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Reviewed, UniProtKB/Swiss-Prot B2RYN7 (SPAST_RAT)

Last modified October 13, 2009. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Spastin
    EC=3.6.4.3
Gene names
Name: Spast
Synonyms: Spg4
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length581 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. Plays a role in axon growth and the formation of axonal branches.

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Homohexamer. Binding to ATP stabilizes the homohexameric form. Binds to microtubules at least in part via the alpha-tubulin and beta-tubulin tails. The hexamer may adopt a ring conformation through which microtubules pass prior to being severed. Does not interact strongly with tubulin heterodimers. Interacts (via MIT domain) with CHMP1B; the interaction is direct. Interacts with ATL1, RTN1, SSNA1 and ZFYVE27 By similarity.

Subcellular location

Membrane; Single-pass membrane protein Potential. Cytoplasmcytoskeletoncentrosome By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmperinuclear region By similarity. Endoplasmic reticulum By similarity. Endosome By similarity. Nucleus By similarity. Cytoplasmcytoskeletonspindle By similarity. Note: Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B. Enriched in the distal axons and branches of postmitotic neurons By similarity.

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
Endoplasmic reticulum
Endosome
Membrane
Microtubule
Nucleus
   DomainTransmembrane
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Hydrolase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processER to Golgi vesicle-mediated transport

Inferred from sequence or structural similarity. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cytokinesis, completion of separation

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule bundle formation

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule severing

Inferred from sequence or structural similarity. Source: UniProtKB

nervous system development

Inferred from electronic annotation. Source: UniProtKB-KW

protein hexamerization

Inferred from sequence or structural similarity. Source: UniProtKB

protein homooligomerization

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentcentrosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

spindle

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 – 581581Spastin
PRO_0000367135

Regions

Transmembrane55 – 7521 Potential
Domain117 – 19276MIT
Nucleotide binding347 – 3548ATP Potential
Region1 – 265265Required for interaction with RTN1 By similarity
Region1 – 191191Required for midbody localization By similarity
Region1 – 7878Required for interaction with ATL1 By similarity
Region1 – 4848Required for nuclear localization By similarity
Region48 – 8538Required for interaction with SSNA1 and microtubules By similarity
Region110 – 19384Sufficient for interaction with CHMP1B By similarity
Region111 – 19484Required for interaction with microtubules By similarity
Region194 – 581388Sufficient for microtubule severing By similarity
Region194 – 293100Sufficient for interaction with microtubules By similarity
Region235 – 29359Required for interaction with microtubules and microtubule severing By similarity
Motif4 – 118Nuclear localization signal By similarity
Motif57 – 659Nuclear export signal By similarity
Motif274 – 2774Nuclear localization signal By similarity

Amino acid modifications

Modified residue2331Phosphoserine By similarity
Modified residue2681Phosphothreonine By similarity
Modified residue2711Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2RYN7-1 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: A404A3B676F9F224

FASTA58163,022
        10         20         30         40         50         60 
MSSPAGRRKK KGSGGASPAP ARPPPPAAVP APAAGPAPAP GSPHKRNLYY FSYPLVVGFA 

        70         80         90        100        110        120 
LLRLLACHLG LLFVWLCQRF SRALMAAKRS SGTAPAPASP STPAPGPGGE AESVRVFHKQ 

       130        140        150        160        170        180 
AFEYISIALR IDEEEKGQKE QAVEWYKKGI EELEKGIAVI VTGQGEQYER ARRLQAKMMT 

       190        200        210        220        230        240 
NLVMAKDRLQ LLESGAVPKK KDPLTHASNS LPRSKTVMKS GSTGLSGHHR APSCSGLSMV 

       250        260        270        280        290        300 
SGARPGSGPA ATTHKGTSKP NRTNKPSTPT TAVRKKKDLK NFRNVDSNLA NLIMNEIVDN 

       310        320        330        340        350        360 
GTAVKFDDIA GQELAKQALQ EIVILPSLRP ELFTGLRAPA RGLLLFGPPG NGKTMLAKAV 

       370        380        390        400        410        420 
AAESNATFFN ISAASLTSKY VGEGEKLVRA LFAVARELQP SIIFIDEVDS LLCERREGEH 

       430        440        450        460        470        480 
DASRRLKTEF LIEFDGVQSA GDDRVLVMGA TNRPQELDEA VLRRFIKRVY VSLPNEETRL 

       490        500        510        520        530        540 
LLLKNLLCKQ GSPLTQKELA QLARMTDGYS GSDLTALAKD AALGPIRELK PEQVKNMSAS 

       550        560        570        580 
EMRNIRLSDF TESLKKIKRS VSPQTLEAYI RWNKDFGDTT V 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[2]"The microtubule-severing proteins spastin and katanin participate differently in the formation of axonal branches."
Yu W., Qiang L., Solowska J.M., Karabay A., Korulu S., Baas P.W.
Mol. Biol. Cell 19:1485-1498(2008) [PubMed: 18234839] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

BC166846 mRNA. Translation: AAI66846.1.
IPIIPI00365573.
UniGeneRn.41645

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB2RYN7.

Organism-specific databases

RGD1308494. Spast.

Gene expression databases

GenevestigatorB2RYN7.

Family and domain databases

InterProIPR003593. ATPase_AAA+_core.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR007330. MIT.
IPR017179. Spastin.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF04212. MIT. 1 hit.
[Graphical view]
PIRSFPIRSF037338. Spastin. 1 hit.
SMARTSM00382. AAA. 1 hit.
SM00745. MIT. 1 hit.
[Graphical view]
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPAST_RAT
AccessionPrimary (citable) accession number: B2RYN7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: October 13, 2009
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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