ID   SPAST_XENTR             Reviewed;         603 AA.
AC   Q05AS3; Q28H96;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   10-JUN-2026, entry version 115.
DE   RecName: Full=Spastin {ECO:0000255|HAMAP-Rule:MF_03021};
DE            EC=5.6.1.1 {ECO:0000255|HAMAP-Rule:MF_03021};
GN   Name=spast {ECO:0000255|HAMAP-Rule:MF_03021};
GN   Synonyms=spg4 {ECO:0000255|HAMAP-Rule:MF_03021};
GN   ORFNames=TEgg045n18.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=N6; TISSUE=Skin;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent microtubule severing protein that specifically
CC       recognizes and cuts microtubules that are polyglutamylated.
CC       Preferentially recognizes and acts on microtubules decorated with short
CC       polyglutamate tails: severing activity increases as the number of
CC       glutamates per tubulin rises from one to eight, but decreases beyond
CC       this glutamylation threshold. Microtubule severing promotes
CC       reorganization of cellular microtubule arrays and the release of
CC       microtubules from the centrosome following nucleation. Required for
CC       membrane traffic from the endoplasmic reticulum (ER) to the Golgi and
CC       for completion of the abscission stage of cytokinesis. Also plays a
CC       role in axon growth and the formation of axonal branches.
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.
CC       {ECO:0000255|HAMAP-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}. Cytoplasm, perinuclear region
CC       {ECO:0000255|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000255|HAMAP-
CC       Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in
CC       the membrane. {ECO:0000255|HAMAP-Rule:MF_03021}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q05AS3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q05AS3-2; Sequence=VSP_036649;
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03021}.
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DR   EMBL; CR760974; CAJ82090.1; -; mRNA.
DR   EMBL; BC123973; AAI23974.1; -; mRNA.
DR   RefSeq; NP_001016453.1; NM_001016453.2.
DR   RefSeq; XP_012818464.1; XM_012963010.3. [Q05AS3-1]
DR   AlphaFoldDB; Q05AS3; -.
DR   SMR; Q05AS3; -.
DR   FunCoup; Q05AS3; 3248.
DR   STRING; 8364.ENSXETP00000031690; -.
DR   PaxDb; 8364-ENSXETP00000031690; -.
DR   DNASU; 549207; -.
DR   Ensembl; ENSXETT00000112709; ENSXETP00000118808; ENSXETG00000011392. [Q05AS3-1]
DR   GeneID; 549207; -.
DR   KEGG; xtr:549207; -.
DR   AGR; Xenbase:XB-GENE-947839; -.
DR   CTD; 6683; -.
DR   Xenbase; XB-GENE-947839; spast.
DR   eggNOG; KOG0740; Eukaryota.
DR   GeneTree; ENSGT00940000156258; -.
DR   HOGENOM; CLU_000688_21_5_1; -.
DR   InParanoid; Q05AS3; -.
DR   OMA; KSREPML; -.
DR   OrthoDB; 10251136at2759; -.
DR   PhylomeDB; Q05AS3; -.
DR   Reactome; R-XTR-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   Proteomes; UP000008143; Chromosome 5.
DR   Bgee; ENSXETG00000011392; Expressed in ovary and 15 other cell types or tissues.
DR   ExpressionAtlas; Q05AS3; baseline.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IBA:GO_Central.
DR   GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0008568; F:microtubule severing ATPase activity; ISS:UniProtKB.
DR   GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR   GO; GO:0019896; P:axonal transport of mitochondrion; ISS:UniProtKB.
DR   GO; GO:0021955; P:central nervous system neuron axonogenesis; IBA:GO_Central.
DR   GO; GO:0032506; P:cytokinetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
DR   GO; GO:0090148; P:membrane fission; ISS:UniProtKB.
DR   GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR   GO; GO:0051013; P:microtubule severing; ISS:UniProtKB.
DR   GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR   GO; GO:0051228; P:mitotic spindle disassembly; ISS:UniProtKB.
DR   GO; GO:0031468; P:nuclear membrane reassembly; ISS:UniProtKB.
DR   GO; GO:0031117; P:positive regulation of microtubule depolymerization; IEA:UniProtKB-UniRule.
DR   GO; GO:0034214; P:protein hexamerization; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   CDD; cd02679; MIT_spastin; 1.
DR   CDD; cd19524; RecA-like_spastin; 1.
DR   FunFam; 3.40.50.300:FF:000093; Fidgetin-like 1; 1.
DR   FunFam; 1.10.8.60:FF:000036; Spastin; 1.
DR   FunFam; 1.20.58.80:FF:000006; Spastin; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 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; IPR050304; MT-severing_AAA_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015415; Spast_Vps4_C.
DR   InterPro; IPR017179; Spastin.
DR   InterPro; IPR035106; Spastin_chordate.
DR   PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR23074:SF86; SPASTIN; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF09336; Vps4_C; 1.
DR   PIRSF; PIRSF037338; Spastin; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00745; MIT; 1.
DR   SUPFAM; SSF116846; MIT domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cell cycle; Cell division; Cytoplasm;
KW   Cytoskeleton; Developmental protein; Differentiation; Isomerase; Membrane;
KW   Microtubule; Neurogenesis; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..603
FT                   /note="Spastin"
FT                   /id="PRO_0000367139"
FT   TOPO_DOM        1..54
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT   INTRAMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT   TOPO_DOM        76..603
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT   DOMAIN          113..188
FT                   /note="MIT"
FT                   /evidence="ECO:0000255"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..32
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..294
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         369..376
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT   VAR_SEQ         189..220
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_036649"
FT   CONFLICT        9
FT                   /note="N -> D (in Ref. 1; CAJ82090)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   603 AA;  66279 MW;  DF159AB3E69DAC00 CRC64;
     MNSPGGRNNK KKPVTPAAET GPGPPTPPPP PAETQVLLAP PSLHKRNLYL FSYPLLAAFS
     LLRFLAFQLG LLFVWFCERL SRRVMADKGS TAARTAAAPA QDRPQEPEVV RSYHQQAFQY
     ISMALRIDEE EKDQKEQAIQ WYKKGIEELE KGIAVTITGK GEQYDRARRL QAKMSTNLLM
     AKDRLQLLAK LKADIQGQHS QMEVCSDNTN LPCRNGLLKP EKGAVPKKKD PPSISSNSYS
     RVKAAPKSGS LGNRIPNCTG VSSSARQAGP NAPSNRGAAG KNNTRTNKPT TPTTAVRKKD
     MKNLRNVDSN LANLILNEIV DSGPTVKFAD IAGQDLAKQA LQEIVILPSI RPELFTGLRA
     PARGLLLFGP PGNGKTMLAK AVAAESNATF FNISAASLTS KYVGEGEKLV RALFSVAREL
     QPSIIFIDEV DSLLCERREG EHDASRRLKT EFLIEFDGVQ SGGDDRVLVM GATNRPQELD
     DAVLRRFTKR VYVSLPNEET RLLLLKNLLS KQGNPLNEKE LTQLSRLTEG YSGSDITALA
     KDAALGPIRE LKPEQVKNMA ASEMRNIKYS DFLSSLKKIK CSVSPSTLES YIRWNKEFGD
     TTV
//