CLASP_DROME
ID CLASP_DROME Reviewed; 1491 AA.
AC Q9NBD7; A4V279; Q9NL57;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=CLIP-associating protein;
DE AltName: Full=Misexpression suppressor of ras 7;
DE AltName: Full=Protein Multiple asters;
DE Short=Mast;
DE AltName: Full=Protein Orbit;
DE AltName: Full=Protein chromosome bows;
GN Name=chb; Synonyms=CLASP, Mast, MESR7, orbit; ORFNames=CG32435;
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 [MRNA], FUNCTION, INTERACTION WITH MICROTUBULES,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10899121; DOI=10.1093/emboj/19.14.3668;
RA Lemos C.L., Sampaio P., Maiato H., Costa M., Omel'yanchuk L.V., Liberal V.,
RA Sunkel C.E.;
RT "Mast, a conserved microtubule-associated protein required for bipolar
RT mitotic spindle organization.";
RL EMBO J. 19:3668-3682(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11063696; DOI=10.1093/genetics/156.3.1219;
RA Huang A.M., Rubin G.M.;
RT "A misexpression screen identifies genes that can modulate RAS1 pathway
RT signaling in Drosophila melanogaster.";
RL Genetics 156:1219-1230(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MICROTUBULES,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=10747094; DOI=10.1083/jcb.149.1.153;
RA Inoue Y.H., do Carmo Avides M., Shiraki M., Deak P., Yamaguchi M.,
RA Nishimoto Y., Matsukage A., Glover D.M.;
RT "Orbit, a novel microtubule-associated protein essential for mitosis in
RT Drosophila melanogaster.";
RL J. Cell Biol. 149:153-166(2000).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [7]
RP FUNCTION.
RX PubMed=12034769; DOI=10.1083/jcb.200201101;
RA Maiato H., Sampaio P., Lemos C.L., Findlay J., Carmena M., Earnshaw W.C.,
RA Sunkel C.E.;
RT "MAST/Orbit has a role in microtubule-kinetochore attachment and is
RT essential for chromosome alignment and maintenance of spindle bipolarity.";
RL J. Cell Biol. 157:749-760(2002).
RN [8]
RP FUNCTION, INTERACTION WITH CLIP-190, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12538517; DOI=10.1242/dev.00315;
RA Mathe E., Inoue Y.H., Palframan W., Brown G., Glover D.M.;
RT "Orbit/Mast, the CLASP orthologue of Drosophila, is required for asymmetric
RT stem cell and cystocyte divisions and development of the polarised
RT microtubule network that interconnects oocyte and nurse cells during
RT oogenesis.";
RL Development 130:901-915(2003).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15240569; DOI=10.1083/jcb.200402052;
RA Inoue Y.H., Savoian M.S., Suzuki T., Mathe E., Yamamoto M.-T., Glover D.M.;
RT "Mutations in orbit/mast reveal that the central spindle is comprised of
RT two microtubule populations, those that initiate cleavage and those that
RT propagate furrow ingression.";
RL J. Cell Biol. 166:49-60(2004).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15207236; DOI=10.1016/j.neuron.2004.05.020;
RA Lee H., Engel U., Rusch J., Scherrer S., Sheard K., Van Vactor D.;
RT "The microtubule plus end tracking protein Orbit/MAST/CLASP acts downstream
RT of the tyrosine kinase Abl in mediating axon guidance.";
RL Neuron 42:913-926(2004).
RN [11]
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 [12]
RP FUNCTION.
RX PubMed=15592460; DOI=10.1038/ncb1207;
RA Maiato H., Khodjakov A., Rieder C.L.;
RT "Drosophila CLASP is required for the incorporation of microtubule subunits
RT into fluxing kinetochore fibres.";
RL Nat. Cell Biol. 7:42-47(2005).
RN [13]
RP FUNCTION.
