Gene

KWMTBOMO15342

Pre Gene Modal

BGIBMGA005075

Annotation

PREDICTED:_spastin_isoform_X3_[Bombyx_mori]

Location

Bomo_Chr25(+):9686426-9716582      View in EpiBrowser

Full name

Spastin      

Alternative Name

D-Spastin
Dm-Spastin
Dspastin

Location in the cell

Mitochondrial   Reliability : 1.444 Nuclear   Reliability : 1.824

CDS

ATGAAAAAGCCTCGTAAGATCGGCGAGTGCAACTTAGAAGTTGTAGTGAAAGACGGTATAGTGTCCACAGAGATAGCTCAAGAAGATATGTCTCATCACGTCGGACCAGGCGATCCACTGCTGGCCAAGCAGAAGCATCATCATCGCAAAGCTTTTGAATACATATCGAAAGCTTTGAAGATTGATGAGGAAAACGAAGGCCAAAAGGAGCTAGCAATAGAACTGTACAAGAAAGGGATTTTTGAATTGGAGCGAGGTATCGCTGTCGACTGCTGGGGAGGTAGAGGAGACGCTTGGCAAAGAGCTCAAAAACTACACGACAAGATGAAAACAAACCTTGGAATGGCTAAGGATCGTTTACATTTCCTTGTTGCAGGACGAAAACTGACGACGGCAGGCCGAAGAGTGCCTAGCAGTGGAGGAGGGCCCTTGATGAAATCTCAGACTTTGCCGAGGTCCATGGGCAGATCATCCTCCCAGCCGAACAGCTCTAACGGGGGCTACACACGGTACCCCATGAAGCCTGCGTCTACACCGCCGGCTGTTAAAAGACAGTTGTCTGTGCCGGTAAACGGTTCGCCAGTCCGCCGGGCGGTGAGTGGCTCGCAACGCGGTACGCCCACCAGAAGCAGGACTCCGCAGCCCGCGCTAACCGTCCGAGGCGTCGACCCGAAGCTGGTCCAGCTTATACTGGACGAGATAGTCGAAGGAGGACCCAAAGTAAACTGGGACGATATAGCTGGCCAAGAGGCAGCAAAACAAGCATTGCAAGAAATGGTTGTTCTACCTTCGTTGAGGCCCGAACTCTTCACCGGACTCCGATCGCCAGCCCGAGGCTTACTTTTGTTTGGACCTCCAGGAAATGGCAAGACTCTGCTAGCGCGATGCGTAGCGGCCGAATGCTCAGCGACTTTCTTCTCGATATCCGCCGCGAGTCTGACCAGCAAATATGTGGGCGAAGGCGAGAAGATGGTGAGGGCTCTGTTCCAAGTCGCTAGAGAACTGCAGCCTTCAATAATATTCGTGGATGAGGTAGACTCGCTGCTGTGCGAGAGATCGTCCGGCGAGCACGAGGCGTCTCGGCGGCTGAAGACAGAGTTCCTGGTGGAATTCGACGGACTCCCGGCGGCCGGAGCCGACAGACTCATCGTGATGGCCGCCACGAACCGACCTCAGGAACTGGACGAGGCTGCGTTGAGACGGTTCCCGAAGCGCGTGTACGTGTCGCTGCCGGACGCGCGGGTGCGGGCGGCGCTGGTGCGCGGCGTGCTGGCCCGCGGCGCCGCGCAGACCGAGCTCGCGGACGACGAGCTGGTGCGCCTCGCCGCGCTCACTGACGGCTACTCCGGCAGCGACCTCACCGCGCTCTGCAGGGACGCCGCGCTCGGCCCCATACGAGAGCTGGATCCCGAGGAAGTCAAATGTCTGGACCTGTCATTGGTCCGGAGCATTACCTTCCAAGATTTCCTAGATTCGCTGAAAAGGATCCGACCTTCTGTGTCTCCGCACAGCCTCGTCGCGTACGAGAAGTGGTCCGTGCAGTATGGCGATTTGGGATTTTGA

Protein

MKKPRKIGECNLEVVVKDGIVSTEIAQEDMSHHVGPGDPLLAKQKHHHRKAFEYISKALKIDEENEGQKELAIELYKKGIFELERGIAVDCWGGRGDAWQRAQKLHDKMKTNLGMAKDRLHFLVAGRKLTTAGRRVPSSGGGPLMKSQTLPRSMGRSSSQPNSSNGGYTRYPMKPASTPPAVKRQLSVPVNGSPVRRAVSGSQRGTPTRSRTPQPALTVRGVDPKLVQLILDEIVEGGPKVNWDDIAGQEAAKQALQEMVVLPSLRPELFTGLRSPARGLLLFGPPGNGKTLLARCVAAECSATFFSISAASLTSKYVGEGEKMVRALFQVARELQPSIIFVDEVDSLLCERSSGEHEASRRLKTEFLVEFDGLPAAGADRLIVMAATNRPQELDEAALRRFPKRVYVSLPDARVRAALVRGVLARGAAQTELADDELVRLAALTDGYSGSDLTALCRDAALGPIRELDPEEVKCLDLSLVRSITFQDFLDSLKRIRPSVSPHSLVAYEKWSVQYGDLGF

Description

ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the microtubule organizing center following nucleation.
ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in axon regeneration by regulating microtubule severing.
ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle (PubMed:15242610, PubMed:15562320, PubMed:15823537, PubMed:16276413, PubMed:17452528, PubMed:25875445, PubMed:18202664, PubMed:19341724). Regulates microtubule stability in the neuromuscular junction synapse (PubMed:15242610, PubMed:15562320, PubMed:19341724). Involved in lipid metabolism by regulating the size and distribution of lipid droplets (PubMed:25875445). Involved in axon regeneration by regulating microtubule severing (PubMed:23122959).
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. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and for completion of the abscission stage of cytokinesis. Also plays a role in axon growth and the formation of axonal branches.

Catalytic Activity

n ATP + n H(2)O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.

Subunit

Homohexamer. The homohexamer is stabilized by ATP-binding. The homohexamer may adopt a ring conformation through which microtubules pass prior to being severed. Interacts with microtubules.
Homohexamer. The homohexamer is stabilized by ATP-binding. The homohexamer may adopt a ring conformation through which microtubules pass prior to being severed. Interacts with microtubules. Interacts with atl; may be involved in microtubule dynamics.
Homohexamer. The homohexamer is stabilized by ATP-binding. The homohexamer may adopt a ring conformation through which microtubules pass prior to being severed (PubMed:18202664). Interacts with microtubules (PubMed:15823537, PubMed:18202664). Interacts with atl; may be involved in microtubule dynamics (PubMed:19341724).

Similarity

Belongs to the AAA ATPase family. Spastin subfamily.
Belongs to the AAA ATPase family.

Keywords

ATP-binding   Cell cycle   Cell division   Chromosome   Complete proteome   Cytoplasm   Cytoskeleton   Developmental protein   Differentiation   Isomerase   Lipid droplet   Membrane   Microtubule   Mitosis   Neurogenesis   Nucleotide-binding   Reference proteome   3D-structure   Phosphoprotein   Alternative splicing   Nucleus  

Feature

chain  Spastin
splice variant  In isoform 2.

