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Spastin (EC 3.6.4.3) (Spastic paraplegia 4 protein)

 SPAST_HUMAN             Reviewed;         616 AA.
Q9UBP0; A7E2A7; Q9UPR9;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 172.
RecName: Full=Spastin {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000303|PubMed:10610178};
EC=3.6.4.3 {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:15716377, ECO:0000269|PubMed:16219033, ECO:0000269|PubMed:16815977, ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:18410514, ECO:0000269|PubMed:22637577};
AltName: Full=Spastic paraplegia 4 protein;
Name=SPAST {ECO:0000255|HAMAP-Rule:MF_03021,
ECO:0000312|HGNC:HGNC:11233};
Synonyms=ADPSP, FSP2, KIAA1083 {ECO:0000303|PubMed:10470851},
SPG4 {ECO:0000255|HAMAP-Rule:MF_03021};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND VARIANTS SPG4 CYS-362; TYR-448
AND CYS-499.
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS SPG4
ARG-370; CYS-381; LYS-386; ARG-388; VAL-426; TYR-448; LEU-460; CYS-499
AND VAL-556.
PubMed=11809724; DOI=10.1093/hmg/11.2.153;
Errico A., Ballabio A., Rugarli E.I.;
"Spastin, the protein mutated in autosomal dominant hereditary spastic
paraplegia, is involved in microtubule dynamics.";
Hum. Mol. Genet. 11:153-163(2002).
[6]
DOMAIN MIT, AND PROBABLE FUNCTION.
PubMed=12676568; DOI=10.1016/S0888-7543(03)00011-9;
Ciccarelli F.D., Proukakis C., Patel H., Cross H., Azam S.,
Patton M.A., Bork P., Crosby A.H.;
"The identification of a conserved domain in both spartin and spastin,
mutated in hereditary spastic paraplegia.";
Genomics 81:437-441(2003).
[7]
SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
PubMed=15147984; DOI=10.1016/j.bbrc.2004.03.195;
Beetz C., Brodhun M., Moutzouris K., Kiehntopf M., Berndt A.,
Lehnert D., Deufel T., Bastmeyer M., Schickel J.;
"Identification of nuclear localisation sequences in spastin (SPG4)
using a novel Tetra-GFP reporter system.";
Biochem. Biophys. Res. Commun. 318:1079-1084(2004).
[8]
INTERACTION WITH SSNA1 AND MICROTUBULES, AND SUBCELLULAR LOCATION.
PubMed=15269182; DOI=10.1093/hmg/ddh223;
Errico A., Claudiani P., D'Addio M., Rugarli E.I.;
"Spastin interacts with the centrosomal protein NA14, and is enriched
in the spindle pole, the midbody and the distal axon.";
Hum. Mol. Genet. 13:2121-2132(2004).
[9]
ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNALS,
AND MUTAGENESIS OF MET-1 AND MET-87.
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).
[10]
INTERACTION WITH CHMP1B, AND SUBCELLULAR LOCATION.
PubMed=15537668; DOI=10.1093/hmg/ddi003;
Reid E., Connell J.W., Edwards T.L., Duley S., Brown S.E.,
Sanderson C.M.;
"The hereditary spastic paraplegia protein spastin interacts with the
ESCRT-III complex-associated endosomal protein CHMP1B.";
Hum. Mol. Genet. 14:19-38(2005).
[11]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION, MUTAGENESIS OF
LYS-388 AND GLU-442, AND CHARACTERIZATION OF VARIANTS SPG4 LYS-344;
LYS-347; LYS-386; ARG-388 AND CYS-499.
PubMed=15716377; DOI=10.1083/jcb.200409058;
Evans K.J., Gomes E.R., Reisenweber S.M., Gundersen G.G.,
Lauring B.P.;
"Linking axonal degeneration to microtubule remodeling by Spastin-
mediated microtubule severing.";
J. Cell Biol. 168:599-606(2005).
[12]
FUNCTION, CATALYTIC ACTIVITY, AND ASSOCIATION WITH MICROTUBULES.
PubMed=16219033; DOI=10.1111/j.1471-4159.2005.03472.x;
Salinas S., Carazo-Salas R.E., Proukakis C., Cooper J.M., Weston A.E.,
Schiavo G., Warner T.T.;
"Human spastin has multiple microtubule-related functions.";
J. Neurochem. 95:1411-1420(2005).
[13]
SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT SPG4 ARG-388.
PubMed=15891913; DOI=10.1007/s10048-005-0219-2;
Svenson I.K., Kloos M.T., Jacon A., Gallione C., Horton A.C.,
Pericak-Vance M.A., Ehlers M.D., Marchuk D.A.;
"Subcellular localization of spastin: implications for the
pathogenesis of hereditary spastic paraplegia.";
Neurogenetics 6:135-141(2005).
[14]
INTERACTION WITH ZFYVE27.
PubMed=16826525; DOI=10.1086/504927;
Mannan A.U., Krawen P., Sauter S.M., Boehm J., Chronowska A.,
Paulus W., Neesen J., Engel W.;
"ZFYVE27 (SPG33), a novel spastin-binding protein, is mutated in
hereditary spastic paraplegia.";
Am. J. Hum. Genet. 79:351-357(2006).
[15]
INTERACTION WITH ATL1, AND CHARACTERIZATION OF VARIANT SPG4 ARG-388.
PubMed=16339213; DOI=10.1093/hmg/ddi447;
Sanderson C.M., Connell J.W., Edwards T.L., Bright N.A., Duley S.,
Thompson A., Luzio J.P., Reid E.;
"Spastin and atlastin, two proteins mutated in autosomal-dominant
hereditary spastic paraplegia, are binding partners.";
Hum. Mol. Genet. 15:307-318(2006).
[16]
INTERACTION WITH RTN1, AND SUBCELLULAR LOCATION.
PubMed=16602018; DOI=10.1007/s10048-006-0034-4;
Mannan A.U., Boehm J., Sauter S.M., Rauber A., Byrne P.C., Neesen J.,
Engel W.;
"Spastin, the most commonly mutated protein in hereditary spastic
paraplegia interacts with Reticulon 1 an endoplasmic reticulum
protein.";
Neurogenetics 7:93-103(2006).
[17]
CATALYTIC ACTIVITY, INTERACTION WITH ATL1, AND MUTAGENESIS OF GLU-442.
PubMed=16815977; DOI=10.1073/pnas.0510863103;
Evans K.J., Keller C., Pavur K., Glasgow K., Conn B., Lauring B.P.;
"Interaction of two hereditary spastic paraplegia gene products,
spastin and atlastin, suggests a common pathway for axonal
maintenance.";
Proc. Natl. Acad. Sci. U.S.A. 103:10666-10671(2006).
[18]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
HOMOHEXAMERIZATION, INTERACTION WITH TUBULIN AND MICROTUBULES,
SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-415; GLU-442; ARG-451 AND
ALA-457, AND CHARACTERIZATION OF VARIANT SPG4 TYR-448.
PubMed=17389232; DOI=10.1083/jcb.200610072;
White S.R., Evans K.J., Lary J., Cole J.L., Lauring B.P.;
"Recognition of C-terminal amino acids in tubulin by pore loops in
Spastin is important for microtubule severing.";
J. Cell Biol. 176:995-1005(2007).
[19]
ALTERNATIVE PROMOTER USAGE, AND CHARACTERIZATION OF VARIANT LEU-44.
PubMed=18613979; DOI=10.1186/1741-7007-6-31;
Mancuso G., Rugarli E.I.;
"A cryptic promoter in the first exon of the SPG4 gene directs the
synthesis of the 60-kDa spastin isoform.";
BMC Biol. 6:31-31(2008).
[20]
CATALYTIC ACTIVITY, HOMOHEXAMERIZATION, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF GLU-442.
PubMed=18410514; DOI=10.1111/j.1471-4159.2008.05414.x;
Pantakani D.V.K., Swapna L.S., Srinivasan N., Mannan A.U.;
"Spastin oligomerizes into a hexamer and the mutant spastin (E442Q)
redistribute the wild-type spastin into filamentous microtubule.";
J. Neurochem. 106:613-624(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268 AND THR-306, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[23]
FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), AND
CHARACTERIZATION OF VARIANT SPG4 ARG-388.
PubMed=19000169; DOI=10.1111/j.1600-0854.2008.00847.x;
Connell J.W., Lindon C., Luzio J.P., Reid E.;
"Spastin couples microtubule severing to membrane traffic in
completion of cytokinesis and secretion.";
Traffic 10:42-56(2009).
[24]
INTERACTION WITH REEP1, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), AND
TOPOLOGY (ISOFORM 1).
PubMed=20200447; DOI=10.1172/JCI40979;
Park S.H., Zhu P.P., Parker R.L., Blackstone C.;
"Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1
coordinate microtubule interactions with the tubular ER network.";
J. Clin. Invest. 120:1097-1110(2010).
[25]
FUNCTION.
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).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[28]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21310966; DOI=10.1126/science.1201847;
Guizetti J., Schermelleh L., Maentler J., Maar S., Poser I.,
Leonhardt H., Mueller-Reichert T., Gerlich D.W.;
"Cortical constriction during abscission involves helices of ESCRT-
III-dependent filaments.";
Science 331:1616-1620(2011).
[29]
HOMOHEXAMERIZATION, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION,
KINETIC PARAMETERS, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
COOPERATIVITY, AND MUTAGENESIS OF GLU-442.
PubMed=22637577; DOI=10.1074/jbc.M111.291898;
Eckert T., Link S., Le D.T., Sobczak J.P., Gieseke A., Richter K.,
Woehlke G.;
"Subunit Interactions and cooperativity in the microtubule-severing
AAA ATPase spastin.";
J. Biol. Chem. 287:26278-26290(2012).
[30]
INTERACTION WITH RTN2.
