MSPS_DROME
ID MSPS_DROME Reviewed; 2042 AA.
AC Q9VEZ3; Q4QQC0;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Protein mini spindles;
GN Name=msps; ORFNames=CG5000 {ECO:0000312|FlyBase:FBgn0027948};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10477755; DOI=10.1083/jcb.146.5.1005;
RA Cullen C.F., Deak P., Glover D.M., Ohkura H.;
RT "mini spindles: A gene encoding a conserved microtubule-associated protein
RT required for the integrity of the mitotic spindle in Drosophila.";
RL J. Cell Biol. 146:1005-1018(1999).
RN [5]
RP FUNCTION, INTERACTION WITH TACC, AND SUBCELLULAR LOCATION.
RX PubMed=11433295; DOI=10.1038/35083025;
RA Cullen C.F., Ohkura H.;
RT "Msps protein is localized to acentrosomal poles to ensure bipolarity of
RT Drosophila meiotic spindles.";
RL Nat. Cell Biol. 3:637-642(2001).
RN [6]
RP FUNCTION.
RX PubMed=15530399; DOI=10.1016/j.cub.2004.10.023;
RA Moon W., Hazelrigg T.;
RT "The Drosophila microtubule-associated protein mini spindles is required
RT for cytoplasmic microtubules in oogenesis.";
RL Curr. Biol. 14:1957-1961(2004).
RN [7]
RP FUNCTION.
RX PubMed=16303556; DOI=10.1016/j.cub.2005.09.054;
RA Goshima G., Wollman R., Stuurman N., Scholey J.M., Vale R.D.;
RT "Length control of the metaphase spindle.";
RL Curr. Biol. 15:1979-1988(2005).
RN [8]
RP FUNCTION.
RX PubMed=15775959; DOI=10.1038/sj.emboj.7600629;
RA Brittle A.L., Ohkura H.;
RT "Mini spindles, the XMAP215 homologue, suppresses pausing of interphase
RT microtubules in Drosophila.";
RL EMBO J. 24:1387-1396(2005).
RN [9]
RP FUNCTION, AND INTERACTION WITH DGT6.
RX PubMed=19836241; DOI=10.1016/j.cub.2009.09.043;
RA Bucciarelli E., Pellacani C., Naim V., Palena A., Gatti M., Somma M.P.;
RT "Drosophila Dgt6 interacts with Ndc80, Msps/XMAP215, and gamma-tubulin to
RT promote kinetochore-driven MT formation.";
RL Curr. Biol. 19:1839-1845(2009).
RN [10]
RP FUNCTION, TOG DOMAIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 546-LYS--LYS-549 AND 1102-LYS--ARG-1107.
RX PubMed=21965297; DOI=10.1091/mbc.e11-06-0520;
RA Currie J.D., Stewman S., Schimizzi G., Slep K.C., Ma A., Rogers S.L.;
RT "The microtubule lattice and plus-end association of Drosophila Mini
RT spindles is spatially regulated to fine-tune microtubule dynamics.";
RL Mol. Biol. Cell 22:4343-4361(2011).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26953351; DOI=10.1083/jcb.201503047;
RA Chen K., Koe C.T., Xing Z.B., Tian X., Rossi F., Wang C., Tang Q., Zong W.,
RA Hong W.J., Taneja R., Yu F., Gonzalez C., Wu C., Endow S., Wang H.;
RT "Arl2- and Msps-dependent microtubule growth governs asymmetric division.";
RL J. Cell Biol. 212:661-676(2016).
RN [12]
RP INTERACTION WITH MV, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=33725482; DOI=10.1016/j.devcel.2021.02.019;
RA Lattao R., Rangone H., Llamazares S., Glover D.M.;
RT "Mauve/LYST limits fusion of lysosome-related organelles and promotes
RT centrosomal recruitment of microtubule nucleating proteins.";
RL Dev. Cell 56:1000-1013.e6(2021).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 267-505, TOG DOMAIN, FUNCTION,
RP AND MUTAGENESIS OF TRP-21 AND TRP-292.
