SPAST_ANOGA
ID SPAST_ANOGA Reviewed; 827 AA.
AC Q7QBW0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 6.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Spastin {ECO:0000255|HAMAP-Rule:MF_03021};
DE EC=5.6.1.1 {ECO:0000255|HAMAP-Rule:MF_03021};
GN Name=spas; ORFNames=AGAP002334;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
CC -!- FUNCTION: ATP-dependent microtubule severing protein. Microtubule
CC severing may promote reorganization of cellular microtubule arrays and
CC the release of microtubules from the microtubule organizing center
CC following nucleation. {ECO:0000255|HAMAP-Rule:MF_03021}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1)
CC alpha/beta tubulin heterodimers.; EC=5.6.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
CC -!- SUBUNIT: Homohexamer. The homohexamer is stabilized by ATP-binding. The
CC homohexamer may adopt a ring conformation through which microtubules
CC pass prior to being severed. Interacts with microtubules.
CC {ECO:0000255|HAMAP-Rule:MF_03021}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton
CC {ECO:0000255|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-
CC like structure in the membrane. {ECO:0000255|HAMAP-Rule:MF_03021}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03021}.
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DR EMBL; AAAB01008859; EAA07487.5; -; Genomic_DNA.
DR RefSeq; XP_312634.5; XM_312634.5.
DR AlphaFoldDB; Q7QBW0; -.
DR SMR; Q7QBW0; -.
DR STRING; 7165.AGAP002334-PA; -.
DR PaxDb; Q7QBW0; -.
DR PRIDE; Q7QBW0; -.
DR GeneID; 1273633; -.
DR KEGG; aga:AgaP_AGAP002334; -.
DR CTD; 1273633; -.
DR VEuPathDB; VectorBase:AGAP002334; -.
DR eggNOG; KOG0740; Eukaryota.
DR HOGENOM; CLU_000688_21_5_1; -.
DR InParanoid; Q7QBW0; -.
DR OMA; DNEHEAT; -.
DR OrthoDB; 1176820at2759; -.
DR PhylomeDB; Q7QBW0; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0008568; F:microtubule severing ATPase activity; ISS:UniProtKB.
DR GO; GO:0051013; P:microtubule severing; ISS:UniProtKB.
DR GO; GO:0031117; P:positive regulation of microtubule depolymerization; IEA:UniProtKB-UniRule.
DR GO; GO:0034214; P:protein hexamerization; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03021; Spastin; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR017179; Spastin.
DR InterPro; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Cytoskeleton; Isomerase; Membrane; Microtubule;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..827
FT /note="Spastin"
FT /id="PRO_0000367140"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT INTRAMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT TOPO_DOM 101..827
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT DOMAIN 231..306
FT /note="MIT"
FT /evidence="ECO:0000255"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..143
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 592..599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
SQ SEQUENCE 827 AA; 90536 MW; 9FF79CF9DBA406A6 CRC64;
MVRNKYTLTT AGKSPSKKSR TGSLSKQHDA TGDDDGETGT LDGSGSAAGS PVGGGTDAAA
KRCDGGSVHK QNLYIISFPV IFVFNVLRSL LYQLFIVFRY VYNFTTKVVY RPVRKECGLE
IVINTDQHGH HHHHHHRHSS HSIHSTAAAH QLQQHQQQQQ HQYSLLQQEQ HGVTEPQQQQ
QQQHQAAHPL QCSQSGILVN GEGREMSIQR SASGSQVGPG DPLLAKQKHH HRRAFEYISK
ALKIDEDNED QKELAIELYR KGILELERGI AVECWGGRGE VWERAQRLHD KMQTNLSMAR
DRLQFLGMLC VCVSVQRKHL HPTRTTLPYR DVKSKLHTTP TENRMVSFNE NCTITTNHHP
ARGTAASSRP TTAATAPATP SLPIKQTASE ASGRKLTVGY KRPGNLGVMN KSQTLPRSMG
GTRTTPTGTG GAGGIAGGLG NGGTYGGSIV GGGAGMPKIV PKPAATPPAI RRQFSVSIPI
PGSSPVRKAS NGYGSKNTPP PRSKTPLAGQ QPQQPQQQQQ QQPQISVKGV EPKLVQIIMD
EIVEGGAKVQ WQDIAGQEVA KQALQEMVIL PSVRPELFTG LRTPAKGLLL FGPPGNGKTL
LARAVATECS ATFFSISAAT LTSKYVGDGE KLVRALFAVA RELQPSIIFI DEVDSVLSER
SSNEHEATRR LKTEFLVQFD GLPANSEADR IVVMAATNRP QELDEAALRR FPKRVYVTLP
DRDTRELLLR RLLQKQGSPL SDADLAHLAQ LTEGYSGSDL TALARDAALE PIRELNVEEV
KNMDPTKLRS IRESDFHNSL KRIRRSVAPQ SLAAYEKWLQ DFGDVTL
