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Spastin (EC 3.6.4.3)

 SPAST_MOUSE             Reviewed;         614 AA.
Q9QYY8; Q6ZPY6; Q80VE0; Q9CVK0;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
24-MAR-2009, sequence version 3.
28-MAR-2018, entry version 155.
RecName: Full=Spastin {ECO:0000255|HAMAP-Rule:MF_03021};
EC=3.6.4.3 {ECO:0000255|HAMAP-Rule:MF_03021};
Name=Spast {ECO:0000255|HAMAP-Rule:MF_03021};
Synonyms=Kiaa1083 {ECO:0000303|PubMed:14621295}, Spg4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryonic tail;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N-3; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-614.
STRAIN=C57BL/6J; TISSUE=Pancreas;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 111-614, AND TISSUE SPECIFICITY.
PubMed=10610178; DOI=10.1038/15472;
Hazan J., Fonknechten N., Mavel D., Paternotte C., Samson D.,
Artiguenave F., Davoine C.-S., Cruaud C., Durr A., Wincker P.,
Brottier P., Cattolico L., Barbe V., Burgunder J.-M.,
Prud'homme J.-F., Brice A., Fontaine B., Heilig R., Weissenbach J.;
"Spastin, a new AAA protein, is altered in the most frequent form of
autosomal dominant spastic paraplegia.";
Nat. Genet. 23:296-303(1999).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[6]
TISSUE SPECIFICITY.
PubMed=16026783; DOI=10.1016/j.yexcr.2005.06.009;
Claudiani P., Riano E., Errico A., Andolfi G., Rugarli E.I.;
"Spastin subcellular localization is regulated through usage of
different translation start sites and active export from the
nucleus.";
Exp. Cell Res. 309:358-369(2005).
[7]
DISRUPTION PHENOTYPE.
PubMed=17101632; DOI=10.1093/hmg/ddl431;
Tarrade A., Fassier C., Courageot S., Charvin D., Vitte J., Peris L.,
Thorel A., Mouisel E., Fonknechten N., Roblot N., Seilhean D.,
Dierich A., Hauw J.J., Melki J.;
"A mutation of spastin is responsible for swellings and impairment of
transport in a region of axon characterized by changes in microtubule
composition.";
Hum. Mol. Genet. 15:3544-3558(2006).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18234839; DOI=10.1091/mbc.E07-09-0878;
Yu W., Qiang L., Solowska J.M., Karabay A., Korulu S., Baas P.W.;
"The microtubule-severing proteins spastin and katanin participate
differently in the formation of axonal branches.";
Mol. Biol. Cell 19:1485-1498(2008).
[9]
INDUCTION.
PubMed=18495362; DOI=10.1016/j.neuroscience.2008.04.025;
Ferrari-Toninelli G., Bonini S.A., Bettinsoli P., Uberti D., Memo M.;
"Microtubule stabilizing effect of notch activation in primary
cortical neurons.";
Neuroscience 154:946-952(2008).
[10]
FUNCTION.
PubMed=19141076; DOI=10.1111/j.1471-4159.2009.05875.x;
Riano E., Martignoni M., Mancuso G., Cartelli D., Crippa F., Toldo I.,
Siciliano G., Di Bella D., Taroni F., Bassi M.T., Cappelletti G.,
Rugarli E.I.;
"Pleiotropic effects of spastin on neurite growth depending on
expression levels.";
J. Neurochem. 108:1277-1288(2009).
[11]
DISRUPTION PHENOTYPE.
PubMed=19453301; DOI=10.1111/j.1471-4159.2009.06104.x;
Kasher P.R., De Vos K.J., Wharton S.B., Manser C., Bennett E.J.,
Bingley M., Wood J.D., Milner R., McDermott C.J., Miller C.C.,
Shaw P.J., Grierson A.J.;
"Direct evidence for axonal transport defects in a novel mouse model
of mutant spastin-induced hereditary spastic paraplegia (HSP) and
human HSP patients.";
J. Neurochem. 110:34-44(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Liver, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
FUNCTION, AND MUTAGENESIS OF SER-360 AND ASP-553.
