SPAST_MOUSE
ID SPAST_MOUSE Reviewed; 614 AA.
AC Q9QYY8; Q6ZPY6; Q80VE0; Q9CVK0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 176.
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=Kiaa1083 {ECO:0000303|PubMed:14621295}, Spg4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-614.
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 111-614, AND TISSUE SPECIFICITY.
RX PubMed=10610178; DOI=10.1038/15472;
RA Hazan J., Fonknechten N., Mavel D., Paternotte C., Samson D.,
RA Artiguenave F., Davoine C.-S., Cruaud C., Durr A., Wincker P., Brottier P.,
RA Cattolico L., Barbe V., Burgunder J.-M., Prud'homme J.-F., Brice A.,
RA Fontaine B., Heilig R., Weissenbach J.;
RT "Spastin, a new AAA protein, is altered in the most frequent form of
RT autosomal dominant spastic paraplegia.";
RL Nat. Genet. 23:296-303(1999).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=16026783; DOI=10.1016/j.yexcr.2005.06.009;
RA Claudiani P., Riano E., Errico A., Andolfi G., Rugarli E.I.;
RT "Spastin subcellular localization is regulated through usage of different
RT translation start sites and active export from the nucleus.";
RL Exp. Cell Res. 309:358-369(2005).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=17101632; DOI=10.1093/hmg/ddl431;
RA Tarrade A., Fassier C., Courageot S., Charvin D., Vitte J., Peris L.,
RA Thorel A., Mouisel E., Fonknechten N., Roblot N., Seilhean D., Dierich A.,
RA Hauw J.J., Melki J.;
RT "A mutation of spastin is responsible for swellings and impairment of
RT transport in a region of axon characterized by changes in microtubule
RT composition.";
RL Hum. Mol. Genet. 15:3544-3558(2006).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18234839; DOI=10.1091/mbc.e07-09-0878;
RA Yu W., Qiang L., Solowska J.M., Karabay A., Korulu S., Baas P.W.;
RT "The microtubule-severing proteins spastin and katanin participate
RT differently in the formation of axonal branches.";
RL Mol. Biol. Cell 19:1485-1498(2008).
RN [9]
RP INDUCTION.
RX PubMed=18495362; DOI=10.1016/j.neuroscience.2008.04.025;
RA Ferrari-Toninelli G., Bonini S.A., Bettinsoli P., Uberti D., Memo M.;
RT "Microtubule stabilizing effect of notch activation in primary cortical
RT neurons.";
RL Neuroscience 154:946-952(2008).
RN [10]
RP FUNCTION.
RX PubMed=19141076; DOI=10.1111/j.1471-4159.2009.05875.x;
RA Riano E., Martignoni M., Mancuso G., Cartelli D., Crippa F., Toldo I.,
RA Siciliano G., Di Bella D., Taroni F., Bassi M.T., Cappelletti G.,
RA Rugarli E.I.;
RT "Pleiotropic effects of spastin on neurite growth depending on expression
RT levels.";
RL J. Neurochem. 108:1277-1288(2009).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=19453301; DOI=10.1111/j.1471-4159.2009.06104.x;
RA Kasher P.R., De Vos K.J., Wharton S.B., Manser C., Bennett E.J.,
RA Bingley M., Wood J.D., Milner R., McDermott C.J., Miller C.C., Shaw P.J.,
RA Grierson A.J.;
RT "Direct evidence for axonal transport defects in a novel mouse model of
RT mutant spastin-induced hereditary spastic paraplegia (HSP) and human HSP
RT patients.";
RL J. Neurochem. 110:34-44(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF SER-360 AND ASP-553.
RX PubMed=20530212; DOI=10.1083/jcb.201001024;
RA Lacroix B., van Dijk J., Gold N.D., Guizetti J., Aldrian-Herrada G.,
RA Rogowski K., Gerlich D.W., Janke C.;
RT "Tubulin polyglutamylation stimulates spastin-mediated microtubule
RT severing.";
RL J. Cell Biol. 189:945-954(2010).
RN [14]
RP DISRUPTION PHENOTYPE.
RX PubMed=22773755; DOI=10.1242/dmm.008946;
RA Fassier C., Tarrade A., Peris L., Courageot S., Mailly P., Dalard C.,
RA Delga S., Roblot N., Lefevre J., Job D., Hazan J., Curmi P.A., Melki J.;
RT "Microtubule-targeting drugs rescue axonal swellings in cortical neurons
RT from spastin knockout mice.";
RL Dis. Model. Mech. 6:72-83(2013).
