MYO10_RAT
ID MYO10_RAT Reviewed; 2060 AA.
AC D3ZJP6;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Unconventional myosin-X;
DE AltName: Full=Unconventional myosin-10;
GN Name=Myo10;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-961; SER-964; SER-967 AND
RP THR-1160, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) OF 1178-1385, FUNCTION, SUBCELLULAR
RP LOCATION, DOMAIN, AND INTERACTION WITH
RP PHOSPHATIDYLINOSITOL-3,4,5-TRISPHOSPHATE.
RX PubMed=21965296; DOI=10.1091/mbc.e11-04-0354;
RA Lu Q., Yu J., Yan J., Wei Z., Zhang M.;
RT "Structural basis of the myosin X PH1(N)-PH2-PH1(C) tandem as a specific
RT and acute cellular PI(3,4,5)P(3) sensor.";
RL Mol. Biol. Cell 22:4268-4278(2011).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. MYO10 binds to
CC actin filaments and actin bundles and functions as a plus end-directed
CC motor. Moves with higher velocity and takes larger steps on actin
CC bundles than on single actin filaments (By similarity). The tail domain
CC binds to membranous compartments containing phosphatidylinositol 3,4,5-
CC trisphosphate or integrins, and mediates cargo transport along actin
CC filaments. Regulates cell shape, cell spreading and cell adhesion.
CC Stimulates the formation and elongation of filopodia. In hippocampal
CC neurons it induces the formation of dendritic filopodia by trafficking
CC the actin-remodeling protein VASP to the tips of filopodia, where it
CC promotes actin elongation. Plays a role in formation of the podosome
CC belt in osteoclasts (By similarity). {ECO:0000250|UniProtKB:Q9HD67,
CC ECO:0000269|PubMed:21965296}.
CC -!- SUBUNIT: Monomer, when in an inactive conformation in the cytosol.
CC Homodimer in its active, membrane-bound conformation; antiparallel
CC coiled coil-mediated dimer formation. Interacts with ECPAS. Interacts
CC with DCC and ITGB5; the presence of DCC inhibits ITGB5 binding.
CC Interacts with tubulin; ITGB5 or DCC binding inhibits tubulin binding.
CC Interacts strongly with CALM3 and weakly with CALM, the CALM3
CC interaction is essential for function in filopodial extension and
CC motility. Interacts with ITGB1, ITGB3 and ITGB5. Interacts with NEO1.
CC Interacts with VASP (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell
CC projection, lamellipodium {ECO:0000250}. Cell projection, ruffle
CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection,
CC filopodium tip {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}.
CC Cell projection, filopodium membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:21965296};
CC Peripheral membrane protein {ECO:0000269|PubMed:21965296}; Cytoplasmic
CC side {ECO:0000269|PubMed:21965296}. Note=May be in an inactive,
CC monomeric conformation in the cytosol. Detected in cytoplasmic punctae
CC and in cell projections. Colocalizes with actin fibers. Interacts with
CC microtubules. Undergoes forward and rearward movements within
CC filopodia. Interaction with membranes containing phosphatidylinositol
CC 3,4,5-trisphosphate mediates localization at filopodium membranes (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: Interaction between the motor domain and the tail leads to an
CC inactive, monomeric conformation. Phospholipid binding via the PH
CC domains leads to the formation of the active, dimeric form of the
CC protein and strongly increases actin-dependent ATPase activity and
CC motor activity (By similarity). {ECO:0000250}.
CC -!- DOMAIN: Interacts with membranes containing phosphatidylinositol-3,4,5-
CC trisphosphate via the PH domains. {ECO:0000269|PubMed:21965296}.
CC -!- DOMAIN: IQ 3 domain mediates high-affinity calcium-dependent binding to
CC CALM3/CLP. {ECO:0000250}.
CC -!- DOMAIN: The SAH (single alpha-helix) region is characterized by a high
CC content of charged residues which are predicted to stabilize the alpha-
CC helical structure by ionic bonds (By similarity). It can refold after
CC extension suggesting an in vivo force-dependent function (By
CC similarity). An anti-parallel coiled coil is located C-terminal to the
CC SAH domain and mediates dimerization (By similarity).
CC {ECO:0000250|UniProtKB:F8VQB6, ECO:0000250|UniProtKB:P79114,
CC ECO:0000250|UniProtKB:Q9HD67}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-10 (MYH10). {ECO:0000305}.
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DR RefSeq; XP_008758990.2; XM_008760768.2.
DR PDB; 3TFM; X-ray; 2.53 A; A=1178-1385.
DR PDBsum; 3TFM; -.
DR AlphaFoldDB; D3ZJP6; -.
DR SMR; D3ZJP6; -.
DR STRING; 10116.ENSRNOP00000063102; -.
DR iPTMnet; D3ZJP6; -.
DR PaxDb; D3ZJP6; -.
DR PeptideAtlas; D3ZJP6; -.
DR Ensembl; ENSRNOT00000065897; ENSRNOP00000063102; ENSRNOG00000010161.
DR GeneID; 310178; -.
DR CTD; 4651; -.
DR RGD; 1307193; Myo10.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000155469; -.
DR InParanoid; D3ZJP6; -.
DR OMA; CEKGNIQ; -.
DR OrthoDB; 16113at2759; -.
DR TreeFam; TF316834; -.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR PRO; PR:D3ZJP6; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000010161; Expressed in lung and 18 other tissues.
DR ExpressionAtlas; D3ZJP6; baseline and differential.
DR Genevisible; D3ZJP6; RN.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; ISO:RGD.
DR GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032433; C:filopodium tip; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; ISS:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0060002; F:plus-end directed microfilament motor activity; ISS:UniProtKB.
DR GO; GO:0030507; F:spectrin binding; ISO:RGD.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; ISS:UniProtKB.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0051489; P:regulation of filopodium assembly; ISS:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13202; FERM_C_MyoX; 1.
DR CDD; cd14873; MYSc_Myo10; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.25.40.530; -; 1.
DR Gene3D; 2.30.29.30; -; 4.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR031971; MYO10_CC.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR041797; MyoX_FERM_C.
DR InterPro; IPR040640; MyoX_N_SH3.
DR InterPro; IPR036124; MYSc_Myo10.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF16735; MYO10_CC; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00784; MyTH4; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF18597; SH3_19; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00295; B41; 1.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00139; MyTH4; 1.
DR SMART; SM00233; PH; 2.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; ATP-binding; Calmodulin-binding;
KW Cell membrane; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Membrane; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..2060
FT /note="Unconventional myosin-X"
FT /id="PRO_0000416245"
FT DOMAIN 63..739
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 742..771
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 765..794
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 788..817
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1214..1312
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1394..1499
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1549..1697
FT /note="MyTH4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1702..2046
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 619..641
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 814..882
FT /note="SAH"
FT /evidence="ECO:0000250|UniProtKB:Q9HD67"
FT REGION 971..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 883..933
FT /evidence="ECO:0000250|UniProtKB:Q9HD67"
FT COMPBIAS 1004..1033
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HD67"
FT BINDING 113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HD67"
FT BINDING 160..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HD67"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HD67"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD67"
FT MOD_RES 961
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 964
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 967
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1160
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT STRAND 1180..1186
FT /evidence="ECO:0007829|PDB:3TFM"
FT TURN 1189..1191
FT /evidence="ECO:0007829|PDB:3TFM"
FT STRAND 1195..1202
FT /evidence="ECO:0007829|PDB:3TFM"
FT STRAND 1205..1211
FT /evidence="ECO:0007829|PDB:3TFM"
FT STRAND 1215..1223
FT /evidence="ECO:0007829|PDB:3TFM"
FT HELIX 1225..1227
FT /evidence="ECO:0007829|PDB:3TFM"
FT STRAND 1229..1231
FT /evidence="ECO:0007829|PDB:3TFM"
FT HELIX 1233..1235
FT /evidence="ECO:0007829|PDB:3TFM"
FT STRAND 1237..1243
FT /evidence="ECO:0007829|PDB:3TFM"
FT STRAND 1245..1253
FT /evidence="ECO:0007829|PDB:3TFM"
FT STRAND 1258..1264
FT /evidence="ECO:0007829|PDB:3TFM"
FT HELIX 1265..1267
FT /evidence="ECO:0007829|PDB:3TFM"
FT STRAND 1269..1273
FT /evidence="ECO:0007829|PDB:3TFM"
FT TURN 1275..1277
FT /evidence="ECO:0007829|PDB:3TFM"
FT STRAND 1278..1284
FT /evidence="ECO:0007829|PDB:3TFM"
FT STRAND 1289..1293
FT /evidence="ECO:0007829|PDB:3TFM"
FT HELIX 1297..1311
FT /evidence="ECO:0007829|PDB:3TFM"
FT HELIX 1315..1318
FT /evidence="ECO:0007829|PDB:3TFM"
FT TURN 1328..1330
FT /evidence="ECO:0007829|PDB:3TFM"
FT STRAND 1332..1336
FT /evidence="ECO:0007829|PDB:3TFM"
FT HELIX 1337..1339
FT /evidence="ECO:0007829|PDB:3TFM"
FT STRAND 1340..1345
FT /evidence="ECO:0007829|PDB:3TFM"
FT STRAND 1354..1359
FT /evidence="ECO:0007829|PDB:3TFM"
FT STRAND 1362..1367
FT /evidence="ECO:0007829|PDB:3TFM"
FT HELIX 1371..1381
FT /evidence="ECO:0007829|PDB:3TFM"
SQ SEQUENCE 2060 AA; 237262 MW; 15CA25765D084CE6 CRC64;
MDSFFPEGAR VWLRENGQHF PSTVNSCAEG VVVFQTDYGQ VFTYKQSTIT NQKVTAMHPL
HEEGVDDMAS LTELHGGSIM YNLFQRYKRN QIYTYIGSII ASVNPYQPIA GLYERATMEQ
YSRCHLGELP PHIFAIANEC YRCLWKRHDN QCVLISGESG AGKTESTKLI LKFLSVISQH
SLDLCLQEKS SSVEQAILQS SPIMEAFGNA KTVYNNNSSR FGKFVQLNIC QKGNIQGGRI
VDYLLEKNRV VRQNPGERNY HIFYALLAGL DQGEREEFYL SLPENYHYLN QSGCTEDKTI
SDQESFRQVI EAMEVMQFSK EEVREVLRLL AGILHLGNIE FITAGGAQIS FKTALGRSAE
LLGLDPTQLT DALTQRSMFL RGEEILTPLS VQQAVDSRDS LAMALYARCF EWVIKKINSR
IKGKDDFKSI GILDIFGFEN FEVNHFEQFN INYANEKLQE YFNKHIFSLE QLEYSREGLV
WEDIDWIDNG ECLDLIEKKL GLLALINEES HFPQATDSTL LEKLHNQHAN NHFYVKPRVA
VNNFGVKHYA GEVQYDVRGI LEKNRDTFRD DLLNLLRESR FDFIYDLFEH ISSRNNQDTL
KCGSKHRRPT VSSQFKDSLH SLMATLSSSN PFFVRCIKPN TQKMPDQFDQ AVVLNQLRYS
GMLETVRIRK AGYAVRRPFQ DFYKRYKVLM RDLALPEDIR GKCTVLLQFY DASNSEWQLG
KTKVFLRESL EQKLEKRREE EIDRAAMVIR AHILGYLARK QYRKVLCGVV TIQKNYRAFL
ARKRFLHLKK AAIVFQKQLR GRLARKVYRQ LLAEKRELEE RKRLEEEKKR EEEERERKRA
QREADLLRAQ QEAETRKQQE LEALQKNQRE ADLTRELEKQ RENKQVEEIL RLEKEIEDLQ
RMKEQQELSL TEASLQKLQQ LRDEELRRLE DEACRAAQEF LESLNFDEID ECVRNIERSL
SVGSEISGEL SELAENASGE KPNFNFSQPY PEEEVDEGFE ADDDAFKDSP NPSEHGHSDQ
RTSGIRTSDD SSEEDPYMNY TVVPTSPSAD STVLLAASVQ DSASLHNSSS GESTYCMPQN
NGDLPSPDGD YDYDQDDYED GAITSGSSVT FSNSYGSQWS PDYRYSVGTY NSSGAYRFSS
EGAQSSFEDS EEDFDSRFDT DDELSYRRDS VYSCVTLPYF HSFLYMKGGL MNSWKRRWCV
LKDETFLWFR SKQEALKQGW LHKKGGGSST LSRRNWKKRW FVLRQSKLMY FENDSEEKLK
GTVEVRSAKE IIDNTNKENG IDIIMADRTF HLIAESPEDA SQWFSVLSQV HSSTDQEIRE
MHDEQANPQN AVGTLDVGLI DSVCASDSPD RPNSFVIITA NRVLHCNADT PEEMHHWITL
LQRSKGDTRV EGQEFIVRGW LHKEVKNSPK MSSLKLKKRW FVLTHNSLDY YKSSEKNALK
LGTLVLNSLC SVVPPDEKIF KETGYWNVTV YGRKHCYRLY TKLLNEATRW SSAIQNVTDT
KAPIDTPTQQ LIQDIKENCL NSDVVEQIYK RNPILRYTHH PLHSPLLPLP YGDINLNLLK
DKGYTTLQDE AIKIFNSLQQ LESMSDPIPI IQGILQTGHD LRPLRDELYC QLIKQTNKVP
HPGSVGNLYS WQILTCLSCT FLPSRGILKY LKFHLKRIRE QFPGTEMEKY ALFIYESLKK
TKCREFVPSR DEIEALIHRQ EMTSTVYCHG GGSCKITINS HTTAGEVVEK LIRGLAMEDS
RNMFALFEYN GQVDKAIESR TIVADVLAKF EKLAATSEAG DAPWKFYFKL YCFLDTDSMP
KDSVEFAFMF EQAHEAVIHG HHPAPEESLQ VLAALRLQYL QGDYTLHTSV PPLEEVYSLQ
RLKARISQST KTFTPYERLE KRRTSFLEGT LRRSFRTGTV ARQKVEEEQM LDMWIKEEIC
SARASIIDKW KKLQGVSQEQ AMAKYMALIK EWPGYGSTLF DVECKEGGFP QELWLGVSAD
AVSVYKRGEG KPLEVFQYEH ILSFGAPLAN TYKIVVDERE LLFETSEVVD VAKLMKAYIS
MIVKKRYSTT RSLSSQGSSR