RX PubMed=16723741; DOI=10.1242/jcs.02957;
RA Laycock J.E., Savoian M.S., Glover D.M.;
RT "Antagonistic activities of Klp10A and Orbit regulate spindle length,
RT bipolarity and function in vivo.";
RL J. Cell Sci. 119:2354-2361(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582; SER-626; SER-1120 AND
RP SER-1123, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634; THR-648; SER-806;
RP SER-817; SER-820; SER-822; SER-824; SER-1120; SER-1123 AND SER-1124, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Microtubule plus-end tracking protein that promotes the
CC stabilization of dynamic microtubules. Required for several aspects of
CC mitotic spindle formation including the formation of the overlapping
CC central spindle microtubules and kinetochore attachment. Required for
CC the incorporation of tubulin subunits at the plus ends of kinetochore
CC microtubules during poleward microtubule flux. Acts antagonistically to
CC Klp10A and Klp67A to maintain metaphase spindle length. Also required
CC for guidance of CNS axons downstream of Abl. May function to identify a
CC subset of microtubules that probe the peripheral growth cone domain,
CC where guidance signals exert their influence on cytoskeletal
CC organization. Also required during oogenesis for the organization of
CC the polarized microtubule network inside the 16-cell cyst that ensures
CC oocyte differentiation. {ECO:0000269|PubMed:10747094,
CC ECO:0000269|PubMed:10899121, ECO:0000269|PubMed:12034769,
CC ECO:0000269|PubMed:12538517, ECO:0000269|PubMed:15207236,
CC ECO:0000269|PubMed:15240569, ECO:0000269|PubMed:15592460,
CC ECO:0000269|PubMed:16303556, ECO:0000269|PubMed:16723741}.
CC -!- SUBUNIT: Interacts with CLIP-190 and microtubules.
CC {ECO:0000269|PubMed:10747094, ECO:0000269|PubMed:10899121,
CC ECO:0000269|PubMed:12538517}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome. Cytoplasm,
CC cytoskeleton, spindle. Cell projection, growth cone. Cleavage furrow.
CC Note=Localizes to punctate cytoplasmic foci in interphase. Concentrates
CC on spindle microtubules from prophase to late anaphase. Accumulates on
CC the mid-part of the central spindle during telophase where it remains
CC until cleavage. Subsequently appears at the periphery of the reforming
CC karyomeres. Also localizes to the spindle remnant, cleavage furrows and
CC the fusome of the 16-cell ovarian cyst. Localizes to the axonal growth
CC cone within neurons.
CC -!- TISSUE SPECIFICITY: Expressed in testis and ovary.
CC {ECO:0000269|PubMed:10899121, ECO:0000269|PubMed:12538517}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, although
CC expression is low in pupae. At late developmental stages expression
CC becomes pronounced in muscles and the nervous system, particularly
CC within the intersegmental nerve b (ISNb). {ECO:0000269|PubMed:10747094,
CC ECO:0000269|PubMed:10899121, ECO:0000269|PubMed:15207236}.
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA94248.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF250842; AAF66060.1; -; mRNA.
DR EMBL; AF195498; AAG28470.1; -; mRNA.
DR EMBL; AB031048; BAA94248.1; ALT_FRAME; mRNA.
DR EMBL; AE014296; AAN12151.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12152.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12153.1; -; Genomic_DNA.
DR EMBL; AY069579; AAL39724.1; -; mRNA.
DR RefSeq; NP_524651.2; NM_079912.4.
DR RefSeq; NP_730596.1; NM_168882.2.
DR RefSeq; NP_730597.1; NM_168883.1.
DR PDB; 4G3A; X-ray; 1.99 A; A/B=1-229.
DR PDBsum; 4G3A; -.
DR AlphaFoldDB; Q9NBD7; -.
DR SMR; Q9NBD7; -.
DR BioGRID; 68704; 37.
DR IntAct; Q9NBD7; 4.
DR STRING; 7227.FBpp0088469; -.
DR iPTMnet; Q9NBD7; -.
DR PaxDb; Q9NBD7; -.
DR PRIDE; Q9NBD7; -.
DR DNASU; 43901; -.
DR EnsemblMetazoa; FBtr0089460; FBpp0088469; FBgn0021760.
DR EnsemblMetazoa; FBtr0089461; FBpp0088470; FBgn0021760.
DR EnsemblMetazoa; FBtr0089462; FBpp0088471; FBgn0021760.
DR GeneID; 43901; -.
DR KEGG; dme:Dmel_CG32435; -.