CC -!- FUNCTION: ATP-dependent microtubule severing protein that specifically
CC recognizes and cuts microtubules that are polyglutamylated
CC (PubMed:19141076 PubMed:20530212). Preferentially recognizes and acts
CC on microtubules decorated with short polyglutamate tails: severing
CC activity increases as the number of glutamates per tubulin rises from
CC one to eight, but decreases beyond this glutamylation threshold (By
CC similarity). Severing activity is not dependent on tubulin acetylation
CC or detyrosination (By similarity). Microtubule severing promotes
CC reorganization of cellular microtubule arrays and the release of
CC microtubules from the centrosome following nucleation (By similarity).
CC It is critical for the biogenesis and maintenance of complex
CC microtubule arrays in axons, spindles and cilia (By similarity). SPAST
CC is involved in abscission step of cytokinesis and nuclear envelope
CC reassembly during anaphase in cooperation with the ESCRT-III complex
CC (By similarity). Recruited at the midbody, probably by IST1, and
CC participates in membrane fission during abscission together with the
CC ESCRT-III complex (By similarity). Recruited to the nuclear membrane by
CC IST1 and mediates microtubule severing, promoting nuclear envelope
CC sealing and mitotic spindle disassembly during late anaphase (By
CC similarity). Required for membrane traffic from the endoplasmic
CC reticulum (ER) to the Golgi and endosome recycling (By similarity).
CC Recruited by IST1 to endosomes and regulates early endosomal tubulation
CC and recycling by mediating microtubule severing (By similarity).
CC Probably plays a role in axon growth and the formation of axonal
CC branches (PubMed:18234839). {ECO:0000250|UniProtKB:Q9UBP0,
CC ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:18234839,
CC ECO:0000269|PubMed:19141076, ECO:0000269|PubMed:20530212}.
CC -!- FUNCTION: [Isoform 1]: Involved in lipid metabolism by regulating the
CC size and distribution of lipid droplets.
CC {ECO:0000250|UniProtKB:Q9UBP0}.
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 -!- ACTIVITY REGULATION: Allosteric enzyme with a cooperative mechanism; at
CC least two neighbor subunits influence each other strongly in spastin
CC hexamers. Microtubule binding promotes cooperative interactions among
CC spastin subunits. {ECO:0000255|HAMAP-Rule:MF_03021}.
CC -!- SUBUNIT: Homohexamer. Mostly monomeric, but assembles into hexameric
CC structure for short periods of time. Oligomerization seems to be a
CC prerequisite for catalytic activity. Binding to ATP in a cleft between
CC two adjacent subunits stabilizes the homohexameric form. Binds to
CC microtubules at least in part via the alpha-tubulin and beta-tubulin
CC tails. The hexamer adopts a ring conformation through which
CC microtubules pass prior to being severed. Does not interact strongly
CC with tubulin heterodimers. Interacts (via MIT domain) with CHMP1B; the
CC interaction is direct. Interacts with SSNA1. Interacts with ATL1.
CC Interacts with RTN1. Interacts with ZFYVE27. Interacts with REEP1.
CC Interacts (via MIT domain) with IST1. {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 Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03021}. Midbody
CC {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}.
CC Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm,
CC perinuclear region {ECO:0000255|HAMAP-Rule:MF_03021}. Nucleus
CC {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm {ECO:0000255|HAMAP-
CC Rule:MF_03021}. Cell projection, axon {ECO:0000250|UniProtKB:Q9UBP0}.
CC Note=Forms an intramembrane hairpin-like structure in the membrane.
CC Localization to the centrosome is independent of microtubules.
CC Localizes to the midbody of dividing cells, and this requires CHMP1B
CC (By similarity). Enriched in the distal axons and branches of
CC postmitotic neurons (By similarity). Evenly distributed along early
CC axons and concentrates in the growth cone of the axons of late stage 3
CC neurons (PubMed:18234839). Mainly nuclear in interphase cells and
CC becomes associated with the centrosomes, spindle microtubules, midzone
CC and finally the midbody during cell division (By similarity).
