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Spastin (EC

 E5KRP5_HUMAN            Unreviewed;       616 AA.
08-FEB-2011, integrated into UniProtKB/TrEMBL.
08-FEB-2011, sequence version 1.
16-JAN-2019, entry version 71.
RecName: Full=Spastin {ECO:0000256|HAMAP-Rule:MF_03021};
EC= {ECO:0000256|HAMAP-Rule:MF_03021};
Name=SPAST {ECO:0000256|HAMAP-Rule:MF_03021,
Synonyms=SPG4 {ECO:0000256|HAMAP-Rule:MF_03021};
ORFNames=hCG_23080 {ECO:0000313|EMBL:EAX00461.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000313|EMBL:ADP91574.1};
[1] {ECO:0000313|EMBL:EAX00461.1}
PubMed=11181995; DOI=10.1126/science.1058040;
Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D.,
Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q.,
Kodira C.D., Zheng X.H., Chen L., Skupski M., Subramanian G.,
Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S.,
Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J.,
Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R.,
Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A.,
Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K.,
Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V.,
Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z.,
Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A.,
Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V.,
Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B.,
Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J.,
Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C.,
Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L.,
Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S.,
Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A.,
Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D.,
Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L.,
Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N.,
Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S.,
Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F.,
Kline L., Koduru S., Love A., Mann F., May D., McCawley S.,
McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K.,
Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N.,
Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M.,
Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F.,
Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A.,
Mi H., Lazareva B., Hatton T., Narechania A., Diemer K.,
Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R.,
Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J.,
Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H.,
Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D.,
Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A.,
Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S.,
Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L.,
Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W.,
McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M.,
Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
"The sequence of the human genome.";
Science 291:1304-1351(2001).
[2] {ECO:0000313|EMBL:EAX00461.1}
Mural R.J., Istrail S., Sutton 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.
[3] {ECO:0000313|EMBL:ADP91574.1}
PubMed=20843780; DOI=10.1093/nar/gkq750;
Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R.,
Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W.,
Mindrinos M., Speed T.P., Scharfe C.;
"Identification of rare DNA variants in mitochondrial disorders with
improved array-based sequencing.";
Nucleic Acids Res. 39:44-58(2011).
-!- FUNCTION: ATP-dependent microtubule severing protein that
specifically recognizes and cuts microtubules that are
polyglutamylated. 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. Severing activity is not dependent on tubulin
acetylation or detyrosination. 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.
Recruited at the midbody, probably by IST1, and participates in
membrane fission during abscission together with the ESCRT-III
complex. Recruited to the nuclear membrane by IST1 and mediates
microtubule severing, promoting nuclear envelope sealing and
mitotic spindle disassembly during late anaphase. Required for
membrane traffic from the endoplasmic reticulum (ER) to the Golgi
and endosome recycling. Recruited by IST1 to endosomes and
regulates early endosomal tubulation and recycling by mediating
microtubule severing. Probably plays a role in axon growth and the
formation of axonal branches. {ECO:0000256|HAMAP-Rule:MF_03021}.
Reaction=n ATP + n H(2)O + a microtubule = n ADP + n phosphate +
(n+1) alpha/beta tubulin heterodimers.; EC=;
-!- ACTIVITY 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.
-!- 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:0000256|HAMAP-Rule:MF_03021}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|HAMAP-Rule:MF_03021};
Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03021}.
Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03021}. Midbody
{ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome {ECO:0000256|HAMAP-
Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-
Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000256|HAMAP-
Rule:MF_03021}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03021}.
Cytoplasm, cytoskeleton, spindle {ECO:0000256|HAMAP-
Rule:MF_03021}. Cytoplasm {ECO:0000256|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. Enriched in the distal axons and branches of postmitotic
neurons. Localizes to endoplasmic reticulum tubular network.
-!- SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; HQ205746; ADP91574.1; -; Genomic_DNA.
EMBL; HQ205747; ADP91576.1; -; Genomic_DNA.
EMBL; HQ205748; ADP91578.1; -; Genomic_DNA.
EMBL; HQ205749; ADP91580.1; -; Genomic_DNA.
EMBL; HQ205750; ADP91582.1; -; Genomic_DNA.
EMBL; HQ205751; ADP91584.1; -; Genomic_DNA.
EMBL; HQ205752; ADP91586.1; -; Genomic_DNA.
EMBL; HQ205753; ADP91588.1; -; Genomic_DNA.
EMBL; HQ205754; ADP91590.1; -; Genomic_DNA.
EMBL; HQ205755; ADP91592.1; -; Genomic_DNA.
EMBL; HQ205756; ADP91594.1; -; Genomic_DNA.
EMBL; HQ205757; ADP91596.1; -; Genomic_DNA.
EMBL; HQ205758; ADP91598.1; -; Genomic_DNA.
EMBL; HQ205759; ADP91600.1; -; Genomic_DNA.
EMBL; HQ205760; ADP91602.1; -; Genomic_DNA.
EMBL; HQ205761; ADP91604.1; -; Genomic_DNA.
EMBL; HQ205762; ADP91606.1; -; Genomic_DNA.
EMBL; HQ205763; ADP91608.1; -; Genomic_DNA.
EMBL; HQ205764; ADP91610.1; -; Genomic_DNA.
EMBL; HQ205765; ADP91612.1; -; Genomic_DNA.
EMBL; HQ205766; ADP91614.1; -; Genomic_DNA.
EMBL; HQ205767; ADP91616.1; -; Genomic_DNA.
EMBL; HQ205768; ADP91618.1; -; Genomic_DNA.
EMBL; HQ205769; ADP91620.1; -; Genomic_DNA.
EMBL; HQ205770; ADP91622.1; -; Genomic_DNA.
EMBL; HQ205771; ADP91624.1; -; Genomic_DNA.
EMBL; HQ205772; ADP91626.1; -; Genomic_DNA.
EMBL; HQ205773; ADP91628.1; -; Genomic_DNA.
EMBL; HQ205774; ADP91630.1; -; Genomic_DNA.
EMBL; HQ205775; ADP91632.1; -; Genomic_DNA.
EMBL; HQ205776; ADP91634.1; -; Genomic_DNA.
EMBL; HQ205777; ADP91636.1; -; Genomic_DNA.
EMBL; HQ205778; ADP91638.1; -; Genomic_DNA.
EMBL; HQ205779; ADP91640.1; -; Genomic_DNA.
EMBL; HQ205780; ADP91642.1; -; Genomic_DNA.
EMBL; HQ205781; ADP91644.1; -; Genomic_DNA.
EMBL; HQ205782; ADP91646.1; -; Genomic_DNA.
EMBL; HQ205783; ADP91648.1; -; Genomic_DNA.
EMBL; HQ205784; ADP91650.1; -; Genomic_DNA.
EMBL; HQ205785; ADP91652.1; -; Genomic_DNA.
EMBL; CH471053; EAX00461.1; -; Genomic_DNA.
RefSeq; NP_055761.2; NM_014946.3.
UniGene; Hs.468091; -.
SMR; E5KRP5; -.
GeneID; 6683; -.
KEGG; hsa:6683; -.
CTD; 6683; -.
EuPathDB; HostDB:ENSG00000021574.11; -.
eggNOG; KOG0740; Eukaryota.
eggNOG; COG0464; LUCA.
KO; K13254; -.
OrthoDB; 1176820at2759; -.
ChiTaRS; SPAST; human.
GenomeRNAi; 6683; -.
Bgee; ENSG00000021574; Expressed in 219 organ(s), highest expression level in cerebral cortex.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IEA:UniProtKB-UniRule.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule.
GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0008017; F:microtubule binding; IEA:UniProtKB-UniRule.
GO; GO:0008568; F:microtubule-severing ATPase activity; IEA:UniProtKB-UniRule.
GO; GO:0008089; P:anterograde axonal transport; IEA:Ensembl.
GO; GO:0019896; P:axonal transport of mitochondrion; IEA:Ensembl.
GO; GO:0007409; P:axonogenesis; IEA:UniProtKB-UniRule.
GO; GO:0032506; P:cytokinetic process; IEA:UniProtKB-UniRule.
GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:UniProtKB-UniRule.
GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
GO; GO:0031117; P:positive regulation of microtubule depolymerization; IEA:UniProtKB-UniRule.
GO; GO:0034214; P:protein hexamerization; IEA:UniProtKB-UniRule.
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.
3: Inferred from homology;
Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03021};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03021,
ECO:0000256|RuleBase:RU003651, ECO:0000256|SAAS:SAAS00552105};
Cell cycle {ECO:0000256|HAMAP-Rule:MF_03021};
Cell division {ECO:0000256|HAMAP-Rule:MF_03021};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03021};
Cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03021};
Developmental protein {ECO:0000256|HAMAP-Rule:MF_03021};
Differentiation {ECO:0000256|HAMAP-Rule:MF_03021};
Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03021};
Isomerase {ECO:0000256|HAMAP-Rule:MF_03021};
Membrane {ECO:0000256|SAM:Phobius};
Microtubule {ECO:0000256|HAMAP-Rule:MF_03021};
Neurogenesis {ECO:0000256|HAMAP-Rule:MF_03021};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03021,
ECO:0000256|RuleBase:RU003651, ECO:0000256|SAAS:SAAS00552105};
Nucleus {ECO:0000256|HAMAP-Rule:MF_03021};
Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius}.
TOPO_DOM 1 56 Cytoplasmic. {ECO:0000256|HAMAP-
TRANSMEM 57 78 Helical. {ECO:0000256|SAM:Phobius}.
INTRAMEM 57 77 Helical. {ECO:0000256|HAMAP-
TOPO_DOM 78 616 Cytoplasmic. {ECO:0000256|HAMAP-
DOMAIN 116 194 MIT. {ECO:0000259|SMART:SM00745}.
DOMAIN 374 510 AAA. {ECO:0000259|SMART:SM00382}.
NP_BIND 382 389 ATP. {ECO:0000256|HAMAP-Rule:MF_03021}.
MOTIF 4 11 Nuclear localization signal.
MOTIF 59 67 Nuclear export signal.
MOTIF 309 312 Nuclear localization signal.
SEQUENCE 616 AA; 67197 MW; 75E5FC5787132B4C CRC64;

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