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CLIP-associating protein (Misexpression suppressor of ras 7) (Protein Multiple asters) (Mast) (Protein Orbit) (Protein chromosome bows)

 CLASP_DROME             Reviewed;        1491 AA.
Q9NBD7; A4V279; Q9NL57;
23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
27-SEP-2017, entry version 132.
RecName: Full=CLIP-associating protein;
AltName: Full=Misexpression suppressor of ras 7;
AltName: Full=Protein Multiple asters;
Short=Mast;
AltName: Full=Protein Orbit;
AltName: Full=Protein chromosome bows;
Name=chb; Synonyms=CLASP, Mast, MESR7, orbit; ORFNames=CG32435;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MICROTUBULES,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=10899121; DOI=10.1093/emboj/19.14.3668;
Lemos C.L., Sampaio P., Maiato H., Costa M., Omel'yanchuk L.V.,
Liberal V., Sunkel C.E.;
"Mast, a conserved microtubule-associated protein required for bipolar
mitotic spindle organization.";
EMBO J. 19:3668-3682(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11063696;
Huang A.M., Rubin G.M.;
"A misexpression screen identifies genes that can modulate RAS1
pathway signaling in Drosophila melanogaster.";
Genetics 156:1219-1230(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MICROTUBULES,
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=10747094; DOI=10.1083/jcb.149.1.153;
Inoue Y.H., do Carmo Avides M., Shiraki M., Deak P., Yamaguchi M.,
Nishimoto Y., Matsukage A., Glover D.M.;
"Orbit, a novel microtubule-associated protein essential for mitosis
in Drosophila melanogaster.";
J. Cell Biol. 149:153-166(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[7]
FUNCTION.
PubMed=12034769; DOI=10.1083/jcb.200201101;
Maiato H., Sampaio P., Lemos C.L., Findlay J., Carmena M.,
Earnshaw W.C., Sunkel C.E.;
"MAST/Orbit has a role in microtubule-kinetochore attachment and is
essential for chromosome alignment and maintenance of spindle
bipolarity.";
J. Cell Biol. 157:749-760(2002).
[8]
FUNCTION, INTERACTION WITH CLIP-190, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=12538517; DOI=10.1242/dev.00315;
Mathe E., Inoue Y.H., Palframan W., Brown G., Glover D.M.;
"Orbit/Mast, the CLASP orthologue of Drosophila, is required for
asymmetric stem cell and cystocyte divisions and development of the
polarised microtubule network that interconnects oocyte and nurse
cells during oogenesis.";
Development 130:901-915(2003).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15240569; DOI=10.1083/jcb.200402052;
Inoue Y.H., Savoian M.S., Suzuki T., Mathe E., Yamamoto M.-T.,
Glover D.M.;
"Mutations in orbit/mast reveal that the central spindle is comprised
of two microtubule populations, those that initiate cleavage and those
that propagate furrow ingression.";
J. Cell Biol. 166:49-60(2004).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=15207236; DOI=10.1016/j.neuron.2004.05.020;
Lee H., Engel U., Rusch J., Scherrer S., Sheard K., Van Vactor D.;
"The microtubule plus end tracking protein Orbit/MAST/CLASP acts
downstream of the tyrosine kinase Abl in mediating axon guidance.";
Neuron 42:913-926(2004).
[11]
FUNCTION.
PubMed=16303556; DOI=10.1016/j.cub.2005.09.054;
Goshima G., Wollman R., Stuurman N., Scholey J.M., Vale R.D.;
"Length control of the metaphase spindle.";
Curr. Biol. 15:1979-1988(2005).
[12]
FUNCTION.
PubMed=15592460; DOI=10.1038/ncb1207;
Maiato H., Khodjakov A., Rieder C.L.;
"Drosophila CLASP is required for the incorporation of microtubule
subunits into fluxing kinetochore fibres.";
Nat. Cell Biol. 7:42-47(2005).
[13]
FUNCTION.
PubMed=16723741; DOI=10.1242/jcs.02957;
Laycock J.E., Savoian M.S., Glover D.M.;
"Antagonistic activities of Klp10A and Orbit regulate spindle length,
bipolarity and function in vivo.";
J. Cell Sci. 119:2354-2361(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582; SER-626; SER-1120
AND SER-1123, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17372656; DOI=10.1039/b617545g;
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy
for (quantitative) phosphoproteomics: application to Drosophila
melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634; THR-648; SER-806;
SER-817; SER-820; SER-822; SER-824; SER-1120; SER-1123 AND SER-1124,
AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Microtubule plus-end tracking protein that promotes the
stabilization of dynamic microtubules. Required for several
aspects of mitotic spindle formation including the formation of
the overlapping central spindle microtubules and kinetochore
attachment. Required for the incorporation of tubulin subunits at
the plus ends of kinetochore microtubules during poleward
microtubule flux. Acts antagonistically to Klp10A and Klp67A to
maintain metaphase spindle length. Also required for guidance of
CNS axons downstream of Abl. May function to identify a subset of
microtubules that probe the peripheral growth cone domain, where
guidance signals exert their influence on cytoskeletal
organization. Also required during oogenesis for the organization
of the polarized microtubule network inside the 16-cell cyst that
ensures oocyte differentiation. {ECO:0000269|PubMed:10747094,
ECO:0000269|PubMed:10899121, ECO:0000269|PubMed:12034769,
ECO:0000269|PubMed:12538517, ECO:0000269|PubMed:15207236,
ECO:0000269|PubMed:15240569, ECO:0000269|PubMed:15592460,
ECO:0000269|PubMed:16303556, ECO:0000269|PubMed:16723741}.
-!- SUBUNIT: Interacts with CLIP-190 and microtubules.
{ECO:0000269|PubMed:10747094, ECO:0000269|PubMed:10899121,
ECO:0000269|PubMed:12538517}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome.
Cytoplasm, cytoskeleton, spindle. Cell projection, growth cone.
Cleavage furrow. Note=Localizes to punctate cytoplasmic foci in
interphase. Concentrates on spindle microtubules from prophase to
late anaphase. Accumulates on the mid-part of the central spindle
during telophase where it remains until cleavage. Subsequently
appears at the periphery of the reforming karyomeres. Also
localizes to the spindle remnant, cleavage furrows and the fusome
of the 16-cell ovarian cyst. Localizes to the axonal growth cone
within neurons.
-!- TISSUE SPECIFICITY: Expressed in testis and ovary.
{ECO:0000269|PubMed:10899121, ECO:0000269|PubMed:12538517}.
-!- DEVELOPMENTAL STAGE: Expressed throughout development, although
expression is low in pupae. At late developmental stages
expression becomes pronounced in muscles and the nervous system,
particularly within the intersegmental nerve b (ISNb).
{ECO:0000269|PubMed:10747094, ECO:0000269|PubMed:10899121,
ECO:0000269|PubMed:15207236}.
-!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA94248.1; Type=Frameshift; Positions=914, 917, 922; Evidence={ECO:0000305};
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EMBL; AF250842; AAF66060.1; -; mRNA.
EMBL; AF195498; AAG28470.1; -; mRNA.
EMBL; AB031048; BAA94248.1; ALT_FRAME; mRNA.
EMBL; AE014296; AAN12151.1; -; Genomic_DNA.
EMBL; AE014296; AAN12152.1; -; Genomic_DNA.
EMBL; AE014296; AAN12153.1; -; Genomic_DNA.
EMBL; AY069579; AAL39724.1; -; mRNA.
RefSeq; NP_524651.2; NM_079912.4.
RefSeq; NP_730596.1; NM_168882.2.
RefSeq; NP_730597.1; NM_168883.1.
UniGene; Dm.1413; -.
PDB; 4G3A; X-ray; 1.99 A; A/B=1-229.
PDBsum; 4G3A; -.
ProteinModelPortal; Q9NBD7; -.
SMR; Q9NBD7; -.
BioGrid; 68704; 36.
IntAct; Q9NBD7; 7.
MINT; MINT-955479; -.
STRING; 7227.FBpp0088469; -.
iPTMnet; Q9NBD7; -.
PaxDb; Q9NBD7; -.
PRIDE; Q9NBD7; -.
EnsemblMetazoa; FBtr0089460; FBpp0088469; FBgn0021760.
EnsemblMetazoa; FBtr0089461; FBpp0088470; FBgn0021760.
EnsemblMetazoa; FBtr0089462; FBpp0088471; FBgn0021760.
GeneID; 43901; -.
KEGG; dme:Dmel_CG32435; -.
CTD; 43901; -.
FlyBase; FBgn0021760; chb.
eggNOG; KOG2956; Eukaryota.
eggNOG; ENOG410ZMY0; LUCA.
GeneTree; ENSGT00390000001762; -.
InParanoid; Q9NBD7; -.
KO; K16578; -.
OMA; NPQYVWD; -.
OrthoDB; EOG091G026T; -.
PhylomeDB; Q9NBD7; -.
GenomeRNAi; 43901; -.
PRO; PR:Q9NBD7; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0021760; -.
Genevisible; Q9NBD7; DM.
GO; GO:0005813; C:centrosome; IDA:FlyBase.
GO; GO:0000775; C:chromosome, centromeric region; IDA:FlyBase.
GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005881; C:cytoplasmic microtubule; IEA:InterPro.
GO; GO:0045169; C:fusome; IDA:FlyBase.
GO; GO:0045172; C:germline ring canal; IDA:FlyBase.
GO; GO:0030426; C:growth cone; IDA:FlyBase.
GO; GO:0005828; C:kinetochore microtubule; IEA:InterPro.
GO; GO:0005875; C:microtubule associated complex; IDA:FlyBase.
GO; GO:0005815; C:microtubule organizing center; IDA:FlyBase.
GO; GO:0035371; C:microtubule plus-end; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0005827; C:polar microtubule; IDA:FlyBase.
GO; GO:0005876; C:spindle microtubule; IDA:FlyBase.
GO; GO:0000922; C:spindle pole; IDA:FlyBase.
GO; GO:0005525; F:GTP binding; IDA:FlyBase.
GO; GO:0043515; F:kinetochore binding; IEA:InterPro.
GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
GO; GO:0051010; F:microtubule plus-end binding; IEA:InterPro.
GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:FlyBase.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0007282; P:cystoblast division; IMP:FlyBase.
GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:FlyBase.
GO; GO:0035099; P:hemocyte migration; IMP:FlyBase.
GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:FlyBase.
GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
GO; GO:0000022; P:mitotic spindle elongation; IMP:FlyBase.
GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IGI:FlyBase.
GO; GO:0016325; P:oocyte microtubule cytoskeleton organization; IMP:FlyBase.
GO; GO:0048477; P:oogenesis; IMP:FlyBase.
GO; GO:0030723; P:ovarian fusome organization; IMP:FlyBase.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:UniProtKB.
GO; GO:0046602; P:regulation of mitotic centrosome separation; IMP:FlyBase.
GO; GO:0051225; P:spindle assembly; IMP:FlyBase.
GO; GO:0007051; P:spindle organization; IMP:FlyBase.
GO; GO:0019827; P:stem cell population maintenance; IMP:FlyBase.
Gene3D; 1.25.10.10; -; 2.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR028399; CLASP_1.
InterPro; IPR024395; CLASP_N_dom.
InterPro; IPR021133; HEAT_type_2.
InterPro; IPR034085; TOG.
PANTHER; PTHR21567:SF49; PTHR21567:SF49; 1.
Pfam; PF12348; CLASP_N; 2.
SMART; SM01349; TOG; 4.
SUPFAM; SSF48371; SSF48371; 5.
PROSITE; PS50077; HEAT_REPEAT; 2.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein;
Differentiation; Microtubule; Mitosis; Nucleus; Oogenesis;
Phosphoprotein; Reference proteome; Repeat.
CHAIN 1 1491 CLIP-associating protein.
/FTId=PRO_0000272276.
REPEAT 44 82 HEAT 1.
REPEAT 85 123 HEAT 2.
REPEAT 163 201 HEAT 3.
REPEAT 402 440 HEAT 4.
REPEAT 874 912 HEAT 5.
REPEAT 955 993 HEAT 6.
REPEAT 1289 1327 HEAT 7.
REPEAT 1408 1446 HEAT 8.
COMPBIAS 1057 1133 Ser-rich.
MOD_RES 582 582 Phosphoserine.
{ECO:0000269|PubMed:17372656}.
MOD_RES 626 626 Phosphoserine.
{ECO:0000269|PubMed:17372656}.
MOD_RES 634 634 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 648 648 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 806 806 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 817 817 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 820 820 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 822 822 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 824 824 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1120 1120 Phosphoserine.
{ECO:0000269|PubMed:17372656,
ECO:0000269|PubMed:18327897}.
MOD_RES 1123 1123 Phosphoserine.
{ECO:0000269|PubMed:17372656,
ECO:0000269|PubMed:18327897}.
MOD_RES 1124 1124 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CONFLICT 744 744 A -> P (in Ref. 3; BAA94248).
{ECO:0000305}.
HELIX 9 15 {ECO:0000244|PDB:4G3A}.
TURN 16 18 {ECO:0000244|PDB:4G3A}.
HELIX 21 36 {ECO:0000244|PDB:4G3A}.
HELIX 47 58 {ECO:0000244|PDB:4G3A}.
HELIX 63 80 {ECO:0000244|PDB:4G3A}.
HELIX 81 86 {ECO:0000244|PDB:4G3A}.
HELIX 88 98 {ECO:0000244|PDB:4G3A}.
HELIX 104 119 {ECO:0000244|PDB:4G3A}.
HELIX 125 136 {ECO:0000244|PDB:4G3A}.
HELIX 142 159 {ECO:0000244|PDB:4G3A}.
TURN 161 163 {ECO:0000244|PDB:4G3A}.
HELIX 167 169 {ECO:0000244|PDB:4G3A}.
HELIX 170 175 {ECO:0000244|PDB:4G3A}.
HELIX 176 178 {ECO:0000244|PDB:4G3A}.
HELIX 182 199 {ECO:0000244|PDB:4G3A}.
HELIX 200 202 {ECO:0000244|PDB:4G3A}.
HELIX 203 208 {ECO:0000244|PDB:4G3A}.
STRAND 211 213 {ECO:0000244|PDB:4G3A}.
HELIX 215 229 {ECO:0000244|PDB:4G3A}.
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


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