DR CTD; 43901; -.
DR FlyBase; FBgn0021760; chb.
DR VEuPathDB; VectorBase:FBgn0021760; -.
DR eggNOG; KOG2956; Eukaryota.
DR GeneTree; ENSGT00940000168069; -.
DR HOGENOM; CLU_005060_0_0_1; -.
DR InParanoid; Q9NBD7; -.
DR OMA; MFMDTHT; -.
DR OrthoDB; 66632at2759; -.
DR PhylomeDB; Q9NBD7; -.
DR SignaLink; Q9NBD7; -.
DR BioGRID-ORCS; 43901; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 43901; -.
DR PRO; PR:Q9NBD7; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0021760; Expressed in embryonic/larval hemocyte (Drosophila) and 24 other tissues.
DR Genevisible; Q9NBD7; DM.
DR GO; GO:0045180; C:basal cortex; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:FlyBase.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0070938; C:contractile ring; IDA:CACAO.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0045169; C:fusome; IDA:FlyBase.
DR GO; GO:0045172; C:germline ring canal; IDA:FlyBase.
DR GO; GO:0030426; C:growth cone; IDA:FlyBase.
DR GO; GO:0000776; C:kinetochore; IDA:FlyBase.
DR GO; GO:0005875; C:microtubule associated complex; IDA:FlyBase.
DR GO; GO:0005815; C:microtubule organizing center; IDA:FlyBase.
DR GO; GO:0035371; C:microtubule plus-end; IDA:FlyBase.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IDA:CACAO.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005827; C:polar microtubule; IDA:FlyBase.
DR GO; GO:0045170; C:spectrosome; IDA:CACAO.
DR GO; GO:0005819; C:spindle; IDA:FlyBase.
DR GO; GO:0070732; C:spindle envelope; IDA:CACAO.
DR GO; GO:0005876; C:spindle microtubule; IDA:FlyBase.
DR GO; GO:0000922; C:spindle pole; IDA:FlyBase.
DR GO; GO:0005525; F:GTP binding; IDA:FlyBase.
DR GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007282; P:cystoblast division; IMP:FlyBase.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:FlyBase.
DR GO; GO:0035099; P:hemocyte migration; IMP:FlyBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:FlyBase.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0000022; P:mitotic spindle elongation; IMP:FlyBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
DR GO; GO:0016325; P:oocyte microtubule cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0030723; P:ovarian fusome organization; IMP:FlyBase.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:UniProtKB.
DR GO; GO:0046602; P:regulation of mitotic centrosome separation; IMP:FlyBase.
DR GO; GO:0051225; P:spindle assembly; IMP:FlyBase.
DR GO; GO:0007051; P:spindle organization; IMP:FlyBase.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:FlyBase.
DR Gene3D; 1.25.10.10; -; 4.
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 Pfam; PF12348; CLASP_N; 2.
DR SMART; SM01349; TOG; 4.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell projection; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Microtubule; Mitosis;
KW Nucleus; Oogenesis; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1491
FT /note="CLIP-associating protein"
FT /id="PRO_0000272276"
FT REPEAT 44..82
FT /note="HEAT 1"
FT REPEAT 85..123
FT /note="HEAT 2"
FT REPEAT 163..201
FT /note="HEAT 3"
FT REPEAT 402..440
FT /note="HEAT 4"
FT REPEAT 874..912
FT /note="HEAT 5"
FT REPEAT 955..993
FT /note="HEAT 6"
FT REPEAT 1289..1327
FT /note="HEAT 7"
FT REPEAT 1408..1446
FT /note="HEAT 8"
FT REGION 537..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 648
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1120
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 1123
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 1124
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 744
FT /note="A -> P (in Ref. 3; BAA94248)"
FT /evidence="ECO:0000305"
FT HELIX 9..15
FT /evidence="ECO:0007829|PDB:4G3A"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:4G3A"
FT HELIX 21..36
FT /evidence="ECO:0007829|PDB:4G3A"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:4G3A"
FT HELIX 63..80
FT /evidence="ECO:0007829|PDB:4G3A"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:4G3A"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:4G3A"
FT HELIX 104..119
FT /evidence="ECO:0007829|PDB:4G3A"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:4G3A"
FT HELIX 142..159
FT /evidence="ECO:0007829|PDB:4G3A"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:4G3A"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:4G3A"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:4G3A"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:4G3A"
FT HELIX 182..199
FT /evidence="ECO:0007829|PDB:4G3A"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:4G3A"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:4G3A"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:4G3A"
FT HELIX 215..229
FT /evidence="ECO:0007829|PDB:4G3A"
SQ SEQUENCE 1491 AA; 165576 MW; 166792C05E4E842F CRC64;
MAYRKPSDLD GFIQQMPKAD MRVKVQLAED LVTFLSDDTN SIVCTDMGFL IDGLMPWLTG
SHFKIAQKSL EAFSELIKRL GSDFNAYTAT VLPHVIDRLG DSRDTVREKA QLLLRDLMEH
RVLPPQALID KLATSCFKHK NAKVREEFLQ TIVNALHEYG TQQLSVRVYI PPVCALLGDP
TVNVREAAIQ TLVEIYKHVG DRLRPDLRRM DDVPASKLAM LEQKFDQVKQ EGLLLPSALK
NTNGNGVGLD EADNIGLRER PTRMIKRPLH SAVSSSLRPK PNVNDVTGDA GAVTMESFES
SFEVVPQLNI FHAKDMDDIY KQVLVIISDK NADWEKRVDA LKKIRALLIL SYHTQPQFVA
VQLKELSLSF VDILKEELRS QVIREACITI AYMSKTLRNK LDAFCWSILE HLINLIQNSA
KVIASASTIA LKYIIKYTHA PKLLKIYTDT LNQSKSKDIR STLCELMVLL FEEWQTKALE
RNATVLRDTL KKSIGDADCD ARRHSRYAYW AFRRHFPELA DQIYGTLDIA AQRALERERE
GGGGGGTGTG TGTAPETRRT VSRIGRTPGT LQKPTPSMRS ISAVDTAAAQ RAKVRAQYTL
YSRQRKPLGP NNSNQASMTG AAASGSLPRP RLNSNSGGTP ATTPGSVTPR PRGRAGVSQS
QPGSRSTSPS TKLRDQYGGI GNYYRGATGA IPKKASGIPR STASSRETSP TRSGGGLMKR
SMYSTGAGSR RTPERNNPVR PSAAARLLAQ SREAEHTLGV GDDGQPDYVS GDYMRSGGMR
MGRKLMGRDE SDDIDSEASS VCSERSFDSS YTRGNKSNYS LSGSHTRLDW STQRAPFDDI
ETIIQFCAST HWSERKDGLI SLTQYLADGK ELTQQQLKCV LDMFRKMFMD THTKVYSLFL
DTVTELILVH ANELHEWLFI LLTRLFNKLG TDLLNSMHSK IWKTLQVVHE YFPTQLQLKE
LFRIISDSTQ TPTTKTRIAI LRFLTDLANT YCKSSDFPSD QSQACERTVL KLAQLAADQK
SMELRSQARS CLVALYNLNT PQMTLLLADL PKVYQDSARS CIHSHMRRQS QSCNSGANSP
SSSPLSSSSP KPLQSPSVGP FASLQSHHHQ LSISSTSPRS RQSSVEQELL FSSELDIQHN
IQKTSEEIRH CFGGQYQTAL APNGFNGHLQ YHDQGQQDSC ASLSSNSKTQ SSANTTQSNT
PESATMRLDN LERERTTQNA KSPTDDAKVI TVSINMAENG ELILASNLME SEVVRVALTL
TKDQPVELLQ TSLTNLGICI KGGNCELPNK HFRSIMRMLL NILEAEHTDV VIAGLHVLSK
IMRSNKMRHN WMHFLELILL KIIQCYQHSK EALRDIDSMI PRIAPSLPLD LSINIVNPVI
ATGEFPTNLC AIKILLEVTE HHGSEITDAH LDIVFPNLAR SADDTQSMVR KAAVFCIVKL
YFVLGEEKVK PKLSVLNPSK VRLLNVYIEK QRNCISGGGS STKNSSAASS S
