MYO10_HUMAN
ID MYO10_HUMAN Reviewed; 2058 AA.
AC Q9HD67; A7E2D1; O94893; Q8IVX5; Q9NYM7; Q9P110; Q9P111; Q9UHF6;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Unconventional myosin-X;
DE AltName: Full=Unconventional myosin-10;
GN Name=MYO10; Synonyms=KIAA0799;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND VARIANTS TRP-324 AND THR-1663.
RX PubMed=10984435; DOI=10.1242/jcs.113.19.3439;
RA Berg J.S., Derfler B.H., Pennisi C.M., Corey D.P., Cheney R.E.;
RT "Myosin-X, a novel myosin with pleckstrin homology domains, associates with
RT regions of dynamic actin.";
RL J. Cell Sci. 113:3439-3451(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS TYR-148 AND THR-1663, AND
RP INTERACTION WITH CALM3/CLP.
RX PubMed=11278607; DOI=10.1074/jbc.m010056200;
RA Rogers M.S., Strehler E.E.;
RT "The tumor-sensitive calmodulin-like protein is a specific light chain of
RT human unconventional myosin X.";
RL J. Biol. Chem. 276:12182-12189(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT TRP-324.
RC TISSUE=Colon adenocarcinoma;
RA Takada T., O'Farrell T.J., Anderson J.T., Pourmotabbed T.;
RT "Cloning of human myosin X.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-1663.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [5]
RP SEQUENCE REVISION.
RA Nagase T., Kikuno R., Yamakawa H., Ohara O.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP THR-1663.
RC TISSUE=Brain, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-126 (ISOFORM HEADLESS).
RA Hillier L., Allen M., Bowles L., Dubuque T., Geisel G., Jost S.,
RA Krizman D., Kucaba T., Lacy M., Le N., Lennon G., Marra M., Martin J.,
RA Moore B., Schellenberg K., Steptoe M., Tan F., Theising B., White Y.,
RA Wylie T., Waterston R., Wilson R.;
RT "The WashU-Merck EST project.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 347-495 (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=10610710; DOI=10.1006/geno.1999.5997;
RA Rojas K., Serrano de la Pena L., Gallardo T., Simmons A., Nyce K.,
RA McGrath R., Considine E., Vasko A.J., Peterson E., Grady D., Cox R.,
RA Andrew L.J., Lovett M., Overhauser J., Williams C.J.;
RT "Physical map and characterization of transcripts in the candidate interval
RT for familial chondrocalcinosis at chromosome 5p15.1.";
RL Genomics 62:177-183(1999).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-965, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP ALTERNATIVE SPLICING (ISOFORM HEADLESS).
RX PubMed=16371656; DOI=10.1242/jcs.02726;
RA Sousa A.D., Berg J.S., Robertson B.W., Meeker R.B., Cheney R.E.;
RT "Myo10 in brain: developmental regulation, identification of a headless
RT isoform and dynamics in neurons.";
RL J. Cell Sci. 119:184-194(2006).
RN [12]
RP FUNCTION IN REGULATION OF FILOPODIA ASSEMBLY AND REGULATION OF CELL SHAPE.
RX PubMed=16894163; DOI=10.1073/pnas.0602443103;
RA Bohil A.B., Robertson B.W., Cheney R.E.;
RT "Myosin-X is a molecular motor that functions in filopodia formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12411-12416(2006).
RN [13]
RP FUNCTION, IQ3 DOMAIN, AND MUTAGENESIS OF PHE-795.
RX PubMed=18570893; DOI=10.1016/j.febslet.2008.05.051;
RA Bennett R.D., Caride A.J., Mauer A.S., Strehler E.E.;
RT "Interaction with the IQ3 motif of myosin-10 is required for calmodulin-
RT like protein-dependent filopodial extension.";
RL FEBS Lett. 582:2377-2381(2008).
RN [14]
RP INTERACTION WITH ECPAS.
