MYO10_BOVIN
ID MYO10_BOVIN Reviewed; 2052 AA.
AC P79114;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Unconventional myosin-X;
DE AltName: Full=Unconventional myosin-10;
GN Name=MYO10;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Aorta;
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 FUNCTION, AND INTERACTION WITH CALM.
RX PubMed=11457842; DOI=10.1074/jbc.m104785200;
RA Homma K., Saito J., Ikebe R., Ikebe M.;
RT "Motor function and regulation of myosin X.";
RL J. Biol. Chem. 276:34348-34354(2001).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=11854753; DOI=10.1038/ncb762;
RA Berg J.S., Cheney R.E.;
RT "Myosin-X is an unconventional myosin that undergoes intrafilopodial
RT motility.";
RL Nat. Cell Biol. 4:246-250(2002).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ITGB1; ITGB3 AND
RP ITGB5.
RX PubMed=15156152; DOI=10.1038/ncb1136;
RA Zhang H., Berg J.S., Li Z., Wang Y., Lang P., Sousa A.D., Bhaskar A.,
RA Cheney R.E., Stromblad S.;
RT "Myosin-X provides a motor-based link between integrins and the
RT cytoskeleton.";
RL Nat. Cell Biol. 6:523-531(2004).
RN [5]
RP FUNCTION IN ACTIN BINDING AND ATP HYDROLYSIS.
RX PubMed=15705568; DOI=10.1074/jbc.m500616200;
RA Kovacs M., Wang F., Sellers J.R.;
RT "Mechanism of action of myosin X, a membrane-associated molecular motor.";
RL J. Biol. Chem. 280:15071-15083(2005).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=20081229; DOI=10.1074/jbc.m109.017269;
RA McMichael B.K., Cheney R.E., Lee B.S.;
RT "Myosin X regulates sealing zone patterning in osteoclasts through linkage
RT of podosomes and microtubules.";
RL J. Biol. Chem. 285:9506-9515(2010).
RN [8]
RP FUNCTION.
RX PubMed=20392702; DOI=10.1074/jbc.m109.093864;
RA Watanabe T.M., Tokuo H., Gonda K., Higuchi H., Ikebe M.;
RT "Myosin-X induces filopodia by multiple elongation mechanism.";
RL J. Biol. Chem. 285:19605-19614(2010).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND
RP PHOSPHATIDYLINOSITOL-3,4,5-TRISPHOSPHATE BINDING.
RX PubMed=20930142; DOI=10.1242/jcs.069609;
RA Plantard L., Arjonen A., Lock J.G., Nurani G., Ivaska J., Stromblad S.;
RT "PtdIns(3,4,5)P is a regulator of myosin-X localization and filopodia
RT formation.";
RL J. Cell Sci. 123:3525-3534(2010).
RN [10]
RP FUNCTION, AND INTERACTION WITH CALM.
RX PubMed=20364131; DOI=10.1038/nsmb.1785;
RA Sun Y., Sato O., Ruhnow F., Arsenault M.E., Ikebe M., Goldman Y.E.;
RT "Single-molecule stepping and structural dynamics of myosin X.";
RL Nat. Struct. Mol. Biol. 17:485-491(2010).
RN [11]
RP FUNCTION, DOMAIN, INTERACTION WITH CALM, AND SUBUNIT.
RX PubMed=21666676; DOI=10.1038/nsmb.2065;
RA Umeki N., Jung H.S., Sakai T., Sato O., Ikebe R., Ikebe M.;
RT "Phospholipid-dependent regulation of the motor activity of myosin X.";
RL Nat. Struct. Mol. Biol. 18:783-788(2011).
RN [12]
RP SAH DOMAIN.
RX PubMed=25122759; DOI=10.1074/jbc.m114.585679;
RA Wolny M., Batchelor M., Knight P.J., Paci E., Dougan L., Peckham M.;
RT "Stable single alpha-helices are constant force springs in proteins.";
RL J. Biol. Chem. 289:27825-27835(2014).
RN [13] {ECO:0007744|PDB:2N9B}
RP STRUCTURE BY NMR OF 884-923, AND COILED COIL.
RX PubMed=27276269; DOI=10.1016/j.bpj.2016.04.048;
RA Vavra K.C., Xia Y., Rock R.S.;
RT "Competition between Coiled-Coil Structures and the Impact on Myosin-10
RT Bundle Selection.";
RL Biophys. J. 110:2517-2527(2016).
RN [14] {ECO:0007744|PDB:5HMO}
RP X-RAY CRYSTALLOGRAPHY (3.49 ANGSTROMS) OF 796-929, SAH DOMAIN, AND COILED
RP COIL.
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 (By similarity). The tail domain
CC binds to membranous compartments containing phosphatidylinositol 3,4,5-
CC trisphosphate, which are then moved relative to actin filaments.