CC {ECO:0000250|UniProtKB:Q9UBP0, ECO:0000255|HAMAP-Rule:MF_03021,
CC ECO:0000269|PubMed:18234839}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9UBP0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9UBP0}. Nucleus membrane
CC {ECO:0000250|UniProtKB:Q9UBP0}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q9UBP0}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9UBP0}. Endosome
CC {ECO:0000250|UniProtKB:Q9UBP0}. Note=Forms an intramembrane hairpin-
CC like structure in the membrane. Recruited to nuclear membrane by IST1
CC during late anaphase. Localizes to endoplasmic reticulum tubular
CC network. {ECO:0000250|UniProtKB:Q9UBP0}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000250|UniProtKB:Q9UBP0}. Endosome
CC {ECO:0000250|UniProtKB:Q9UBP0}. Nucleus membrane
CC {ECO:0000250|UniProtKB:Q9UBP0}. Note=Constitutes the main endosomal
CC form. Recruited to nuclear membrane by IST1 during late anaphase.
CC {ECO:0000250|UniProtKB:Q9UBP0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=68 kDa {ECO:0000250|UniProtKB:Q9UBP0}, M1
CC {ECO:0000250|UniProtKB:Q9UBP0};
CC IsoId=Q9QYY8-1; Sequence=Displayed;
CC Name=2; Synonyms=Short, Short variant 1, 60 kDa
CC {ECO:0000250|UniProtKB:Q9UBP0}, M87 {ECO:0000250|UniProtKB:Q9UBP0};
CC IsoId=Q9QYY8-2; Sequence=VSP_058335;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, liver, lung, skeletal
CC muscle, spinal cord, spleen and testis. {ECO:0000269|PubMed:10610178,
CC ECO:0000269|PubMed:16026783}.
CC -!- INDUCTION: Expressed is decreased following activation of the Notch
CC pathway by JAG1/Jagged1. {ECO:0000269|PubMed:18495362}.
CC -!- DISRUPTION PHENOTYPE: Mice develop gait abnormalities that correlate
CC with phenotypes seen in hereditary spastic paraplegia (HSP) patients
CC (PubMed:19453301). Adults are sterile (PubMed:17101632). Progressive
CC axonal degeneration characterized by focal axonal swellings and the
CC accumulation of organelles and cytoskeletal components, which is
CC suggestive of impaired axonal transport (PubMed:17101632,
CC PubMed:19453301). Primary cortical neurons develop swellings at the
CC border between stable and dynamic microtubules (PubMed:17101632). In
CC neurons with axonal swellings, the mitochondrial axonal transport
CC defects are exacerbated: distal to axonal swellings both anterograde
CC and retrograde transport are severely reduced (PubMed:19453301). In
CC cortical neurons, axonal swellings is probably due to impaired
CC microtubule dynamics all along the axons (PubMed:22773755).
CC {ECO:0000269|PubMed:17101632, ECO:0000269|PubMed:19453301,
CC ECO:0000269|PubMed:22773755}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03021}.
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DR EMBL; AK129282; BAC98092.1; -; mRNA.
DR EMBL; BC046286; AAH46286.1; -; mRNA.
DR EMBL; AK007793; BAB25259.1; -; mRNA.
DR EMBL; AJ246002; CAB60143.1; -; mRNA.
DR CCDS; CCDS50181.1; -. [Q9QYY8-1]
DR RefSeq; NP_001156342.1; NM_001162870.1. [Q9QYY8-1]
DR RefSeq; NP_058658.2; NM_016962.2.
DR AlphaFoldDB; Q9QYY8; -.
DR SMR; Q9QYY8; -.
DR BioGRID; 206134; 44.
DR IntAct; Q9QYY8; 41.
DR STRING; 10090.ENSMUSP00000024869; -.
DR iPTMnet; Q9QYY8; -.
DR PhosphoSitePlus; Q9QYY8; -.
DR EPD; Q9QYY8; -.
DR MaxQB; Q9QYY8; -.
DR PaxDb; Q9QYY8; -.
DR PeptideAtlas; Q9QYY8; -.
DR PRIDE; Q9QYY8; -.
DR ProteomicsDB; 257303; -. [Q9QYY8-1]
DR ProteomicsDB; 257304; -. [Q9QYY8-2]
DR Antibodypedia; 2246; 255 antibodies from 30 providers.
DR DNASU; 50850; -.
DR Ensembl; ENSMUST00000024869; ENSMUSP00000024869; ENSMUSG00000024068. [Q9QYY8-1]
DR GeneID; 50850; -.
DR KEGG; mmu:50850; -.
DR UCSC; uc008dnz.2; mouse. [Q9QYY8-1]
DR CTD; 6683; -.
DR MGI; MGI:1858896; Spast.
DR VEuPathDB; HostDB:ENSMUSG00000024068; -.
DR eggNOG; KOG0740; Eukaryota.
DR GeneTree; ENSGT00940000156258; -.
DR HOGENOM; CLU_000688_21_5_1; -.