RX PubMed=20682791; DOI=10.1074/jbc.m110.154120;
RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E.,
RA Rechsteiner M.;
RT "A protein interaction network for Ecm29 links the 26 S proteasome to
RT molecular motors and endosomal components.";
RL J. Biol. Chem. 285:31616-31633(2010).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1486-2058 IN COMPLEX WITH DCC,
RP INTERACTION WITH DCC; ITGB5 AND TUBULIN, AND MUTAGENESIS OF LYS-1647;
RP LYS-1650 AND PHE-2002.
RX PubMed=21642953; DOI=10.1038/emboj.2011.177;
RA Hirano Y., Hatano T., Takahashi A., Toriyama M., Inagaki N., Hakoshima T.;
RT "Structural basis of cargo recognition by the myosin-X MyTH4-FERM domain.";
RL EMBO J. 30:2734-2747(2011).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1503-2047 IN COMPLEX WITH DCC,
RP INTERACTION WITH DCC, AND MUTAGENESIS OF 1718-SER-HIS-1719.
RX PubMed=21321230; DOI=10.1073/pnas.1016567108;
RA Wei Z., Yan J., Lu Q., Pan L., Zhang M.;
RT "Cargo recognition mechanism of myosin X revealed by the structure of its
RT tail MyTH4-FERM tandem in complex with the DCC P3 domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:3572-3577(2011).
RN [18]
RP STRUCTURE BY NMR OF 883-933, SUBUNIT, SAH DOMAIN, COILED COIL, AND
RP MUTAGENESIS OF LEU-893 AND LYS-904.
RX PubMed=23012428; DOI=10.1073/pnas.1208642109;
RA Lu Q., Ye F., Wei Z., Wen Z., Zhang M.;
RT "Antiparallel coiled-coil-mediated dimerization of myosin X.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17388-17393(2012).
RN [19] {ECO:0007744|PDB:5I0H, ECO:0007744|PDB:5I0I, ECO:0007744|PDB:5KG8}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-741 IN COMPLEX WITH ADP, AND
RP FUNCTION.
RX PubMed=27580874; DOI=10.1038/ncomms12456;
RA Ropars V., Yang Z., Isabet T., Blanc F., Zhou K., Lin T., Liu X.,
RA Hissier P., Samazan F., Amigues B., Yang E.D., Park H., Pylypenko O.,
RA Cecchini M., Sindelar C.V., Sweeney H.L., Houdusse A.;
RT "The myosin X motor is optimized for movement on actin bundles.";
RL Nat. Commun. 7:12456-12456(2016).
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 (PubMed:27580874). The tail
CC domain binds to membranous compartments containing phosphatidylinositol
CC 3,4,5-trisphosphate or integrins, and mediates cargo transport along
CC actin filaments. Regulates cell shape, cell spreading and cell
CC adhesion. Stimulates the formation and elongation of filopodia. In
CC hippocampal neurons it induces the formation of dendritic filopodia by
CC trafficking the actin-remodeling protein VASP to the tips of filopodia,
CC where it promotes actin elongation. Plays a role in formation of the
CC podosome belt in osteoclasts. {ECO:0000269|PubMed:16894163,
CC ECO:0000269|PubMed:18570893, ECO:0000269|PubMed:27580874}.
CC -!- FUNCTION: [Isoform Headless]: Functions as a dominant-negative
CC regulator of isoform 1, suppressing its filopodia-inducing and axon
CC outgrowth-promoting activities. In hippocampal neurons, it increases
CC VASP retention in spine heads to induce spine formation and spine head
CC expansion (By similarity). {ECO:0000250|UniProtKB:F8VQB6}.
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 strongly with CALM3 and
CC weakly with CALM, the CALM3 interaction is essential for function in
CC filopodial extension and motility. Interacts with ECPAS. Interacts with
CC NEO1. Interacts with ITGB1 and ITGB3. Interacts with VASP (By
CC similarity). Interacts with DCC and ITGB5; the presence of DCC inhibits
CC ITGB5 binding. Interacts with tubulin; ITGB5 or DCC binding inhibits
CC tubulin binding. {ECO:0000250, ECO:0000269|PubMed:11278607,
CC ECO:0000269|PubMed:20682791, ECO:0000269|PubMed:21321230,
CC ECO:0000269|PubMed:21642953, ECO:0000269|PubMed:23012428}.
CC -!- INTERACTION:
CC Q9HD67; P62158: CALM3; NbExp=2; IntAct=EBI-307061, EBI-397435;
CC Q9HD67; P27482: CALML3; NbExp=3; IntAct=EBI-307061, EBI-747537;
CC Q9HD67; P43146: DCC; NbExp=7; IntAct=EBI-307061, EBI-1222919;
CC Q9HD67; P18084: ITGB5; NbExp=2; IntAct=EBI-307061, EBI-1223434;
CC Q9HD67; Q63155: Dcc; Xeno; NbExp=3; IntAct=EBI-307061, EBI-1798965;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10984435}.
CC Cell projection, lamellipodium {ECO:0000269|PubMed:10984435}. Cell
CC projection, ruffle {ECO:0000269|PubMed:10984435}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:10984435}. Cell projection, filopodium
CC tip {ECO:0000269|PubMed:10984435}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:10984435}. Cell projection, filopodium membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=May be
CC in an inactive, monomeric conformation in the cytosol. Detected in
CC cytoplasmic punctae and in cell projections. Colocalizes with actin
CC fibers. Undergoes forward and rearward movements within filopodia.
CC Interacts with microtubules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9HD67-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HD67-2; Sequence=VSP_054976, VSP_054977;
CC Name=Headless;
CC IsoId=Q9HD67-3; Sequence=VSP_054975;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10984435}.
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:0000250}.
CC -!- DOMAIN: IQ 3 domain mediates high-affinity calcium-dependent binding to
CC CALM3/CLP.
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 (PubMed:23012428).
CC {ECO:0000250|UniProtKB:F8VQB6, ECO:0000250|UniProtKB:P79114,
CC ECO:0000269|PubMed:23012428}.
CC -!- PTM: The initiator methionine for isoform Headless is removed.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Headless]: Produced by alternative promoter
CC usage. {ECO:0000305}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34519.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF247457; AAF68025.2; -; mRNA.
DR EMBL; AF234532; AAF37875.1; -; mRNA.
DR EMBL; AF132021; AAF36524.1; -; mRNA.
DR EMBL; AF132022; AAF36525.1; -; mRNA.
DR EMBL; AB018342; BAA34519.2; ALT_INIT; mRNA.
DR EMBL; AC010310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC024588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041694; AAH41694.1; -; mRNA.
DR EMBL; BC050682; AAH50682.1; -; mRNA.
DR EMBL; BC108736; AAI08737.1; -; mRNA.
DR EMBL; BC137168; AAI37169.1; -; mRNA.
DR EMBL; BC150285; AAI50286.1; -; mRNA.
DR EMBL; AI878891; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF184153; AAF17363.1; -; mRNA.
DR CCDS; CCDS54834.1; -. [Q9HD67-1]
DR PIR; A59267; A59267.
DR RefSeq; NP_036466.2; NM_012334.2. [Q9HD67-1]
DR RefSeq; XP_005248364.1; XM_005248307.2. [Q9HD67-3]
DR RefSeq; XP_011512348.1; XM_011514046.2. [Q9HD67-3]
DR PDB; 2LW9; NMR; -; A/B=883-933.
DR PDB; 3AU4; X-ray; 1.90 A; A=1486-2058.
DR PDB; 3AU5; X-ray; 2.55 A; A/B=1486-2058.
DR PDB; 3PZD; X-ray; 2.50 A; A=1503-2047.
DR PDB; 5I0H; X-ray; 1.80 A; A/B=1-741.
DR PDB; 5I0I; X-ray; 3.15 A; A/B=3-793.
