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Q719N1 (SPAST_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Spastin

EC=3.6.4.3
Gene names
Name:SPAST
Synonyms:SPG4
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length613 AA.
Sequence statusFragment.
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. Also plays a role in axon growth and the formation of axonal branches By similarity.

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.

Sequence caution

The sequence AAQ11224.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Differentiation
Neurogenesis
   Cellular componentCytoplasm
Cytoskeleton
Endoplasmic reticulum
Endosome
Membrane
Microtubule
Nucleus
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Hydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
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 componentendoplasmic 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-KW

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

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

Chain‹1 – 613›613Spastin
PRO_0000367134

Regions

Transmembrane54 – 7421Helical; Potential
Domain116 – 19277MIT
Nucleotide binding379 – 3868ATP Potential
Region1 – 297297Required for interaction with RTN1 By similarity
Region1 – 191191Required for midbody localization By similarity
Region1 – 7777Required for interaction with ATL1 By similarity
Region1 – 4747Required for nuclear localization By similarity
Region47 – 8438Required for interaction with SSNA1 and microtubules By similarity
Region109 – 19385Sufficient for interaction with CHMP1B By similarity
Region111 – 19787Required for interaction with microtubules By similarity
Region224 – 325102Sufficient for interaction with microtubules By similarity
Region225 – 613389Sufficient for microtubule severing By similarity
Region267 – 32559Required for interaction with microtubules and microtubule severing By similarity
Motif1 – 88Nuclear localization signal By similarity
Motif56 – 649Nuclear export signal By similarity
Motif306 – 3094Nuclear localization signal By similarity
Compositional bias13 – 4230Pro-rich

Amino acid modifications

Modified residue2651Phosphoserine By similarity
Modified residue3001Phosphothreonine By similarity
Modified residue3031Phosphothreonine By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q719N1 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: CD0E0273530C38BD

FASTA61367,381
        10         20         30         40         50         60 
PGGRGKKKGS GGPSSPVPPR PPPPCLASSR PAPRPAPPPQ SPHKRNLYYF SYPLFLGFAL 

        70         80         90        100        110        120 
LRLVAFHLGL LFVWLCQRFS RALMAAKRSS RAAPAPASAS PPAPVPGGEV ERVRAFHKQA 

       130        140        150        160        170        180 
FEYISVALRI DEDEKVGQKE QAVEWYKKGI EELEKGIAVV VTGQGEQCER ARRLQAKMMT 

       190        200        210        220        230        240 
NLVMAKDRLQ LLEKLQPVLQ FSKSQMDVYN DSTNLTCRNG HLQSESGAVP KRKDPLTHPS 

       250        260        270        280        290        300 
NSLPRSKAIM KTGSTGLSGH HRAPSCSGLS IVSGMRQGPG PTTATHKSTP KTNRTNKPST 

       310        320        330        340        350        360 
PTTAPRKKKD LKNFRNVDSN LANFIMNEIV DNGTAVKFDD IAGQELAKQA LQEIVILPSL 

       370        380        390        400        410        420 
RPELFTGLRA PARGLLLFGP PGNGKTMLAK AVAAESNATF FNISAASLTS KYVGEGEKLV 

       430        440        450        460        470        480 
RALFAVAREL QPSIIFIDEV DSLLRERREG EHDASRRLKT EFLIEFDGVQ SAGDDRVLVM 

       490        500        510        520        530        540 
GATNRPQELD EAVLRRFIKR VYVSLPNEET RLLLLKNLLC KQGSPLTQKE LAQLARLTDG 

       550        560        570        580        590        600 
YSGSDLTALA KDAALGPIRE LKPEQVKNMS ASEMRNIRLS DFTESLKKIK RSVSPQTLEA 

       610 
YIRWNKDFGD TTV 

« Hide

References

[1]"Analysis and mapping of CACNB4, CHRNA1, KCNJ3, SCN2A and SPG4, physiological candidate genes for porcine congenital progressive ataxia and spastic paresis."
Genini S., Kratzsch A., Korczak B., Neuenschwander S., Brenig B., Jorg H., Burgi E., Ossent P., Stranzinger G., Vogeli P.
J. Anim. Breed. Genet. 124:269-276(2007) [PubMed: 17868079] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF540879 mRNA. Translation: AAQ11224.1. Different initiation.
RefSeqNP_998914.1. NM_213749.1.
UniGeneSsc.19685.

3D structure databases

HSSPHSSP built from PDB template 1XWI based on UniProtKB O75351.
ProteinModelPortalQ719N1.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ719N1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396584.
KEGGssc:396584.

Organism-specific databases

CTD6683.

Phylogenomic databases

GeneTreeENSGT00570000078874.
HOVERGENHBG108502.
OrthoDBEOG4NZTTF.

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.
SM00745. MIT. 1 hit.
[Graphical view]
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPAST_PIG
AccessionPrimary (citable) accession number: Q719N1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: November 16, 2011
This is version 58 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