Uniprot

A0A2A4IUU0   A0A194Q7H6   A0A2A4IU74   A0A0N1I5K3   H9J6D3   A0A212EZS7   + More
A0A2W1B7L8   A0A1Y1KFA1   A0A1Y1KL42   A0A158NSN8   A0A1Y1KHQ5   A0A1Y1KMR0   A0A1Q3EUM0   A0A1Q3EUZ1   D6WR93   N6SRM3   A0A3B0JKI5   A0A034W3J6   A0A1W4U7W3   A0A0K8UYH1   A0A0R3NH26   A0A0A1WSU7   A0A1L8DU08   A0A1L8DTP0   A0A1I8NNF4   E0VYI4   A0A0M4F6S0   W8C8D8   A0A0Q9WIN0   A0A1W4W830   A0A0P8XY81   A0A0Q9WTF8   A0A1B6I365   A0A0Q9WY76   A0A1W4ULF9   A0A126GV13   A0A0B4LHJ5   A0A146L6H0   A0A126GV10   A0A0A9ZEL2   A0A0A9ZIL4   B4HGG6   Q8I0P1   A0A1B6KIZ5   A0A088A016   B4QSF0   F4W8A4   E2AI24   A0A195CAZ2   A0A1B6GJT6   A0A069DV18   A0A0V0G8F5   A0A224XLX6   A0A0P4VTL2   A0A182P867   A0A1B0D797   A0A0P4W909   A0A3Q0JEE6   A0A2J7Q240   A0A1B6DYR9   R7TU42   A0A2R5L4N1   A0A0L7R7C7   E2BI57   A0A2A3E4B6   A0A3Q2E8P7   A0A3L8DA27   A0A026WUX2   A0A151I5Z7   A0A195DUQ1   A0A154P359   A0A1B6CUX1   A0A1Z5KY73   A0A2L2YK85   A0A0C9PQF2   A0A151XDP6   A0A0T6B521   A0A2J7Q222   A0A2J7Q234   A0A0C9QYQ7   A0A3P8UBX3   A0A3Q1CK62   A0A1B6G657   A0A146MUH2   A0A3Q2TUE9   A0A3B3YLW5   A0A3Q1EVP2   M3ZW57   A0A1L1RP85   A0A146RUZ8   A0A2M4BN30   A0A1V4JL95   A0A3B3CL24   E9HN60   K7J219   A0A2U9CEW3   Q5ZK92-2   A0A3B4ZRW5   A0A146VQQ2   I3JUV2  

EC Number

5.6.1.1

Pubmed

26354079    19121390    22118469    28756777    28004739    21347285    + More
18362917    19820115    23537049    25348373    15632085    17994087    25830018    20566863    24495485    10731132    12537568    12537572    12537573    12537574    16110336    17569856    17569867    26109357    26109356    26823975    25401762    12537569    12908108    15242610    15562320    15823537    16276413    17452528    18327897    19341724    23122959    25875445    18202664    21719571    20798317    26334808    27129103    23254933    30249741    24508170    28528879    26561354    23542700    15592404    29451363    21292972    20075255    15642098    25186727   

EMBL

NWSH01007192    PCG63044.1    KQ459324    KPJ01492.1    PCG63046.1    KQ460973    + More
KPJ10059.1    BABH01019775    BABH01019776    BABH01019777    BABH01019778    AGBW02011239    OWR46982.1    KZ150250    PZC71832.1    GEZM01085201    JAV60129.1    GEZM01085204    JAV60126.1    ADTU01025081    ADTU01025082    GEZM01085202    JAV60128.1    GEZM01085203    JAV60127.1    GFDL01016026    JAV19019.1    GFDL01016027    JAV19018.1    KQ971354    EFA07037.1    APGK01059436    APGK01059437    KB741293    KB632046    ENN70269.1    ERL88278.1    OUUW01000007    SPP82735.1    GAKP01009678    JAC49274.1    GDHF01020658    JAI31656.1    CM000070    KRT00353.1    GBXI01012712    JAD01580.1    GFDF01004204    JAV09880.1    GFDF01004265    JAV09819.1    DS235845    EEB18440.1    CP012526    ALC47445.1    GAMC01007521    GAMC01007519    JAB99034.1    CH940650    KRF83798.1    CH902617    KPU79694.1    CH964232    KRF99403.1    GECU01026344    JAS81362.1    CH933806    KRG00934.1    AE014297    ALI30635.1    AHN57493.1    GDHC01014581    JAQ04048.1    ALI30634.1    GBHO01000730    JAG42874.1    GBHO01000729    GBRD01006505    JAG42875.1    JAG59316.1    CH480815    AY069522    BT001254    BT001351    BT044258    GEBQ01028549    JAT11428.1    CM000364    GL887898    EGI69599.1    GL439621    EFN66932.1    KQ978023    KYM97977.1    GECZ01007062    JAS62707.1    GBGD01000996    JAC87893.1    GECL01001705    JAP04419.1    GFTR01006986    JAW09440.1    GDKW01003380    JAI53215.1    AJVK01026762    AJVK01026763    GDRN01107862    JAI57357.1    NEVH01019373    PNF22640.1    GEDC01006501    JAS30797.1    AMQN01012240    KB309387    ELT94540.1    GGLE01000281    MBY04407.1    KQ414643    KOC66661.1    GL448450    EFN84628.1    KZ288379    PBC26603.1    QOIP01000011    RLU16973.1    KK107111    EZA58904.1    KQ976400    KYM92670.1    KQ980322    KYN16603.1    KQ434809    KZC06365.1    GEDC01020127    JAS17171.1    GFJQ02007072    JAV99897.1    IAAA01030916    LAA08532.1    GBYB01003436    GBYB01003438    JAG73203.1    JAG73205.1    KQ982275    KYQ58440.1    LJIG01009785    KRT82385.1    PNF22641.1    PNF22642.1    GBYB01005787    JAG75554.1    GECZ01011849    JAS57920.1    GCES01163570    JAQ22752.1    AADN05000005    GCES01114120    JAQ72202.1    GGFJ01005346    MBW54487.1    LSYS01007194    OPJ72527.1    GL732693    EFX66831.1    CP026257    AWP14239.1    EU849599    EU849600    AJ720192    AADN03003400    AADN03003564    GCES01066581    JAR19742.1    AERX01006480   