DR PDB; 5KG8; EM; 9.10 A; A=3-741.
DR PDBsum; 2LW9; -.
DR PDBsum; 3AU4; -.
DR PDBsum; 3AU5; -.
DR PDBsum; 3PZD; -.
DR PDBsum; 5I0H; -.
DR PDBsum; 5I0I; -.
DR PDBsum; 5KG8; -.
DR AlphaFoldDB; Q9HD67; -.
DR BMRB; Q9HD67; -.
DR SASBDB; Q9HD67; -.
DR SMR; Q9HD67; -.
DR BioGRID; 110735; 45.
DR DIP; DIP-46151N; -.
DR IntAct; Q9HD67; 29.
DR MINT; Q9HD67; -.
DR STRING; 9606.ENSP00000421280; -.
DR iPTMnet; Q9HD67; -.
DR PhosphoSitePlus; Q9HD67; -.
DR BioMuta; MYO10; -.
DR DMDM; 205371854; -.
DR EPD; Q9HD67; -.
DR jPOST; Q9HD67; -.
DR MassIVE; Q9HD67; -.
DR MaxQB; Q9HD67; -.
DR PaxDb; Q9HD67; -.
DR PeptideAtlas; Q9HD67; -.
DR PRIDE; Q9HD67; -.
DR ProteomicsDB; 70789; -.
DR ProteomicsDB; 81840; -. [Q9HD67-1]
DR Antibodypedia; 4455; 130 antibodies from 24 providers.
DR DNASU; 4651; -.
DR Ensembl; ENST00000507288.1; ENSP00000426664.1; ENSG00000145555.15. [Q9HD67-2]
DR Ensembl; ENST00000513610.6; ENSP00000421280.1; ENSG00000145555.15. [Q9HD67-1]
DR GeneID; 4651; -.
DR KEGG; hsa:4651; -.
DR MANE-Select; ENST00000513610.6; ENSP00000421280.1; NM_012334.3; NP_036466.2.
DR UCSC; uc003jft.5; human. [Q9HD67-1]
DR CTD; 4651; -.
DR DisGeNET; 4651; -.
DR GeneCards; MYO10; -.
DR HGNC; HGNC:7593; MYO10.
DR HPA; ENSG00000145555; Low tissue specificity.
DR MIM; 601481; gene.
DR neXtProt; NX_Q9HD67; -.
DR OpenTargets; ENSG00000145555; -.
DR PharmGKB; PA31394; -.
DR VEuPathDB; HostDB:ENSG00000145555; -.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000155469; -.
DR HOGENOM; CLU_001626_1_0_1; -.
DR InParanoid; Q9HD67; -.
DR OMA; CEKGNIQ; -.
DR OrthoDB; 16113at2759; -.
DR PhylomeDB; Q9HD67; -.
DR TreeFam; TF316834; -.
DR PathwayCommons; Q9HD67; -.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-373752; Netrin-1 signaling.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; Q9HD67; -.
DR SIGNOR; Q9HD67; -.
DR BioGRID-ORCS; 4651; 24 hits in 1077 CRISPR screens.
DR ChiTaRS; MYO10; human.
DR EvolutionaryTrace; Q9HD67; -.
DR GeneWiki; MYO10; -.
DR GenomeRNAi; 4651; -.
DR Pharos; Q9HD67; Tbio.
DR PRO; PR:Q9HD67; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9HD67; protein.
DR Bgee; ENSG00000145555; Expressed in buccal mucosa cell and 206 other tissues.
DR ExpressionAtlas; Q9HD67; baseline and differential.
DR Genevisible; Q9HD67; HS.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030175; C:filopodium; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; IDA:MGI.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; ISS:UniProtKB.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0051489; P:regulation of filopodium assembly; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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 InterPro; IPR000159; RA_dom.
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; PF00788; RA; 1.
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; 2.
