SPAST_XENTR
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 03-AUG-2022, entry version 101.
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}; 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_012963010.2. [Q05AS3-1]
DR AlphaFoldDB; Q05AS3; -.
DR SMR; Q05AS3; -.
DR STRING; 8364.ENSXETP00000024877; -.
DR PaxDb; Q05AS3; -.
DR DNASU; 549207; -.
DR Ensembl; ENSXETT00000024877; ENSXETP00000024877; ENSXETG00000011392.
DR GeneID; 549207; -.
DR KEGG; xtr:549207; -.
DR CTD; 6683; -.
DR Xenbase; XB-GENE-947839; spast.
DR eggNOG; KOG0740; Eukaryota.
DR HOGENOM; CLU_000688_21_5_1; -.
DR InParanoid; Q05AS3; -.
DR OrthoDB; 1176820at2759; -.
DR PhylomeDB; Q05AS3; -.
DR Reactome; R-XTR-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000011392; Expressed in ovary and 15 other tissues.
DR ExpressionAtlas; Q05AS3; baseline.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
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; IEA:UniProtKB-UniRule.
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; IEA:InterPro.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
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:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0019896; P:axonal transport of mitochondrion; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IEA:UniProtKB-UniRule.
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 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 InterPro; IPR035106; Spastin_chordate.
DR InterPro; IPR015415; Vps4_C.
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; SSF116846; 1.
DR SUPFAM; SSF52540; SSF52540; 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 18..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..294
FT /note="Polar residues"
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
