Reviewed, UniProtKB/Swiss-Prot Q8MNV0 (SPAST_CAEEL)

Names and origin

Protein names

Recommended name:
    Probable spastin homolog spas-1
    EC=3.6.4.3

Gene names

Name:	spas-1
ORF Names:	C24B5.2

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	512 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Severs microtubules, probably in an ATP-dependent fashion. Ref.2 Ref.3
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. Ref.3
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › perinuclear region. Note: Localized to the perinuclear region of the cytoplasm in early embryos. Also present in the cytoskeletal fraction. Ref.2
Developmental stage	Highly expressed in the embryo and at lower levels in L3-L4 larvae. Isoform spas-1L is highly expressed in the embryo while isoform spas-1S is expressed throughout development. Ref.2
Disruption phenotype	Slow growth, reduced brood size, abnormal oogenesis and multiple vulvae. Increased numbers of centrosomal microtubules in early embryos. Ref.2
Sequence similarities	Belongs to the AAA ATPase family. Spastin subfamily.
Caution	Lacks the conserved MIT domain, which is one of the features of the spastin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	microtubule bundle formation Ref.2 Non-traceable author statement. Source: UniProtKB microtubule severing Ref.3 Inferred from direct assay. Source: UniProtKB positive regulation of microtubule depolymerization Ref.2 Ref.3 Inferred from direct assay. Source: UniProtKB protein hexamerization Ref.3 Inferred from direct assay. Source: UniProtKB protein homooligomerization Ref.3 Inferred from direct assay. Source: UniProtKB
Cellular component	microtubule Inferred from electronic annotation. Source: UniProtKB-KW perinuclear region of cytoplasm Ref.2 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Ref.2 Ref.3 Non-traceable author statement. Source: UniProtKB microtubule-severing ATPase activity Ref.3 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform spas-1L (identifier: Q8MNV0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform spas-1S (identifier: Q8MNV0-2)

Also known as: a;

The sequence of this isoform differs from the canonical sequence as follows:
     139-199: Missing.

Note: No experimental confirmation available.