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; Alternative promoter usage;
KW Alternative splicing; ATP-binding; Calmodulin-binding; Cell membrane;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Membrane;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..2058
FT /note="Unconventional myosin-X"
FT /id="PRO_0000123473"
FT DOMAIN 63..739
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 742..763
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 764..787
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 1212..1310
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1392..1497
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1547..1695
FT /note="MyTH4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1700..2044
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..883
FT /note="SAH"
FT /evidence="ECO:0000269|PubMed:23012428"
FT REGION 819..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 884..934
FT /evidence="ECO:0000269|PubMed:23012428"
FT COMPBIAS 1002..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1078
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:0007744|PDB:5I0H, ECO:0007744|PDB:5I0I"
FT BINDING 113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:5I0H, ECO:0007744|PDB:5I0I"
FT BINDING 160..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:5I0H, ECO:0007744|PDB:5I0I"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:5I0H, ECO:0007744|PDB:5I0I"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZJP6"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 968
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZJP6"
FT MOD_RES 1158
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D3ZJP6"
FT VAR_SEQ 1..643
FT /note="Missing (in isoform Headless)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_054975"
FT VAR_SEQ 94..97
FT /note="TYIG -> VQIG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054976"
FT VAR_SEQ 98..2058
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054977"
FT VARIANT 32
FT /note="V -> I (in dbSNP:rs17707947)"
FT /id="VAR_046328"
FT VARIANT 148
FT /note="H -> Y (in dbSNP:rs7737765)"
FT /evidence="ECO:0000269|PubMed:11278607"
FT /id="VAR_061366"
FT VARIANT 273
FT /note="E -> D (in dbSNP:rs6870170)"
FT /id="VAR_046329"
FT VARIANT 324
FT /note="R -> W (in dbSNP:rs11750538)"
FT /evidence="ECO:0000269|PubMed:10984435, ECO:0000269|Ref.3"
FT /id="VAR_046330"
FT VARIANT 700
FT /note="R -> Q (in dbSNP:rs26740)"
FT /id="VAR_046331"
FT VARIANT 1663
FT /note="S -> T (in dbSNP:rs25901)"
FT /evidence="ECO:0000269|PubMed:10984435,
FT ECO:0000269|PubMed:11278607, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9872452"
FT /id="VAR_046332"
FT MUTAGEN 795
FT /note="F->A: Abolishes interaction with CALM3."
FT /evidence="ECO:0000269|PubMed:18570893"
FT MUTAGEN 893
FT /note="L->Q: Abolishes dimerization."
FT /evidence="ECO:0000269|PubMed:23012428"
FT MUTAGEN 904
FT /note="K->A: Abolishes dimerization."
FT /evidence="ECO:0000269|PubMed:23012428"
FT MUTAGEN 1647
FT /note="K->D: Abolishes interaction with tubulin; when
FT associated with D-1650."
FT /evidence="ECO:0000269|PubMed:21642953"
FT MUTAGEN 1650
FT /note="K->D: Abolishes interaction with tubulin; when
FT associated with D-1647."
FT /evidence="ECO:0000269|PubMed:21642953"
FT MUTAGEN 1718..1719
FT /note="SH->AA: Almost abolishes interaction with DCC."
FT /evidence="ECO:0000269|PubMed:21321230"
FT MUTAGEN 2002
FT /note="F->K: Abolishes interaction with DCC."