PubMed=22232211; DOI=10.1172/JCI60560;
Montenegro G., Rebelo A.P., Connell J., Allison R., Babalini C.,
D'Aloia M., Montieri P., Schule R., Ishiura H., Price J.,
Strickland A., Gonzalez M.A., Baumbach-Reardon L., Deconinck T.,
Huang J., Bernardi G., Vance J.M., Rogers M.T., Tsuji S.,
De Jonghe P., Pericak-Vance M.A., Schols L., Orlacchio A., Reid E.,
Zuchner S.;
"Mutations in the ER-shaping protein reticulon 2 cause the axon-
degenerative disorder hereditary spastic paraplegia type 12.";
J. Clin. Invest. 122:538-544(2012).
[31]
INTERACTION WITH MICROTUBULES, OLIGOMERIZATION, AND MUTAGENESIS OF
310-LYS--LYS-312 AND GLU-442.
PubMed=23272056; DOI=10.1371/journal.pone.0050161;
Eckert T., Le D.T., Link S., Friedmann L., Woehlke G.;
"Spastin's microtubule-binding properties and comparison to katanin.";
PLoS ONE 7:E50161-E50161(2012).
[32]
ENZYME REGULATION, AND MUTAGENESIS OF GLU-442 AND CYS-448.
PubMed=23745751; DOI=10.1111/febs.12385;
Wen M., Wang C.;
"The nucleotide cycle of spastin correlates with its microtubule-
binding properties.";
FEBS J. 280:3868-3877(2013).
[33]
FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), AND INTERACTION
WITH IST1.
PubMed=23897888; DOI=10.1083/jcb.201211045;
Allison R., Lumb J.H., Fassier C., Connell J.W., Ten Martin D.,
Seaman M.N., Hazan J., Reid E.;
"An ESCRT-spastin interaction promotes fission of recycling tubules
from the endosome.";
J. Cell Biol. 202:527-543(2013).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-268 AND
SER-597, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[35]
SUBCELLULAR LOCATION, AND INTERACTION WITH ZFYVE27.
PubMed=23969831; DOI=10.1073/pnas.1307391110;
Chang J., Lee S., Blackstone C.;
"Protrudin binds atlastins and endoplasmic reticulum-shaping proteins
and regulates network formation.";
Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[37]
FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), AND INTERACTION
WITH IST1.
PubMed=26040712; DOI=10.1038/nature14408;
Vietri M., Schink K.O., Campsteijn C., Wegner C.S., Schultz S.W.,
Christ L., Thoresen S.B., Brech A., Raiborg C., Stenmark H.;
"Spastin and ESCRT-III coordinate mitotic spindle disassembly and
nuclear envelope sealing.";
Nature 522:231-235(2015).
[38]
FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1), AND
MUTAGENESIS OF ARG-65 AND 81-ARG--ARG-84.
PubMed=25875445; DOI=10.1371/journal.pgen.1005149;
Papadopoulos C., Orso G., Mancuso G., Herholz M., Gumeni S.,
Tadepalle N., Juengst C., Tzschichholz A., Schauss A., Hoening S.,
Trifunovic A., Daga A., Rugarli E.I.;
"Spastin binds to lipid droplets and affects lipid metabolism.";
PLoS Genet. 11:E1005149-E1005149(2015).
[39]
FUNCTION.
PubMed=26875866; DOI=10.1016/j.cell.2016.01.019;
Valenstein M.L., Roll-Mecak A.;
"Graded control of microtubule severing by tubulin glutamylation.";
Cell 164:911-921(2016).
[40]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 112-196 IN COMPLEX WITH
CHMP1B, INTERACTION WITH CHMP1B, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF HIS-120 AND PHE-124.
PubMed=18997780; DOI=10.1038/nsmb.1512;
Yang D., Rismanchi N., Renvoise B., Lippincott-Schwartz J.,
Blackstone C., Hurley J.H.;
"Structural basis for midbody targeting of spastin by the ESCRT-III
protein CHMP1B.";
Nat. Struct. Mol. Biol. 15:1278-1286(2008).
[41]
X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 228-616 OF MUTANT GLN-442,
AND MUTAGENESIS OF GLU-442.
PubMed=22446388; DOI=10.1016/j.jsb.2012.03.002;
Taylor J.L., White S.R., Lauring B., Kull F.J.;
"Crystal structure of the human spastin AAA domain.";
J. Struct. Biol. 179:133-137(2012).
[42]
VARIANT SPG4 GLY-441.
PubMed=11039577; DOI=10.1038/sj.ejhg.5200528;
Buerger J., Fonknechten N., Hoeltzenbein M., Neumann L., Bratanoff E.,
Hazan J., Reis A.;
"Hereditary spastic paraplegia caused by mutations in the SPG4 gene.";
Eur. J. Hum. Genet. 8:771-776(2000).
[43]
VARIANTS SPG4 CYS-362; ARG-370; CYS-381; LYS-386; ARG-388; VAL-426;
TYR-448; LEU-460; CYS-499; ASN-555 AND VAL-556.
PubMed=10699187; DOI=10.1093/hmg/9.4.637;
Fonknechten N., Mavel D., Byrne P., Davoine C.-S., Cruaud C.,
Bonsch D., Samson D., Coutinho P., Hutchinson M., McMonagle P.,
Burgunder J.-M., Tartaglione A., Heinzlef O., Feki I., Deufel T.,
Parfrey N., Brice A., Fontaine B., Prud'homme J.-F., Weissenbach J.,
Duerr A., Hazan J.;
"Spectrum of SPG4 mutations in autosomal dominant spastic
paraplegia.";
Hum. Mol. Genet. 9:637-644(2000).
[44]
VARIANTS SPG4 GLY-424 AND HIS-584, AND VARIANT LEU-44.
PubMed=11015453; DOI=10.1136/jmg.37.10.759;
Lindsey J.C., Lusher M.E., McDermott C.J., White K.D., Reid E.,
Rubinsztein D.C., Bashir R., Hazan J., Shaw P.J., Bushby K.M.D.;
"Mutation analysis of the spastin gene (SPG4) in patients with
hereditary spastic paraparesis.";
J. Med. Genet. 37:759-765(2000).
[45]
VARIANTS SPG4 PHE-436 AND ASP-559.
PubMed=11087788; DOI=10.1212/WNL.55.9.1388;
Hentati A., Deng H.-X., Zhai H., Chen W., Yang Y., Hung W.-Y.,
Azim A.C., Bohlega S., Tandan R., Warner C., Laing N.G., Cambi F.,
Mitsumoto H., Roos R.P., Boustany R.-M.N., Ben-Hamida M., Hentati F.,
Siddique T.;
"Novel mutations in spastin gene and absence of correlation with age
at onset of symptoms.";
Neurology 55:1388-1390(2000).
[46]
VARIANTS SPG4 CYS-499 AND GLY-562.
PubMed=11309678; DOI=10.1086/320111;
Svenson I.K., Ashley-Koch A.E., Gaskell P.C., Riney T.J.,
Cumming W.J.K., Kingston H.M., Hogan E.L., Boustany R.-M.N.,
Vance J.M., Nance M.A., Pericak-Vance M.A., Marchuk D.A.;
"Identification and expression analysis of spastin gene mutations in
hereditary spastic paraplegia.";
Am. J. Hum. Genet. 68:1077-1085(2001).
[47]
VARIANT SPG4 VAL-485.
PubMed=12460147; DOI=10.1034/j.1600-0404.2002.01254.x;
Namekawa M., Takiyama Y., Sakoe K., Nagaki H., Shimazaki H.,
Yoshimura M., Ikeguchi K., Nakano I., Nishizawa M.;
"A Japanese SPG4 family with a novel missense mutation of the SPG4
gene: intrafamilial variability in age at onset and clinical
severity.";
Acta Neurol. Scand. 106:387-391(2002).
[48]
VARIANTS SPG4 LEU-399; VAL-426; LEU-489; ASP-559 AND GLN-562.
PubMed=11843700; DOI=10.1001/archneur.59.2.281;
Meijer I.A., Hand C.K., Cossette P., Figlewicz D.A., Rouleau G.A.;
"Spectrum of SPG4 mutations in a large collection of North American
families with hereditary spastic paraplegia.";
Arch. Neurol. 59:281-286(2002).
[49]
VARIANTS SPG4 ARG-407; TYR-551 AND ILE-615.
PubMed=12124993; DOI=10.1002/humu.10105;
Sauter S.M., Miterski B., Klimpe S., Boensch D., Schoels L.,
Visbeck A., Papke T., Hopf H.C., Engel W., Deufel T., Epplen J.T.,
Neesen J.;
"Mutation analysis of the spastin gene (SPG4) in patients in Germany
with autosomal dominant hereditary spastic paraplegia.";
Hum. Mutat. 20:127-132(2002).
[50]
VARIANTS SPG4 LYS-347; ARG-388 AND CYS-499.
PubMed=12161613; DOI=10.1136/jmg.39.8.e46;
Yabe I., Sasaki H., Tashiro K., Matsuura T., Takegami T., Satoh T.;
"Spastin gene mutation in Japanese with hereditary spastic
paraplegia.";
J. Med. Genet. 39:E46-E46(2002).
[51]
VARIANT SPG4 ASP-512.
PubMed=11985387; DOI=10.1007/PL00007865;
Patrono C., Casali C., Tessa A., Cricchi F., Fortini D., Carrozzo R.,
Siciliano G., Bertini E., Santorelli F.M.;
"Missense and splice site mutations in SPG4 suggest loss-of-function
in dominant spastic paraplegia.";
J. Neurol. 249:200-205(2002).
[52]
VARIANT SPG4 PHE-404 DEL.
PubMed=12163196; DOI=10.1016/S0022-510X(02)00192-2;
Proukakis C., Hart P.E., Cornish A., Warner T.T., Crosby A.H.;
"Three novel spastin (SPG4) mutations in families with autosomal
dominant hereditary spastic paraplegia.";
J. Neurol. Sci. 201:65-69(2002).
[53]
VARIANT SPG4 LYS-344.
PubMed=12202986; DOI=10.1007/s100380200068;
Ki C.S., Lee W.Y., Han do H., Sung D.H., Lee K.B., Lee K.A., Cho S.S.,
Cho S., Hwang H., Sohn K.M., Choi Y.J., Kim J.W.;
"A novel missense mutation (I344K) in the SPG4gene in a Korean family
with autosomal-dominant hereditary spastic paraplegia.";
J. Hum. Genet. 47:473-477(2002).
[54]
VARIANT SPG4 LEU-503.
