SPAST_DROSI
ID SPAST_DROSI Reviewed; 758 AA.
AC B4QSF0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 {ECO:0000255|HAMAP-Rule:MF_03021}; ORFNames=GD21056;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: ATP-dependent microtubule severing protein. Stimulates
CC microtubule minus-end depolymerization and poleward microtubule flux in
CC the mitotic spindle. Regulates microtubule stability in the
CC neuromuscular junction synapse. Involved in lipid metabolism by
CC regulating the size and distribution of lipid droplets. Involved in
CC axon regeneration by regulating microtubule severing.
CC {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. Interacts
CC with atl; may be involved in microtubule dynamics. {ECO:0000255|HAMAP-
CC 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}. Chromosome {ECO:0000255|HAMAP-
CC Rule:MF_03021}. Lipid droplet {ECO:0000255|HAMAP-Rule:MF_03021}.
CC Note=Forms an intramembrane hairpin-like structure in the membrane.
CC Colocalizes with cellular microtubule arrays. Localizes to chromosomes
CC from prometaphase/metaphase to anaphase, and this requires
CC microtubules. Localizes to discrete punctate cytoplasmic foci which may
CC correspond to secretory vesicles. {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; CM000364; EDX14149.1; -; Genomic_DNA.
DR AlphaFoldDB; B4QSF0; -.
DR SMR; B4QSF0; -.
DR STRING; 7240.B4QSF0; -.
DR HOGENOM; CLU_000688_21_5_1; -.
DR OMA; GMTNEPM; -.
DR PhylomeDB; B4QSF0; -.
DR Proteomes; UP000000304; Chromosome 3r.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule.
DR GO; GO:0031594; C:neuromuscular junction; IEA:EnsemblMetazoa.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-UniRule.
DR GO; GO:0008021; C:synaptic vesicle; IEA:EnsemblMetazoa.
DR GO; GO:0043195; C:terminal bouton; IEA:EnsemblMetazoa.
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:0008344; P:adult locomotory behavior; IEA:UniProtKB-UniRule.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0035099; P:hemocyte migration; IEA:EnsemblMetazoa.
DR GO; GO:0051013; P:microtubule severing; ISS:UniProtKB.
DR GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; IEA:UniProtKB-UniRule.
DR GO; GO:0000022; P:mitotic spindle elongation; IEA:UniProtKB-UniRule.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:EnsemblMetazoa.
DR GO; GO:1900074; P:negative regulation of neuromuscular synaptic transmission; IEA:EnsemblMetazoa.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IEA:EnsemblMetazoa.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0048691; P:positive regulation of axon extension involved in regeneration; IEA:EnsemblMetazoa.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0045834; P:positive regulation of lipid metabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0031117; P:positive regulation of microtubule depolymerization; IEA:UniProtKB-UniRule.
DR GO; GO:1900075; P:positive regulation of neuromuscular synaptic transmission; IEA:EnsemblMetazoa.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IEA:EnsemblMetazoa.
DR GO; GO:0034214; P:protein hexamerization; IEA:UniProtKB-UniRule.
DR GO; GO:2000331; P:regulation of terminal button organization; IEA:EnsemblMetazoa.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03021; Spastin; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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; 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; Cell cycle; Cell division; Chromosome; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Isomerase;
KW Lipid droplet; Membrane; Microtubule; Mitosis; Neurogenesis;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..758
FT /note="Spastin"
FT /id="PRO_0000367149"
FT TOPO_DOM 1..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT INTRAMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT TOPO_DOM 143..758
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT DOMAIN 233..308
FT /note="MIT"
FT /evidence="ECO:0000255"
FT REGION 1..210
FT /note="Required for localization to punctate cytoplasmic
FT foci"
FT /evidence="ECO:0000250|UniProtKB:Q8I0P1"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..758
FT /note="Sufficient for interaction with microtubules and
FT microtubule severing"
FT /evidence="ECO:0000250|UniProtKB:Q8I0P1"
FT REGION 323..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..455
FT /note="Required for interaction with microtubules"
FT /evidence="ECO:0000250|UniProtKB:Q8I0P1"
FT COMPBIAS 1..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 523..530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
SQ SEQUENCE 758 AA; 82818 MW; 50500FDD3F9B1E49 CRC64;
MVRTKNQSSS SSASSSSTKS PIKSSSGAGS SGGGVGGRQS THRSSSASNV AAVVAGGSSA
AGGGSSSNRR SPGSSPDGDD DTTTTDDLTP TTCSPRSGHH HSYGGYSSSV HKQNLYVVSF
PIIFLFNVLR SLIYQLFCIF RYLYGASTKV IYRPHRRDCN IEIVVQNSSK EQQQSLNHPS
ELNREGDGQE QQLSNQPQRF RPIQPLEMAA NRPGGGYSPG PGDPLLAKQK HHHRRAFEYI
SKALKIDEEN EGHKELAIEL YRKGIKELED GIAVDCWSGR GDVWDRAQRL HDKMQTNLSM
ARDRLHFLAL REQDLQMQRL SLKEKQKEEA RSKPQKSREP MLAGMTNEPM KLRVRSSGYG
PKATTSAQPT ASGRKLTIGS KRPVNLAVAN KSQTLPRNLG SKTSVGAVQR QPAKTAATPP
AVRRQFSSGR NTPPQRSRTP INNNGPSGSG ASTPVVSVKG VEQKLVQLIL DEIVEGGAKV
EWTDIAGQDV AKQALQEMVI LPSVRPELFT GLRAPAKGLL LFGPPGNGKT LLARAVATEC
SATFLNISAA SLTSKYVGDG EKLVRALFAV ARHMQPSIIF IDEVDSLLSE RSSSEHEASR
RLKTEFLVEF DGLPGNPDGD RIVVLAATNR PQELDEAALR RFTKRVYVSL PDEQTRELLL
NRLLQKQGSP LDTEALRRLA KITDGYSGSD LTARPKDAAL EPIRELNVEQ VKCLDISAMR
AITEQDFHSS LKRIRRSVAP QSLNSYEKWS QDYGDITI