FT /evidence="ECO:0000269|PubMed:21642953"
FT CONFLICT 98
FT /note="S -> P (in Ref. 3; AAF36524)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="G -> W (in Ref. 1; AAF68025)"
FT /evidence="ECO:0000305"
FT CONFLICT 1186
FT /note="G -> C (in Ref. 3; AAF36524)"
FT /evidence="ECO:0000305"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 18..28
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:5I0H"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:5I0H"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 163..180
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 193..208
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 221..229
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 302..315
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 320..336
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 341..349
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 352..362
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 366..374
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 391..421
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 426..434
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 446..466
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 468..476
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 490..497
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 502..510
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 517..528
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 543..548
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 551..556
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 560..565
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 570..577
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 582..588
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 611..627
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 629..637
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 650..659
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 662..671
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 675..678
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 679..686
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 687..690
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 699..710
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 716..719
FT /evidence="ECO:0007829|PDB:5I0H"
FT STRAND 721..726
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 728..740
FT /evidence="ECO:0007829|PDB:5I0H"
FT HELIX 885..911
FT /evidence="ECO:0007829|PDB:2LW9"
FT HELIX 915..926
FT /evidence="ECO:0007829|PDB:2LW9"
FT HELIX 1505..1514
FT /evidence="ECO:0007829|PDB:3AU4"
FT TURN 1515..1518
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1520..1529
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1531..1533
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1554..1559
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1565..1578
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1586..1598
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1602..1613
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1623..1636
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1643..1659
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1664..1676
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1688..1695
FT /evidence="ECO:0007829|PDB:3AU4"
FT STRAND 1700..1706
FT /evidence="ECO:0007829|PDB:3AU4"
FT TURN 1707..1709
FT /evidence="ECO:0007829|PDB:3AU5"
FT STRAND 1711..1716
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1722..1732
FT /evidence="ECO:0007829|PDB:3AU4"
FT STRAND 1740..1750
FT /evidence="ECO:0007829|PDB:3AU4"
FT STRAND 1752..1754
