SPAST_CHICK
ID SPAST_CHICK Reviewed; 613 AA.
AC Q5ZK92; B5AH49; B5AH50; E1C6S3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Spastin {ECO:0000255|HAMAP-Rule:MF_03021};
DE EC=5.6.1.1 {ECO:0000255|HAMAP-Rule:MF_03021};
GN Name=SPAST {ECO:0000255|HAMAP-Rule:MF_03021};
GN Synonyms=SPG4 {ECO:0000255|HAMAP-Rule:MF_03021};
GN ORFNames=RCJMB04_12e12 {ECO:0000303|PubMed:15642098};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 93-613 (ISOFORM 2).
RA Karabay A., Akbalik G.;
RT "Redundant microtubule severing proteins in neurons.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
CC -!- FUNCTION: ATP-dependent microtubule severing protein that specifically
CC recognizes and cuts microtubules that are polyglutamylated.
CC Preferentially recognizes and acts on microtubules decorated with short
CC polyglutamate tails: severing activity increases as the number of
CC glutamates per tubulin rises from one to eight, but decreases beyond
CC this glutamylation threshold. Microtubule severing promotes
CC reorganization of cellular microtubule arrays and the release of
CC microtubules from the centrosome following nucleation. Required for
CC membrane traffic from the endoplasmic reticulum (ER) to the Golgi and
CC for completion of the abscission stage of cytokinesis. Also plays a
CC role in axon growth and the formation of axonal branches.
CC {ECO:0000255|HAMAP-Rule:MF_03021}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1)
CC alpha/beta tubulin heterodimers.; EC=5.6.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
CC -!- SUBUNIT: Homohexamer. The homohexamer is stabilized by ATP-binding. The
CC homohexamer may adopt a ring conformation through which microtubules
CC pass prior to being severed. Interacts with microtubules.
CC {ECO:0000255|HAMAP-Rule:MF_03021}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton
CC {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region
CC {ECO:0000255|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000255|HAMAP-
CC Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in
CC the membrane. {ECO:0000255|HAMAP-Rule:MF_03021}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5ZK92-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5ZK92-2; Sequence=VSP_036648;
CC -!- SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03021}.
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DR EMBL; EU849599; ACF60960.1; -; mRNA.
DR EMBL; EU849600; ACF60961.1; -; mRNA.
DR EMBL; AJ720192; CAG31851.1; -; mRNA.
DR EMBL; AADN03003400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN03003564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001026232.1; NM_001031061.1.
DR RefSeq; XP_015139215.1; XM_015283729.1. [Q5ZK92-2]
DR AlphaFoldDB; Q5ZK92; -.
DR SMR; Q5ZK92; -.
DR STRING; 9031.ENSGALP00000017259; -.
DR Ensembl; ENSGALT00000017279; ENSGALP00000017259; ENSGALG00000010620. [Q5ZK92-1]
DR GeneID; 421481; -.
DR KEGG; gga:421481; -.
DR CTD; 6683; -.
DR VEuPathDB; HostDB:geneid_421481; -.
DR GeneTree; ENSGT00940000156258; -.
DR InParanoid; Q5ZK92; -.
DR OMA; GMTNEPM; -.
DR OrthoDB; 1176820at2759; -.
DR PRO; PR:Q5ZK92; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000010620; Expressed in spermatid and 13 other tissues.
DR ExpressionAtlas; Q5ZK92; baseline and differential.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:Ensembl.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0008568; F:microtubule severing ATPase activity; ISS:UniProtKB.
DR GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0019896; P:axonal transport of mitochondrion; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0032506; P:cytokinetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:UniProtKB-UniRule.
DR GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
DR GO; GO:0090148; P:membrane fission; ISS:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0051013; P:microtubule severing; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0051228; P:mitotic spindle disassembly; ISS:UniProtKB.
DR GO; GO:0031468; P:nuclear membrane reassembly; ISS:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IEA:Ensembl.
DR GO; GO:0031117; P:positive regulation of microtubule depolymerization; IEA:UniProtKB-UniRule.
DR GO; GO:0034214; P:protein hexamerization; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03021; Spastin; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR017179; Spastin.
DR InterPro; IPR035106; Spastin_chordate.
DR InterPro; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR PIRSF; PIRSF037338; Spastin; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Isomerase; Membrane;
KW Microtubule; Neurogenesis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..613
FT /note="Spastin"
FT /id="PRO_0000367136"
FT TOPO_DOM 1..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT INTRAMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT TOPO_DOM 83..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT DOMAIN 117..192
FT /note="MIT"
FT /evidence="ECO:0000255"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 379..386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03021"
FT VAR_SEQ 193..224
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_036648"
FT CONFLICT 45
FT /note="A -> T (in Ref. 1; ACF60960)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="L -> S (in Ref. 1; ACF60960/ACF60961)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="A -> V (in Ref. 1; ACF60960/ACF60961 and 2;
FT CAG31851)"
SQ SEQUENCE 613 AA; 66238 MW; D30630024CFC1C96 CRC64;
MNSPGGRGKK KGSAGSSSAP PAAGASPSAP SGPAPPAPPA GAAAAAAASP HKRNLYYFSY
PLFAAFALLR FVAFQLGLLV AWLCERLSRG ALMAAKSSRA GDAPEPGGAA ERVRACHKRA
FECISMALRI DEDERAGQKE QAVEWYKKGI EELERGIAVL VVGQGDQCER ARRLQSKMMT
NLAMAKDRLQ LLEKLQADLQ ISKPQMEVYN DSTNLACRNG HLQSESGAVP KKKDPLTHTS
NSLPRSKTVA KTGSTGLSGH HRTPSYSGIS TASVSRPAAN PATSTHKAAP KNSRTNKPST
PTPAARKKKD TKVFRNVDSN LANLILNEIV DSGPAVKFDD IAGQELAKQA LQEIVILPSL
RPELFTGLRA PARGLLLFGP PGNGKTMLAK AVAAESNATF FNISAASLTS KYVGEGEKLV
RALFAVAREL QPSIIFIDEV DSLLCERREG EHDASRRLKT EFLIEFDGVQ SSGEDRILVM
GATNRPQELD DAVLRRFTKR VYVSLPNEET RLILLKNLLS KQGSPLTQKE LAQLARMTDG
YSGSDLTALA KDAALGPIRE LKPEQVKNMS ASEMRNIKLS DFTESLKKIK RSLSPQTLEA
YIRWNKDFGD TTV
