8.8. Temperature dependence: Optimum temperature is 25-30 degrees Celsius.

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Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Nucleus
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP metabolic process Ref.2 Inferred from direct assay. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from physical interaction. Source: IntAct magnesium ion binding Ref.2 Inferred from direct assay. Source: UniProtKB nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
itself		1	EBI-320880,EBI-320880
	Q22174	1	EBI-320880,EBI-311938
atn-1	Q23158	1	EBI-320880,EBI-314014
mrt-2	Q9U2I2	1	EBI-320880,EBI-323732
smo-1	P55853	1	EBI-320880,EBI-313647

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 594

594

Fidgetin-like protein 1

PRO_0000302729

Regions

Nucleotide binding

356 – 363

ATP Probable

Experimental info

Mutagenesis

360

T → C: No effect on ATPase activity. Ref.2

Mutagenesis

362

K → A: Abolishes ATPase activity. Ref.3

Mutagenesis

368

C → A: Strongly inhibits ATPase activity. Ref.2

Mutagenesis

373

C → A: Slightly inhibits ATPase activity. Ref.2

Mutagenesis

416

E → A: Abolishes ATPase activity. Ref.3

Mutagenesis

461

N → A: Abolishes ATPase activity. Ref.3

Mutagenesis

471

R → A: Abolishes ATPase activity. Ref.3

Mutagenesis

472

R → A: Abolishes ATPase activity. Ref.3

Mutagenesis

473

R → A: Abolishes ATPase activity. Ref.3

Mutagenesis

527

C → A: Slightly inhibits ATPase activity. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

O16299-1 [UniParc].

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

594

66,187

        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

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References

	« Hide 'large scale' referencesShow '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: 9851916] [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: 15581640] [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: 16621600] [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: 17878235] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

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Cross-references

Sequence databases
	AF016427 Genomic DNA. Translation: AAB65351.1.
PIR	T03922.
RefSeq	NP_504197.1.
UniGene	Cel.6491
3D structure databases
HSSP	HSSP built from PDB template 1IY0 based on UniProtKB Q9LCZ4.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:25869N.
IntAct	O16299. 6 interactions.
Genome annotation databases
Ensembl	F32D1.1. Caenorhabditis elegans. [Contig view]
GeneID	178829.
KEGG	cel:F32D1.1.
NMPDR	fig\|6239.3.peg.17579.
Organism-specific databases
WormBase	WBGene00017981. figl-1.
WormPep	F32D1.1. CE09865. [WorfDB]
Phylogenomic databases
OMA	O16299. HFDENII.
Gene expression databases
ArrayExpress	O16299.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR003959. ATPase_AAA_core. IPR003960. ATPase_AAA_CS. [Graphical view]
Pfam	PF00004. AAA. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
PROSITE	PS00674. AAA. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	902732.

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Entry information

Entry name

FIGL1_CAEEL

Accession

Primary (citable) accession number: O16299

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project

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Relevant documents

Caenorhabditis elegans

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents