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Spastin (EC 3.6.4.3)

 G3VXV2_SARHA            Unreviewed;       522 AA.
G3VXV2;
16-NOV-2011, integrated into UniProtKB/TrEMBL.
16-NOV-2011, sequence version 1.
28-MAR-2018, entry version 42.
RecName: Full=Spastin {ECO:0000256|HAMAP-Rule:MF_03021};
EC=3.6.4.3 {ECO:0000256|HAMAP-Rule:MF_03021};
Name=SPAST {ECO:0000256|HAMAP-Rule:MF_03021,
ECO:0000313|Ensembl:ENSSHAP00000008007};
Synonyms=SPG4 {ECO:0000256|HAMAP-Rule:MF_03021};
Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000008007, ECO:0000313|Proteomes:UP000007648};
[1] {ECO:0000313|Ensembl:ENSSHAP00000008007}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=21709235; DOI=10.1073/pnas.1102838108;
Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E.,
Miller J., Walenz B., Knight J., Qi J., Zhao F., Wang Q.,
Bedoya-Reina O.C., Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A.,
Woodbridge P., Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S.,
Helgen K.M., Lesk A.M., Pringle T.H., Patterson N., Zhang Y.,
Kreiss A., Woods G.M., Jones M.E., Schuster S.C.;
"Genetic diversity and population structure of the endangered
marsupial Sarcophilus harrisii (Tasmanian devil).";
Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
[2] {ECO:0000313|Ensembl:ENSSHAP00000008007}
IDENTIFICATION.
Ensembl;
Submitted (SEP-2011) to UniProtKB.
-!- 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}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000256|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:0000256|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: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.
{ECO:0000256|HAMAP-Rule:MF_03021}.
-!- SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily.
{ECO:0000256|HAMAP-Rule:MF_03021}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03021}.
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EMBL; AEFK01025423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AEFK01025424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AEFK01025425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AEFK01025426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AEFK01025427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
STRING; 9305.ENSSHAP00000008007; -.
Ensembl; ENSSHAT00000008071; ENSSHAP00000008007; ENSSHAG00000006946.
eggNOG; KOG0740; Eukaryota.
eggNOG; COG0464; LUCA.
GeneTree; ENSGT00570000078874; -.
InParanoid; G3VXV2; -.
OMA; SEMRNIK; -.
OrthoDB; EOG091G0Q8J; -.
TreeFam; TF105014; -.
Proteomes; UP000007648; Unassembled WGS sequence.
GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0031965; C:nuclear membrane; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
GO; GO:0008017; F:microtubule binding; IEA:UniProtKB-UniRule.
GO; GO:0008568; F:microtubule-severing ATPase activity; IEA:UniProtKB-UniRule.
GO; GO:0007409; P:axonogenesis; IEA:UniProtKB-UniRule.
GO; GO:0032506; P:cytokinetic process; IEA:UniProtKB-UniRule.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IEA:UniProtKB-UniRule.
GO; GO:0010458; P:exit from mitosis; IEA:Ensembl.
GO; GO:0090148; P:membrane fission; IEA:Ensembl.
GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
GO; GO:0001578; P:microtubule bundle formation; IEA:Ensembl.
GO; GO:0000281; P:mitotic cytokinesis; IEA:Ensembl.
GO; GO:0051228; P:mitotic spindle disassembly; IEA:Ensembl.
GO; GO:0031468; P:nuclear envelope reassembly; IEA:Ensembl.
GO; GO:0032467; P:positive regulation of cytokinesis; IEA:Ensembl.
GO; GO:0031117; P:positive regulation of microtubule depolymerization; IEA:UniProtKB-UniRule.
GO; GO:0034214; P:protein hexamerization; IEA:UniProtKB-UniRule.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
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; IPR015415; Vps4_C.
Pfam; PF00004; AAA; 1.
Pfam; PF09336; Vps4_C; 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};
Complete proteome {ECO:0000313|Proteomes:UP000007648};
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};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_03021};
Membrane {ECO:0000256|HAMAP-Rule:MF_03021};
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};
Reference proteome {ECO:0000313|Proteomes:UP000007648}.
TOPO_DOM 1 12 Cytoplasmic. {ECO:0000256|HAMAP-
Rule:MF_03021}.
TOPO_DOM 12 522 Cytoplasmic. {ECO:0000256|HAMAP-
Rule:MF_03021}.
DOMAIN 22 100 MIT. {ECO:0000259|SMART:SM00745}.
DOMAIN 280 416 AAA. {ECO:0000259|SMART:SM00382}.
NP_BIND 288 295 ATP. {ECO:0000256|HAMAP-Rule:MF_03021}.
MOTIF 4 11 Nuclear localization signal.
{ECO:0000256|HAMAP-Rule:MF_03021}.
MOTIF 215 218 Nuclear localization signal.
{ECO:0000256|HAMAP-Rule:MF_03021}.
SEQUENCE 522 AA; 57414 MW; 04AEA23DD432E01F CRC64;
APRPAPSLAP QPVPAGGEAE RVRAFHKQAF EYISFALRID EDEKAGQKDQ AVEWYKKGIE
ELEKGIAVVV SGQGDQCDRA RRLQAKMMTN LVMAKDRLQL LEKLQPVLQF PKSQTDVYND
TTNLTCRNGH LQSESGAVPK RKDPLTHTSN SLPRSKAVAK TASTGLSGHH RAPSCSGLSM
LSSARQGTVP ATTSHKGTPK TNRTNKPSTP MTAARKKKDL KNFRNVDSNL ANLIMNEIVD
NGTAVKFDDI AGQELAKQAL QEIVILPSLR PELFTGLRAP ARGLLLFGPP GNGKTMLAKA
VAAESNATFF NISAASLTSK YVGEGEKLVR ALFAVARELQ PSIIFIDEVD SLLCERREGE
HDASRRLKTE FLIEFDGVQS AGDDRVLVMG ATNRPQELDE AVLRRFIKRV YVSLPNEETR
LLLLKNLLSK QGSPLTQKEL AQLARMTEGY SGSDLTALAK DAALGPIREL KPEQVKNMSA
SEMRNIRLSD FTESLKKIKR SVSPQTLEAY IRWNKDFGDT TV


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