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Spastin (EC 3.6.4.3)

 SPAST_BOVIN             Reviewed;         614 AA.
A2VDN5;
24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 1.
10-OCT-2018, entry version 93.
RecName: Full=Spastin {ECO:0000255|HAMAP-Rule:MF_03021};
EC=3.6.4.3 {ECO:0000255|HAMAP-Rule:MF_03021};
Name=SPAST {ECO:0000255|HAMAP-Rule:MF_03021};
Synonyms=SPG4 {ECO:0000255|HAMAP-Rule:MF_03021};
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Brain cortex;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[2]
INVOLVEMENT IN BSD, AND VARIANT BSD GLN-560.
PubMed=19714378; DOI=10.1007/s10048-009-0214-0;
Thomsen B., Nissen P.H., Agerholm J.S., Bendixen C.;
"Congenital bovine spinal dysmyelination is caused by a missense
mutation in the SPAST gene.";
Neurogenetics 11:175-183(2010).
-!- 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:0000255|HAMAP-Rule:MF_03021}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000255|HAMAP-Rule:MF_03021}.
-!- 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.
{ECO:0000255|HAMAP-Rule:MF_03021}.
-!- SUBUNIT: Homohexamer. Mostly monomeric, but assembles into
hexameric structure for short periods of time. Oligomerization
seems to be a prerequisite for catalytic activity. Binding to ATP
in a cleft between two adjacent subunits stabilizes the
homohexameric form. Binds to microtubules at least in part via the
alpha-tubulin and beta-tubulin tails. The hexamer adopts a ring
conformation through which microtubules pass prior to being
severed. Does not interact strongly with tubulin heterodimers.
Interacts (via MIT domain) with CHMP1B; the interaction is direct.
Interacts with SSNA1. Interacts with ATL1. Interacts with RTN1.
Interacts with ZFYVE27. Interacts with REEP1. Interacts (via MIT
domain) with IST1. {ECO:0000255|HAMAP-Rule:MF_03021}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021};
Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}.
Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03021}. Midbody
{ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome {ECO:0000255|HAMAP-
Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-
Rule:MF_03021}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03021}.
Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-
Rule:MF_03021}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03021}.
Note=Forms a intramembrane hairpin-like structure in the membrane.
Localization to the centrosome is independent of microtubules.
Localizes to the midbody of dividing cells, and this requires
CHMP1B. Enriched in the distal axons and branches of postmitotic
neurons. Localizes to endoplasmic reticulum tubular network.
{ECO:0000250|UniProtKB:Q9UBP0, ECO:0000255|HAMAP-Rule:MF_03021}.
-!- DISEASE: Note=Defects in SPAST are the cause of bovine spinal
dysmyelination (BSD), a neurodegenerative disorder characterized
by pathological changes of the myelin sheaths in the spinal cord.
Defects appear immediately at birth and include lateral recumbency
with slight to moderate opisthotonos, body tremor, and spastic
extension of the limbs. General muscle atrophy due to denervation
occurs to variable degrees and is most obvious in the hind limbs.
BSD is a longstanding problem in the American Brown Swiss (ABS)
breed and in several European cattle breeds upgraded with ABS. The
morphological cause of the phenotype is bilateral symmetrical
hypo- and demyelination of axons in the cervical and thoracic
segments of the spinal cord. The disease is caused by mutations
affecting the gene represented in this entry.
{ECO:0000269|PubMed:19714378}.
-!- SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily.
{ECO:0000255|HAMAP-Rule:MF_03021}.
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EMBL; BC133327; AAI33328.1; -; mRNA.
RefSeq; NP_001075060.1; NM_001081591.1.
UniGene; Bt.46123; -.
ProteinModelPortal; A2VDN5; -.
SMR; A2VDN5; -.
STRING; 9913.ENSBTAP00000044166; -.
PaxDb; A2VDN5; -.
PRIDE; A2VDN5; -.
Ensembl; ENSBTAT00000046919; ENSBTAP00000044166; ENSBTAG00000021694.
GeneID; 521442; -.
KEGG; bta:521442; -.
CTD; 6683; -.
VGNC; VGNC:35174; SPAST.
eggNOG; KOG0740; Eukaryota.
eggNOG; COG0464; LUCA.
GeneTree; ENSGT00570000078874; -.
HOGENOM; HOG000225146; -.
HOVERGEN; HBG108502; -.
InParanoid; A2VDN5; -.
KO; K13254; -.
OMA; SEMRNIK; -.
OrthoDB; EOG091G0Q8J; -.
TreeFam; TF105014; -.
Proteomes; UP000009136; Chromosome 11.
Bgee; ENSBTAG00000021694; Expressed in 10 organ(s), highest expression level in testis.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
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; ISS:UniProtKB.
GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS: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; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
GO; GO:0008568; F:microtubule-severing ATPase activity; ISS:UniProtKB.
GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
GO; GO:0019896; P:axonal transport of mitochondrion; ISS:UniProtKB.
GO; GO:0007409; P:axonogenesis; IEA:UniProtKB-UniRule.
GO; GO:0032506; P:cytokinetic process; ISS:UniProtKB.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; ISS:UniProtKB.
GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
GO; GO:0090148; P:membrane fission; ISS:UniProtKB.
GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
GO; GO:0051013; P:microtubule severing; ISS:UniProtKB.
GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
GO; GO:0051228; P:mitotic spindle disassembly; ISS:UniProtKB.
GO; GO:0031468; P:nuclear envelope reassembly; ISS:UniProtKB.
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; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
HAMAP; MF_03021; Spastin; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR007330; MIT.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR017179; Spastin.
InterPro; IPR035106; Spastin_chordate.
InterPro; IPR015415; Vps4_C.
Pfam; PF00004; AAA; 1.
Pfam; PF09336; Vps4_C; 1.
PIRSF; PIRSF037338; Spastin; 1.
SMART; SM00382; AAA; 1.
SMART; SM00745; MIT; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00674; AAA; 1.
1: Evidence at protein level;
Allosteric enzyme; ATP-binding; Cell cycle; Cell division;
Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein;
Differentiation; Disease mutation; Endoplasmic reticulum; Hydrolase;
Membrane; Microtubule; Neurogenesis; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome.
CHAIN 1 614 Spastin.
/FTId=PRO_0000367133.
TOPO_DOM 1 56 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_03021}.
INTRAMEM 57 77 Helical. {ECO:0000255|HAMAP-
Rule:MF_03021}.
TOPO_DOM 78 614 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_03021}.
DOMAIN 118 193 MIT. {ECO:0000255}.
NP_BIND 380 387 ATP. {ECO:0000255|HAMAP-Rule:MF_03021}.
REGION 1 298 Required for interaction with RTN1.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 1 192 Required for midbody localization.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 1 80 Required for interaction with ATL1.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 1 50 Required for nuclear localization.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 50 87 Required for interaction with SSNA1 and
microtubules.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 110 194 Sufficient for interaction with CHMP1B.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 112 198 Required for interaction with
microtubules.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 226 614 Sufficient for microtubule severing.
{ECO:0000250|UniProtKB:Q9UBP0}.
REGION 268 326 Required for interaction with
microtubules and microtubule severing.
{ECO:0000250|UniProtKB:Q9UBP0}.
MOTIF 4 11 Nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_03021}.
MOTIF 59 67 Nuclear export signal.
{ECO:0000255|HAMAP-Rule:MF_03021}.
MOTIF 307 310 Nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_03021}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UBP0}.
MOD_RES 266 266 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UBP0}.
MOD_RES 304 304 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UBP0}.
MOD_RES 595 595 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UBP0}.
VARIANT 560 560 R -> Q (in BSD).
{ECO:0000269|PubMed:19714378}.
SEQUENCE 614 AA; 67225 MW; B284B6EBF04D358F CRC64;
MNSPGGRGKK KGSGGPSSPV PPRPPPPCQA RSRPAPKPAP PPQSPHKRNL YYFSYPLFLG
FALLRLVAFH LGLLFVWLCQ RFSRALMAAK RSSGAAPASA SPPAPVPGGE AERVRAFHKQ
AFEYISVALR IDEDEKVGQK DQAVEWYKKG IEELEKGIAV VVTGQGEQCE RARRLQAKMM
TNLVMAKDRL QLLEKLQPSL QFSKSQTDVY NDSTNLTCRN GHLQSESGAV PKRKDPLTHA
SNSLPRSKTV MKTGPTGLSG HHRAPSCSGL SMVSGVRQGP GSAAATHKST PKTNRTNKPS
TPTTAARKKK DLKNFRNVDS NLANLIMNEI VDNGTAVKFD DIAGQELAKQ ALQEIVILPS
LRPELFTGLR APARGLLLFG PPGNGKTMLA KAVAAESNAT FFNISAASLT SKYVGEGEKL
VRALFAVARE LQPSIIFIDE VDSLLCERRE GEHDASRRLK TEFLIEFDGV QSAGDDRVLV
MGATNRPQEL DEAVLRRFTK RVYVSLPNEE TRLLLLKNLL CKQGSPLTQK ELAQLARMTN
GYSGSDLTAL AKDAALGPIR ELKPEQVKNM SASEMRNIRL SDFTESLKKI KRSVSPQTLE
AYIRWNKDFG DTTV


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