SPAST_DROWI
ID SPAST_DROWI Reviewed; 777 AA.
AC B4NBP4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=GK11148;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
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; CH964232; EDW81208.1; -; Genomic_DNA.
DR RefSeq; XP_002070222.1; XM_002070186.2.
DR AlphaFoldDB; B4NBP4; -.
DR SMR; B4NBP4; -.
DR STRING; 7260.FBpp0240291; -.
DR PRIDE; B4NBP4; -.
DR EnsemblMetazoa; FBtr0241799; FBpp0240291; FBgn0213159.
DR GeneID; 6648037; -.
DR KEGG; dwi:6648037; -.
DR eggNOG; KOG0740; Eukaryota.
DR HOGENOM; CLU_000688_21_5_1; -.
DR InParanoid; B4NBP4; -.
DR OMA; GMTNEPM; -.
DR OrthoDB; 1176820at2759; -.
DR PhylomeDB; B4NBP4; -.
DR Proteomes; UP000007798; 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..777
FT /note="Spastin"
FT /id="PRO_0000367151"
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..777
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT DOMAIN 238..313
FT /note="MIT"
FT /evidence="ECO:0000255"
FT REGION 1..215
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 213..777
FT /note="Sufficient for interaction with microtubules and
FT microtubule severing"
FT /evidence="ECO:0000250|UniProtKB:Q8I0P1"
FT REGION 327..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..474
FT /note="Required for interaction with microtubules"
FT /evidence="ECO:0000250|UniProtKB:Q8I0P1"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 542..549
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
SQ SEQUENCE 777 AA; 85093 MW; 9C3C6569E4BAD42D CRC64;
MVRTKSSSSS ASSSSQKSPI KSNNGAGGGG SSSSHRQSHR TSIDERKSSS HAHSNNSNVS
SSSRRAATAT SGSSSPEGDD DTTTDDLTPT GSSPRSCNGR GHSSVHKQNL YVVSFPIIFL
FNVLRSLIYQ LFCIFRYLYG ASTKVLYRPH RRDCNIEIVV QNSKEQQLQL QQHQHNQTLS
YSLETGGVSG GSGGEQQVQV QPQRIRALQP LEMATNRPGG GYSPGPGDPL LAKQKHHHRR
AFEYISKALK IDEENEGHKE LAIELYRKGI KELEDGIAVD CWNGRGDVWD RAQRLHDKMQ
TNLSMARDRL HFLALREEDL QMQRLSLKEK QPAPKQPQRS QTKDPVKQPM LTSLNADPVK
MKVRSSGYGP KQNGTSSSRP APSGQTATGA SGRKLTVGTK RPGNLPVTNK SQTLPRNLGS
KTTVGAVQRQ PAKTAATPPA VRRQFSSGRN TPPQRSRTPI NNNASSGSGA STPMVSVKGV
EQKLVQLILD EIVEGGAKVE WTDIAGQDVA KQALQEMVIL PSVRPELFTG LRAPAKGLLL
FGPPGNGKTL LARAVATECS ATFLNISAAS LTSKYVGDGE KLVRALFAVA RHMQPSIIFI
DEVDSLLSER SSNEHEASRR LKTEFLVEFD GLPGNPDGDR IVVLAATNRP QELDEAALRR
FTKRVYVSLP DEQTRELLLN RLLQKQGSPL DTEALRRLAK ITEGYSGSDL TALAKDAALE
PIRELNVEQV KCLDISAMRP ITEKDFHNSL KRIRRSVAPQ SLNSYEKWSQ DYGDITI
