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Protein

Spastin

Gene

Spast

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent microtubule severing protein that specifically regognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Severing activity is not dependent on tubulin acetylation or detyrosination. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex. Recruited at the midbody, probably by IST1, and participates to membrane fission during abscission together with the ESCRT-III complex. Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling. Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing (By similarity). Probably plays a role in axon growth and the formation of axonal branches (PubMed:18234839).UniRule annotation1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation

Enzyme regulationi

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.UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi347 – 3548ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase

Keywords - Biological processi

Cell cycle, Cell division, Differentiation, Neurogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
SpastinUniRule annotation (EC:3.6.4.3UniRule annotation)
Gene namesi
Name:SpastUniRule annotation
Synonyms:Spg4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi1308494. Spast.

Subcellular locationi

  • Membrane UniRule annotation; Peripheral membrane protein UniRule annotation
  • Endoplasmic reticulum UniRule annotation
  • Midbody UniRule annotation
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome UniRule annotation
  • Cytoplasmcytoskeleton UniRule annotation
  • Cytoplasmperinuclear region UniRule annotation
  • Nucleus UniRule annotation
  • Cytoplasmcytoskeletonspindle UniRule annotation
  • Cytoplasm UniRule annotation

  • Note: Forms a intramembrane hairpin-like structure in the membrane. 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.UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5454CytoplasmicUniRule annotationAdd
BLAST
Intramembranei55 – 7521HelicalUniRule annotationAdd
BLAST
Topological domaini76 – 581506CytoplasmicUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Endoplasmic reticulum, Membrane, Microtubule, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 581581SpastinPRO_0000367135Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei210 – 2101PhosphoserineCombined sources
Modified residuei233 – 2331PhosphoserineBy similarity
Modified residuei271 – 2711PhosphothreonineBy similarity
Modified residuei562 – 5621PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiB2RYN7.
PeptideAtlasiB2RYN7.
PRIDEiB2RYN7.

PTM databases

iPTMnetiB2RYN7.

Expressioni

Gene expression databases

ExpressionAtlasiB2RYN7. baseline and differential.
GenevisibleiB2RYN7. RN.

Interactioni

Subunit structurei

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 SSNA1. Interacts with ATL1. Interacts with RTN1. Interacts with ZFYVE27. Interacts with REEP1. Interacts (via MIT domain) with IST1.UniRule annotation

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000033763.

Structurei

3D structure databases

ProteinModelPortaliB2RYN7.
SMRiB2RYN7. Positions 289-573.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini118 – 19275MITSequence analysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 265265Required for interaction with RTN1By similarityAdd
BLAST
Regioni1 – 191191Required for midbody localizationBy similarityAdd
BLAST
Regioni1 – 7878Required for interaction with ATL1By similarityAdd
BLAST
Regioni1 – 4848Required for nuclear localizationBy similarityAdd
BLAST
Regioni48 – 8538Required for interaction with SSNA1 and microtubulesBy similarityAdd
BLAST
Regioni193 – 581389Sufficient for microtubule severingBy similarityAdd
BLAST
Regioni235 – 29359Required for interaction with microtubules and microtubule severingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi4 – 118Nuclear localization signalUniRule annotation
Motifi57 – 659Nuclear export signalUniRule annotation
Motifi274 – 2774Nuclear localization signalUniRule annotation

Sequence similaritiesi

Belongs to the AAA ATPase family. Spastin subfamily.UniRule annotation
Contains 1 MIT domain.Sequence analysis

Phylogenomic databases

eggNOGiKOG0740. Eukaryota.
COG0464. LUCA.
HOGENOMiHOG000225146.
HOVERGENiHBG108502.
InParanoidiB2RYN7.
KOiK13254.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_03021. Spastin.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR007330. MIT.
IPR027417. P-loop_NTPase.
IPR017179. Spastin.
IPR015415. Vps4_C.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00745. MIT. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2RYN7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSPAGRRKK KGSGGASPAP ARPPPPAAVP APAAGPAPAP GSPHKRNLYY
60 70 80 90 100
FSYPLVVGFA LLRLLACHLG LLFVWLCQRF SRALMAAKRS SGTAPAPASP
110 120 130 140 150
STPAPGPGGE AESVRVFHKQ AFEYISIALR IDEEEKGQKE QAVEWYKKGI
160 170 180 190 200
EELEKGIAVI VTGQGEQYER ARRLQAKMMT NLVMAKDRLQ LLESGAVPKK
210 220 230 240 250
KDPLTHASNS LPRSKTVMKS GSTGLSGHHR APSCSGLSMV SGARPGSGPA
260 270 280 290 300
ATTHKGTSKP NRTNKPSTPT TAVRKKKDLK NFRNVDSNLA NLIMNEIVDN
310 320 330 340 350
GTAVKFDDIA GQELAKQALQ EIVILPSLRP ELFTGLRAPA RGLLLFGPPG
360 370 380 390 400
NGKTMLAKAV AAESNATFFN ISAASLTSKY VGEGEKLVRA LFAVARELQP
410 420 430 440 450
SIIFIDEVDS LLCERREGEH DASRRLKTEF LIEFDGVQSA GDDRVLVMGA
460 470 480 490 500
TNRPQELDEA VLRRFIKRVY VSLPNEETRL LLLKNLLCKQ GSPLTQKELA
510 520 530 540 550
QLARMTDGYS GSDLTALAKD AALGPIRELK PEQVKNMSAS EMRNIRLSDF
560 570 580
TESLKKIKRS VSPQTLEAYI RWNKDFGDTT V
Length:581
Mass (Da):63,022
Last modified:July 1, 2008 - v1
Checksum:iA404A3B676F9F224
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC166846 mRNA. Translation: AAI66846.1.
RefSeqiNP_001102172.2. NM_001108702.2.
UniGeneiRn.41645.

Genome annotation databases

EnsembliENSRNOT00000039375; ENSRNOP00000033763; ENSRNOG00000027136.
GeneIDi362700.
KEGGirno:362700.
UCSCiRGD:1308494. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC166846 mRNA. Translation: AAI66846.1.
RefSeqiNP_001102172.2. NM_001108702.2.
UniGeneiRn.41645.

3D structure databases

ProteinModelPortaliB2RYN7.
SMRiB2RYN7. Positions 289-573.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000033763.

PTM databases

iPTMnetiB2RYN7.

Proteomic databases

PaxDbiB2RYN7.
PeptideAtlasiB2RYN7.
PRIDEiB2RYN7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000039375; ENSRNOP00000033763; ENSRNOG00000027136.
GeneIDi362700.
KEGGirno:362700.
UCSCiRGD:1308494. rat.

Organism-specific databases

CTDi6683.
RGDi1308494. Spast.

Phylogenomic databases

eggNOGiKOG0740. Eukaryota.
COG0464. LUCA.
HOGENOMiHOG000225146.
HOVERGENiHBG108502.
InParanoidiB2RYN7.
KOiK13254.

Miscellaneous databases

PROiB2RYN7.

Gene expression databases

ExpressionAtlasiB2RYN7. baseline and differential.
GenevisibleiB2RYN7. RN.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_03021. Spastin.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR007330. MIT.
IPR027417. P-loop_NTPase.
IPR017179. Spastin.
IPR015415. Vps4_C.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00745. MIT. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSPAST_RAT
AccessioniPrimary (citable) accession number: B2RYN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: July 6, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.