Q7QBW0 (SPAST_ANOGA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Spastin
EC=3.6.4.3

Gene names

Name:	spas
ORF Names:	AGAP002334

Organism

Anopheles gambiae (African malaria mosquito)

Taxonomic identifier

7165 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Anophelinae › Anopheles

Protein attributes

Sequence length	778 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 microtubule organizing center following nucleation 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	Membrane; Single-pass membrane protein Potential. Cytoplasm › cytoskeleton › centrosome By similarity. Cytoplasm › cytoskeleton By similarity.
Sequence similarities	Belongs to the AAA ATPase family. Spastin subfamily. Contains 1 MIT domain.
Sequence caution	The sequence EAA07487.4 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cytoplasm Cytoskeleton Membrane Microtubule
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW microtubule severing Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	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
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 778	778	Spastin		PRO_0000367140
Regions
	Transmembrane	78 – 98	21	Helical; Potential
	Domain	230 – 306	77	MIT
	Nucleotide binding	543 – 550	8	ATP Potential
	Compositional bias	128 – 161	34	His-rich
	Compositional bias	151 – 194	44	Gln-rich
	Compositional bias	420 – 455	36	Gly-rich

Sequences

	Sequence		Length	Mass (Da)
	Q7QBW0 [UniParc]. Last modified March 24, 2009. Version 5. Checksum: 62507ABC78E8F796	FASTA	778	85,276
	10 20 30 40 50 60 MVRNKYTLTT AGKSPSKKSR TGSLSKQHDA TGDDDGETGT LDGSGSAAGS PVGGGTDAAA 70 80 90 100 110 120 KRCDGGSVHK QNLYIISFPV IFVFNVLRSL LYQLFIVFRY VYNFTTKVVY RPVRKECGLE 130 140 150 160 170 180 IVINTDQHGH HHHHHHRHSS HSIHSTAAAH QLQQHQQQQQ HQYSLLQQEQ HGVTEPQQQQ 190 200 210 220 230 240 QQQHQAAHPL QCSQSGILVN GEGREMSIQR SASGSQVGPG DPLLAKQKHH HRRAFEYISK 250 260 270 280 290 300 ALKIDEDNED QKELAIELYR KGILELERGI AVECWGGRGE VWERAQRLHD KMQTNLSMAR 310 320 330 340 350 360 DRLQFLGMLC VCVSVQRKHL HPTRTTLPYR DVKSKLHTTP TENRMVSFNE NCTITTNHHP 370 380 390 400 410 420 ARGTAASSRP TTAATAPATP SLPIKQTASE ASGRKLTVGY KRPGNLGVMN KSQTLPRSMG 430 440 450 460 470 480 GTRTTPTGTG GAGGIAGGLG NGGTYGGSIV GGGAGMPKIV PKPAATPPAI RRQFSVSIPG 490 500 510 520 530 540 VEPKLVQIIM DEIVEGGAKV QWQDIAGQEV AKQALQEMVI LPSVRPELFT GLRTPAKGLL 550 560 570 580 590 600 LFGPPGNGKT LLARAVATEC SATFFSISAA TLTSKYVGDG EKLVRALFAV ARELQPSIIF 610 620 630 640 650 660 IDEVDSVLSE RSSNEHEATR RLKTEFLVQF DGLPANSEAD RIVVMAATNR PQELDEAALR 670 680 690 700 710 720 RFPKRVYVTL PDRDTRELLL RRLLQKQGSP LSDADLAHLA QLTEGYSGSD LTALARDAAL 730 740 750 760 770 EPIRELNVEE VKNMDPTKLR SIRESDFHNS LKRIRRSVAP QSLAAYEKWL QDFGDVTL

References

[1]

"The genome sequence of the malaria mosquito Anopheles gambiae." Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F. , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L. Science 298:129-149(2002) [PubMed: 12364791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PEST.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAAB01008859 Genomic DNA. Translation: EAA07487.4. Different initiation.
RefSeq	XP_312634.5. XM_312634.5.
3D structure databases
HSSP	HSSP built from PDB template 1XWI based on UniProtKB O75351.
ProteinModelPortal	Q7QBW0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1273633.
KEGG	aga:AgaP_AGAP002334.
VectorBase	AGAP002334. Anopheles gambiae.
Organism-specific databases
CTD	1273633.
Phylogenomic databases
eggNOG	inNOG06289.
GeneTree	EMGT00050000004565.
HOGENOM	HBG724153.
OrthoDB	EOG44XGXW.
PhylomeDB	Q7QBW0.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR003959. ATPase_AAA_core. IPR003960. ATPase_AAA_CS. IPR007330. MIT. [Graphical view]
KO	K13254.
Pfam	PF00004. AAA. 1 hit. PF04212. MIT. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. SM00745. MIT. 1 hit. [Graphical view]
PROSITE	PS00674. AAA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SPAST_ANOGA

Accession

Primary (citable) accession number: Q7QBW0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	March 24, 2009
Last modified:	December 14, 2011
This is version 65 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)