PubMed=12552568; DOI=10.1002/humu.9108;
Proukakis C., Auer-Grumbach M., Wagner K., Wilkinson P.A., Reid E.,
Patton M.A., Warner T.T., Crosby A.H.;
"Screening of patients with hereditary spastic paraplegia reveals
seven novel mutations in the SPG4 (Spastin) gene.";
Hum. Mutat. 21:170-170(2003).
[55]
VARIANT SPG4 PRO-534.
PubMed=12939659; DOI=10.1038/sj.ejhg.5201027;
Molon A., Montagna P., Angelini C., Pegoraro E.;
"Novel spastin mutations and their expression analysis in two Italian
families.";
Eur. J. Hum. Genet. 11:710-713(2003).
[56]
VARIANTS SPG4 GLN-378; VAL-390 AND LEU-515 DEL.
PubMed=14732620; DOI=10.1001/archneur.61.1.49;
Tang B., Zhao G., Xia K., Pan Q., Luo W., Shen L., Long Z., Dai H.,
Zi X., Jiang H.;
"Three novel mutations of the spastin gene in Chinese patients with
hereditary spastic paraplegia.";
Arch. Neurol. 61:49-55(2004).
[57]
VARIANT SPG4 SER-386.
PubMed=15210521; DOI=10.1001/archneur.61.6.849;
Orlacchio A., Kawarai T., Totaro A., Errico A., St George-Hyslop P.H.,
Rugarli E.I., Bernardi G.;
"Hereditary spastic paraplegia: clinical genetic study of 15
families.";
Arch. Neurol. 61:849-855(2004).
[58]
VARIANT SPG4 GLN-490 DEL.
PubMed=15667412; DOI=10.1111/j.1468-1331.2004.00888.x;
Nielsen J.E., Johnsen B., Koefoed P., Scheuer K.H.,
Groenbech-Jensen M., Law I., Krabbe K., Noerremoelle A., Eiberg H.,
Soendergaard H., Dam M., Rehfeld J.F., Krarup C., Paulson O.B.,
Hasholt L., Soerensen S.A.;
"Hereditary spastic paraplegia with cerebellar ataxia: a complex
phenotype associated with a new SPG4 gene mutation.";
Eur. J. Neurol. 11:817-824(2004).
[59]
VARIANTS SPG4 VAL-470 AND GLY-562, AND VARIANTS LEU-44 AND GLN-45.
PubMed=15248095; DOI=10.1007/s10048-004-0186-z;
Svenson I.K., Kloos M.T., Gaskell P.C., Nance M.A., Garbern J.Y.,
Hisanaga S., Pericak-Vance M.A., Ashley-Koch A.E., Marchuk D.A.;
"Intragenic modifiers of hereditary spastic paraplegia due to spastin
gene mutations.";
Neurogenetics 5:157-164(2004).
[60]
VARIANTS SPG4 GLY-459 AND CYS-460.
PubMed=15482961; DOI=10.1016/j.nmd.2004.05.017;
Falco M., Scuderi C., Musumeci S., Sturnio M., Neri M., Bigoni S.,
Caniatti L., Fichera M.;
"Two novel mutations in the spastin gene (SPG4) found by DHPLC
mutation analysis.";
Neuromuscul. Disord. 14:750-753(2004).
[61]
VARIANT SPG4 ILE-614.
PubMed=15159500; DOI=10.1212/01.WNL.0000125324.32082.D9;
Orlacchio A., Gaudiello F., Totaro A., Floris R.,
St George-Hyslop P.H., Bernardi G., Kawarai T.;
"A new SPG4 mutation in a variant form of spastic paraplegia with
congenital arachnoid cysts.";
Neurology 62:1875-1878(2004).
[62]
VARIANT SPG4 LEU-361, AND VARIANT LEU-44.
PubMed=15326248; DOI=10.1212/01.WNL.0000135346.63675.3E;
Chinnery P.F., Keers S.M., Holden M.J., Ramesh V., Dalton A.;
"Infantile hereditary spastic paraparesis due to codominant mutations
in the spastin gene.";
Neurology 63:710-712(2004).
[63]
VARIANTS SPG4 VAL-195; VAL-406; GLY-493; HIS-499; TRP-503 AND CYS-607.
PubMed=16682546; DOI=10.1001/archneur.63.5.750;
Crippa F., Panzeri C., Martinuzzi A., Arnoldi A., Redaelli F.,
Tonelli A., Baschirotto C., Vazza G., Mostacciuolo M.L., Daga A.,
Orso G., Profice P., Trabacca A., D'Angelo M.G., Comi G.P.,
Galbiati S., Lamperti C., Bonato S., Pandolfo M., Meola G.,
Musumeci O., Toscano A., Trevisan C.P., Bresolin N., Bassi M.T.;
"Eight novel mutations in SPG4 in a large sample of patients with
hereditary spastic paraplegia.";
Arch. Neurol. 63:750-755(2006).
[64]
VARIANT SPG4 LEU-435.
PubMed=16684598; DOI=10.1016/j.nmd.2006.03.009;
Magariello A., Muglia M., Patitucci A., Mazzei R., Conforti F.L.,
Gabriele A.L., Sprovieri T., Ungaro C., Gambardella A., Mancuso M.,
Siciliano G., Branca D., Aguglia U., de Angelis M.V., Longo K.,
Quattrone A.;
"Novel spastin (SPG4) mutations in Italian patients with hereditary
spastic paraplegia.";
Neuromuscul. Disord. 16:387-390(2006).
[65]
VARIANT [LARGE SCALE ANALYSIS] LEU-423.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[66]
VARIANTS SPG4 THR-364; HIS-380 AND HIS-579, AND VARIANT LEU-44.
PubMed=17594340; DOI=10.1111/j.1468-1331.2007.01861.x;
Erichsen A.K., Inderhaug E., Mattingsdal M., Eiklid K.,
Tallaksen C.M.;
"Seven novel mutations and four exon deletions in a collection of
Norwegian patients with SPG4 hereditary spastic paraplegia.";
Eur. J. Neurol. 14:809-814(2007).
[67]
VARIANTS LEU-44 AND GLY-229, AND VARIANTS SPG4 ILE-162; PHE-426 AND
SER-460.
PubMed=20214791; DOI=10.1186/1471-2377-10-17;
Braschinsky M., Tamm R., Beetz C., Sachez-Ferrero E., Raukas E.,
Luus S.M., Gross-Paju K., Boillot C., Canzian F., Metspalu A.,
Haldre S.;
"Unique spectrum of SPAST variants in Estonian HSP patients: presence
of benign missense changes but lack of exonic rearrangements.";
BMC Neurol. 10:17-17(2010).
[68]
VARIANTS SPG4 THR-287 DEL; LEU-293; LEU-328; ARG-378; HIS-380;
PRO-391; 393-LYS--ALA-396 DEL; THR-409; ARG-410; PRO-436; ASN-441;
SER-460; ALA-463; PHE-492; GLY-498; ARG-503 INS; GLY-514 AND THR-580.
PubMed=20932283; DOI=10.1186/1471-2377-10-89;
Alvarez V., Sanchez-Ferrero E., Beetz C., Diaz M., Alonso B.,
Corao A.I., Gamez J., Esteban J., Gonzalo J.F., Pascual-Pascual S.I.,
Lopez de Munain A., Moris G., Ribacoba R., Marquez C., Rosell J.,
Marin R., Garcia-Barcina M.J., Del Castillo E., Benito C., Coto E.;
"Mutational spectrum of the SPG4 (SPAST) and SPG3A (ATL1) genes in
Spanish patients with hereditary spastic paraplegia.";
BMC Neurol. 10:89-89(2010).
[69]
VARIANTS SPG4 ILE-162; LYS-356; SER-365; ARG-382; ILE-; PHE-422;
ASN-445; SER-460; LEU-482; GLU-512 DEL; VAL-534 AND PRO-562, AND
VARIANT LEU-44.
PubMed=20562464; DOI=10.1136/jnnp.2009.201103;
de Bot S.T., van den Elzen R.T., Mensenkamp A.R., Schelhaas H.J.,
Willemsen M.A., Knoers N.V., Kremer H.P., van de Warrenburg B.P.,
Scheffer H.;
"Hereditary spastic paraplegia due to SPAST mutations in 151 Dutch
patients: new clinical aspects and 27 novel mutations.";
J. Neurol. Neurosurg. Psych. 81:1073-1078(2010).
[70]
VARIANTS SPG4 THR-97; ASP-201; SER-314; VAL-360; ALA-464; GLY-498 AND
ILE-550.
PubMed=20718791; DOI=10.1111/j.1399-0004.2010.01501.x;
McCorquodale D.S. III, Ozomaro U., Huang J., Montenegro G.,
Kushman A., Citrigno L., Price J., Speziani F., Pericak-Vance M.A.,
Zuchner S.;
"Mutation screening of spastin, atlastin, and REEP1 in hereditary
spastic paraplegia.";
Clin. Genet. 79:523-530(2011).
[71]
VARIANTS SPG4 LEU-413 AND LYS-454.
PubMed=20550563; DOI=10.1111/j.1468-1331.2010.03102.x;
Battini R., Fogli A., Borghetti D., Michelucci A., Perazza S.,
Baldinotti F., Conidi M.E., Ferreri M.I., Simi P., Cioni G.;
"Clinical and genetic findings in a series of Italian children with
pure hereditary spastic paraplegia.";
Eur. J. Neurol. 18:150-157(2011).
[72]
VARIANTS SPG4 MET-364; LEU-368; GLU-377 AND SER-450.
PubMed=21546041; DOI=10.1016/j.jns.2011.03.043;
Proukakis C., Moore D., Labrum R., Wood N.W., Houlden H.;
"Detection of novel mutations and review of published data suggests
that hereditary spastic paraplegia caused by spastin (SPAST) mutations
is found more often in males.";
J. Neurol. Sci. 306:62-65(2011).
[73]
VARIANTS SPG4 THR-95; 112-GLU--VAL-616 DEL; 135-GLU--VAL-616 DEL;
LEU-399; ARG-406; THR-409; VAL-426; 431-ARG--VAL-616 DEL; CYS-460;
TRP-503; ARG-559 AND 562-ARG--VAL-616 DEL.
