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Q9QYY8 (SPAST_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:Kiaa1083, Spg4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length614 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 development of axonal processes and for axonal branching. Ref.8 Ref.10

Catalytic activity

ATP + H2O = ADP + phosphate. HAMAP-Rule MF_03021

Enzyme regulation

Allosteric enzyme with a cooperative mechanism; at least two neighbor subunits influence each other strongly in spastin hexamers. Microtubule binding promotes cooperative interactions among spastin subunits By similarity. HAMAP-Rule MF_03021

Subunit structure

Homohexamer. Mostly monomeric, but assembles into hexameric structure for short periods of time. Oligomerization seems to be a prerequisite for catalytic activity. Binding to ATP in a cleft between two adjacent subunits stabilizes the homohexameric form. Binds to microtubules at least in part via the alpha-tubulin and beta-tubulin tails. The hexamer adopts 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. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 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 By similarity. Evenly distributed along early axons and concentrates in the growth cone of the axons of late stage 3 neurons. Ref.8

Tissue specificity

Expressed in brain, heart, liver, lung, skeletal muscle, spinal cord, spleen and testis. Ref.4 Ref.6

Induction

Expressed is decreased following activation of the Notch pathway by JAG1/Jagged1. Ref.9

Disruption phenotype

Progressive axonal degeneration characterized by focal axonal swellings and the accumulation of organelles and cytoskeletal components, which is suggestive of impaired axonal transport. Late development of mild motor defects. Adults are sterile. Primary cortical neurons develop swellings at the border between stable and dynamic microtubules. Ref.7

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
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Hydrolase
   PTMPhosphoprotein
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence or structural similarity. Source: GOC

ER to Golgi vesicle-mediated transport

Inferred from sequence or structural similarity. Source: UniProtKB

axonogenesis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

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

positive regulation of microtubule depolymerization

Inferred from electronic annotation. Source: UniProtKB-HAMAP

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-HAMAP

cytoplasmic vesicle

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule

Inferred from electronic annotation. Source: UniProtKB-HAMAP

microtubule cytoskeleton

Inferred from direct assay PubMed 20530212. Source: MGI

midbody

Inferred from electronic annotation. Source: UniProtKB-HAMAP

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-HAMAP

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 – 614614Spastin HAMAP-Rule MF_03021
PRO_0000084764

Regions

Transmembrane55 – 7723Helical; Potential
Domain118 – 19376MIT
Nucleotide binding380 – 3878ATP Potential
Region1 – 298298Required for interaction with RTN1 By similarity
Region1 – 192192Required 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 – 19485Sufficient for interaction with CHMP1B By similarity
Region112 – 19887Required for interaction with microtubules By similarity
Region224 – 326103Sufficient for interaction with microtubules By similarity
Region226 – 614389Sufficient for microtubule severing By similarity
Region268 – 32659Required for interaction with microtubules and microtubule severing By similarity
Region308 – 3103Required for interaction with microtubules HAMAP-Rule MF_03021
Motif4 – 118Nuclear localization signal By similarity
Motif57 – 659Nuclear export signal By similarity
Motif307 – 3104Nuclear localization signal By similarity

Amino acid modifications

Modified residue2431Phosphoserine By similarity
Modified residue2661Phosphoserine By similarity
Modified residue3041Phosphothreonine By similarity

Experimental info

Sequence conflict1041E → A in BAC98092. Ref.1
Sequence conflict1041E → A in AAH46286. Ref.2
Sequence conflict1371Missing in AAH46286. Ref.2
Sequence conflict1371Missing in BAB25259. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9QYY8 [UniParc].

Last modified March 24, 2009. Version 3.
Checksum: C0D235031A7E4C8F

FASTA61466,456
        10         20         30         40         50         60 
MSSPAGRRKK KGSGGASPAP ARPPPPAAVP APAAGPAPAA GSPPKRNPSS FSSPLVVGFA 

        70         80         90        100        110        120 
LLRLLACHLG LLFAWLCQRF SRALMAAKRS SGTAPAPASP SPPEPGPGGE AESVRVFHKQ 

       130        140        150        160        170        180 
AFEYISIALR IDEEEKAGQK EQAVEWYKKG IEELEKGIAV IVTGQGEQYE RARRLQAKMM 

       190        200        210        220        230        240 
TNLVMAKDRL QLLEKLQPVL QFSKSQTDVY NESTNLTCRN GHLQSESGAV PKRKDPLTHA 

       250        260        270        280        290        300 
SNSLPRSKTV LKSGSAGLSG HHRAPSCSGL SMVSGARPGP GPAATTHKGT PKPNRTNKPS 

