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Database: UniProt
Entry: Q0WMJ4_ARATH
LinkDB: Q0WMJ4_ARATH
Original site: Q0WMJ4_ARATH 
ID   Q0WMJ4_ARATH            Unreviewed;       487 AA.
AC   Q0WMJ4;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=microtubule-severing ATPase {ECO:0000256|ARBA:ARBA00038871};
DE            EC=5.6.1.1 {ECO:0000256|ARBA:ARBA00038871};
GN   OrderedLocusNames=At2g45500 {ECO:0000313|Araport:AT2G45500,
GN   ECO:0000313|EMBL:AEC10563.1};
GN   ORFNames=F17K2.3 {ECO:0000313|EMBL:AEC10563.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000313|EMBL:BAF01657.1};
RN   [1] {ECO:0000313|EMBL:AEC10563.1, ECO:0000313|Proteomes:UP000006548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S., Shea T.P., Benito M.I., Town C.D.,
RA   Fujii C.Y., Mason T., Bowman C.L., Barnstead M., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2] {ECO:0000313|EMBL:BAF01657.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Morosawa T.,
RA   Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K.,
RA   Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K.,
RA   Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AEC10563.1}
RP   NUCLEOTIDE SEQUENCE.
RG   TAIR;
RA   Swarbreck D., Lamesch P., Wilks C., Huala E.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AEC10563.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Krishnakumar V., Cheng C.-Y., Chan A.P., Schobel S., Kim M., Ferlanti E.S.,
RA   Belyaeva I., Rosen B.D., Micklem G., Miller J.R., Vaughn M., Town C.D.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|Proteomes:UP000006548}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
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:0000256|ARBA:ARBA00036378};
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|RuleBase:RU003651}.
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DR   EMBL; CP002685; AEC10563.1; -; Genomic_DNA.
DR   EMBL; AK229827; BAF01657.1; -; mRNA.
DR   RefSeq; NP_001078063.1; NM_001084594.2.
DR   AlphaFoldDB; Q0WMJ4; -.
DR   SMR; Q0WMJ4; -.
DR   ProteomicsDB; 191722; -.
DR   EnsemblPlants; AT2G45500.2; AT2G45500.2; AT2G45500.
DR   GeneID; 819158; -.
DR   Gramene; AT2G45500.2; AT2G45500.2; AT2G45500.
DR   KEGG; ath:AT2G45500; -.
DR   Araport; AT2G45500; -.
DR   TAIR; AT2G45500; -.
DR   HOGENOM; CLU_000688_21_12_1; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q0WMJ4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:UniProt.
DR   CDD; cd02679; MIT_spastin; 1.
DR   CDD; cd19524; RecA-like_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   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   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   SMART; SM00382; AAA; 1.
DR   SMART; SM00745; MIT; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|RuleBase:RU003651};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q0WMJ4,
KW   ECO:0007829|ProteomicsDB:Q0WMJ4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006548}.
FT   DOMAIN          52..129
FT                   /note="MIT"
FT                   /evidence="ECO:0000259|SMART:SM00745"
FT   DOMAIN          248..384
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          19..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   487 AA;  53944 MW;  4C79B7E240D2B15B CRC64;
     MSFLRGIIDS FSSILNEESK KDPSVSSSST SSESMNGIDG VPVTNERIAY KLKGYFDLAK
     EEIAKGVRAE EWGLHDDALL HYRNAQRIMN EATSTPSPSY ISSSEKEKVR SYREKISNWQ
     NQVSERLQAL GVGMSENKRT VAYPSSASVS STASRYRKTL SQKTPVARGG VATPRNPKDA
     AASPKPVKES GNVYDDKLVE MINTTIVDRS PSVKWDDVAG LNGAKQALLE MVILPAKRRD
     LFTGLRRPAR GLLLFGPPGN GKTMLAKAVA SESQATFFNV SASSLTSKWV GEAEKLVKTL
     FQVAISRQPS VIFMDEIDSI MSTRSTSENE ASRRLKSEFL IQFDGVTSNP DDLVIIIGAT
     NKPQELDDAV LRRLVKRIYV PLPDSNVRKL LFKTKLKCQP HSLSDGDIDK IVKETEGYSG
     SDLQALCEEA AMMPIRELGA NILTIQANKV RSLRYDDFRK SMAVIRPSLS KSKWEELERW
     NSEFGSN
//
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