RX PubMed=17889670; DOI=10.1016/j.molcel.2007.07.023;
RA Slep K.C., Vale R.D.;
RT "Structural basis of microtubule plus end tracking by XMAP215, CLIP-170,
RT and EB1.";
RL Mol. Cell 27:976-991(2007).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 848-1084, TOG DOMAIN, AND
RP MUTAGENESIS OF TRP-21; TRP-292; TRP-606 AND TRP-874.
RX PubMed=24966168; DOI=10.1091/mbc.e13-08-0501;
RA Fox J.C., Howard A.E., Currie J.D., Rogers S.L., Slep K.C.;
RT "The XMAP215 family drives microtubule polymerization using a structurally
RT diverse TOG array.";
RL Mol. Biol. Cell 25:2375-2392(2014).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 582-825, AND TOG DOMAIN.
RX PubMed=25720490; DOI=10.1074/jbc.m114.633826;
RA Howard A.E., Fox J.C., Slep K.C.;
RT "Drosophila melanogaster mini spindles TOG3 utilizes unique structural
RT elements to promote domain stability and maintain a TOG1- and TOG2-like
RT tubulin-binding surface.";
RL J. Biol. Chem. 290:10149-10162(2015).
CC -!- FUNCTION: Binds to the plus end of microtubules and regulates
CC microtubule dynamics and microtubule organization. Promotes cytoplasmic
CC microtubule nucleation and elongation. May act as a microtubule
CC antipause factor that rapidly catalyzes the transition from pause to
CC either growth or shrinkage. Involved in mitotic spindle elongation.
CC Involved in the establishment of cell polarity and mitotic spindle
CC orientation in neuroblasts. Required for maintaining the bipolarity of
CC acentrosomal meiotic spindles; the function is dependent on tacc and
CC involves ncd. Involved in oocyte microtubule cytoskeleton organization
CC and bicoid mRNA localization. Seems to be involved in elongation of
CC kinetochore-derived microtubule fibers. {ECO:0000269|PubMed:10477755,
CC ECO:0000269|PubMed:11433295, ECO:0000269|PubMed:15530399,
CC ECO:0000269|PubMed:15775959, ECO:0000269|PubMed:16303556,
CC ECO:0000269|PubMed:17889670, ECO:0000269|PubMed:26953351,
CC ECO:0000305|PubMed:21965297}.
CC -!- SUBUNIT: Interacts with tacc, dgt6 (PubMed:11433295, PubMed:19836241).
CC Interacts with mv (PubMed:33725482). {ECO:0000269|PubMed:11433295,
CC ECO:0000269|PubMed:19836241, ECO:0000269|PubMed:33725482}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:10477755,
CC ECO:0000269|PubMed:26953351, ECO:0000269|PubMed:33725482}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:10477755,
CC ECO:0000269|PubMed:11433295, ECO:0000269|PubMed:33725482}.
CC Note=Localizes to the plus ends of growing microtubules in the cell
CC interior in a Eb1-dependent manner. Localizes to the lattice of growing
CC and shrinking microtubule in a discontinuous pattern in the peripheral
CC regions of interphase cells. Localized at acentrosomal poles of female
CC meiotic spindle. In embryos, associates with centrosomes in prophase
CC and metaphase, then associates with spindle microtubules.
CC {ECO:0000269|PubMed:11433295, ECO:0000269|PubMed:21965297,
CC ECO:0000269|PubMed:33725482}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos (at protein level).
CC {ECO:0000269|PubMed:33725482}.
CC -!- DOMAIN: The TOG (tumor overexpressed gene) domains are arranged in a N-
CC terminal pentameric array with each domain composed of six (for the
CC most part non-canonical) HEAT repeats forming a oblong paddle-like
CC structure. Intra-HEAT loops are positioned along a face of the TOG
CC domain and bind to a single alpha/beta-tubulin heterodimer. The TOG
CC domains in the array seem to be structurally and functionally
CC polarized. Differential functions may range from microtubule (MT)
CC lattice binding and/or free tubulin heterodimer binding to potentiating
CC stable incorporation of tubulin into the MT lattice. TOG 1-2 show
CC strong and TOG 3-4 weak tubulin binding; TOG 1-5 are required for full
CC ability to promote MT polymerization. {ECO:0000305|PubMed:21965297,
CC ECO:0000305|PubMed:24966168, ECO:0000305|PubMed:25720490}.
CC -!- SIMILARITY: Belongs to the TOG/XMAP215 family. {ECO:0000305}.
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DR EMBL; AE014297; AAF55269.3; -; Genomic_DNA.
DR EMBL; BT023496; AAY84896.1; -; mRNA.
DR RefSeq; NP_732105.2; NM_169698.3.
DR PDB; 2QK2; X-ray; 2.10 A; A=267-505.
DR PDB; 4QMH; X-ray; 1.65 A; A=848-1084.
DR PDB; 4Y5J; X-ray; 2.30 A; A=582-825.
DR PDB; 5VJC; X-ray; 2.00 A; A/B=1141-1411.
DR PDBsum; 2QK2; -.
DR PDBsum; 4QMH; -.
DR PDBsum; 4Y5J; -.
DR PDBsum; 5VJC; -.
DR AlphaFoldDB; Q9VEZ3; -.
DR SMR; Q9VEZ3; -.
DR IntAct; Q9VEZ3; 6.
DR STRING; 7227.FBpp0293341; -.
DR PRIDE; Q9VEZ3; -.
DR DNASU; 41952; -.
DR EnsemblMetazoa; FBtr0301480; FBpp0290695; FBgn0027948.
DR GeneID; 41952; -.
DR KEGG; dme:Dmel_CG5000; -.
DR UCSC; CG5000-RA; d. melanogaster.
DR CTD; 41952; -.
DR FlyBase; FBgn0027948; msps.
DR VEuPathDB; VectorBase:FBgn0027948; -.
DR eggNOG; KOG1820; Eukaryota.
DR GeneTree; ENSGT00390000014757; -.
DR HOGENOM; CLU_000539_2_1_1; -.
DR SignaLink; Q9VEZ3; -.
DR BioGRID-ORCS; 41952; 1 hit in 1 CRISPR screen.
DR EvolutionaryTrace; Q9VEZ3; -.
DR GenomeRNAi; 41952; -.
DR PRO; PR:Q9VEZ3; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0027948; Expressed in eye disc (Drosophila) and 53 other tissues.
DR ExpressionAtlas; Q9VEZ3; baseline and differential.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; IDA:FlyBase.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0061863; F:microtubule plus end polymerase; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:InterPro.
DR GO; GO:0015631; F:tubulin binding; IDA:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0045450; P:bicoid mRNA localization; IMP:FlyBase.
DR GO; GO:0051298; P:centrosome duplication; IBA:GO_Central.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:FlyBase.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:FlyBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:FlyBase.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IBA:GO_Central.
DR GO; GO:0045196; P:establishment or maintenance of neuroblast polarity; IMP:FlyBase.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0046785; P:microtubule polymerization; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
DR GO; GO:0000022; P:mitotic spindle elongation; IMP:FlyBase.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0016325; P:oocyte microtubule cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0090063; P:positive regulation of microtubule nucleation; IDA:FlyBase.
DR GO; GO:0007344; P:pronuclear fusion; IMP:FlyBase.
DR Gene3D; 1.25.10.10; -; 5.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR045110; XMAP215.
DR PANTHER; PTHR12609; PTHR12609; 1.
DR Pfam; PF12348; CLASP_N; 2.
DR SMART; SM01349; TOG; 5.
