SPAST_IXOSC
ID SPAST_IXOSC Reviewed; 648 AA.
AC B7PXE3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=ISCW020482;
OS Ixodes scapularis (Black-legged tick) (Deer tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=6945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wikel;
RG Ixodes scapularis Genome Project Consortium;
RA Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT "Annotation of Ixodes scapularis.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; DS813618; EEC11265.1; -; Genomic_DNA.
DR RefSeq; XP_002400359.1; XM_002400315.1.
DR AlphaFoldDB; B7PXE3; -.
DR SMR; B7PXE3; -.
DR STRING; 6945.B7PXE3; -.
DR KEGG; isc:IscW_ISCW020482; -.
DR VEuPathDB; VectorBase:ISCI020482; -.
DR VEuPathDB; VectorBase:ISCW020482; -.
DR HOGENOM; CLU_000688_21_5_1; -.
DR InParanoid; B7PXE3; -.
DR OMA; DNEHEAT; -.
DR OrthoDB; 1176820at2759; -.
DR PhylomeDB; B7PXE3; -.
DR Proteomes; UP000001555; Unassembled WGS sequence.
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..648
FT /note="Spastin"
FT /id="PRO_0000367153"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT INTRAMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT TOPO_DOM 62..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT DOMAIN 99..174
FT /note="MIT"
FT /evidence="ECO:0000255"
FT REGION 188..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 414..421
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
SQ SEQUENCE 648 AA; 72474 MW; 384CF5270F3FF3A4 CRC64;
MASTVALLRD SSDDRENFDD GETDCVQVGR KRKLTVFFYP LLLVFWLLRW VFYQFFLVLC
FVCRGFVPRR HLATAETTTT MATAEEPDAN LLIRQKQHHK KAFDFISKAL KYDEENEDFK
EMSIDLYRKG IEELQKGIAI DFSKGQGTTW ERAHRLSDKM KVNLEMARDR LDFLESMVKI
EHLGDHLPWH GGVAPAQRGQ RRRAWQKAAP SAPSEPGTGP SWLKMAENGP AKGGPCPTSP
RLQRSNTGVT LRRQQQQQLG GVSTVSRSQT LPRNSVPCPR MSARSPSRKA GNNEAVPTPN
TARRRASQPQ VPPVHPRGRQ PTTRGGAAHR GGPPTVSQRS LLSSRVPPLK GVDSRLAHLI
LDEVVDGAPP VLFSDIAGQE VAKQALSEMV ILPTDRPELF TGLRAPPKGL LLFGPPGNGK
TMLAKAVAHE SNSTFLNISA ASLTSKYVGE GEKLVRALFA VARELQPSII FIDEVDSLLS
ERKDNEHEAT RRLKTEFLVE FDGLHTGSEE RVLVMGATNR PQELDDAALR RFTKRVYVTL
PDHNTRVILL EKLLKKHNNP LSADKLKYLA RLTEGYSGSD LTALAKDAAL GPIRELNPEQ
VRCVDPKKMR NISLQDFLDS LKKVRRSVTP QSLDFFDRWN REFGDITV