PubMed=22960362; DOI=10.1016/j.neulet.2012.08.036;
Nanetti L., Baratta S., Panzeri M., Tomasello C., Lovati C.,
Azzollini J., Gellera C., Di Bella D., Taroni F., Mariotti C.;
"Novel and recurrent spastin mutations in a large series of SPG4
Italian families.";
Neurosci. Lett. 528:42-45(2012).
[74]
VARIANT SPG4 HIS-309.
PubMed=23279441; DOI=10.1111/ene.12000;
Magariello A., Tortorella C., Patitucci A., Tortelli R., Liguori M.,
Mazzei R., Conforti F.L., Citrigno L., Ungaro C., Simone I.L.,
Muglia M.;
"First mutation in the nuclear localization signal sequence of spastin
protein identified in a patient with hereditary spastic paraplegia.";
Eur. J. Neurol. 20:E22-E23(2013).
[75]
VARIANTS SPG4 244-ASN--VAL-616 DEL; PRO-461; GLY-555 AND
581-ARG--VAL-616 DEL.
PubMed=25421405; DOI=10.1186/s12883-014-0216-x;
Lan M.Y., Chang Y.Y., Yeh T.H., Lai S.C., Liou C.W., Kuo H.C.,
Wu Y.R., Lyu R.K., Hung J.W., Chang Y.C., Lu C.S.;
"High frequency of SPG4 in Taiwanese families with autosomal dominant
hereditary spastic paraplegia.";
BMC Neurol. 14:216-216(2014).
[76]
VARIANTS SPG4 44-SER--VAL-616 DEL; 245-SER--VAL-616 DEL;
254-LYS--VAL-616 DEL; GLY-372; LEU-399; ARG-451 DEL; ARG-458; HIS-499
AND 581-ARG--VAL-616 DEL.
PubMed=25045380; DOI=10.3988/jcn.2014.10.3.257;
Kim T.H., Lee J.H., Park Y.E., Shin J.H., Nam T.S., Kim H.S.,
Jang H.J., Semenov A., Kim S.J., Kim D.S.;
"Mutation analysis of SPAST, ATL1, and REEP1 in Korean Patients with
Hereditary Spastic Paraplegia.";
J. Clin. Neurol. 10:257-261(2014).
[77]
VARIANTS SPG4 PRO-363; LEU-399; VAL-441 AND ARG-595.
PubMed=24824479; DOI=10.1016/j.parkreldis.2014.04.021;
Wei Q.Q., Chen Y., Zheng Z.Z., Chen X., Huang R., Yang Y.,
Burgunder J., Shang H.F.;
"Spastin mutation screening in Chinese patients with pure hereditary
spastic paraplegia.";
Parkinsonism Relat. Disord. 20:845-849(2014).
[78]
VARIANTS SPG4 LYS-328; LYS-366; LEU-368; VAL-368; THR-372; TYR-386;
THR-390; ALA-418; TYR-470; THR-485; MET-498 AND 546-GLY--VAL-616 DEL.
PubMed=28572275; DOI=10.1136/jnnp-2017-315796;
Chelban V., Tucci A., Lynch D.S., Polke J.M., Santos L., Jonvik H.,
Groppa S., Wood N.W., Houlden H.;
"Truncating mutations in SPAST patients are associated with a high
rate of psychiatric comorbidities in hereditary spastic paraplegia.";
J. Neurol. Neurosurg. Psych. 88:681-687(2017).
-!- FUNCTION: ATP-dependent microtubule severing protein that
specifically recognizes and cuts microtubules that are
polyglutamylated (PubMed:11809724, PubMed:15716377,
PubMed:16219033, PubMed:17389232, PubMed:20530212,
PubMed:22637577, PubMed:26875866). 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 (PubMed:26875866). Severing activity is
not dependent on tubulin acetylation or detyrosination
(PubMed:26875866). Microtubule severing promotes reorganization of
cellular microtubule arrays and the release of microtubules from
the centrosome following nucleation. It is critical for the
biogenesis and maintenance of complex microtubule arrays in axons,
spindles and cilia. SPAST is involved in abscission step of
cytokinesis and nuclear envelope reassembly during anaphase in
cooperation with the ESCRT-III complex (PubMed:19000169,
PubMed:21310966, PubMed:26040712). Recruited at the midbody,
probably by IST1, and participates in membrane fission during
abscission together with the ESCRT-III complex (PubMed:21310966).
Recruited to the nuclear membrane by IST1 and mediates microtubule
severing, promoting nuclear envelope sealing and mitotic spindle
disassembly during late anaphase (PubMed:26040712). Required for
membrane traffic from the endoplasmic reticulum (ER) to the Golgi
and endosome recycling (PubMed:23897888). Recruited by IST1 to
endosomes and regulates early endosomal tubulation and recycling
by mediating microtubule severing (PubMed:23897888). Probably
plays a role in axon growth and the formation of axonal branches
(PubMed:15716377). {ECO:0000255|HAMAP-Rule:MF_03021,
ECO:0000269|PubMed:11809724, ECO:0000269|PubMed:15716377,
ECO:0000269|PubMed:16219033, ECO:0000269|PubMed:17389232,
ECO:0000269|PubMed:19000169, ECO:0000269|PubMed:20530212,
ECO:0000269|PubMed:21310966, ECO:0000269|PubMed:22637577,
ECO:0000269|PubMed:23897888, ECO:0000269|PubMed:26040712,
ECO:0000269|PubMed:26875866}.
-!- FUNCTION: Isoform 1: Involved in lipid metabolism by regulating
the size and distribution of lipid droplets.
{ECO:0000269|PubMed:25875445}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:15716377,
ECO:0000269|PubMed:16219033, ECO:0000269|PubMed:16815977,
ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:18410514,
ECO:0000269|PubMed:22637577}.
-!- ENZYME REGULATION: Allosteric enzyme with a cooperative mechanism;
at least two neighbor subunits influence each other strongly in
spastin hexamers (PubMed:22637577). Microtubule binding promotes
cooperative interactions among spastin subunits (PubMed:22637577).
ATP-bound enzyme interacts strongly and cooperatively with
microtubules; this interaction stimulates ATP hydrolysis
(PubMed:23745751). {ECO:0000255|HAMAP-Rule:MF_03021,
ECO:0000269|PubMed:22637577, ECO:0000269|PubMed:23745751}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.45 mM for ATP {ECO:0000269|PubMed:15716377,
ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:22637577};
Vmax=1.2 nmol/min/ug enzyme {ECO:0000269|PubMed:15716377,
ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:22637577};
Note=Kinetic parameters shown are for full-length enzyme. N-
terminally truncated spastin (residues 228-616), which has been
shown to exhibit full severing activity, shows a basal ATP
turnover rate of 0.78 sec(-1) in the absence of microtubules, a
KM of 0.16 mM for ATP, and the ATP turnover rate is extrapolated
to 3.83 sec(-1) in the presence of microtubules. ATPase activity
shows non-Michaelis-Menten kinetics in the presence of
microtubules, but is close to non-cooperative behavior in their
absence (PubMed:22637577). {ECO:0000269|PubMed:22637577};
-!- SUBUNIT: Homohexamer (PubMed:17389232, PubMed:22637577). Mostly
monomeric, but assembles into hexameric structure for short
periods of time. Oligomerization seems to be a prerequisite for
catalytic activity (PubMed:17389232, PubMed:22637577). Binding to
ATP in a cleft between two adjacent subunits stabilizes the
homohexameric form (PubMed:17389232, PubMed:22637577). Binds to
microtubules at least in part via the alpha-tubulin and beta-
tubulin tails (PubMed:15269182, PubMed:15716377, PubMed:23272056).
The hexamer adopts a ring conformation through which microtubules
pass prior to being severed (PubMed:17389232, PubMed:22637577).
Does not interact strongly with tubulin heterodimers
(PubMed:15269182, PubMed:15716377, PubMed:23272056). Interacts
(via MIT domain) with CHMP1B; the interaction is direct
(PubMed:15537668, PubMed:18997780). Interacts with SSNA1
(PubMed:15269182). Interacts with ATL1 (PubMed:16339213,
PubMed:16815977). Interacts with RTN1 (PubMed:16602018). Interacts
with ZFYVE27 (PubMed:16826525, PubMed:23969831). Isoform 1 but not
isoform 3 interacts with RTN2 (PubMed:22232211). Interacts with
REEP1 (PubMed:20200447). Interacts (via MIT domain) with IST1
(PubMed:23897888, PubMed:26040712). {ECO:0000255|HAMAP-
Rule:MF_03021, ECO:0000269|PubMed:15269182,
ECO:0000269|PubMed:15537668, ECO:0000269|PubMed:15716377,
ECO:0000269|PubMed:16339213, ECO:0000269|PubMed:16602018,
ECO:0000269|PubMed:16815977, ECO:0000269|PubMed:16826525,
ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:18997780,
ECO:0000269|PubMed:20200447, ECO:0000269|PubMed:22232211,
ECO:0000269|PubMed:22637577, ECO:0000269|PubMed:23272056,
ECO:0000269|PubMed:23897888, ECO:0000269|PubMed:23969831,
ECO:0000269|PubMed:26040712}.
-!- INTERACTION:
Q8WXF7-1:ATL1; NbExp=4; IntAct=EBI-1222832, EBI-15590227;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021,
ECO:0000269|PubMed:19000169}; Peripheral membrane protein
{ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000305|PubMed:20200447}.
Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03021,
ECO:0000269|PubMed:16602018}. Midbody {ECO:0000255|HAMAP-
Rule:MF_03021, ECO:0000269|PubMed:18997780,
ECO:0000269|PubMed:21310966}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021,
ECO:0000269|PubMed:15891913}. Cytoplasm, cytoskeleton
{ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:15716377,
ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:18410514,
ECO:0000269|PubMed:19000169, ECO:0000269|PubMed:20200447}.
Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03021,
ECO:0000269|PubMed:11809724, ECO:0000269|PubMed:15269182,
ECO:0000269|PubMed:15537668}. Nucleus {ECO:0000255|HAMAP-
Rule:MF_03021, ECO:0000269|PubMed:15147984,
ECO:0000269|PubMed:16026783}. Cytoplasm, cytoskeleton, spindle
{ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:15269182}.
Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03021,
ECO:0000269|PubMed:16026783, ECO:0000269|PubMed:20200447}.
Note=Forms a intramembrane hairpin-like structure in the membrane
(PubMed:20200447). Localization to the centrosome is independent
of microtubules (PubMed:15891913). Localizes to the midbody of
dividing cells, and this requires CHMP1B (PubMed:18997780).
Enriched in the distal axons and branches of postmitotic neurons
(PubMed:15269182). {ECO:0000255|HAMAP-Rule:MF_03021,
ECO:0000269|PubMed:15269182, ECO:0000269|PubMed:15891913,
ECO:0000269|PubMed:18997780, ECO:0000305|PubMed:20200447}.
-!- SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:19000169, ECO:0000269|PubMed:23969831};
Peripheral membrane protein {ECO:0000305|PubMed:20200447}. Nucleus
membrane {ECO:0000269|PubMed:26040712}. Lipid droplet
{ECO:0000269|PubMed:25875445}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:19000169, ECO:0000269|PubMed:20200447}.
Endosome {ECO:0000269|PubMed:23897888}. Note=Forms a intramembrane
hairpin-like structure in the membrane (PubMed:20200447).
Recruited to nuclear membrane by IST1 during late anaphase
(PubMed:26040712). Localizes to endoplasmic reticulum tubular
network (PubMed:23969831). {ECO:0000269|PubMed:23969831,
ECO:0000269|PubMed:26040712, ECO:0000305|PubMed:20200447}.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm
{ECO:0000269|PubMed:20200447, ECO:0000269|PubMed:23969831}.
Endosome {ECO:0000269|PubMed:19000169,
ECO:0000269|PubMed:23897888}. Nucleus membrane
{ECO:0000269|PubMed:16026783, ECO:0000269|PubMed:26040712}.
Note=Constitutes the main endosomal form (PubMed:19000169).
Recruited to nuclear membrane by IST1 during late anaphase
(PubMed:26040712). {ECO:0000269|PubMed:19000169,
ECO:0000269|PubMed:26040712}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing, Alternative initiation; Named isoforms=4;
Comment=Alternative promoter usage of a cryptic promoter in exon
1 can direct the synthesis of N-terminally truncated isoforms,
which may also arise from alternative initiation.
{ECO:0000269|PubMed:16026783, ECO:0000269|PubMed:18613979};
Name=1; Synonyms=Long, Long variant 1, 68 kDa
{ECO:0000303|PubMed:19000169}, M1 {ECO:0000303|PubMed:20200447};
IsoId=Q9UBP0-1; Sequence=Displayed;
Name=2; Synonyms=Long variant 2;
IsoId=Q9UBP0-2; Sequence=VSP_000024;
Name=3; Synonyms=Short, Short variant 1, 60 kDa
{ECO:0000303|PubMed:19000169}, M87 {ECO:0000303|PubMed:20200447};
IsoId=Q9UBP0-3; Sequence=VSP_036650;
Note=Produced by alternative promoter usage. May also be
produced by alternative initiation at Met-87 of isoform 1. Major
isoform.;
Name=4; Synonyms=Short variant 2;
IsoId=Q9UBP0-4; Sequence=VSP_036650, VSP_000024;
Note=Produced by alternative promoter usage and alternative
splicing. May also be produced by alternative initiation at
Met-87 of isoform 2.;
-!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver,
lung, pancreas, placenta and skeletal muscle. The short isoforms
may predominate in brain and spinal cord.
{ECO:0000269|PubMed:10610178}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal brain, heart, kidney,
liver, lung, skeletal muscle, spleen and thymus.
{ECO:0000269|PubMed:10610178}.
-!- DISEASE: Spastic paraplegia 4, autosomal dominant (SPG4)
[MIM:182601]: A form of spastic paraplegia, a neurodegenerative
disorder characterized by a slow, gradual, progressive weakness
and spasticity of the lower limbs. Rate of progression and the
severity of symptoms are quite variable. Initial symptoms may
include difficulty with balance, weakness and stiffness in the
legs, muscle spasms, and dragging the toes when walking. In some
forms of the disorder, bladder symptoms (such as incontinence) may
appear, or the weakness and stiffness may spread to other parts of
the body. {ECO:0000269|PubMed:10610178,
ECO:0000269|PubMed:10699187, ECO:0000269|PubMed:11015453,
ECO:0000269|PubMed:11039577, ECO:0000269|PubMed:11087788,
ECO:0000269|PubMed:11309678, ECO:0000269|PubMed:11809724,
ECO:0000269|PubMed:11843700, ECO:0000269|PubMed:11985387,
ECO:0000269|PubMed:12124993, ECO:0000269|PubMed:12161613,
ECO:0000269|PubMed:12163196, ECO:0000269|PubMed:12202986,
ECO:0000269|PubMed:12460147, ECO:0000269|PubMed:12552568,
ECO:0000269|PubMed:12939659, ECO:0000269|PubMed:14732620,
ECO:0000269|PubMed:15159500, ECO:0000269|PubMed:15210521,
ECO:0000269|PubMed:15248095, ECO:0000269|PubMed:15326248,
ECO:0000269|PubMed:15482961, ECO:0000269|PubMed:15667412,
ECO:0000269|PubMed:15716377, ECO:0000269|PubMed:15891913,
ECO:0000269|PubMed:16339213, ECO:0000269|PubMed:16682546,
ECO:0000269|PubMed:16684598, ECO:0000269|PubMed:17389232,
ECO:0000269|PubMed:17594340, ECO:0000269|PubMed:19000169,
ECO:0000269|PubMed:20214791, ECO:0000269|PubMed:20550563,
ECO:0000269|PubMed:20562464, ECO:0000269|PubMed:20718791,
ECO:0000269|PubMed:20932283, ECO:0000269|PubMed:21546041,
ECO:0000269|PubMed:22960362, ECO:0000269|PubMed:23279441,
ECO:0000269|PubMed:24824479, ECO:0000269|PubMed:25045380,
ECO:0000269|PubMed:25421405, ECO:0000269|PubMed:28572275}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily.
{ECO:0000255|HAMAP-Rule:MF_03021}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The making of crooked
- Issue 104 of April 2009;
URL="https://web.expasy.org/spotlight/back_issues/104";
-----------------------------------------------------------------------
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EMBL; AJ246001; CAB60141.1; -; mRNA.
EMBL; AJ246003; CAB60208.1; -; Genomic_DNA.
EMBL; AB029006; BAA83035.1; -; mRNA.
EMBL; CH471053; EAX00462.1; -; Genomic_DNA.
EMBL; BC150260; AAI50261.1; -; mRNA.
CCDS; CCDS1778.1; -. [Q9UBP0-1]
CCDS; CCDS1779.1; -. [Q9UBP0-2]
RefSeq; NP_055761.2; NM_014946.3. [Q9UBP0-1]
RefSeq; NP_955468.1; NM_199436.1. [Q9UBP0-2]
UniGene; Hs.468091; -.
PDB; 3EAB; X-ray; 2.50 A; A/B/C/D/E/F=112-196.
PDB; 3VFD; X-ray; 3.30 A; A=228-616.
PDBsum; 3EAB; -.
PDBsum; 3VFD; -.
ProteinModelPortal; Q9UBP0; -.
SMR; Q9UBP0; -.
BioGrid; 112562; 29.
CORUM; Q9UBP0; -.
DIP; DIP-38418N; -.
ELM; Q9UBP0; -.
IntAct; Q9UBP0; 14.
STRING; 9606.ENSP00000320885; -.
iPTMnet; Q9UBP0; -.
PhosphoSitePlus; Q9UBP0; -.
BioMuta; SPAST; -.
DMDM; 12230611; -.
EPD; Q9UBP0; -.
PaxDb; Q9UBP0; -.
PeptideAtlas; Q9UBP0; -.
PRIDE; Q9UBP0; -.
Ensembl; ENST00000315285; ENSP00000320885; ENSG00000021574. [Q9UBP0-1]
Ensembl; ENST00000345662; ENSP00000340817; ENSG00000021574. [Q9UBP0-2]
Ensembl; ENST00000615843; ENSP00000480893; ENSG00000021574. [Q9UBP0-1]
Ensembl; ENST00000621856; ENSP00000482496; ENSG00000021574. [Q9UBP0-3]
GeneID; 6683; -.
KEGG; hsa:6683; -.
UCSC; uc002roc.4; human. [Q9UBP0-1]
CTD; 6683; -.
DisGeNET; 6683; -.
EuPathDB; HostDB:ENSG00000021574.11; -.
GeneCards; SPAST; -.
GeneReviews; SPAST; -.
HGNC; HGNC:11233; SPAST.
HPA; HPA017311; -.
MalaCards; SPAST; -.
MIM; 182601; phenotype.
MIM; 604277; gene.
neXtProt; NX_Q9UBP0; -.
OpenTargets; ENSG00000021574; -.
Orphanet; 100985; Autosomal dominant spastic paraplegia type 4.
PharmGKB; PA36063; -.
eggNOG; KOG0740; Eukaryota.
eggNOG; COG0464; LUCA.
GeneTree; ENSGT00570000078874; -.
HOGENOM; HOG000225146; -.
HOVERGEN; HBG108502; -.
InParanoid; Q9UBP0; -.
KO; K13254; -.
OMA; FCIFRYL; -.
OrthoDB; EOG091G0Q8J; -.
PhylomeDB; Q9UBP0; -.
TreeFam; TF105014; -.
BRENDA; 3.6.4.3; 2681.
SABIO-RK; Q9UBP0; -.
ChiTaRS; SPAST; human.
EvolutionaryTrace; Q9UBP0; -.
GeneWiki; Spastin; -.
GenomeRNAi; 6683; -.
