SPAST_DROGR
ID SPAST_DROGR Reviewed; 782 AA.
AC B4JII0;
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=GH18484;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916369; EDV93061.1; -; Genomic_DNA.
DR RefSeq; XP_001989999.1; XM_001989963.1.
DR AlphaFoldDB; B4JII0; -.
DR SMR; B4JII0; -.
DR STRING; 7222.FBpp0152390; -.
DR PRIDE; B4JII0; -.
DR EnsemblMetazoa; FBtr0153898; FBpp0152390; FBgn0125951.
DR GeneID; 6563377; -.
DR KEGG; dgr:6563377; -.
DR eggNOG; KOG0740; Eukaryota.
DR HOGENOM; CLU_000688_21_5_1; -.
DR InParanoid; B4JII0; -.
DR OMA; GMTNEPM; -.
DR OrthoDB; 1176820at2759; -.
DR PhylomeDB; B4JII0; -.
DR Proteomes; UP000001070; 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..782
FT /note="Spastin"
FT /id="PRO_0000367143"
FT TOPO_DOM 1..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT INTRAMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT TOPO_DOM 137..782
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT DOMAIN 235..310
FT /note="MIT"
FT /evidence="ECO:0000255"
FT REGION 1..212
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 210..782
FT /note="Sufficient for interaction with microtubules and
FT microtubule severing"
FT /evidence="ECO:0000250|UniProtKB:Q8I0P1"
FT REGION 325..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..479
FT /note="Required for interaction with microtubules"
FT /evidence="ECO:0000250|UniProtKB:Q8I0P1"
FT COMPBIAS 1..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 547..554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
SQ SEQUENCE 782 AA; 85732 MW; E47DD91851C1DEA3 CRC64;
MVRTKNQSSS SSASSSTKSP VKISGGTTNR SRSCSDALID DGNSKSSSKP TSNNRQRTTT
NNNTTAITTT PGSSPDNDDD DTTTTDADLT PTSGNAPRGG NSSVHKQNLY VVSFPIIFLF
NVLRSLIYQL FCIFRYLYGA STKVIYRSPN RRDCNIEIVV QNSKEQQQQH QHQQAIIHCP
LERRGNISGI EQTLAQALPQ RQRAIQPLEM AGNRAGGNYS PGPGDPLLAK QKHHHRRAFE
YISKALKIDE ENEGHKELAI ELYRKGIKEL EDGIAVDCWS GRGDVWDRAQ RLHDKMQTNL
SMARDRLHFL ALREEDLQLQ RLSLKEQQQK KKSPQQQPQQ QQQHTFKQPM LVGQTNSSGG
SGSTKVPLRS SGYGLKPSAT NISRAMPAAS GRKLTIGNKR PGNLPVVNKS QTLPRNLGSK
TSSTSVGAAL QRQPGKTAAT PPAVRRQFSS GRNTPPQRSR TPINNNAAGG SGSGASTPMV
SVKGVEQKLV QLILDEIVEG GAKVEWTDIA GQDVAKQALQ EMVILPSVRP ELFTGLRAPA
KGLLLFGPPG NGKTLLARAV ATECSATFLN ISAASLTSKY VGDGEKLVRA LFAVARHMQP
SIIFIDEVDS LLSERSSNEH EASRRLKTEF LVEFDGLPGN PDGDRIVVLA ATNRPQELDE
AALRRFTKRV YVSLPDVQTR ELLLNRLLQK QGSPLDSDAL GRLAKITEGY SGSDLTALAK
DAALEPIREL NVEQVKCLDI SAMRQITEKD FHNSLKRIRR SVAPQSLNSY EKWSQDYGDI
TI