CC Regulates cell shape, cell spreading and cell adhesion. Stimulates the
CC formation and elongation of filopodia. In hippocampal neurons it
CC induces the formation of dendritic filopodia by trafficking the actin-
CC remodeling protein VASP to the tips of filopodia, where it promotes
CC actin elongation (By similarity). Plays a role in formation of the
CC podosome belt in osteoclasts. {ECO:0000250|UniProtKB:Q9HD67,
CC ECO:0000269|PubMed:11457842, ECO:0000269|PubMed:15156152,
CC ECO:0000269|PubMed:15705568, ECO:0000269|PubMed:16894163,
CC ECO:0000269|PubMed:20081229, ECO:0000269|PubMed:20364131,
CC ECO:0000269|PubMed:20392702, ECO:0000269|PubMed:20930142,
CC ECO:0000269|PubMed:21666676}.
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 NEO 1. Interacts with VASP. Interacts with DCC and ITGB5; the
CC presence of DCC inhibits ITGB5 binding. Interacts with tubulin; ITGB5
CC or DCC binding inhibits tubulin binding. Interacts strongly with CALM3
CC and weakly with CALM, the CALM3 interaction is essential for function
CC in filopodial extension and motility (By similarity). Interacts with
CC ITGB1, ITGB3 and ITGB5. {ECO:0000250, ECO:0000269|PubMed:11457842,
CC ECO:0000269|PubMed:15156152, ECO:0000269|PubMed:20364131,
CC ECO:0000269|PubMed:21666676}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell projection,
CC lamellipodium. Cell projection, ruffle. Cytoplasm, cytoskeleton. Cell
CC projection, filopodium tip. Cytoplasm, cell cortex. Cell projection,
CC filopodium membrane; Peripheral membrane protein. Note=May be in an
CC inactive, monomeric conformation in the cytosol. Detected in
CC cytoplasmic punctae and in cell projections. Colocalizes with actin
CC fibers. Interacts with microtubules. Undergoes forward and rearward
CC movements within filopodia. Interaction with membranes containing
CC phosphatidylinositol 3,4,5-trisphosphate mediates localization at
CC filopodium membranes.
CC -!- TISSUE SPECIFICITY: Detected in kidney, testis, liver, kidney,
CC cerebellum and brain cortex (at protein level).
CC {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.
CC -!- DOMAIN: Interacts with membranes containing phosphatidylinositol-3,4,5-
CC trisphosphate via the PH domains.
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 (PubMed:25122759). It can refold after
CC extension suggesting an in vivo force-dependent function
CC (PubMed:25122759). An anti-parallel coiled coil is located C-terminal
CC to the SAH domain and mediates dimerization (PubMed:27276269,
CC PubMed:27580874). {ECO:0000269|PubMed:25122759,
CC ECO:0000269|PubMed:27276269, ECO:0000269|PubMed:27580874}.
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 EMBL; U55042; AAB39486.1; -; mRNA.
DR PIR; T18519; T18519.
DR RefSeq; NP_776819.1; NM_174394.2.
DR PDB; 2N9B; NMR; -; A/B=884-921.
DR PDB; 5HMO; X-ray; 3.49 A; A/C=796-929.
DR PDB; 6HR1; X-ray; 1.90 A; A/B=826-837.
DR PDBsum; 2N9B; -.
DR PDBsum; 5HMO; -.
DR PDBsum; 6HR1; -.
DR AlphaFoldDB; P79114; -.
DR SMR; P79114; -.
DR DIP; DIP-46150N; -.
DR IntAct; P79114; 8.
DR STRING; 9913.ENSBTAP00000026812; -.
DR BindingDB; P79114; -.
DR ChEMBL; CHEMBL4295791; -.
DR PaxDb; P79114; -.
DR PRIDE; P79114; -.
DR GeneID; 281935; -.
DR KEGG; bta:281935; -.
DR CTD; 4651; -.
DR eggNOG; KOG4229; Eukaryota.
DR InParanoid; P79114; -.