PubMed=20530212; DOI=10.1083/jcb.201001024;
Lacroix B., van Dijk J., Gold N.D., Guizetti J., Aldrian-Herrada G.,
Rogowski K., Gerlich D.W., Janke C.;
"Tubulin polyglutamylation stimulates spastin-mediated microtubule
severing.";
J. Cell Biol. 189:945-954(2010).
[14]
DISRUPTION PHENOTYPE.
PubMed=22773755; DOI=10.1242/dmm.008946;
Fassier C., Tarrade A., Peris L., Courageot S., Mailly P., Dalard C.,
Delga S., Roblot N., Lefevre J., Job D., Hazan J., Curmi P.A.,
Melki J.;
"Microtubule-targeting drugs rescue axonal swellings in cortical
neurons from spastin knockout mice.";
Dis. Model. Mech. 6:72-83(2013).
-!- FUNCTION: ATP-dependent microtubule severing protein that
specifically recognizes and cuts microtubules that are
polyglutamylated (PubMed:19141076 PubMed:20530212). Preferentially
recognizes and acts on microtubules decorated with short
polyglutamate tails: severing activity increases as the number of
glutamates per tubulin rises from one to eight, but decreases
beyond this glutamylation threshold (By similarity). Severing
activity is not dependent on tubulin acetylation or detyrosination
(By similarity). Microtubule severing promotes reorganization of
cellular microtubule arrays and the release of microtubules from
the centrosome following nucleation (By similarity). It is
critical for the biogenesis and maintenance of complex microtubule
arrays in axons, spindles and cilia (By similarity). SPAST is
involved in abscission step of cytokinesis and nuclear envelope
reassembly during anaphase in cooperation with the ESCRT-III
complex (By similarity). Recruited at the midbody, probably by
IST1, and participates in membrane fission during abscission
together with the ESCRT-III complex (By similarity). Recruited to
the nuclear membrane by IST1 and mediates microtubule severing,
promoting nuclear envelope sealing and mitotic spindle disassembly
during late anaphase (By similarity). Required for membrane
traffic from the endoplasmic reticulum (ER) to the Golgi and
endosome recycling (By similarity). Recruited by IST1 to endosomes
and regulates early endosomal tubulation and recycling by
mediating microtubule severing (By similarity). Probably plays a
role in axon growth and the formation of axonal branches
(PubMed:18234839). {ECO:0000250|UniProtKB:Q9UBP0,
ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:18234839,
ECO:0000269|PubMed:19141076, ECO:0000269|PubMed:20530212}.
-!- FUNCTION: Isoform 1: Involved in lipid metabolism by regulating
the size and distribution of lipid droplets.
{ECO:0000250|UniProtKB:Q9UBP0}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000255|HAMAP-Rule:MF_03021}.
-!- ENZYME REGULATION: Allosteric enzyme with a cooperative mechanism;
at least two neighbor subunits influence each other strongly in
spastin hexamers. Microtubule binding promotes cooperative
interactions among spastin subunits. {ECO:0000255|HAMAP-
Rule:MF_03021}.
-!- SUBUNIT: Homohexamer. Mostly monomeric, but assembles into
hexameric structure for short periods of time. Oligomerization
seems to be a prerequisite for catalytic activity. Binding to ATP
in a cleft between two adjacent subunits stabilizes the
homohexameric form. Binds to microtubules at least in part via the
alpha-tubulin and beta-tubulin tails. The hexamer adopts a ring
conformation through which microtubules pass prior to being
severed. Does not interact strongly with tubulin heterodimers.
Interacts (via MIT domain) with CHMP1B; the interaction is direct.
Interacts with SSNA1. Interacts with ATL1. Interacts with RTN1.
Interacts with ZFYVE27. Interacts with REEP1. Interacts (via MIT
domain) with IST1. {ECO:0000255|HAMAP-Rule:MF_03021}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021};
Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}.
Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03021}. Midbody
{ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome {ECO:0000255|HAMAP-
Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-
Rule:MF_03021}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03021}.
Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-
Rule:MF_03021}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03021}.
Note=Forms a intramembrane hairpin-like structure in the membrane.
Localization to the centrosome is independent of microtubules.
Localizes to the midbody of dividing cells, and this requires
CHMP1B (By similarity). Enriched in the distal axons and branches
of postmitotic neurons (By similarity). Evenly distributed along
early axons and concentrates in the growth cone of the axons of
late stage 3 neurons (PubMed:18234839). {ECO:0000255|HAMAP-
Rule:MF_03021, ECO:0000269|PubMed:18234839}.
