Reviewed, UniProtKB/Swiss-Prot A8XV40 (SPAST_CAEBR)

Names and origin

Protein names

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

Gene names

Name:	spas-1
ORF Names:	CBG19220

Organism

Caenorhabditis briggsae [Complete proteome]

Taxonomic identifier

6238 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	542 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Severs microtubules, probably in an ATP-dependent fashion By similarity.
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 By similarity.
Subcellular location	Cytoplasm › cytoskeleton By similarity. Cytoplasm › perinuclear region By similarity. Note: Localized to the perinuclear region of the cytoplasm in early embryos By similarity. Present in the cytoskeletal fraction By similarity.
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
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein hexamerization Inferred from sequence or structural similarity. Source: UniProtKB protein homooligomerization Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	microtubule Inferred from electronic annotation. Source: UniProtKB-KW perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule-severing ATPase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 542	542	Probable spastin homolog spas-1		PRO_0000367131
Regions
	Nucleotide binding	309 – 316	8	ATP Potential
	Coiled coil	29 – 66	38	Potential

Sequences

	Sequence		Length	Mass (Da)
	A8XV40-1 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: 38AD69F081E85355	FASTA	542	60,735
	10 20 30 40 50 60 MFAFSKAPAG CSTYERVTQK FQDGSNKLRA AIEMDELTKQ NGTINEKLQT AELYKQARQM 70 80 90 100 110 120 LKEANEFNIM DIPESKRSEV REKREKTLNL EKSAQDRLIK ICNEVDPNMK RASTAADPCR 130 140 150 160 170 180 AARITPRNTR ATVPGDKKVS KVKQTEKAPH VCSRGDRCGA HQPPPEKKST PLKPVNQIRT 190 200 210 220 230 240 RVKENKNPIG VQQQVFSFIL SCCMRRNCRR PHYLFPCMIS LKMNYFKFQA TLPNQLNTVN 250 260 270 280 290 300 RSNLLKGVDK AIGERLLDEI LDSTGVRMDD VAGCHSAKAT LEEAVILPAL NPNLFSGLRQ 310 320 330 340 350 360 PVKGILLFGP PGNGKTLLAK AVAGESKQMF FNISASSLTS KWVGDSEKTI RGLFQIARNG 370 380 390 400 410 420 QPSIIFIDEI DSILCERSEK DAEVSRRMKT EFLVQFDGAT SSPDDRILVI GATNRPYELD 430 440 450 460 470 480 DAVLRRFPKR IMLNLPDTEA RKELITNTLK KHDMMDGLSS SDIRYIASNT SGFSNSDLVA 490 500 510 520 530 540 LCKEAAMVPV REIHRSKLSV TDGDKIRKIR ASDFDTALRT IRPSTSDRIL SKLSDFSRNF GC

References

[1]

"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. , Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., Waterston R.H. PLoS Biol. 1:166-192(2003) [PubMed: 14624247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CAAC02000558 Genomic DNA. Translation: CAP36507.2.
3D structure databases
ModBase	Search...
Organism-specific databases
WormBase	WBGene00038478. Cbr-spas-1.
Phylogenomic databases
HOGENOM	HBG724153.
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...

Entry information

Entry name

SPAST_CAEBR

Accession

Primary (citable) accession number: A8XV40

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	December 16, 2008
Last modified:	February 9, 2010
This is version 22 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project