DR SUPFAM; SSF48371; SSF48371; 3.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Meiosis;
KW Mitosis; Reference proteome; Repeat.
FT CHAIN 1..2042
FT /note="Protein mini spindles"
FT /id="PRO_0000437574"
FT REPEAT 120..157
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 160..197
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 270..311
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 315..353
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 357..394
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 396..433
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 440..478
FT /note="HEAT 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00103"
FT REPEAT 587..624
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 625..662
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 672..710
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 745..782
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 856..893
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 896..933
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 937..974
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT REPEAT 1017..1054
FT /note="HEAT 15"
FT /evidence="ECO:0000255"
FT REPEAT 1205..1242
FT /note="HEAT 16"
FT /evidence="ECO:0000255"
FT REPEAT 1272..1309
FT /note="HEAT 17"
FT /evidence="ECO:0000255"
FT REPEAT 1311..1344
FT /note="HEAT 18"
FT /evidence="ECO:0000255"
FT REPEAT 1346..1383
FT /note="HEAT 19"
FT /evidence="ECO:0000255"
FT REGION 1..516
FT /note="Promotes microtubule polymerization"
FT /evidence="ECO:0000269|PubMed:24966168"
FT REGION 1..505
FT /note="Binds tubulin"
FT /evidence="ECO:0000269|PubMed:24966168"
FT REGION 1..229
FT /note="TOG 1"
FT /evidence="ECO:0000305|PubMed:17889670"
FT REGION 267..505
FT /note="TOG 2"
FT /evidence="ECO:0000305|PubMed:17889670"
FT REGION 498..821
FT /note="Association with microtubule lattice"
FT /evidence="ECO:0000269|PubMed:21965297"
FT REGION 506..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..1080
FT /note="Promotes microtubule polymerization"
FT /evidence="ECO:0000269|PubMed:24966168"
FT REGION 581..814
FT /note="TOG 3"
FT /evidence="ECO:0000305|PubMed:17889670"
FT REGION 804..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..1087
FT /note="TOG 4"
FT /evidence="ECO:0000305|PubMed:17889670"
FT REGION 1083..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1428
FT /note="Association with microtubule lattice"
FT /evidence="ECO:0000269|PubMed:21965297"
FT REGION 1179..1415
FT /note="TOG 5"
FT /evidence="ECO:0000305|PubMed:17889670"
FT REGION 1407..1455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1940..1959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1940..1956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 21
FT /note="W->E: Impairs microtubule polymerization. Disrupts
FT tubulin binding; when associated with E-292."
FT /evidence="ECO:0000269|PubMed:17889670,
FT ECO:0000269|PubMed:24966168"
FT MUTAGEN 292
FT /note="W->E: Impairs microtubule polymerization. Disrupts
FT tubulin binding; when associated with E-21."
FT /evidence="ECO:0000269|PubMed:17889670,
FT ECO:0000269|PubMed:24966168"
FT MUTAGEN 546..549
FT /note="KVLK->EAAE: Disrupts microtubule lattice binding."
FT /evidence="ECO:0000269|PubMed:21965297"
FT MUTAGEN 606
FT /note="W->E: Impairs microtubule polymerization, decreases
FT microtubule lattice localization."
FT /evidence="ECO:0000269|PubMed:24966168"
FT MUTAGEN 874
FT /note="W->E: Impairs microtubule polymerization, decreases
FT microtubule lattice localization."
FT /evidence="ECO:0000269|PubMed:24966168"
FT MUTAGEN 1102..1107
FT /note="KLKTVR->ELEAAA: Disrupts microtubule lattice
FT binding."