Proteomes

UP000218220    UP000053268    UP000053240    UP000005204    UP000007151    UP000005205    + More
UP000007266    UP000019118    UP000030742    UP000268350    UP000192221    UP000001819    UP000095300    UP000009046    UP000092553    UP000008792    UP000192223    UP000007801    UP000007798    UP000009192    UP000000803    UP000001292    UP000005203    UP000000304    UP000007755    UP000000311    UP000078542    UP000075885    UP000092462    UP000079169    UP000235965    UP000014760    UP000053825    UP000008237    UP000242457    UP000265020    UP000279307    UP000053097    UP000078540    UP000078492    UP000076502    UP000075809    UP000265080    UP000257160    UP000265000    UP000261480    UP000257200    UP000002852    UP000000539    UP000190648    UP000261560    UP000000305    UP000002358    UP000246464    UP000261400    UP000005207   

PRIDE

H9J6D3    B4HGG6    Q8I0P1    B4QSF0   

Pfam

PF17862   AAA_lid_3        + More
PF00004   AAA
PF09336   Vps4_C
PF04212   MIT
PF17906   HTH_48

Interpro

IPR003593   AAA+_ATPase        + More
IPR041569   AAA_lid_3       
IPR003959   ATPase_AAA_core       
IPR007330   MIT       
IPR017179   Spastin       
IPR015415   Vps4_C       
IPR036181   MIT_dom_sf       
IPR027417   P-loop_NTPase       
IPR003960   ATPase_AAA_CS       
IPR036388   WH-like_DNA-bd_sf       
IPR041426   Mos1_HTH       
IPR035106   Spastin_chordate       

