MYOI_DICDI
ID MYOI_DICDI Reviewed; 2357 AA.
AC Q9U1M8; P90536; Q555A2; Q869S1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Myosin-I heavy chain;
DE AltName: Full=Class VII unconventional myosin;
DE AltName: Full=DdMVII;
DE Short=DdM7;
GN Name=myoI; ORFNames=DDB_G0274455;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=JH10;
RX PubMed=10574761; DOI=10.1016/s0960-9822(00)80051-2;
RA Titus M.A.;
RT "A class VII unconventional myosin is required for phagocytosis.";
RL Curr. Biol. 9:1297-1303(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1783-2357.
RC STRAIN=AX4;
RA Iranfar N., Loomis W.F.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11267868; DOI=10.1016/s0960-9822(01)00097-5;
RA Tuxworth R.I., Weber I., Wessels D., Addicks G.C., Soll D.R., Gerisch G.,
RA Titus M.A.;
RT "A role for myosin VII in dynamic cell adhesion.";
RL Curr. Biol. 11:318-329(2001).
RN [6]
RP FUNCTION, INTERACTION WITH TALA, AND SUBUNIT.
RX PubMed=15826949; DOI=10.1074/jbc.m503699200;
RA Tuxworth R.I., Stephens S., Ryan Z.C., Titus M.A.;
RT "Identification of a myosin VII-talin complex.";
RL J. Biol. Chem. 280:26557-26564(2005).
RN [7]
RP NOMENCLATURE.
RX PubMed=16857047; DOI=10.1186/1471-2164-7-183;
RA Kollmar M.;
RT "Thirteen is enough: the myosins of Dictyostelium discoideum and their
RT light chains.";
RL BMC Genomics 7:183-183(2006).
RN [8]
RP DOMAIN, AND INTERACTION WITH TALA.
RX PubMed=17671169; DOI=10.1091/mbc.e06-07-0586;
RA Galdeen S.A., Stephens S., Thomas D.D., Titus M.A.;
RT "Talin influences the dynamics of the myosin VII-membrane interaction.";
RL Mol. Biol. Cell 18:4074-4084(2007).
RN [9]
RP STRUCTURE BY NMR OF 1620-1690.
RX PubMed=17189480; DOI=10.1110/ps.062496807;
RA Wang Q., Deloia M.A., Kang Y., Litchke C., Zhang N., Titus M.A.,
RA Walters K.J.;
RT "The SH3 domain of a M7 interacts with its C-terminal proline-rich
RT region.";
RL Protein Sci. 16:189-196(2007).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Involved in the early steps of phagocytosis and adhesion.
CC {ECO:0000269|PubMed:10574761, ECO:0000269|PubMed:11267868,
CC ECO:0000269|PubMed:15826949}.
CC -!- SUBUNIT: Monomer. Interacts with talA. {ECO:0000269|PubMed:15826949,
CC ECO:0000269|PubMed:17671169}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11267868}.
CC Note=Enriched in filopodia.
CC -!- DOMAIN: The coiled-coil and the proline-rich region are responsible to
CC the binding to talA. {ECO:0000269|PubMed:17671169}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40932.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L35321; AAF06035.1; -; Genomic_DNA.
DR EMBL; AAFI02000012; EAL70120.1; -; Genomic_DNA.
DR EMBL; U83089; AAB40932.1; ALT_INIT; mRNA.
DR PIR; A59249; A59249.
DR RefSeq; XP_644171.1; XM_639079.1.
DR PDB; 2I0N; NMR; -; A=1620-1690.
DR PDB; 5EJQ; X-ray; 2.19 A; A=1119-1620.
DR PDB; 5EJR; X-ray; 2.00 A; A=1851-2357.
DR PDB; 5EJS; X-ray; 2.70 A; A/B=1854-2357.
DR PDB; 5EJY; X-ray; 1.90 A; A=1118-1618.
DR PDBsum; 2I0N; -.
DR PDBsum; 5EJQ; -.
DR PDBsum; 5EJR; -.
DR PDBsum; 5EJS; -.
DR PDBsum; 5EJY; -.
DR AlphaFoldDB; Q9U1M8; -.
DR SMR; Q9U1M8; -.
DR STRING; 44689.DDB0185049; -.
DR PaxDb; Q9U1M8; -.
DR PRIDE; Q9U1M8; -.
DR EnsemblProtists; EAL70120; EAL70120; DDB_G0274455.
DR GeneID; 8619600; -.
DR KEGG; ddi:DDB_G0274455; -.
DR dictyBase; DDB_G0274455; myoI.
DR eggNOG; KOG4229; Eukaryota.