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1761..1771
FT /evidence="ECO:0007829|PDB:3AU4"
FT STRAND 1783..1790
FT /evidence="ECO:0007829|PDB:3AU4"
FT STRAND 1794..1797
FT /evidence="ECO:0007829|PDB:3PZD"
FT HELIX 1802..1816
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1824..1839
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1851..1853
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1858..1866
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1906..1912
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1914..1929
FT /evidence="ECO:0007829|PDB:3AU4"
FT TURN 1930..1933
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1936..1947
FT /evidence="ECO:0007829|PDB:3AU4"
FT TURN 1951..1954
FT /evidence="ECO:0007829|PDB:3AU4"
FT STRAND 1956..1967
FT /evidence="ECO:0007829|PDB:3AU4"
FT STRAND 1969..1975
FT /evidence="ECO:0007829|PDB:3AU4"
FT STRAND 1977..1984
FT /evidence="ECO:0007829|PDB:3AU4"
FT STRAND 1991..1995
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 1996..1998
FT /evidence="ECO:0007829|PDB:3AU4"
FT STRAND 1999..2006
FT /evidence="ECO:0007829|PDB:3AU4"
FT STRAND 2009..2014
FT /evidence="ECO:0007829|PDB:3AU4"
FT STRAND 2017..2022
FT /evidence="ECO:0007829|PDB:3AU4"
FT HELIX 2026..2044
FT /evidence="ECO:0007829|PDB:3AU4"
SQ SEQUENCE 2058 AA; 237347 MW; 269C9E6566BD6D0B CRC64;
MDNFFTEGTR VWLRENGQHF PSTVNSCAEG IVVFRTDYGQ VFTYKQSTIT HQKVTAMHPT
NEEGVDDMAS LTELHGGSIM YNLFQRYKRN QIYTYIGSIL ASVNPYQPIA GLYEPATMEQ
YSRRHLGELP PHIFAIANEC YRCLWKRHDN QCILISGESG AGKTESTKLI LKFLSVISQQ
SLELSLKEKT SCVERAILES SPIMEAFGNA KTVYNNNSSR FGKFVQLNIC QKGNIQGGRI
VDYLLEKNRV VRQNPGERNY HIFYALLAGL EHEEREEFYL STPENYHYLN QSGCVEDKTI
SDQESFREVI TAMDVMQFSK EEVREVSRLL AGILHLGNIE FITAGGAQVS FKTALGRSAE
LLGLDPTQLT DALTQRSMFL RGEEILTPLN VQQAVDSRDS LAMALYACCF EWVIKKINSR
IKGNEDFKSI GILDIFGFEN FEVNHFEQFN INYANEKLQE YFNKHIFSLE QLEYSREGLV
WEDIDWIDNG ECLDLIEKKL GLLALINEES HFPQATDSTL LEKLHSQHAN NHFYVKPRVA
VNNFGVKHYA GEVQYDVRGI LEKNRDTFRD DLLNLLRESR FDFIYDLFEH VSSRNNQDTL
KCGSKHRRPT VSSQFKDSLH SLMATLSSSN PFFVRCIKPN MQKMPDQFDQ AVVLNQLRYS
GMLETVRIRK AGYAVRRPFQ DFYKRYKVLM RNLALPEDVR GKCTSLLQLY DASNSEWQLG
KTKVFLRESL EQKLEKRREE EVSHAAMVIR AHVLGFLARK QYRKVLYCVV IIQKNYRAFL
LRRRFLHLKK AAIVFQKQLR GQIARRVYRQ LLAEKREQEE KKKQEEEEKK KREEEERERE
RERREAELRA QQEEETRKQQ ELEALQKSQK EAELTRELEK QKENKQVEEI LRLEKEIEDL
QRMKEQQELS LTEASLQKLQ ERRDQELRRL EEEACRAAQE FLESLNFDEI DECVRNIERS
LSVGSEFSSE LAESACEEKP NFNFSQPYPE EEVDEGFEAD DDAFKDSPNP SEHGHSDQRT
SGIRTSDDSS EEDPYMNDTV VPTSPSADST VLLAPSVQDS GSLHNSSSGE STYCMPQNAG
DLPSPDGDYD YDQDDYEDGA ITSGSSVTFS NSYGSQWSPD YRCSVGTYNS SGAYRFSSEG
AQSSFEDSEE DFDSRFDTDD ELSYRRDSVY SCVTLPYFHS FLYMKGGLMN SWKRRWCVLK
DETFLWFRSK QEALKQGWLH KKGGGSSTLS RRNWKKRWFV LRQSKLMYFE NDSEEKLKGT
VEVRTAKEII DNTTKENGID IIMADRTFHL IAESPEDASQ WFSVLSQVHA STDQEIQEMH
DEQANPQNAV GTLDVGLIDS VCASDSPDRP NSFVIITANR VLHCNADTPE EMHHWITLLQ
RSKGDTRVEG QEFIVRGWLH KEVKNSPKMS SLKLKKRWFV LTHNSLDYYK SSEKNALKLG
TLVLNSLCSV VPPDEKIFKE TGYWNVTVYG RKHCYRLYTK LLNEATRWSS AIQNVTDTKA
PIDTPTQQLI QDIKENCLNS DVVEQIYKRN PILRYTHHPL HSPLLPLPYG DINLNLLKDK
GYTTLQDEAI KIFNSLQQLE SMSDPIPIIQ GILQTGHDLR PLRDELYCQL IKQTNKVPHP
GSVGNLYSWQ ILTCLSCTFL PSRGILKYLK FHLKRIREQF PGSEMEKYAL FTYESLKKTK
CREFVPSRDE IEALIHRQEM TSTVYCHGGG SCKITINSHT TAGEVVEKLI RGLAMEDSRN
MFALFEYNGH VDKAIESRTV VADVLAKFEK LAATSEVGDL PWKFYFKLYC FLDTDNVPKD
SVEFAFMFEQ AHEAVIHGHH PAPEENLQVL AALRLQYLQG DYTLHAAIPP LEEVYSLQRL
KARISQSTKT FTPCERLEKR RTSFLEGTLR RSFRTGSVVR QKVEEEQMLD MWIKEEVSSA
RASIIDKWRK FQGMNQEQAM AKYMALIKEW PGYGSTLFDV ECKEGGFPQE LWLGVSADAV
SVYKRGEGRP LEVFQYEHIL SFGAPLANTY KIVVDERELL FETSEVVDVA KLMKAYISMI
VKKRYSTTRS ASSQGSSR