       310        320        330        340        350        360 
TPTTAVRKKK DLKNFRNVDS NLANLIMNEI VDNGTAVKFD DIAGQELAKQ ALQEIVILPS 

       370        380        390        400        410        420 
LRPELFTGLR APARGLLLFG PPGNGKTMLA KAVAAESNAT FFNISAASLT SKYVGEGEKL 

       430        440        450        460        470        480 
VRALFAVARE LQPSIIFIDE VDSLLCERRE GEHDASRRLK TEFLIEFDGV QSAGDDRVLV 

       490        500        510        520        530        540 
MGATNRPQEL DEAVLRRFIK RVYVSLPNEE TRLLLLKNLL CKQGSPLTQK ELAQLARMTD 

       550        560        570        580        590        600 
GYSGSDLTAL AKDAALGPIR ELKPEQVKNM SASEMRNIRL SDFTESLKKI KRSVSPQTLE 

       610 
AYIRWNKDFG DTTV 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryonic tail.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N-3.
Tissue: Mammary tumor.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-614.
Strain: C57BL/6J.
Tissue: Pancreas.
[4]"Spastin, a new AAA protein, is altered in the most frequent form of autosomal dominant spastic paraplegia."
Hazan J., Fonknechten N., Mavel D., Paternotte C., Samson D., Artiguenave F., Davoine C.-S., Cruaud C., Durr A., Wincker P., Brottier P., Cattolico L., Barbe V., Burgunder J.-M., Prud'homme J.-F., Brice A., Fontaine B., Heilig R., Weissenbach J.
Nat. Genet. 23:296-303(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 111-614, TISSUE SPECIFICITY.
[5]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[6]"Spastin subcellular localization is regulated through usage of different translation start sites and active export from the nucleus."
Claudiani P., Riano E., Errico A., Andolfi G., Rugarli E.I.
Exp. Cell Res. 309:358-369(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"A mutation of spastin is responsible for swellings and impairment of transport in a region of axon characterized by changes in microtubule composition."
Tarrade A., Fassier C., Courageot S., Charvin D., Vitte J., Peris L., Thorel A., Mouisel E., Fonknechten N., Roblot N., Seilhean D., Dierich A., Hauw J.J., Melki J.
Hum. Mol. Genet. 15:3544-3558(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[8]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"Microtubule stabilizing effect of notch activation in primary cortical neurons."
Ferrari-Toninelli G., Bonini S.A., Bettinsoli P., Uberti D., Memo M.
Neuroscience 154:946-952(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[10]"Pleiotropic effects of spastin on neurite growth depending on expression levels."
Riano E., Martignoni M., Mancuso G., Cartelli D., Crippa F., Toldo I., Siciliano G., Di Bella D., Taroni F., Bassi M.T., Cappelletti G., Rugarli E.I.
J. Neurochem. 108:1277-1288(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK129282 mRNA. Translation: BAC98092.1.
BC046286 mRNA. Translation: AAH46286.1.
AK007793 mRNA. Translation: BAB25259.1.
AJ246002 mRNA. Translation: CAB60143.1.
CCDSCCDS50181.1.
RefSeqNP_001156342.1. NM_001162870.1.
NP_058658.2. NM_016962.2.
UniGeneMm.19804.

3D structure databases

ProteinModelPortalQ9QYY8.
SMRQ9QYY8. Positions 110-194, 322-610.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9QYY8.

Proteomic databases

PaxDbQ9QYY8.
PRIDEQ9QYY8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024869; ENSMUSP00000024869; ENSMUSG00000024068.
GeneID50850.
KEGGmmu:50850.
UCSCuc008dnz.2. mouse.

Organism-specific databases

CTD6683.
MGIMGI:1858896. Spast.
RougeSearch...

Phylogenomic databases

eggNOGCOG0464.
GeneTreeENSGT00570000078874.
HOGENOMHOG000225146.
HOVERGENHBG108502.
InParanoidQ9QYY8.
KOK13254.
OMASEMRNIK.
OrthoDBEOG7GXPCR.
PhylomeDBQ9QYY8.
TreeFamTF105014.

Gene expression databases

BgeeQ9QYY8.
CleanExMM_SPAST.
GenevestigatorQ9QYY8.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_03021. Spastin.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR007330. MIT.
IPR027417. P-loop_NTPase.
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]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio307827.
PROQ9QYY8.
SOURCESearch...

Entry information

Entry nameSPAST_MOUSE
AccessionPrimary (citable) accession number: Q9QYY8
Secondary accession number(s): Q6ZPY6, Q80VE0, Q9CVK0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: March 24, 2009
Last modified: July 9, 2014
This is version 124 of the entry and version 3 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot