SPAST_DROMO
ID SPAST_DROMO Reviewed; 765 AA.
AC B4K799;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=GI24145;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22;
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; CH933806; EDW14223.1; -; Genomic_DNA.
DR RefSeq; XP_001998762.1; XM_001998726.2.
DR AlphaFoldDB; B4K799; -.
DR SMR; B4K799; -.
DR STRING; 7230.FBpp0173362; -.
DR PRIDE; B4K799; -.
DR EnsemblMetazoa; FBtr0174870; FBpp0173362; FBgn0146868.
DR GeneID; 6572656; -.
DR KEGG; dmo:Dmoj_GI24145; -.
DR eggNOG; KOG0740; Eukaryota.
DR HOGENOM; CLU_000688_21_5_1; -.
DR InParanoid; B4K799; -.
DR OMA; GMTNEPM; -.
DR OrthoDB; 1176820at2759; -.
DR PhylomeDB; B4K799; -.
DR Proteomes; UP000009192; 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; IPR036181; MIT_dom_sf.
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; SSF116846; SSF116846; 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..765
FT /note="Spastin"
FT /id="PRO_0000367145"
FT TOPO_DOM 1..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT INTRAMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT TOPO_DOM 129..765
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT DOMAIN 218..293
FT /note="MIT"
FT /evidence="ECO:0000255"
FT REGION 1..195
FT /note="Required for localization to punctate cytoplasmic
FT foci"
FT /evidence="ECO:0000250|UniProtKB:Q8I0P1"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..765
FT /note="Sufficient for interaction with microtubules and
FT microtubule severing"
FT /evidence="ECO:0000250|UniProtKB:Q8I0P1"
FT REGION 329..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..462
FT /note="Required for interaction with microtubules"
FT /evidence="ECO:0000250|UniProtKB:Q8I0P1"
FT COMPBIAS 350..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 530..537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
SQ SEQUENCE 765 AA; 83294 MW; 4049BE0D4F9F20A8 CRC64;
MVRTKNQSSS SSASSSTKSP VKISGGGSSG ANRSRSCSEA LIDDGKTSSK LSSNRQRATI
TTTTTSTTPG SSPDDDTTDA DLTPTSGYGP RGGTSVHKQN LYVVSFPIIF LFNVLRSLIY
QLFCIFRYLY CASTKVIYRS PHRRDCNIEI VVQNSKEQQS IICPLERNTS DGIEKAQQLL
PQRQRALLPL EMATNRGGSG GYSPGPGDPL LAKQKHHHRR AFEYISKALK IDEENEGHKE
LAIELYRKGI KELEDGIAVD CWSGRGDVWD RAQRLHEKMQ TNLSMARDRL HFLALREEDL
QMQRLSLMDP PKNKQQVTSK FKQPMLVGQT NSKAAAVEPS KITMRSSGYG PKPVSGTGSS
AGTSKALQAA SGRKLTIGNK RPGNLAVANK SQTLPRNLGS KTTSTSVGAA LQRQPGKTAA
TPPAVRRQFS SGRNTPPQRS RTPINNNAAS GSGSGSGAST PMISVKGVEQ KLVQLIMDEI
VEGGAKVEWT DIAGQDVAKQ ALQEMVILPS VRPELFTGLR APAKGLLLFG PPGNGKTLLA
RAVATECSAT FLNISAASLT SKYVGDGEKL VRALFAVARH LQPSIIFIDE VDSLLSERSS
NEHEASRRLK TEFLVEFDGL PGNPEGDRIV VLAATNRPQE LDEAALRRFT KRVYVSLPEV
QTRELLLSRL LQKQGSPLDT EALARLAKIT DGYSGSDLTA LAKDAALEPI RELNVEQVKC
LDISAMRPIT EKDFHNSLKR IRRSVAPQSL NSYEKWSQDY GDITI