-!- SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q9UBP0}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q9UBP0}. Nucleus membrane
{ECO:0000250|UniProtKB:Q9UBP0}. Lipid droplet
{ECO:0000250|UniProtKB:Q9UBP0}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q9UBP0}. Endosome
{ECO:0000250|UniProtKB:Q9UBP0}. Note=Forms a intramembrane
hairpin-like structure in the membrane. Recruited to nuclear
membrane by IST1 during late anaphase. Localizes to endoplasmic
reticulum tubular network. {ECO:0000250|UniProtKB:Q9UBP0}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000250|UniProtKB:Q9UBP0}. Endosome
{ECO:0000250|UniProtKB:Q9UBP0}. Nucleus membrane
{ECO:0000250|UniProtKB:Q9UBP0}. Note=Constitutes the main
endosomal form. Recruited to nuclear membrane by IST1 during late
anaphase. {ECO:0000250|UniProtKB:Q9UBP0}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=68 kDa {ECO:0000250|UniProtKB:Q9UBP0}, M1
{ECO:0000250|UniProtKB:Q9UBP0};
IsoId=Q9QYY8-1; Sequence=Displayed;
Name=2; Synonyms=Short, Short variant 1, 60 kDa
{ECO:0000250|UniProtKB:Q9UBP0}, M87
{ECO:0000250|UniProtKB:Q9UBP0};
IsoId=Q9QYY8-2; Sequence=VSP_058335;
-!- TISSUE SPECIFICITY: Expressed in brain, heart, liver, lung,
skeletal muscle, spinal cord, spleen and testis.
{ECO:0000269|PubMed:10610178, ECO:0000269|PubMed:16026783}.
-!- INDUCTION: Expressed is decreased following activation of the
Notch pathway by JAG1/Jagged1. {ECO:0000269|PubMed:18495362}.
-!- DISRUPTION PHENOTYPE: Mice develop gait abnormalities that
correlate with phenotypes seen in hereditary spastic paraplegia
(HSP) patients (PubMed:19453301). Adults are sterile
(PubMed:17101632). Progressive axonal degeneration characterized
by focal axonal swellings and the accumulation of organelles and
cytoskeletal components, which is suggestive of impaired axonal
transport (PubMed:17101632, PubMed:19453301). Primary cortical
neurons develop swellings at the border between stable and dynamic
microtubules (PubMed:17101632). In neurons with axonal swellings,
the mitochondrial axonal transport defects are exacerbated: distal
to axonal swellings both anterograde and retrograde transport are
severely reduced (PubMed:19453301). In cortical neurons, axonal
swellings is probably due to impaired microtubule dynamics all
along the axons (PubMed:22773755). {ECO:0000269|PubMed:17101632,
ECO:0000269|PubMed:19453301, ECO:0000269|PubMed:22773755}.
-!- SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily.
{ECO:0000255|HAMAP-Rule:MF_03021}.
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EMBL; AK129282; BAC98092.1; -; mRNA.
EMBL; BC046286; AAH46286.1; -; mRNA.
EMBL; AK007793; BAB25259.1; -; mRNA.
EMBL; AJ246002; CAB60143.1; -; mRNA.
CCDS; CCDS50181.1; -. [Q9QYY8-1]
RefSeq; NP_001156342.1; NM_001162870.1. [Q9QYY8-1]
RefSeq; NP_058658.2; NM_016962.2.
UniGene; Mm.19804; -.
ProteinModelPortal; Q9QYY8; -.
SMR; Q9QYY8; -.
BioGrid; 206134; 41.
IntAct; Q9QYY8; 41.
STRING; 10090.ENSMUSP00000024869; -.
iPTMnet; Q9QYY8; -.
PhosphoSitePlus; Q9QYY8; -.
EPD; Q9QYY8; -.
MaxQB; Q9QYY8; -.
PaxDb; Q9QYY8; -.
PeptideAtlas; Q9QYY8; -.
PRIDE; Q9QYY8; -.
Ensembl; ENSMUST00000024869; ENSMUSP00000024869; ENSMUSG00000024068. [Q9QYY8-1]
GeneID; 50850; -.
KEGG; mmu:50850; -.
UCSC; uc008dnz.2; mouse. [Q9QYY8-1]
CTD; 6683; -.