PRO; PR:Q9UBP0; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000021574; -.
CleanEx; HS_SPAST; -.
ExpressionAtlas; Q9UBP0; baseline and differential.
Genevisible; Q9UBP0; HS.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:UniProtKB.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IPI:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0008568; F:microtubule-severing ATPase activity; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; TAS:ARUK-UCL.
GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
GO; GO:0019896; P:axonal transport of mitochondrion; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0032506; P:cytokinetic process; IMP:UniProtKB.
GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; TAS:ARUK-UCL.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:UniProtKB.
GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB.
GO; GO:0090148; P:membrane fission; IMP:UniProtKB.
GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
GO; GO:0001578; P:microtubule bundle formation; IDA:UniProtKB.
GO; GO:0051013; P:microtubule severing; IDA:UniProtKB.
GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
GO; GO:0051228; P:mitotic spindle disassembly; IMP:UniProtKB.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0031468; P:nuclear envelope reassembly; IMP:UniProtKB.
GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0034214; P:protein hexamerization; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA: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;
3D-structure; Allosteric enzyme; Alternative initiation;
Alternative promoter usage; Alternative splicing; ATP-binding;
Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton;
Developmental protein; Differentiation; Disease mutation;
Endoplasmic reticulum; Endosome; Hereditary spastic paraplegia;
Hydrolase; Lipid droplet; Membrane; Microtubule; Neurodegeneration;
Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 616 Spastin.
/FTId=PRO_0000084763.
TOPO_DOM 1 56 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_03021,
ECO:0000305|PubMed:20200447}.
INTRAMEM 57 77 Helical. {ECO:0000255|HAMAP-
Rule:MF_03021,
ECO:0000305|PubMed:20200447}.
TOPO_DOM 78 616 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_03021,
ECO:0000305|PubMed:20200447}.
DOMAIN 120 195 MIT. {ECO:0000255}.
NP_BIND 382 389 ATP. {ECO:0000255|HAMAP-Rule:MF_03021,
ECO:0000305|PubMed:15716377}.
REGION 1 300 Required for interaction with RTN1.
{ECO:0000269|PubMed:16602018}.
REGION 1 194 Required for midbody localization.
{ECO:0000269|PubMed:18997780}.
REGION 1 80 Required for interaction with ATL1.
{ECO:0000269|PubMed:16339213,
ECO:0000269|PubMed:16815977}.
REGION 1 50 Required for nuclear localization.
{ECO:0000269|PubMed:15147984}.
REGION 50 87 Required for interaction with SSNA1 and
microtubules.
{ECO:0000269|PubMed:15269182}.
REGION 112 196 Sufficient for interaction with CHMP1B.
{ECO:0000269|PubMed:18997780}.
REGION 114 200 Required for interaction with
microtubules.
{ECO:0000269|PubMed:15269182}.
REGION 228 616 Sufficient for microtubule severing.
{ECO:0000269|PubMed:15269182}.
REGION 270 328 Required for interaction with
microtubules and microtubule severing.
{ECO:0000269|PubMed:15269182}.
REGION 310 312 Required for interaction with
microtubules.
{ECO:0000269|PubMed:23272056}.
MOTIF 4 11 Nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_03021,
ECO:0000269|PubMed:15147984}.
MOTIF 59 67 Nuclear export signal.
{ECO:0000255|HAMAP-Rule:MF_03021,
ECO:0000269|PubMed:16026783}.
MOTIF 309 312 Nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_03021,
ECO:0000269|PubMed:15147984}.
MOD_RES 245 245 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 268 268 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 306 306 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 597 597 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 86 Missing (in isoform 3 and isoform 4).
{ECO:0000305}.
/FTId=VSP_036650.
VAR_SEQ 197 228 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:10470851,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_000024.
VARIANT 44 616 Missing (in SPG4).
{ECO:0000269|PubMed:25045380}.
/FTId=VAR_075827.
VARIANT 44 44 S -> L (rare polymorphism; acts as a
disease modifier; patients carrying a
mutated allele of spastin and L-44 on the
other allele are affected by severe
spastic paraplegia with an early age of
onset; may decrease the activity of the
alternative promoter which directs the
synthesis of isoform 3 and isoform 4;
dbSNP:rs121908515).
{ECO:0000269|PubMed:11015453,
ECO:0000269|PubMed:15248095,
ECO:0000269|PubMed:15326248,
ECO:0000269|PubMed:17594340,
ECO:0000269|PubMed:18613979,
ECO:0000269|PubMed:20214791,
ECO:0000269|PubMed:20562464}.
/FTId=VAR_010194.
VARIANT 45 45 P -> Q (rare polymorphism; acts as a
disease modifier; patients carrying a
mutated allele of spastin and Q-45 on the
other allele are affected by severe
spastic paraplegia with an early age of
onset; dbSNP:rs121908517).
{ECO:0000269|PubMed:15248095}.
/FTId=VAR_027205.
VARIANT 95 95 A -> T (in SPG4).
{ECO:0000269|PubMed:22960362}.
/FTId=VAR_075828.
VARIANT 97 97 P -> T (in SPG4; unknown pathological
significance; dbSNP:rs372005558).
{ECO:0000269|PubMed:20718791}.
/FTId=VAR_067628.
VARIANT 112 616 Missing (in SPG4).
{ECO:0000269|PubMed:22960362}.
/FTId=VAR_075829.
VARIANT 135 616 Missing (in SPG4).
{ECO:0000269|PubMed:22960362}.
/FTId=VAR_075830.
VARIANT 162 162 V -> I (in SPG4; unknown pathological
significance; dbSNP:rs141944844).
{ECO:0000269|PubMed:20214791,
ECO:0000269|PubMed:20562464}.
/FTId=VAR_067563.
VARIANT 195 195 L -> V (in SPG4).
{ECO:0000269|PubMed:16682546}.
/FTId=VAR_026758.
VARIANT 201 201 V -> D (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:20718791}.
/FTId=VAR_067629.
VARIANT 229 229 S -> G. {ECO:0000269|PubMed:20214791}.
/FTId=VAR_067630.
VARIANT 244 616 Missing (in SPG4).
{ECO:0000269|PubMed:25421405}.
/FTId=VAR_075831.
VARIANT 245 616 Missing (in SPG4).
{ECO:0000269|PubMed:25045380}.
/FTId=VAR_075832.
VARIANT 254 616 Missing (in SPG4).
{ECO:0000269|PubMed:25045380}.
/FTId=VAR_075833.
VARIANT 287 287 Missing (in SPG4).
{ECO:0000269|PubMed:20932283}.
/FTId=VAR_067631.
VARIANT 293 293 P -> L (in SPG4; dbSNP:rs773193617).
{ECO:0000269|PubMed:20932283}.
/FTId=VAR_067632.
VARIANT 309 309 R -> H (in SPG4; dbSNP:rs202152835).
{ECO:0000269|PubMed:23279441}.
/FTId=VAR_075834.
VARIANT 314 314 L -> S (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:20718791}.
/FTId=VAR_067633.
VARIANT 328 328 I -> K (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:28572275}.
/FTId=VAR_079314.
VARIANT 328 328 I -> L (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:20932283}.
/FTId=VAR_067634.
VARIANT 344 344 I -> K (in SPG4; abrogates ATPase
activity and promotes microtubule
binding; dbSNP:rs121908513).
{ECO:0000269|PubMed:12202986,
ECO:0000269|PubMed:15716377}.
/FTId=VAR_019448.
VARIANT 347 347 Q -> K (in SPG4; promotes microtubule
binding). {ECO:0000269|PubMed:12161613,
ECO:0000269|PubMed:15716377}.
/FTId=VAR_027206.
VARIANT 356 356 E -> K (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:20562464}.
/FTId=VAR_067564.
VARIANT 360 360 L -> V (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:20718791}.
/FTId=VAR_067635.
VARIANT 361 361 P -> L (in SPG4).
{ECO:0000269|PubMed:15326248}.
/FTId=VAR_027207.
VARIANT 362 362 S -> C (in SPG4; dbSNP:rs121908509).
{ECO:0000269|PubMed:10610178,
ECO:0000269|PubMed:10699187}.
/FTId=VAR_010195.
VARIANT 363 363 L -> P (in SPG4).
{ECO:0000269|PubMed:24824479}.
/FTId=VAR_075835.
VARIANT 364 364 R -> M (in SPG4).
{ECO:0000269|PubMed:21546041}.
/FTId=VAR_075836.
VARIANT 364 364 R -> T (in SPG4).
{ECO:0000269|PubMed:17594340}.
/FTId=VAR_067636.
VARIANT 365 365 P -> S (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:20562464}.
/FTId=VAR_067565.
VARIANT 366 366 E -> K (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:28572275}.
/FTId=VAR_079315.
VARIANT 368 368 F -> L (in SPG4).
{ECO:0000269|PubMed:21546041,
ECO:0000269|PubMed:28572275}.
/FTId=VAR_075837.
VARIANT 368 368 F -> V (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:28572275}.
/FTId=VAR_079316.
VARIANT 370 370 G -> R (in SPG4; promotes microtubule
binding and the formation of thick
microtubule bundles).
{ECO:0000269|PubMed:10699187,
ECO:0000269|PubMed:11809724}.
/FTId=VAR_027208.
VARIANT 372 372 R -> G (in SPG4).
{ECO:0000269|PubMed:25045380}.
/FTId=VAR_075838.
VARIANT 372 372 R -> T (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:28572275}.
/FTId=VAR_079317.
VARIANT 377 377 G -> E (in SPG4).
{ECO:0000269|PubMed:21546041}.
/FTId=VAR_075839.
VARIANT 378 378 L -> Q (in SPG4).
{ECO:0000269|PubMed:14732620}.
/FTId=VAR_019439.
VARIANT 378 378 L -> R (in SPG4).
{ECO:0000269|PubMed:20932283}.
/FTId=VAR_067637.
VARIANT 380 380 L -> H (in SPG4).
{ECO:0000269|PubMed:17594340,
ECO:0000269|PubMed:20932283}.
/FTId=VAR_067638.
VARIANT 381 381 F -> C (in SPG4; promotes microtubule
binding and the formation of thick
microtubule bundles).