FT /evidence="ECO:0000269|PubMed:21965297"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 283..287
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 292..308
FT /evidence="ECO:0007829|PDB:2QK2"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 318..330
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 334..351
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 356..368
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 375..389
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 394..404
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 410..424
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 434..448
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 453..470
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 472..475
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 484..496
FT /evidence="ECO:0007829|PDB:2QK2"
FT HELIX 595..602
FT /evidence="ECO:0007829|PDB:4Y5J"
FT HELIX 606..619
FT /evidence="ECO:0007829|PDB:4Y5J"
FT HELIX 620..622
FT /evidence="ECO:0007829|PDB:4Y5J"
FT HELIX 630..639
FT /evidence="ECO:0007829|PDB:4Y5J"
FT STRAND 640..643
FT /evidence="ECO:0007829|PDB:4Y5J"
FT HELIX 644..646
FT /evidence="ECO:0007829|PDB:4Y5J"
FT HELIX 650..666
FT /evidence="ECO:0007829|PDB:4Y5J"
FT HELIX 671..683
FT /evidence="ECO:0007829|PDB:4Y5J"
FT HELIX 684..686
FT /evidence="ECO:0007829|PDB:4Y5J"
FT TURN 688..690
FT /evidence="ECO:0007829|PDB:4Y5J"
FT HELIX 691..704
FT /evidence="ECO:0007829|PDB:4Y5J"
FT HELIX 707..720
FT /evidence="ECO:0007829|PDB:4Y5J"
FT HELIX 724..741
FT /evidence="ECO:0007829|PDB:4Y5J"
FT HELIX 747..758
FT /evidence="ECO:0007829|PDB:4Y5J"
FT HELIX 763..780
FT /evidence="ECO:0007829|PDB:4Y5J"
FT HELIX 782..788
FT /evidence="ECO:0007829|PDB:4Y5J"
FT HELIX 793..806
FT /evidence="ECO:0007829|PDB:4Y5J"
FT HELIX 858..860
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 863..869
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 874..891
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 901..909
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 914..931
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 932..938
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 939..949
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 955..972
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 975..977
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 982..988
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 992..1005
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 1006..1008
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 1011..1013
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 1016..1029
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 1035..1052
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 1054..1064
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 1069..1079
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 1080..1082
FT /evidence="ECO:0007829|PDB:4QMH"
FT HELIX 1153..1162
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1176..1188
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1193..1199
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1204..1217
FT /evidence="ECO:0007829|PDB:5VJC"
FT TURN 1218..1220
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1222..1227
