SPAST_DROPE
ID SPAST_DROPE Reviewed; 788 AA.
AC B4G437;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=GL23394;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH479179; EDW24448.1; -; Genomic_DNA.
DR RefSeq; XP_002013462.1; XM_002013426.1.
DR AlphaFoldDB; B4G437; -.
DR SMR; B4G437; -.
DR STRING; 7234.FBpp0187501; -.
DR EnsemblMetazoa; FBtr0189009; FBpp0187501; FBgn0160984.
DR GeneID; 6588451; -.
DR KEGG; dpe:6588451; -.
DR eggNOG; KOG0740; Eukaryota.
DR HOGENOM; CLU_000688_21_5_1; -.
DR OMA; GMTNEPM; -.
DR PhylomeDB; B4G437; -.
DR Proteomes; UP000008744; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
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; 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 Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 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..788
FT /note="Spastin"
FT /id="PRO_0000367146"
FT TOPO_DOM 1..116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT INTRAMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT TOPO_DOM 138..788
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT DOMAIN 240..315
FT /note="MIT"
FT /evidence="ECO:0000255"
FT REGION 1..227
FT /note="Required for localization to punctate cytoplasmic
FT foci"
FT /evidence="ECO:0000250|UniProtKB:Q8I0P1"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..788
FT /note="Sufficient for interaction with microtubules and
FT microtubule severing"
FT /evidence="ECO:0000250|UniProtKB:Q8I0P1"
FT REGION 331..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..485
FT /note="Required for interaction with microtubules"
FT /evidence="ECO:0000250|UniProtKB:Q8I0P1"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 553..560
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
SQ SEQUENCE 788 AA; 86107 MW; 5E8A278FC3831849 CRC64;
MVRTKNQSSS SSASSSSHKS PIKSHGGSGS AAAGTAGHPV SRSSSSHRTS IDDRKSATNV
SSSSNRRTTP GSSPDGDGDD DTTTTDDLTP TSTSAPRSAG GPSSVHKQNL YVVSFPIIFL
FNVLRSLIYQ LFCIFRYLYG ASTKVIYRPH RRDCNIEIVV QNNSNNKDQK HQQLTSSQSL
NYPLEVTSGE AASEQQVQQP LPQQRYRALQ PLEMAGANRS GSGYSPGPGD PLLAKQKHHH
RRAFEYISKA LKIDEENEGH KELAIELYRK GIKELEDGIA VDCWSGRGDV WDRAQRLHDK
MQTNLSMARD RLHFLALREE DFQMHRLSLK EKQKANESRE QQQKPQKARE AADKPMLTNL
TNDPAKLKTR SSGYGPKNGL TTPRIFATAT TPTSSSSLAS GRKLTIGTKR PGNLAVAANK
SQTLPRNLGS KTSVGAVRQP GKTAATPPAV RRQFSSGRNT PPQRSRTPIN NNGASGSGSG
ASTPVVTVKG VEQKLVQLIL DEIVEGGAKV EWTDIAGQEV AKQALQEMVI LPSVRPELFT
GLRAPAKGLL LFGPPGNGKT LLARAVATEC SATFLNISAA SLTSKYVGDG EKLVRALFAV
ARHLQPSIIF IDEVDSLLSE RSSGEHEASR RLKTEFLVEF DGLPGNPDGD RIVVLAATNR
PQELDEAALR RFTKRVYVSL PDEQTRELLL NRLLQKQGSP LDTDALRRLS KITDGYSGSD
LTALAKDAAL EPIRELNVEQ VKCLDINAMR HITEKDFHNS LKRIRRSVAP QSLSLYEKWS
SDYGDITI