{ECO:0000269|PubMed:10699187,
ECO:0000269|PubMed:11809724}.
/FTId=VAR_027209.
VARIANT 382 382 G -> R (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:20562464}.
/FTId=VAR_067566.
VARIANT 386 386 N -> K (in SPG4; abrogates ATPase
activity, promotes microtubule binding
and the formation of thick microtubule
bundles). {ECO:0000269|PubMed:10699187,
ECO:0000269|PubMed:11809724,
ECO:0000269|PubMed:15716377}.
/FTId=VAR_027210.
VARIANT 386 386 N -> S (in SPG4; dbSNP:rs121908514).
{ECO:0000269|PubMed:15210521}.
/FTId=VAR_019440.
VARIANT 386 386 N -> Y (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:28572275}.
/FTId=VAR_079318.
VARIANT 388 388 K -> R (in SPG4; abrogates ATPase
activity, promotes microtubule binding
and the formation of thick microtubule
bundles and impairs traffic from the ER
to Golgi). {ECO:0000269|PubMed:10699187,
ECO:0000269|PubMed:11809724,
ECO:0000269|PubMed:12161613,
ECO:0000269|PubMed:15716377,
ECO:0000269|PubMed:15891913,
ECO:0000269|PubMed:16339213,
ECO:0000269|PubMed:19000169}.
/FTId=VAR_027211.
VARIANT 390 390 M -> T (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:28572275}.
/FTId=VAR_079319.
VARIANT 390 390 M -> V (in SPG4; dbSNP:rs797044850).
{ECO:0000269|PubMed:14732620}.
/FTId=VAR_019441.
VARIANT 391 391 L -> P (in SPG4).
{ECO:0000269|PubMed:20932283}.
/FTId=VAR_067639.
VARIANT 393 396 Missing (in SPG4).
{ECO:0000269|PubMed:20932283}.
/FTId=VAR_067640.
VARIANT 399 399 S -> L (in SPG4).
{ECO:0000269|PubMed:11843700,
ECO:0000269|PubMed:22960362,
ECO:0000269|PubMed:24824479,
ECO:0000269|PubMed:25045380}.
/FTId=VAR_027212.
VARIANT 404 404 Missing (in SPG4).
{ECO:0000269|PubMed:12163196}.
/FTId=VAR_019449.
VARIANT 406 406 I -> R (in SPG4).
{ECO:0000269|PubMed:22960362}.
/FTId=VAR_075840.
VARIANT 406 406 I -> V (in SPG4; dbSNP:rs587777757).
{ECO:0000269|PubMed:16682546}.
/FTId=VAR_026759.
VARIANT 407 407 S -> I (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:20562464}.
/FTId=VAR_067567.
VARIANT 407 407 S -> R (in SPG4).
{ECO:0000269|PubMed:12124993}.
/FTId=VAR_019450.
VARIANT 409 409 A -> T (in SPG4).
{ECO:0000269|PubMed:20932283,
ECO:0000269|PubMed:22960362}.
/FTId=VAR_067641.
VARIANT 410 410 S -> R (in SPG4).
{ECO:0000269|PubMed:20932283}.
/FTId=VAR_067642.
VARIANT 413 413 S -> L (in SPG4).
{ECO:0000269|PubMed:20550563}.
/FTId=VAR_067568.
VARIANT 418 418 E -> A (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:28572275}.
/FTId=VAR_079320.
VARIANT 422 422 L -> F (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:20562464}.
/FTId=VAR_067569.
VARIANT 423 423 V -> L (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035902.
VARIANT 424 424 R -> G (in SPG4).
{ECO:0000269|PubMed:11015453}.
/FTId=VAR_010196.
VARIANT 426 426 L -> F (in SPG4).
{ECO:0000269|PubMed:20214791}.
/FTId=VAR_067643.
VARIANT 426 426 L -> V (in SPG4; promotes microtubule
binding and the formation of thick
microtubule bundles).
{ECO:0000269|PubMed:10699187,
ECO:0000269|PubMed:11809724,
ECO:0000269|PubMed:11843700,
ECO:0000269|PubMed:22960362}.
/FTId=VAR_027213.
VARIANT 431 616 Missing (in SPG4).
{ECO:0000269|PubMed:22960362}.
/FTId=VAR_075841.
VARIANT 435 435 P -> L (in SPG4).
{ECO:0000269|PubMed:16684598}.
/FTId=VAR_027214.
VARIANT 436 436 S -> F (in SPG4).
{ECO:0000269|PubMed:11087788}.
/FTId=VAR_027215.
VARIANT 436 436 S -> P (in SPG4).
{ECO:0000269|PubMed:20932283}.
/FTId=VAR_067644.
VARIANT 441 441 D -> G (in SPG4; dbSNP:rs121908512).
{ECO:0000269|PubMed:11039577}.
/FTId=VAR_027216.
VARIANT 441 441 D -> N (in SPG4).
{ECO:0000269|PubMed:20932283}.
/FTId=VAR_067645.
VARIANT 441 441 D -> V (in SPG4).
{ECO:0000269|PubMed:24824479}.
/FTId=VAR_075842.
VARIANT 445 445 S -> N (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:20562464}.
/FTId=VAR_067570.
VARIANT 448 448 C -> Y (in SPG4; abrogates binding to the
tail of beta-3-tubulin, abolishes
microtubule severing and promotes the
formation of thick microtubule bundles;
dbSNP:rs121908510).
{ECO:0000269|PubMed:10610178,
ECO:0000269|PubMed:10699187,
ECO:0000269|PubMed:11809724,
ECO:0000269|PubMed:17389232}.
/FTId=VAR_010197.
VARIANT 450 450 R -> S (in SPG4).
{ECO:0000269|PubMed:21546041}.
/FTId=VAR_075843.
VARIANT 451 451 Missing (in SPG4).
{ECO:0000269|PubMed:25045380}.
/FTId=VAR_075844.
VARIANT 454 454 E -> K (in SPG4).
{ECO:0000269|PubMed:20550563}.
/FTId=VAR_067571.
VARIANT 458 458 S -> R (in SPG4).
{ECO:0000269|PubMed:25045380}.
/FTId=VAR_075845.
VARIANT 459 459 R -> G (in SPG4).
{ECO:0000269|PubMed:15482961}.
/FTId=VAR_027217.
VARIANT 460 460 R -> C (in SPG4; dbSNP:rs878854990).
{ECO:0000269|PubMed:15482961,
ECO:0000269|PubMed:22960362}.
/FTId=VAR_027218.
VARIANT 460 460 R -> L (in SPG4; promotes microtubule
binding and the formation of thick
microtubule bundles).
{ECO:0000269|PubMed:10699187,
ECO:0000269|PubMed:11809724}.
/FTId=VAR_027219.
VARIANT 460 460 R -> S (in SPG4).
{ECO:0000269|PubMed:20214791,
ECO:0000269|PubMed:20562464,
ECO:0000269|PubMed:20932283}.
/FTId=VAR_067572.
VARIANT 461 461 L -> P (in SPG4).
{ECO:0000269|PubMed:25421405}.
/FTId=VAR_075846.
VARIANT 463 463 T -> A (in SPG4).
{ECO:0000269|PubMed:20932283}.
/FTId=VAR_067646.
VARIANT 464 464 E -> A (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:20718791}.
/FTId=VAR_067647.
VARIANT 470 470 D -> V (in SPG4; dbSNP:rs28939368).
{ECO:0000269|PubMed:15248095}.
/FTId=VAR_027220.
VARIANT 470 470 D -> Y (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:28572275}.
/FTId=VAR_079321.
VARIANT 482 482 V -> L (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:20562464}.
/FTId=VAR_067573.
VARIANT 485 485 A -> T (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:28572275}.
/FTId=VAR_079322.
VARIANT 485 485 A -> V (in SPG4).
{ECO:0000269|PubMed:12460147}.
/FTId=VAR_027221.
VARIANT 489 489 P -> L (in SPG4).
{ECO:0000269|PubMed:11843700}.
/FTId=VAR_027222.
VARIANT 490 616 Missing (in SPG4).
{ECO:0000269|PubMed:15667412}.
/FTId=VAR_075847.
VARIANT 492 492 L -> F (in SPG4).
{ECO:0000269|PubMed:20932283}.
/FTId=VAR_067648.
VARIANT 493 493 D -> G (in SPG4).
{ECO:0000269|PubMed:16682546}.
/FTId=VAR_026760.
VARIANT 498 498 R -> G (in SPG4).
{ECO:0000269|PubMed:20718791,
ECO:0000269|PubMed:20932283}.
/FTId=VAR_067649.
VARIANT 498 498 R -> M (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:28572275}.
/FTId=VAR_079323.
VARIANT 499 499 R -> C (in SPG4; abrogates ATPase
activity, promotes microtubule binding
and the formation of thick microtubule
bundles; dbSNP:rs121908511).
{ECO:0000269|PubMed:10610178,
ECO:0000269|PubMed:10699187,
ECO:0000269|PubMed:11309678,
ECO:0000269|PubMed:11809724,
ECO:0000269|PubMed:12161613,
ECO:0000269|PubMed:15716377}.
/FTId=VAR_010198.
VARIANT 499 499 R -> H (in SPG4; dbSNP:rs878854991).
{ECO:0000269|PubMed:16682546,
ECO:0000269|PubMed:25045380}.
/FTId=VAR_026761.
VARIANT 503 503 R -> L (in SPG4).
{ECO:0000269|PubMed:12552568}.
/FTId=VAR_019442.
VARIANT 503 503 R -> RR (in SPG4).
{ECO:0000269|PubMed:20932283}.
/FTId=VAR_067650.
VARIANT 503 503 R -> W (in SPG4; dbSNP:rs864622162).
{ECO:0000269|PubMed:16682546,
ECO:0000269|PubMed:22960362}.
/FTId=VAR_026762.
VARIANT 512 512 E -> D (in SPG4).
{ECO:0000269|PubMed:11985387}.
/FTId=VAR_027223.
VARIANT 512 512 Missing (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:20562464}.
/FTId=VAR_067574.