DR InParanoid; Q9QYY8; -.
DR OMA; GMTNEPM; -.
DR OrthoDB; 1176820at2759; -.
DR PhylomeDB; Q9QYY8; -.
DR TreeFam; TF105014; -.
DR Reactome; R-MMU-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR BioGRID-ORCS; 50850; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Spast; mouse.
DR PRO; PR:Q9QYY8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9QYY8; protein.
DR Bgee; ENSMUSG00000024068; Expressed in secondary oocyte and 264 other tissues.
DR ExpressionAtlas; Q9QYY8; baseline and differential.
DR Genevisible; Q9QYY8; MM.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
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:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0019896; P:axonal transport of mitochondrion; IMP:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0032506; P:cytokinetic process; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
DR GO; GO:0090148; P:membrane fission; ISS:UniProtKB.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0051013; P:microtubule severing; IDA:MGI.
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:0032467; P:positive regulation of cytokinesis; ISO:MGI.
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; 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; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Alternative splicing; ATP-binding; Cell cycle;
KW Cell division; Cell projection; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Endoplasmic reticulum; Endosome;
KW Isomerase; Lipid droplet; Membrane; Microtubule; Neurogenesis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..614
FT /note="Spastin"
FT /id="PRO_0000084764"
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..614
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT DOMAIN 118..193
FT /note="MIT"
FT /evidence="ECO:0000255"
FT REGION 1..298
FT /note="Required for interaction with RTN1"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP0"
FT REGION 1..192
FT /note="Required for midbody localization"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP0"
FT REGION 1..78
FT /note="Required for interaction with ATL1"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP0"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..48
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP0"
FT REGION 48..85
FT /note="Required for interaction with SSNA1 and
FT microtubules"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP0"
FT REGION 91..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..194
FT /note="Sufficient for interaction with CHMP1B"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP0"
FT REGION 112..198
FT /note="Required for interaction with microtubules"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP0"
FT REGION 220..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..614
FT /note="Sufficient for microtubule severing"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP0"
FT REGION 268..326
FT /note="Required for interaction with microtubules and
FT microtubule severing"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP0"
FT REGION 308..310
FT /note="Required for interaction with microtubules"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP0"
FT MOTIF 4..11
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT MOTIF 57..65
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT MOTIF 307..310
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT COMPBIAS 18..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 380..387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP0"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP0"
FT MOD_RES 304
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP0"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBP0"
FT VAR_SEQ 1..84
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_058335"
FT MUTAGEN 360
FT /note="S->C: Decreased microtubule severing activity."
FT /evidence="ECO:0000269|PubMed:20530212"
FT MUTAGEN 553
FT /note="D->A: Decreased microtubule severing activity."
FT /evidence="ECO:0000269|PubMed:20530212"
FT CONFLICT 104
FT /note="E -> A (in Ref. 1; BAC98092 and 2; AAH46286)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="Missing (in Ref. 2; AAH46286 and 3; BAB25259)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 614 AA; 66456 MW; C0D235031A7E4C8F CRC64;
MSSPAGRRKK KGSGGASPAP ARPPPPAAVP APAAGPAPAA GSPPKRNPSS FSSPLVVGFA
LLRLLACHLG LLFAWLCQRF SRALMAAKRS SGTAPAPASP SPPEPGPGGE AESVRVFHKQ
AFEYISIALR IDEEEKAGQK EQAVEWYKKG IEELEKGIAV IVTGQGEQYE RARRLQAKMM
TNLVMAKDRL QLLEKLQPVL QFSKSQTDVY NESTNLTCRN GHLQSESGAV PKRKDPLTHA
SNSLPRSKTV LKSGSAGLSG HHRAPSCSGL SMVSGARPGP GPAATTHKGT PKPNRTNKPS
TPTTAVRKKK DLKNFRNVDS NLANLIMNEI VDNGTAVKFD DIAGQELAKQ ALQEIVILPS
LRPELFTGLR APARGLLLFG PPGNGKTMLA KAVAAESNAT FFNISAASLT SKYVGEGEKL
VRALFAVARE LQPSIIFIDE VDSLLCERRE GEHDASRRLK TEFLIEFDGV QSAGDDRVLV
MGATNRPQEL DEAVLRRFIK RVYVSLPNEE TRLLLLKNLL CKQGSPLTQK ELAQLARMTD
GYSGSDLTAL AKDAALGPIR ELKPEQVKNM SASEMRNIRL SDFTESLKKI KRSVSPQTLE
AYIRWNKDFG DTTV