MGI; MGI:1858896; Spast.
eggNOG; KOG0740; Eukaryota.
eggNOG; COG0464; LUCA.
GeneTree; ENSGT00570000078874; -.
HOGENOM; HOG000225146; -.
HOVERGEN; HBG108502; -.
InParanoid; Q9QYY8; -.
KO; K13254; -.
OMA; SEMRNIK; -.
OrthoDB; EOG091G0Q8J; -.
PhylomeDB; Q9QYY8; -.
TreeFam; TF105014; -.
PRO; PR:Q9QYY8; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024068; -.
CleanEx; MM_SPAST; -.
Genevisible; Q9QYY8; MM.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0071782; C:endoplasmic reticulum tubular network; ISO:MGI.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0030496; C:midbody; ISO:MGI.
GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
GO; GO:0008568; F:microtubule-severing ATPase activity; ISS:UniProtKB.
GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
GO; GO:0019896; P:axonal transport of mitochondrion; IMP:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0032506; P:cytokinetic process; ISS:UniProtKB.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; ISS:UniProtKB.
GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
GO; GO:0090148; P:membrane fission; ISS:UniProtKB.
GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
GO; GO:0051013; P:microtubule severing; IDA:MGI.
GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
GO; GO:0051228; P:mitotic spindle disassembly; ISS:UniProtKB.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0031468; P:nuclear envelope reassembly; ISS:UniProtKB.
GO; GO:0032467; P:positive regulation of cytokinesis; ISO:MGI.
GO; GO:0034214; P:protein hexamerization; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
HAMAP; MF_03021; Spastin; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR007330; MIT.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR017179; Spastin.
InterPro; IPR035106; Spastin_chordate.
InterPro; IPR015415; Vps4_C.
Pfam; PF00004; AAA; 1.
Pfam; PF09336; Vps4_C; 1.
PIRSF; PIRSF037338; Spastin; 1.
SMART; SM00382; AAA; 1.
SMART; SM00745; MIT; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00674; AAA; 1.
1: Evidence at protein level;
Allosteric enzyme; Alternative splicing; ATP-binding; Cell cycle;
Cell division; Complete proteome; Cytoplasm; Cytoskeleton;
Developmental protein; Differentiation; Endoplasmic reticulum;
Endosome; Hydrolase; Lipid droplet; Membrane; Microtubule;
Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome.
CHAIN 1 614 Spastin.
/FTId=PRO_0000084764.
TOPO_DOM 1 54 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_03021}.
INTRAMEM 55 75 Helical. {ECO:0000255|HAMAP-
Rule:MF_03021}.
TOPO_DOM 76 614 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_03021}.
DOMAIN 118 193 MIT. {ECO:0000255}.
NP_BIND 380 387 ATP. {ECO:0000255|HAMAP-Rule:MF_03021}.
REGION 1 298 Required for interaction with RTN1.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 1 192 Required for midbody localization.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 1 78 Required for interaction with ATL1.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 1 48 Required for nuclear localization.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 48 85 Required for interaction with SSNA1 and
microtubules.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 110 194 Sufficient for interaction with CHMP1B.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 112 198 Required for interaction with
microtubules.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 226 614 Sufficient for microtubule severing.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 268 326 Required for interaction with
microtubules and microtubule severing.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 308 310 Required for interaction with
microtubules.
{ECO:0000250|UniProtKB:Q9UBP0}.
MOTIF 4 11 Nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_03021}.
MOTIF 57 65 Nuclear export signal.
{ECO:0000255|HAMAP-Rule:MF_03021}.
MOTIF 307 310 Nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_03021}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UBP0}.
MOD_RES 266 266 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UBP0}.
MOD_RES 304 304 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UBP0}.
MOD_RES 595 595 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UBP0}.
VAR_SEQ 1 84 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_058335.
MUTAGEN 360 360 S->C: Decreased microtubule severing
activity. {ECO:0000269|PubMed:20530212}.
MUTAGEN 553 553 D->A: Decreased microtubule severing
activity. {ECO:0000269|PubMed:20530212}.
CONFLICT 104 104 E -> A (in Ref. 1; BAC98092 and 2;
AAH46286). {ECO:0000305}.
CONFLICT 137 137 Missing (in Ref. 2; AAH46286 and 3;
BAB25259). {ECO:0000305}.
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


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