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1229..1239
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1245..1264
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1271..1282
FT /evidence="ECO:0007829|PDB:5VJC"
FT TURN 1283..1286
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1290..1306
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1309..1318
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1319..1321
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1325..1342
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1344..1346
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1349..1357
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1358..1360
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1364..1381
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1382..1384
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1385..1388
FT /evidence="ECO:0007829|PDB:5VJC"
FT HELIX 1394..1404
FT /evidence="ECO:0007829|PDB:5VJC"
SQ SEQUENCE 2042 AA; 225980 MW; F79B31535CE56D2E CRC64;
MAEDTEYKKL PVEERCVHKL WKARVDGYEE AAKIFRELDD EKSPEWSKFA GLIKKMVVDS
NALAQEKGLE AALIFVENSG LAGRTVGDVM TGIVQKCIAA PKTKTKELSV QVALMYVEIE
KQEAVVEELV KGMEAKNPKI VSACVAATTL ALREFGHKVI GVKPLIKKLA PLMSDRDKTV
RDEGKQLAVE IYRWIGAAMK AQISTLPQVT LKELEDEFDK LKGERVEPSR YLKSQQEKQA
KIADAAATED AYNEDDGEAG VEEIDPMDLL DPVDILSKMP KDFYDKLEEK KWTLRKESLE
VLEKLLTDHP KLENGEYGAL VSALKKVITK DSNVVLVAMA GKCLALLAKG LAKRFSNYAS
ACVPSLLEKF KEKKPNVVTA LREAIDAIYA STSLEAQQES IVESLSNKNP SVKSETALFI
ARALTRTQPT ALNKKLLKLL TTSLVKTLNE PDPTVRDSSA EALGTLIKLM GDKAVTPLLA
DVDPLKMAKI KECQEKAEIK IKVAGPKKET RPASAPTAKA AAPAKTVAGS VDPKPVTRPA
TTGARKVLKK PATVSGGGAT SAPTAALKAG GKPLATEREI TPEELQEKSE EILPAEILNG
LVDSNWKNRL AAVEQLLGEI SGFDAKQAGI SQILIRTISG RKPGLKEMNF QVLKFKLDII
RSVAENYPLT TTTVDLVINE IIEKLADAKN GAAAADVLSA FAEATKLEYV VGKVLSFAFE
QKSPKVQSEA FNWVNRSIIE FGFQLQPKTL IEDVRKGVQS TNPTVRASAI QMVGTMSMYM
GKALMMFFDS EKPALKSQIQ VEFDKNVGEK PPKPVRGVQR SSGGTAGNSP DNEDDDGGAA
GEEEPINMAD LLPRVDIAPQ ITEALLKEMS DKDWKTRNEG LTKLQAIISE ARLIKPSIGD
LAPALAHRLV DSNAKIAQTT LAICEQLATA MGAGCRNHVR NLFPGFLHAL GDNKSFVRAA
ALNCINSFGE KGGYKEFFES EMIADALKGG SPALKTELWA WLADKLPGLP PKSVSKEDIH
SMVPHLYAHI CDRNADVRKN ANEAVLGIMI HLGFDAMNRA LDKQKPASKK DILAALEKAR
PNLPVKPLPK GKHQAPIPEE PKLKTVRGGG AGGAPGIQKS ATARVAGGQD KQVPARKKDE
DIDTSPLLCA NSAKNQRLLD EQKMKVLKWT FVTPREEFTE LLRDQMMTAN VNKALIANMF
HDDFRYHLKV IEQLSEDLAG NSKALVCNLD LILKWLTLRF YDTNPSVLIK GLEYLVQVFQ
VLIDEEYILA ENEGSSFVPH LLLKIGDPKD AVRNGVRRVL RQVILVFPFV KVFGYVMEGL
KSKNARQRTE CLDELTFLIE SYGMNICPQS AVREIARQIS DRDNSVRNAA LNCIVQVFFL
SGEKTYKMIG HLNEKDLSML DERIKRAKKT KKPTPPPSVD VPAPQRHDSI EIEDAEVGNG
CDELPPPDED GTFDQAPSSQ LLLLQQQLQQ LQQQAQQQKP SGPFGLDSQV ISEIEKDWVR
VDQMEQKPLL NVDISSLDEP IKVRPTRAGI HYPQEKFDRL ISRQHYMQQT LTTSPSSTAG
MTSGVSPYRS PMRLQHQQPQ QQLENNIPNL ADVLPKHDPQ LVKVIKGVSS TDTLKARAAI
NELAAIIEAP EKQAVLRDYE EIFIQNVLAQ FKNLSQIPSA QSVVVYQPLL SILYTFFHAN
ILGKTLSVAC IKNLMSALLN LMADPKLAVG DDSQYNKVIN GICLKVLDKV DFTNLNCALI
RLLRETCPEA KLPKFTDLLM KCIWRNVKML PERSNELNYD AVILEVHEFM LALPSTWWQN
RPSDTPMRTI KTILHNMAKV KGNAILQHLN QIPTHSELHT YLIRILKNFQ KDGSASGIGA
SPQRAKEIAS KRISHQTHDT VSQIFKLISD RDTKQQGLQK LYDFKQQNPD IDLSTFLQGS
SAPFHKYIEE GLAEIERNQN AGSTQDNRTD VNYQNNGPDP DFWMDRLQYH MTGGAAKLAS
ARSADDGSHM LDNKVVDENL CLNGMNAQKA SLIKREKRDM SPNRLQHLQA KLAQIKKENH
AQ