DR HOGENOM; CLU_229626_0_0_1; -.
DR InParanoid; Q9U1M8; -.
DR OMA; LHRGNKH; -.
DR PhylomeDB; Q9U1M8; -.
DR EvolutionaryTrace; Q9U1M8; -.
DR PRO; PR:Q9U1M8; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0030175; C:filopodium; IDA:dictyBase.
DR GO; GO:0032433; C:filopodium tip; IDA:dictyBase.
DR GO; GO:0016020; C:membrane; IDA:dictyBase.
DR GO; GO:0016459; C:myosin complex; ISS:dictyBase.
DR GO; GO:0001891; C:phagocytic cup; IDA:dictyBase.
DR GO; GO:0003779; F:actin binding; ISS:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; ISS:dictyBase.
DR GO; GO:0003774; F:cytoskeletal motor activity; ISS:dictyBase.
DR GO; GO:0000146; F:microfilament motor activity; ISS:dictyBase.
DR GO; GO:0008017; F:microtubule binding; IDA:dictyBase.
DR GO; GO:0043621; F:protein self-association; IPI:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030048; P:actin filament-based movement; ISS:dictyBase.
DR GO; GO:0000902; P:cell morphogenesis; IMP:dictyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0046847; P:filopodium assembly; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0009847; P:spore germination; IMP:dictyBase.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd14473; FERM_B-lobe; 2.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.25.40.530; -; 3.
DR Gene3D; 2.30.29.30; -; 2.
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; IPR001609; Myosin_head_motor_dom.
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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00784; MyTH4; 2.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00295; B41; 1.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00139; MyTH4; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47031; SSF47031; 2.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50057; FERM_3; 2.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; ATP-binding; Coiled coil; Cytoplasm;
KW Motor protein; Myosin; Nucleotide-binding; Reference proteome; Repeat;
KW SH3 domain.
FT CHAIN 1..2357
FT /note="Myosin-I heavy chain"
FT /id="PRO_0000328606"
FT DOMAIN 13..688
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 691..720
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1155..1313
FT /note="MyTH4 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1318..1620
FT /note="FERM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 1618..1678
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1894..2051
FT /note="MyTH4 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 2060..2357
FT /note="FERM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 579..586
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 787..1076
FT /note="Binding to talin A"
FT REGION 797..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1686..1849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 787..891
FT /evidence="ECO:0000255"
FT COMPBIAS 1003..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1049
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1686..1737
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1758
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1790..1815
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1816..1849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT HELIX 1125..1127
FT /evidence="ECO:0007829|PDB:5EJY"
FT TURN 1128..1130
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1133..1140
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1144..1146
FT /evidence="ECO:0007829|PDB:5EJY"
FT STRAND 1152..1154
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1170..1187
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1193..1196
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1198..1214
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1216..1218
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1219..1229
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1236..1250
FT /evidence="ECO:0007829|PDB:5EJY"
FT TURN 1257..1259
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1260..1272
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1278..1297
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1306..1313
FT /evidence="ECO:0007829|PDB:5EJY"
FT STRAND 1318..1324
FT /evidence="ECO:0007829|PDB:5EJY"
FT STRAND 1329..1334
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1340..1350
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1357..1360
FT /evidence="ECO:0007829|PDB:5EJY"
FT STRAND 1362..1368
FT /evidence="ECO:0007829|PDB:5EJY"
FT STRAND 1371..1373
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1381..1394
FT /evidence="ECO:0007829|PDB:5EJY"
FT STRAND 1396..1399
FT /evidence="ECO:0007829|PDB:5EJQ"
FT STRAND 1403..1409
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1422..1440
FT /evidence="ECO:0007829|PDB:5EJY"
FT TURN 1443..1445
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1449..1464
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1469..1478
FT /evidence="ECO:0007829|PDB:5EJY"
FT TURN 1481..1483
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1486..1491
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1493..1501
FT /evidence="ECO:0007829|PDB:5EJY"
FT TURN 1502..1505
FT /evidence="ECO:0007829|PDB:5EJQ"
FT HELIX 1508..1520
FT /evidence="ECO:0007829|PDB:5EJY"
FT TURN 1523..1526
FT /evidence="ECO:0007829|PDB:5EJY"
FT STRAND 1528..1533
FT /evidence="ECO:0007829|PDB:5EJY"
FT STRAND 1537..1541
FT /evidence="ECO:0007829|PDB:5EJQ"
FT STRAND 1543..1550
FT /evidence="ECO:0007829|PDB:5EJY"
FT STRAND 1553..1558
FT /evidence="ECO:0007829|PDB:5EJY"
FT TURN 1559..1562
FT /evidence="ECO:0007829|PDB:5EJY"
FT STRAND 1563..1568
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1570..1572
FT /evidence="ECO:0007829|PDB:5EJY"
FT STRAND 1582..1588
FT /evidence="ECO:0007829|PDB:5EJY"
FT STRAND 1594..1598
FT /evidence="ECO:0007829|PDB:5EJY"
FT HELIX 1602..1617
FT /evidence="ECO:0007829|PDB:5EJY"
FT STRAND 1622..1627
FT /evidence="ECO:0007829|PDB:2I0N"
FT STRAND 1633..1636
FT /evidence="ECO:0007829|PDB:2I0N"
FT STRAND 1641..1661
FT /evidence="ECO:0007829|PDB:2I0N"
FT STRAND 1664..1669
FT /evidence="ECO:0007829|PDB:2I0N"
FT HELIX 1670..1672
FT /evidence="ECO:0007829|PDB:2I0N"
FT STRAND 1673..1678
FT /evidence="ECO:0007829|PDB:2I0N"
FT HELIX 1855..1861
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 1865..1875
FT /evidence="ECO:0007829|PDB:5EJR"
FT TURN 1876..1878
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 1888..1892
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 1908..1924
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 1936..1949
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 1951..1953
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 1954..1963
FT /evidence="ECO:0007829|PDB:5EJR"
FT TURN 1964..1967
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 1971..1987
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 1992..2009
FT /evidence="ECO:0007829|PDB:5EJR"
FT TURN 2010..2012
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 2014..2028
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 2034..2036
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 2044..2055
FT /evidence="ECO:0007829|PDB:5EJR"
FT STRAND 2061..2065
FT /evidence="ECO:0007829|PDB:5EJR"
FT STRAND 2071..2075
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 2082..2093
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 2097..2102
FT /evidence="ECO:0007829|PDB:5EJR"
FT STRAND 2103..2109
FT /evidence="ECO:0007829|PDB:5EJR"
FT TURN 2110..2113
FT /evidence="ECO:0007829|PDB:5EJR"
FT STRAND 2114..2117
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 2124..2133
FT /evidence="ECO:0007829|PDB:5EJR"
FT STRAND 2140..2146