SUPFAM

SSF52540   SSF52540        + More
SSF116846   SSF116846       

Gene 3D

1.10.10.10    

ProteinModelPortal

A0A2A4IUU0   A0A194Q7H6   A0A2A4IU74   A0A0N1I5K3   H9J6D3   A0A212EZS7   + More
A0A2W1B7L8   A0A1Y1KFA1   A0A1Y1KL42   A0A158NSN8   A0A1Y1KHQ5   A0A1Y1KMR0   A0A1Q3EUM0   A0A1Q3EUZ1   D6WR93   N6SRM3   A0A3B0JKI5   A0A034W3J6   A0A1W4U7W3   A0A0K8UYH1   A0A0R3NH26   A0A0A1WSU7   A0A1L8DU08   A0A1L8DTP0   A0A1I8NNF4   E0VYI4   A0A0M4F6S0   W8C8D8   A0A0Q9WIN0   A0A1W4W830   A0A0P8XY81   A0A0Q9WTF8   A0A1B6I365   A0A0Q9WY76   A0A1W4ULF9   A0A126GV13   A0A0B4LHJ5   A0A146L6H0   A0A126GV10   A0A0A9ZEL2   A0A0A9ZIL4   B4HGG6   Q8I0P1   A0A1B6KIZ5   A0A088A016   B4QSF0   F4W8A4   E2AI24   A0A195CAZ2   A0A1B6GJT6   A0A069DV18   A0A0V0G8F5   A0A224XLX6   A0A0P4VTL2   A0A182P867   A0A1B0D797   A0A0P4W909   A0A3Q0JEE6   A0A2J7Q240   A0A1B6DYR9   R7TU42   A0A2R5L4N1   A0A0L7R7C7   E2BI57   A0A2A3E4B6   A0A3Q2E8P7   A0A3L8DA27   A0A026WUX2   A0A151I5Z7   A0A195DUQ1   A0A154P359   A0A1B6CUX1   A0A1Z5KY73   A0A2L2YK85   A0A0C9PQF2   A0A151XDP6   A0A0T6B521   A0A2J7Q222   A0A2J7Q234   A0A0C9QYQ7   A0A3P8UBX3   A0A3Q1CK62   A0A1B6G657   A0A146MUH2   A0A3Q2TUE9   A0A3B3YLW5   A0A3Q1EVP2   M3ZW57   A0A1L1RP85   A0A146RUZ8   A0A2M4BN30   A0A1V4JL95   A0A3B3CL24   E9HN60   K7J219   A0A2U9CEW3   Q5ZK92-2   A0A3B4ZRW5   A0A146VQQ2   I3JUV2  

PDB

6NYV     E-value=7.87603e-115,     Score=1059

KEGG

101740668    K13254 spastin [EC:5.6.1.1] | (RefSeq) spastin

GO

GO:0005813   GO:0008568   GO:0005874   GO:0008017   GO:0005524   GO:0031117   GO:0016021   GO:0005819   GO:0005737   GO:0034214   GO:0016853   GO:0031122   GO:0005634   GO:0016887   GO:0005694   GO:0005811   GO:0050803   GO:0000022   GO:0008344   GO:0051301   GO:0030154   GO:0007399   GO:0007079   GO:0000502   GO:0045886   GO:2000331   GO:0035099   GO:0045887   GO:0045834   GO:0048691   GO:0051013   GO:0031594   GO:0008021   GO:1900074   GO:0050775   GO:0043195   GO:1900075   GO:0019226   GO:0043014   GO:0007626   GO:0015630   GO:0048167   GO:0000226   GO:0000070   GO:0006888   GO:0007409   GO:0048471   GO:0032506   GO:0007032   GO:0072593   GO:0045773   GO:0048675   GO:0043066   GO:0021955   GO:0031965   GO:0005768   GO:0051228   GO:0010458   GO:0051260   GO:0031468   GO:0005654   GO:0001578   GO:0005829   GO:0030496   GO:0019896   GO:1904115   GO:0000281   GO:0005783   GO:0048487   GO:0090148   GO:0032467   GO:0008089   GO:0006436   GO:0004812   GO:0006418   GO:0004222   GO:0031012   GO:0008233  

Subcellular location

Membrane   Forms an intramembrane hairpin-like structure in the membrane.   With evidence from 1 publications.
Cytoplasm   Forms an intramembrane hairpin-like structure in the membrane.   With evidence from 1 publications.
Cytoskeleton   Forms an intramembrane hairpin-like structure in the membrane.   With evidence from 1 publications.
Microtubule organizing center   Forms an intramembrane hairpin-like structure in the membrane.   With evidence from 1 publications.
Centrosome   Forms an intramembrane hairpin-like structure in the membrane.   With evidence from 1 publications.
Chromosome   Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles.   With evidence from 1 publications.
Lipid droplet   Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles.   With evidence from 1 publications.
Perinuclear region   Forms an intramembrane hairpin-like structure in the membrane.   With evidence from 1 publications.
Nucleus   Forms an intramembrane hairpin-like structure in the membrane.   With evidence from 1 publications.

Length:

520

Number of predicted TMHs:

0

Exp number of AAs in TMHs:

0.01278

Exp number, first 60 AAs:

0

Total prob of N-in:

0.00613

outside

1  -  520

 

 

Pi

269.31313

Theta

195.190418

Tajima's D

0.949433

CLR

0.389685

CSRT

0.649067546622669

Interpretation

Uncertain