SPAST_NEMVE
ID SPAST_NEMVE Reviewed; 597 AA.
AC A7T395;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Spastin {ECO:0000255|HAMAP-Rule:MF_03021};
DE EC=5.6.1.1 {ECO:0000255|HAMAP-Rule:MF_03021};
GN ORFNames=v1g144095;
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6;
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
CC -!- FUNCTION: ATP-dependent microtubule severing protein. Microtubule
CC severing may promote reorganization of cellular microtubule arrays and
CC the release of microtubules from the microtubule organizing center
CC following nucleation. {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}. Note=Forms an intramembrane hairpin-
CC like structure in the membrane. {ECO:0000255|HAMAP-Rule:MF_03021}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03021}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDO29570.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DS470442; EDO29570.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001621670.1; XM_001621620.1.
DR AlphaFoldDB; A7T395; -.
DR SMR; A7T395; -.
DR STRING; 45351.EDO29570; -.
DR PRIDE; A7T395; -.
DR eggNOG; KOG0740; Eukaryota.
DR HOGENOM; CLU_000688_21_5_1; -.
DR InParanoid; A7T395; -.
DR OrthoDB; 1176820at2759; -.
DR PhylomeDB; A7T395; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
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:0005819; C:spindle; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0008568; F:microtubule severing ATPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051013; P:microtubule severing; IEA:UniProtKB-UniRule.
DR GO; GO:0031117; P:positive regulation of microtubule depolymerization; IEA:UniProtKB-UniRule.
DR GO; GO:0034214; P:protein hexamerization; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03021; Spastin; 1.
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 InterPro; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Cytoskeleton; Isomerase; Membrane; Microtubule;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..597
FT /note="Spastin"
FT /id="PRO_0000367154"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT INTRAMEM 21..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT TOPO_DOM 38..597
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT DOMAIN 91..168
FT /note="MIT"
FT /evidence="ECO:0000255"
FT REGION 56..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 66629 MW; C5477D5F3D9446EF CRC64;
MPNNDILRPL AIPAKYVGSF LVFLYNGLYF VFVVNLWSRL FGKATKTEVP PLPKIRKLGK
DMASRAPPRR GQSSEDNEDG LPAEIFNVRR HHKQAYAYIA RALEVDEGQG SLETKKRAVE
FYNRGIEEME AGLLIPCIDE GEEWDKARRL QEKMEANLEN TRERMDELVI IFFIIVVALL
VSAGMMDDQP LLSARKTSSE PSQAWDVSKP TGPSYKQSKS YKNSTTVTTK RSQASPSFSS
SSSSVNSTAG SSRTKPAKPA PMAAPRRYNP QVRRTKSTKP AMMAKQSCVD EQKKKISHLK
GIDPKLANII MDEILESGPA VHFSDIAGVD NAKKALQEIV ILPSLRPELW RGDPTLVLFQ
VLPYPPGSSH ITLPRASTAT SFTSCFFSIS KRSSLVHPVV ASFFVKSLED LASILTTSLF
TIDEVDSLLT ERREGEHEHS RRLKTEFLVS FDGVVADPEE RILVMGATNR PQELDDAALR
RMVKRIHIPL PDKETRKVLL TKLLAKHHNP LSGAEIDRLA RMTEHYSGSD LTALARDAAL
GPIRDLNSDQ LKSMAANEVR NITFQDFVNS LQIIRPSVGP ETLKAYDDWN RLYGSNA
