Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q6NW58 (SPAST_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Spastin

EC=3.6.4.3
Gene names
Name:spast
Synonyms:spg4
ORF Names:zgc:85952, si:ch73-233a22.3
OrganismDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and for completion of the abscission stage of cytokinesis By similarity. Required for axon growth. Ref.1

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Homohexamer. The homohexamer is stabilized by ATP-binding. The homohexamer may adopt a ring conformation through which microtubules pass prior to being severed. Interacts with microtubules By similarity.

Subcellular location

Membrane; Single-pass membrane protein Potential. Cytoplasmcytoskeletoncentrosome By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmperinuclear region By similarity. Nucleus By similarity.

Developmental stage

Maternally expressed. Expressed at low levels throughout the embryo up to 24 hours post-fertilization (hpf). Ref.1

Disruption phenotype

Branchiomotor neurons exhibit reduced axonal outgrowth and aberrant positioning of neuronal cell bodies. Outgrowth of motor axons from the spinal cord is impaired, the number and length of spinal motor neurons is reduced, and elevated levels of apoptosis are observed in the CNS. Thickened bundles of axonal microtubules are observed in the spinal cord. Longitudinal fascicles in the hindbrain are disordered. Most embryos are immotile and fail to hatch, while those that do exhibit reduced motility and swimming defects. Ref.1

Sequence similarities

Belongs to the AAA ATPase family. Spastin subfamily.

Contains 1 MIT domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Differentiation
Neurogenesis
   Cellular componentCytoplasm
Cytoskeleton
Membrane
Microtubule
Nucleus
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processaxon extension involved in development

Inferred from mutant phenotype. Source: ZFIN

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

central nervous system neuron axonogenesis

Inferred from mutant phenotype Ref.1. Source: ZFIN

cytoplasmic microtubule organization

Inferred from mutant phenotype. Source: ZFIN

microtubule bundle formation

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule severing

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.1. Source: ZFIN

positive regulation of axon extension

Inferred from mutant phenotype Ref.1. Source: ZFIN

positive regulation of microtubule depolymerization

Inferred from mutant phenotype Ref.1. Source: ZFIN

protein hexamerization

Inferred from sequence or structural similarity. Source: UniProtKB

protein homooligomerization

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

alpha-tubulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

beta-tubulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule binding

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule-severing ATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 570570Spastin
PRO_0000367137

Regions

Transmembrane38 – 5417Helical; Potential
Domain83 – 15876MIT
Nucleotide binding335 – 3428ATP Potential

Experimental info

Sequence conflict2241C → R in AAH67715. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q6NW58 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: 2EE116D8B18DD9AA

FASTA57063,086
        10         20         30         40         50         60 
MNSGHKARLR GGRACGPVSD GSARGNRLLF YTRSLSRVPE WLLRVLLLLL RWLFQPIRRA 

        70         80         90        100        110        120 
MAARAKECGP DGSEETGERI RNYHKQAFEF ISVALQIDED EKGDKQKAVQ WYRKGIAELE 

       130        140        150        160        170        180 
KGIQIQVTGA GEKADRARKL QDKMITNLSM AEDRLKLLGN LLSQSPAESS SDDSFYSFSN 

       190        200        210        220        230        240 
GNLRPAPASG AVSKKKDTLT ITNQTSLRPK NPPKSTPNAS GLNCTPSAAQ SSRTGPQNNQ 

       250        260        270        280        290        300 
KGPTVKGKNN VKASTTATAS PQRKRDMKNF KNVDSKLASL ILNEIVDSGS VVRFDDIAGQ 

       310        320        330        340        350        360 
DLAKQALQEI VILPALRPEL FTGLRAPARG LLLFGPPGNG KTMLAKAVAM ESNATFFNIS 

       370        380        390        400        410        420 
AATLTSKYVG EGEKLVRALF AVARELQPSI IFIDEIDSLL CERREGEHDA SRRLKTEFLI 

       430        440        450        460        470        480 
EFDGVQSGGD ERVLVMGATN RPQELDEAVL RRFAKRIYVA LPTEETRLKL LKNLLSKHRN 

       490        500        510        520        530        540 
PLSQKELSQL ARLTDGYSGS DLTSLAKDAA LGPIRELKPE QVRNMSAHEM RDIRISDFLE 

       550        560        570 
SLKRIKRSVS PQTLDQYVRW NREYGDTTGV 

« Hide

References

« Hide 'large scale' references
[1]"The microtubule-severing protein spastin is essential for axon outgrowth in the zebrafish embryo."
Wood J.D., Landers J.A., Bingley M., McDermott C.J., Thomas-McArthur V., Gleadall L.J., Shaw P.J., Cunliffe V.T.
Hum. Mol. Genet. 15:2763-2771(2006) [PubMed: 16893913] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[2]The Danio rerio sequencing project at the Sanger Institute
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[3]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY304504 mRNA. Translation: AAQ74774.1.
CU651563 Genomic DNA. Translation: CAX13091.1.
BC067715 mRNA. Translation: AAH67715.1.
IPIIPI00497843.
RefSeqNP_998080.1. NM_212915.1.
UniGeneDr.30307.

3D structure databases

HSSPHSSP built from PDB template 1YPW based on UniProtKB Q01853.
ProteinModelPortalQ6NW58.
SMRQ6NW58. Positions 276-561.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6NW58.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000035150; ENSDARP00000029675; ENSDARG00000024933.
GeneID405851.
KEGGdre:405851.

Organism-specific databases

CTD6683.
ZFINZDB-GENE-040426-2331. spast.

Phylogenomic databases

eggNOGfiNOG13914.
GeneTreeENSGT00570000078874.
HOGENOMHBG724153.
HOVERGENHBG108502.
OMATHKSTPK.
OrthoDBEOG4NZTTF.
PhylomeDBQ6NW58.

Gene expression databases

ArrayExpressQ6NW58.
BgeeQ6NW58.

Family and domain databases

InterProIPR003593. ATPase_AAA+_core.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR007330. MIT.
IPR017179. Spastin.
[Graphical view]
KOK13254.
PfamPF00004. AAA. 1 hit.
PF04212. MIT. 1 hit.
[Graphical view]
PIRSFPIRSF037338. Spastin. 1 hit.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPAST_DANRE
AccessionPrimary (citable) accession number: Q6NW58
Secondary accession number(s): Q6JUU0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: November 16, 2011
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families