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 2153..2158
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 2161..2164
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 2167..2182
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 2191..2205
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 2216..2220
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 2225..2228
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 2233..2244
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 2252..2266
FT /evidence="ECO:0007829|PDB:5EJR"
FT TURN 2268..2271
FT /evidence="ECO:0007829|PDB:5EJR"
FT STRAND 2273..2278
FT /evidence="ECO:0007829|PDB:5EJR"
FT STRAND 2280..2290
FT /evidence="ECO:0007829|PDB:5EJR"
FT STRAND 2292..2298
FT /evidence="ECO:0007829|PDB:5EJR"
FT TURN 2300..2302
FT /evidence="ECO:0007829|PDB:5EJS"
FT STRAND 2305..2311
FT /evidence="ECO:0007829|PDB:5EJR"
FT STRAND 2316..2319
FT /evidence="ECO:0007829|PDB:5EJR"
FT STRAND 2321..2328
FT /evidence="ECO:0007829|PDB:5EJR"
FT STRAND 2329..2333
FT /evidence="ECO:0007829|PDB:5EJS"
FT STRAND 2335..2340
FT /evidence="ECO:0007829|PDB:5EJR"
FT HELIX 2344..2355
FT /evidence="ECO:0007829|PDB:5EJR"
SQ SEQUENCE 2357 AA; 268284 MW; FC667F12F207B0C2 CRC64;
MEDDDTLNGE YFQPVEDMIT LPILTEESLL LNLKMRYKKK EIYTYTGSIL VAVNPYEILP
IYTADIVKSY FAKSRNLMLP HIFAVSDAAF TNMIEEGKNQ SIIISGESGA GKTESTKLII
QYLAARTNRH SQVEQMIVES SPILEAFGNA KTIRNNNSSR FGKFIEIQFN REGHISGARI
INYLLEKSRI SHQASSERNY HIFYQLLAGA SDELKEKLKL GEPEDYHYLS QSGCIRIENI
NDVEDFEHVK YAMNVLGLPE DKQFTIFSIV SAVLHIGNLK FEKSEKTQGA EGSEVSNKDT
LKIIAQLLSV DPVKLETCLT IRHVLIRGQN FVIPLKVNEA EDTRDSLAKA LYGNVFNWLV
VFINSKIHKP QKNSTFIGVL DIFGFENFKK NSFEQFCINF ANEKLQQHFN QHIFKLEQEE
YEKEKINWSK IVYNDNQECL DLIEKRPLGI LSLLDEESRF PQATDLTYLD KLHTNHEKHP
YYEKPRRSKN TFVVKHYAGE VHYDTQGFLD KNKDTVSDDL SSLLQGSKSK FIIELFTPPR
EEGDDSDKGR EKKKTTAGQT FKTQLQSLIN ILSSTQPHYV RCIKPNTTKE PAVYDRELIQ
AQLRYAGMME TIRIRKLGYP IRHTHKEFRD RYLILDYRAR STDHKQTCAG LINLLSGTGG
LERDEWQLGN TKVFIRDHQY LKLEELRKLK LLKKVTLIQS VWRMYRCKKR YQQIRASAKI
LGAAMLSHSS RRDFQEQRQA VQRIKGFFKM LTYQKQFKII QINLRIVQNN IRSFIARRHS
RNAVLLKRDR NARMLEIQRE KDEEERNRQE KEERDRQEKE DKEKETADRR QLQEEQKRRE
EELRAKREEE ELKKLEEKKS QLKELNQIDE LSSLERMLKE QQDKNINELD DFVNSLEAFS
FEGGVDDSQP YSFNHKMYEM SPEALDKISI TDLLQGLKQT VRSVTKFEVD ESKFELPPGI
ENVLKRAPGI KRQASSFLPG QPIPDVYSSP QYPVDEADDD DSNNNYINSN NGDLPLPTSQ
SSDFSLPPPP SSSSMDFGLP PPPPSSSSGG TYSLPPMPVF DFGMIDPILG APPPPPSTSD
STSPSATATG NNTPNSSSAS ASQSTNQVNP QPTVSVVELP QILNDEEISL YSFYDYANKN
FNIEKLKQKD DIFSYQKSHI KSSLLVHSDA EQTKVAVEIF SKVLHYMNSN PLVSKKDPAD
FYSPVKFILT KGLAIESLRD EIYCQLIKQS TSNPIQDLNI RVWELIHFTC STFPPTRKLI
KYFAAYLKTT IQQSDVSKSV KDSAQASYFI LQRFTLNGAR KQVPSVTELE SIKENRPIFV
RITATDGSLK GLHIDSATTC QESSNDLSQR SRMRVNSKEN GFTIIESFNG IERDIAPTDK
LCDVLSKVEN LQATLSSKIQ VNFKFVFKKK LFFDNITNNV PTTSINVENE FYYHQLFNDL
FNSNYCKDQD YQISIGSLKL QFESSDYTDE IRAWLPGNGR GKYFTTDIEK NRFDDFINKY
KSHKGLSPED AKKQMVQLLE KHPLANCSLV VCEHQSESLP YPKNFVLALN VNGINIYDPA
TSKMLESVKY SNQSQQNLKS DDKSVSIILE NKSTLQAFTG DVQKLVSLIK EYSLYLRNNA
KYARALKDYN VSDTSLLPFK RNDIITITFK DQENKWFMGQ LNGKEGSFPV DHVEILLSDV
PPPQPVHPVA TLSPPMSPTI PNITNTPPPP PSISDSMSPP PQVGMLPPPP PPSVMGSTKP
IEIPSLGIPP PPPSSSNSSV PNSPIGSPMM GIPPPPPTIS VHSLSNSGNS TPPPPLPSLS
TPPTLSTPPP ISSPPNFRSS LRVSMLNTSN DGGDNSSDDP SKRLTVSPAI GTDSQLAQWA
STRFRSFKRA STLNQQQATL KRKAPVDPNT AFYFNKDPIK ESLIEMEAKL SKKAIKNFSE
IMMWMGDYPI PKGQTASLVI QSIISRGIEN HELRDEIYCQ AYRQTNKNPK VESAKKGFEL
IYFLSITFSP SDSLLQPFME QLMSRNIAIQ SSSPQLASLI AVCIEKLESH PIPSYQQRKM
GPSATEIQSF RSNLENGDIS TCKIRFIDQS TKLAKINTYT TIREITDTVC RQYGISQQSI
KMFGISAVNE TAGISKVVSE TDMIYDVLAR WEQSEEKGEF YFQVRRRFFL DDVNKILDQE
HLWTDDDICF ELTYCQIRDE WMKGLYTNVN EKDSSIIAAI LIQLLYPNQS KLVLTKEVVR
QVLPDQILNS QNIKVWISMI ESQIFELVSQ TPEYLKLMFI NLIGSKSPLF GCTLFNIQQK
ENPPKAWLAI NKKGVSIFDP HTKESKNFWT FQSISNVAFT DDTFCIMTGN LMKPIKQTFT
TDEHSSIASV YQFYSSQ