DR OrthoDB; 16113at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA: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; IDA:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0060002; F:plus-end directed microfilament motor activity; IDA:UniProtKB.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0051489; P:regulation of filopodium assembly; IDA: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; 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..2052
FT /note="Unconventional myosin-X"
FT /id="PRO_0000123472"
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 1206..1304
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1386..1491
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1541..1689
FT /note="MyTH4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1694..2038
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..884
FT /note="SAH"
FT /evidence="ECO:0000269|PubMed:27580874"
FT REGION 819..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 885..935
FT /evidence="ECO:0000269|PubMed:27580874"
FT COMPBIAS 1002..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1056
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 963
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZJP6"
FT MOD_RES 966
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD67"
FT MOD_RES 1152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D3ZJP6"
FT HELIX 826..837
FT /evidence="ECO:0007829|PDB:6HR1"
FT HELIX 864..872
FT /evidence="ECO:0007829|PDB:5HMO"
FT TURN 873..878
FT /evidence="ECO:0007829|PDB:5HMO"
FT HELIX 879..910
FT /evidence="ECO:0007829|PDB:5HMO"
FT HELIX 914..925
FT /evidence="ECO:0007829|PDB:5HMO"
SQ SEQUENCE 2052 AA; 235839 MW; 43DF13424B4B2D28 CRC64;
MDNFFPEGTR VWLRENGQHF PSTVNSCAEG VVVFQTDYGQ VFTYKQSTIT HQKVMPMQPT
DEEGVDDMAT LTELHGGAIM HNLYQRYKRN QIYTYIGSII ASVNPYKTIT GLYSRDAVDR
YSRCHLGELP PHVFAIANEC YRCLWKRHDN QCVLISGESG AGKTESTKLI LKFLSAISQQ
SVDLSSKEKT SSVEQAILES SPIMEAFGNA KTVYNNNSSR FGKFVQLNIG QKGNIQGGRI
VDYLLEKNRV VRQNPGERNY HIFYALLAGL GHEEREEFYL SVPENYHYLN QSGCVTDRTI
SDQESFREVI MAMEVMQFSK EEVREVLRLL AGILHLGNIE FITAGGAQVS FKTALGRSAE
LLGLDPAQLT DALTQRSMFL RGEEILTPLN VQQAADSRDS LAMALYARCF EWVIKKINSR
IKGKDDFKSI GILDIFGFEN FEVNHFEQFN INYANEKLQE YFNKHIFSLE QLEYSREGLV
WEDIDWIDNG ECLDLIEKKL GLLALINEES HFPQATDSTL LEKLHNQHAN NHFYVKPRVA
VNNFGVKHYA GEVQYDVRGI LEKNRDTFRD DLLNLLRESR FDFIYDLFEH VSSRNNQDTL
KCGSKHRRPT VSSQFKDSLH SLMATLSASN PFFVRCIKPN MQKMPDQFDQ AVVVNQLRYS
GMLETVRIRK AGYAVRRPFQ DFYKRYKVLM RNVALPEDIR GKCTALLQLY DASNSEWQLG
KTKVFLRESL EQKLEKRQEE EVTRAAMVIR AHVLGYLARK QYKKVLDCVV IIQKNYRAFL
LRRRFLHLKK AAVVFQKQLR GQIARRVYRQ LLAEKRAEEE KRKREEEEKR KREEEERERE
RERREAELRA QQEEAARKQR ELEALQQESQ RAAELSRELE KQKENKQVEE ILRLEKEIED
LQRMKERQEL SLTEASLQKL QQLRDEELRR LEDEACRAAQ EFLESLNFDE IDECVRNIER
SLSVGSGCTG EQGAGAEKPS FNFSQPYPEE EEVDEGFEAD DDAFKDSPNP SEHGHSDQRT
SGIRTSDESS EEDPYMNDTV VPTSPSADST VLLAPSEHDS SAGEPTYCLP QTPGALPAPE
GDYDYDQDDY EDGAITSGSS VTFSNSCSSQ WSPDYRCSVG TYNSSGAYRF SSEGAQSSFE
DSEEDFDSRF DTDDELSYRR DSVYSCVTLP YFHSFLYMKG GLMNSWKRRW CVLKDETFLW
FRSKQEALKQ GWLHKKGGGS STLSRRNWKK RWFVLRQAKL MYFENDSEEK LKGTVEVRAA
KEIIDNTSKE NGIDIIMADR TFHLIAESPE DASQWFSVLS QVHASTDQEI REMHDEQANP
QNAVGTLDVG LIDSVCASDS PDRPNSFVII TANRVLHCNA DTPEEMHHWI TLLQRSKGDT
RVEGQEFIVR GWLHKEVKNS PKMSSLKLKK RWFVLTHNSL DYYKSSEKNA LKLGTLVLNS
LCSVVPPDEK IFKETGYWNV TVYGRKHCYR LYTKLLNEAT RWSSAIQNVT DTKAPIDTPT
QQLIQDIKEN CLNSDVVEQI YKRNPILRHT HHPLHSPLLP LPYGDINLNL LKDKGYTTLQ
DEAIKIFNSL QQLESMSDPI PIIQGILQTG HDLRPLRDEL YCQLIKQTNK VPHPGSVGNL
CSWQILTCLS CTFLPSRGIL KYLKFHLRRI REQFPGTEME KYALFIYESL KKTKCREFVP
SRDEIEALIH RQEMTSTVHC HGGGSCKITV NSHTTAGEVV EKLIRGLAME DSRNMFALFE
YNGHVDKAIE SRTIVADVLA KFEKLAATSE VGEQPWKFYF KLYCFLDTDN VPKDSVEFAF
MFEQAHEAVI HGHYPAPEEN LQVLAALRLQ YLQGDYAPHA PVPPLEEVYS LQRLKARISQ
STKSFTPGER LEKRRTSFLE GTLRRSFRTG SAIRQKAEEE QMVDMWVKEE VCSARASILD
KWKKFQGMSQ EQAMAKYMAL IKEWPGYGST LFDVECKEGG FPQDLWLGVS ADAVSVYKRG
EGRPLEVFQY EHILSFGAPL ANTYKIVVDE RELLFETSEV VDVAKLMKAY ISMIVKKRYS
TSRSVSSQGS SR