Isoform b (identifier: Q8MNV0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     139-153: EKKNAAKAKENDENR → VSIQILYNIFYFVTY
     154-512: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 512	512	Probable spastin homolog spas-1		PRO_0000367132
Regions
	Nucleotide binding	279 – 286	8	ATP Probable
	Coiled coil	32 – 97	66	Potential
Natural variations
	Alternative sequence	139 – 199	61	Missing in isoform spas-1S.		VSP_036645
	Alternative sequence	139 – 153	15	EKKNA…NDENR → VSIQILYNIFYFVTY in isoform b.		VSP_036646
	Alternative sequence	154 – 512	359	Missing in isoform b.		VSP_036647
Experimental info
	Mutagenesis	285	1	K → R: Abrogates microtubule severing. Ref.2
	Mutagenesis	312	1	W → A: Abrogates microtubule severing. Ref.2
	Mutagenesis	339	1	E → Q: Abrogates microtubule severing, promotes homohexamerization and promotes association with microtubules. Ref.2 Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform spas-1L [UniParc]. Last modified March 24, 2009. Version 2. Checksum: 8CA8E44B54F713AB	FASTA	512	56,901
	10 20 30 40 50 60 MFAFSKGPAG SSTYDRVAQK FQDGYEKMRA AIEMDELTKH AGSIQEKLRT AELYKEARSL 70 80 90 100 110 120 LKEANEFNIM DIPETRRSEI RDKRQNMMKL EKSAQDRLIA ICNEVDPNVK QSRSATVGPS 130 140 150 160 170 180 RPASAARVTP RPTRATAPEK KNAAKAKEND ENRHVCSRGD RCGAHHQPVT KKSDTVHPEP 190 200 210 220 230 240 PVQASNRKME TVKRVKVDKA SLPMHQNPVN RAALLNGVDK VIGERLLDEV LDNTGVRMDD 250 260 270 280 290 300 VAGCHSAKAA LEEAVILPAL NPNLFKGLRQ PVKGILLFGP PGNGKTLLAK AVAGESKQMF 310 320 330 340 350 360 FNISASSLTS KWVGDSEKTI RGLFQIARNA QPSIIFIDEI DSILCERSEK DAEVSRRMKT 370 380 390 400 410 420 EFLVQFDGAT SSADDRILVI GATNRPHELD DAVLRRFPKR IMLNLPDEEA RKELITKTLK 430 440 450 460 470 480 KHNMMDGLIS SDIRYIASNT SGFSNSDLVA LCKEAAMVPI REIDRSKLSM TDGEKIRKIR 490 500 510 ASDFDTALRT IRPSTSQKIM SKLSDFSRSF GC
	Isoform spas-1S (a). Checksum: 610F9F639F61B4AB	FASTA	451	50,017
	10 20 30 40 50 60 MFAFSKGPAG SSTYDRVAQK FQDGYEKMRA AIEMDELTKH AGSIQEKLRT AELYKEARSL 70 80 90 100 110 120 LKEANEFNIM DIPETRRSEI RDKRQNMMKL EKSAQDRLIA ICNEVDPNVK QSRSATVGPS 130 140 150 160 170 180 RPASAARVTP RPTRATAPAS LPMHQNPVNR AALLNGVDKV IGERLLDEVL DNTGVRMDDV 190 200 210 220 230 240 AGCHSAKAAL EEAVILPALN PNLFKGLRQP VKGILLFGPP GNGKTLLAKA VAGESKQMFF 250 260 270 280 290 300 NISASSLTSK WVGDSEKTIR GLFQIARNAQ PSIIFIDEID SILCERSEKD AEVSRRMKTE 310 320 330 340 350 360 FLVQFDGATS SADDRILVIG ATNRPHELDD AVLRRFPKRI MLNLPDEEAR KELITKTLKK 370 380 390 400 410 420 HNMMDGLISS DIRYIASNTS GFSNSDLVAL CKEAAMVPIR EIDRSKLSMT DGEKIRKIRA 430 440 450 SDFDTALRTI RPSTSQKIMS KLSDFSRSFG C
	Isoform b. Checksum: 8E2DC56BA5268E90	FASTA	153	17,397
	10 20 30 40 50 60 MFAFSKGPAG SSTYDRVAQK FQDGYEKMRA AIEMDELTKH AGSIQEKLRT AELYKEARSL 70 80 90 100 110 120 LKEANEFNIM DIPETRRSEI RDKRQNMMKL EKSAQDRLIA ICNEVDPNVK QSRSATVGPS 130 140 150 RPASAARVTP RPTRATAPVS IQILYNIFYF VTY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING. Strain: Bristol N2.
[2]	"The C. elegans homologue of the spastic paraplegia protein, spastin, disassembles microtubules." Matsushita-Ishiodori Y., Yamanaka K., Ogura T. Biochem. Biophys. Res. Commun. 359:157-162(2007) [PubMed: 17531954] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-285; TRP-312 AND GLU-339.
[3]	"Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin." Roll-Mecak A., Vale R.D. Nature 451:363-367(2008) [PubMed: 18202664] [Abstract] Cited for: 3D-STRUCTURE MODELING, FUNCTION, HOMOHEXAMERIZATION, MUTAGENESIS OF GLU-339.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U53149 Genomic DNA. Translation: AAM29664.1. U53149 Genomic DNA. Translation: AAM29665.1.
RefSeq	NP_741586.1. NP_741587.1.
UniGene	Cel.22726
3D structure databases
HSSP	HSSP built from PDB template 1R7R based on UniProtKB Q01853.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8MNV0.
Proteomic databases
PRIDE	Q8MNV0.
Genome annotation databases
Ensembl	C24B5.2a; C24B5.2a; C24B5.2; Caenorhabditis elegans. [Genome view]
GeneID	179300.
KEGG	cel:C24B5.2.
UCSC	C24B5.2a. c. elegans.
Organism-specific databases
WormBase	WBGene00016045. spas-1.
WormPep	C24B5.2a. CE30731. [WorfDB] C24B5.2b. CE30732. [WorfDB]
Phylogenomic databases
OMA	KACESKK.
Gene expression databases
ArrayExpress	Q8MNV0.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR003959. ATPase_AAA_core. IPR003960. ATPase_AAA_CS. [Graphical view]
Pfam	PF00004. AAA. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
PROSITE	PS00674. AAA. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	904790.

Entry information

Entry name

SPAST_CAEEL

Accession

Primary (citable) accession number: Q8MNV0
Secondary accession number(s): Q7M3K5, Q8MNU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	March 24, 2009
Last modified:	November 3, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project