VARIANT 514 514 R -> G (in SPG4).
{ECO:0000269|PubMed:20932283}.
/FTId=VAR_067651.
VARIANT 515 515 Missing (in SPG4).
{ECO:0000269|PubMed:14732620}.
/FTId=VAR_019443.
VARIANT 534 534 L -> P (in SPG4).
{ECO:0000269|PubMed:12939659}.
/FTId=VAR_019444.
VARIANT 534 534 L -> V (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:20562464}.
/FTId=VAR_067575.
VARIANT 546 616 Missing (in SPG4).
{ECO:0000269|PubMed:28572275}.
/FTId=VAR_079324.
VARIANT 550 550 T -> I (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:20718791}.
/FTId=VAR_067652.
VARIANT 551 551 A -> Y (in SPG4; requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:12124993}.
/FTId=VAR_019451.
VARIANT 555 555 D -> G (in SPG4).
{ECO:0000269|PubMed:25421405}.
/FTId=VAR_075848.
VARIANT 555 555 D -> N (in SPG4).
{ECO:0000269|PubMed:10699187}.
/FTId=VAR_027224.
VARIANT 556 556 A -> V (in SPG4; promotes microtubule
binding and the formation of thick
microtubule bundles).
{ECO:0000269|PubMed:10699187,
ECO:0000269|PubMed:11809724}.
/FTId=VAR_027225.
VARIANT 559 559 G -> D (in SPG4; dbSNP:rs864622179).
{ECO:0000269|PubMed:11087788,
ECO:0000269|PubMed:11843700}.
/FTId=VAR_027226.
VARIANT 559 559 G -> R (in SPG4; dbSNP:rs878854992).
{ECO:0000269|PubMed:22960362}.
/FTId=VAR_075849.
VARIANT 562 616 Missing (in SPG4).
{ECO:0000269|PubMed:22960362}.
/FTId=VAR_075850.
VARIANT 562 562 R -> G (in SPG4; dbSNP:rs121908518).
{ECO:0000269|PubMed:11309678,
ECO:0000269|PubMed:15248095}.
/FTId=VAR_027227.
VARIANT 562 562 R -> P (in SPG4; unknown pathological
significance).
{ECO:0000269|PubMed:20562464}.
/FTId=VAR_067576.
VARIANT 562 562 R -> Q (in SPG4; dbSNP:rs863224923).
{ECO:0000269|PubMed:11843700}.
/FTId=VAR_027228.
VARIANT 579 579 N -> H (in SPG4; unknown pathological
significance; dbSNP:rs144594804).
{ECO:0000269|PubMed:17594340}.
/FTId=VAR_067653.
VARIANT 580 580 I -> T (in SPG4).
{ECO:0000269|PubMed:20932283}.
/FTId=VAR_067654.
VARIANT 581 616 Missing (in SPG4).
{ECO:0000269|PubMed:25045380,
ECO:0000269|PubMed:25421405}.
/FTId=VAR_075851.
VARIANT 584 584 D -> H (in SPG4).
{ECO:0000269|PubMed:11015453}.
/FTId=VAR_010199.
VARIANT 595 595 S -> R (in SPG4).
{ECO:0000269|PubMed:24824479}.
/FTId=VAR_075852.
VARIANT 607 607 W -> C (in SPG4).
{ECO:0000269|PubMed:16682546}.
/FTId=VAR_026763.
VARIANT 614 614 T -> I (in SPG4; variant form with
congenital arachnoid cysts).
{ECO:0000269|PubMed:15159500}.
/FTId=VAR_019445.
VARIANT 615 615 T -> I (in SPG4).
{ECO:0000269|PubMed:12124993}.
/FTId=VAR_019452.
MUTAGEN 1 1 M->V: Cytoplasmic and nuclear.
{ECO:0000269|PubMed:16026783}.
MUTAGEN 65 65 R->G: Abolishes localization to lipid
droplets. {ECO:0000269|PubMed:25875445}.
MUTAGEN 81 84 RFSR->GFSG: Does not affect localization
to lipid droplets.
{ECO:0000269|PubMed:25875445}.
MUTAGEN 87 87 M->V: Exclusively cytoplasmic.
{ECO:0000269|PubMed:16026783}.
MUTAGEN 120 120 H->D: Impairs binding to CHMP1B. Impairs
midbody localization; when associated
with D-124.
{ECO:0000269|PubMed:18997780}.
MUTAGEN 124 124 F->A: Impairs binding to CHMP1B.
{ECO:0000269|PubMed:18997780}.
MUTAGEN 124 124 F->D: Impairs binding to CHMP1B. Impairs
midbody localization; when associated
with D-120.
{ECO:0000269|PubMed:18997780}.
MUTAGEN 310 312 KKK->QQQ: Loss of microtubule-binding.
{ECO:0000269|PubMed:23272056}.
MUTAGEN 388 388 K->A: Abrogates ATPase activity and
abolishes microtubule severing.
{ECO:0000269|PubMed:15716377}.
MUTAGEN 415 415 Y->A: Abrogates binding to the tail of
alpha-tubulin and beta-3-tubulin, impairs
ATPase activity and abolishes microtubule
severing. {ECO:0000269|PubMed:17389232}.
MUTAGEN 442 442 E->Q: Abrogates ATP hydrolysis, abolishes
microtubule severing, stabilizes the
homohexameric form, and promotes
microtubule binding and redistribution
from the endosome to microtubules.
{ECO:0000269|PubMed:15716377,
ECO:0000269|PubMed:16815977,
ECO:0000269|PubMed:17389232,
ECO:0000269|PubMed:18410514,
ECO:0000269|PubMed:22446388,
ECO:0000269|PubMed:22637577,
ECO:0000269|PubMed:23272056,
ECO:0000269|PubMed:23745751}.
MUTAGEN 448 448 C->A,G: Abolishes ATPase activity.
{ECO:0000269|PubMed:23745751}.
MUTAGEN 448 448 C->S: Does not affect ATPase activity.
{ECO:0000269|PubMed:23745751}.
MUTAGEN 451 451 R->G: Abrogates binding to the tail of
alpha-tubulin and beta-3-tubulin, impairs
ATPase activity and abolishes microtubule
severing. {ECO:0000269|PubMed:17389232}.
MUTAGEN 457 457 A->E: Abrogates binding to the tail of
alpha-tubulin and beta-3-tubulin and
abolishes microtubule severing.
{ECO:0000269|PubMed:17389232}.
HELIX 112 136 {ECO:0000244|PDB:3EAB}.
STRAND 139 141 {ECO:0000244|PDB:3EAB}.
HELIX 142 144 {ECO:0000244|PDB:3EAB}.
HELIX 146 161 {ECO:0000244|PDB:3EAB}.
HELIX 169 195 {ECO:0000244|PDB:3EAB}.
HELIX 328 330 {ECO:0000244|PDB:3VFD}.
HELIX 341 343 {ECO:0000244|PDB:3VFD}.
HELIX 348 357 {ECO:0000244|PDB:3VFD}.
HELIX 359 363 {ECO:0000244|PDB:3VFD}.
TURN 365 367 {ECO:0000244|PDB:3VFD}.
HELIX 370 372 {ECO:0000244|PDB:3VFD}.
STRAND 376 383 {ECO:0000244|PDB:3VFD}.
HELIX 388 398 {ECO:0000244|PDB:3VFD}.
STRAND 402 406 {ECO:0000244|PDB:3VFD}.
HELIX 420 432 {ECO:0000244|PDB:3VFD}.
STRAND 433 441 {ECO:0000244|PDB:3VFD}.
HELIX 443 446 {ECO:0000244|PDB:3VFD}.
HELIX 458 472 {ECO:0000244|PDB:3VFD}.
STRAND 480 487 {ECO:0000244|PDB:3VFD}.
HELIX 489 491 {ECO:0000244|PDB:3VFD}.
HELIX 494 497 {ECO:0000244|PDB:3VFD}.
STRAND 502 505 {ECO:0000244|PDB:3VFD}.
HELIX 511 522 {ECO:0000244|PDB:3VFD}.
HELIX 531 540 {ECO:0000244|PDB:3VFD}.
TURN 541 543 {ECO:0000244|PDB:3VFD}.
HELIX 546 556 {ECO:0000244|PDB:3VFD}.
HELIX 559 562 {ECO:0000244|PDB:3VFD}.
STRAND 573 575 {ECO:0000244|PDB:3VFD}.
HELIX 582 591 {ECO:0000244|PDB:3VFD}.
HELIX 598 610 {ECO:0000244|PDB:3VFD}.
SEQUENCE 616 AA; 67197 MW; 75E5FC5787132B4C CRC64;
MNSPGGRGKK KGSGGASNPV PPRPPPPCLA PAPPAAGPAP PPESPHKRNL YYFSYPLFVG
FALLRLVAFH LGLLFVWLCQ RFSRALMAAK RSSGAAPAPA SASAPAPVPG GEAERVRVFH
KQAFEYISIA LRIDEDEKAG QKEQAVEWYK KGIEELEKGI AVIVTGQGEQ CERARRLQAK
MMTNLVMAKD RLQLLEKMQP VLPFSKSQTD VYNDSTNLAC RNGHLQSESG AVPKRKDPLT
HTSNSLPRSK TVMKTGSAGL SGHHRAPSYS GLSMVSGVKQ GSGPAPTTHK GTPKTNRTNK
PSTPTTATRK KKDLKNFRNV DSNLANLIMN EIVDNGTAVK FDDIAGQDLA KQALQEIVIL
PSLRPELFTG LRAPARGLLL FGPPGNGKTM LAKAVAAESN ATFFNISAAS LTSKYVGEGE
KLVRALFAVA RELQPSIIFI DEVDSLLCER REGEHDASRR LKTEFLIEFD GVQSAGDDRV
LVMGATNRPQ ELDEAVLRRF IKRVYVSLPN EETRLLLLKN LLCKQGSPLT QKELAQLARM
TDGYSGSDLT ALAKDAALGP IRELKPEQVK NMSASEMRNI RLSDFTESLK KIKRSVSPQT
LEAYIRWNKD FGDTTV


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