MYO6_ARATH
ID MYO6_ARATH Reviewed; 1505 AA.
AC Q9LKB9; Q0WPF0; Q39158;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Myosin-6;
DE AltName: Full=AtMYA2;
GN Name=XI-2; Synonyms=MYA2; OrderedLocusNames=At5g43900; ORFNames=F6B6.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=7811972; DOI=10.1007/bf00040695;
RA Kinkema M.D., Wang H., Schiefelbein J.;
RT "Molecular analysis of the myosin gene family in Arabidopsis thaliana.";
RL Plant Mol. Biol. 26:1139-1153(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 408-1505.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY.
RX PubMed=10984423; DOI=10.1242/jcs.113.19.3353;
RA Hodge T., Cope M.J.;
RT "A myosin family tree.";
RL J. Cell Sci. 113:3353-3354(2000).
RN [6]
RP GENE FAMILY.
RX PubMed=11516337; DOI=10.1186/gb-2001-2-7-research0024;
RA Reddy A.S., Day I.S.;
RT "Analysis of the myosins encoded in the recently completed Arabidopsis
RT thaliana genome sequence.";
RL Genome Biol. 2:RESEARCH0024.1-RESEARCH0024.17(2001).
RN [7]
RP SUBCELLULAR LOCATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15792961; DOI=10.1093/pcp/pci085;
RA Hashimoto K., Igarashi H., Mano S., Nishimura M., Shimmen T., Yokota E.;
RT "Peroxisomal localization of a myosin XI isoform in Arabidopsis thaliana.";
RL Plant Cell Physiol. 46:782-789(2005).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=17288617; DOI=10.1186/1471-2229-7-6;
RA Reisen D., Hanson M.R.;
RT "Association of six YFP-myosin XI-tail fusions with mobile plant cell
RT organelles.";
RL BMC Plant Biol. 7:6-6(2007).
RN [9]
RP DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=17500056; DOI=10.1074/jbc.m700645200;
RA Li J.F., Nebenfuehr A.;
RT "Organelle targeting of myosin XI is mediated by two globular tail
RT subdomains with separate cargo binding sites.";
RL J. Biol. Chem. 282:20593-20602(2007).
RN [10]
RP DOMAIN, AND ACTIN-BINDING.
RX PubMed=18598361; DOI=10.1186/1471-2229-8-74;
RA Walter N., Holweg C.L.;
RT "Head-neck domain of Arabidopsis myosin XI, MYA2, fused with GFP produces
RT F-actin patterns that coincide with fast organelle streaming in different
RT plant cells.";
RL BMC Plant Biol. 8:74-74(2008).
RN [11]
RP INTERACTION WITH RABD1 AND RABC2A.
RX PubMed=18703495; DOI=10.1093/jxb/ern202;
RA Hashimoto K., Igarashi H., Mano S., Takenaka C., Shiina T., Yamaguchi M.,
RA Demura T., Nishimura M., Shimmen T., Yokota E.;
RT "An isoform of Arabidopsis myosin XI interacts with small GTPases in its C-
RT terminal tail region.";
RL J. Exp. Bot. 59:3523-3531(2008).
RN [12]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18178669; DOI=10.1104/pp.107.113654;
RA Peremyslov V.V., Prokhnevsky A.I., Avisar D., Dolja V.V.;
RT "Two class XI myosins function in organelle trafficking and root hair
RT development in Arabidopsis.";
RL Plant Physiol. 146:1109-1116(2008).
RN [13]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19060218; DOI=10.1073/pnas.0810730105;
RA Prokhnevsky A.I., Peremyslov V.V., Dolja V.V.;
RT "Overlapping functions of the four class XI myosins in Arabidopsis growth,
RT root hair elongation, and organelle motility.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:19744-19749(2008).
RN [14]
RP FUNCTION.
RX PubMed=19369591; DOI=10.1104/pp.109.136853;
RA Avisar D., Abu-Abied M., Belausov E., Sadot E., Hawes C., Sparkes I.A.;
RT "A comparative study of the involvement of 17 Arabidopsis myosin family
RT members on the motility of Golgi and other organelles.";
RL Plant Physiol. 150:700-709(2009).
RN [15]
RP FUNCTION.
RX PubMed=20581304; DOI=10.1105/tpc.110.076315;
RA Peremyslov V.V., Prokhnevsky A.I., Dolja V.V.;
RT "Class XI myosins are required for development, cell expansion, and F-Actin
RT organization in Arabidopsis.";
RL Plant Cell 22:1883-1897(2010).
RN [16]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21233331; DOI=10.1104/pp.110.170720;
RA Peremyslov V.V., Mockler T.C., Filichkin S.A., Fox S.E., Jaiswal P.,
RA Makarova K.S., Koonin E.V., Dolja V.V.;
RT "Expression, splicing, and evolution of the myosin gene family in plants.";
RL Plant Physiol. 155:1191-1204(2011).
RN [17]
RP FUNCTION.
RX PubMed=22672737; DOI=10.1186/1471-2229-12-81;
RA Ojangu E.L., Tanner K., Pata P., Jaerve K., Holweg C.L., Truve E.,
RA Paves H.;
RT "Myosins XI-K, XI-1, and XI-2 are required for development of pavement
RT cells, trichomes, and stigmatic papillae in Arabidopsis.";
RL BMC Plant Biol. 12:81-81(2012).
RN [18]
RP FUNCTION.
RX PubMed=21914656; DOI=10.1093/jxb/err265;
RA Avisar D., Abu-Abied M., Belausov E., Sadot E.;
RT "Myosin XIK is a major player in cytoplasm dynamics and is regulated by two
RT amino acids in its tail.";
RL J. Exp. Bot. 63:241-249(2012).
CC -!- FUNCTION: Myosin heavy chain that is required for the cell cycle-
CC regulated transport of various organelles and proteins for their
CC segregation. Functions by binding with its tail domain to receptor
CC proteins on organelles and exerting force with its N-terminal motor
CC domain against actin filaments, thereby transporting its cargo along
CC polarized actin cables. Involved in the tip growth of root hair cells.
CC Plays a major role in trafficking of Golgi stacks, mitochondria and
CC peroxisomes during root hair development. Targets the peroxisome
CC through an interaction with RABC2A. Required for development of
CC pavement cells, trichomes, and stigmatic papillae.
CC {ECO:0000269|PubMed:15792961, ECO:0000269|PubMed:18178669,
CC ECO:0000269|PubMed:19060218, ECO:0000269|PubMed:19369591,
CC ECO:0000269|PubMed:20581304, ECO:0000269|PubMed:21914656,
CC ECO:0000269|PubMed:22672737}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with RABC2A AND RABD1.
CC {ECO:0000250, ECO:0000269|PubMed:18703495}.
CC -!- INTERACTION:
CC Q9LKB9; O49841: RABC2A; NbExp=3; IntAct=EBI-2009528, EBI-2009559;
CC Q9LKB9; Q9ZRE2: RABD1; NbExp=3; IntAct=EBI-2009528, EBI-2009542;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15792961,
CC ECO:0000269|PubMed:17288617, ECO:0000269|PubMed:17500056}.
CC Note=Colocalizes with peroxisome and cytoplasmic vesicles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LKB9-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in flowers, leaves, roots and stems.
CC {ECO:0000269|PubMed:7811972}.
CC -!- DOMAIN: Head-neck domain associates with cytoplasmic (transvacuolar) F-
CC actin in areas coinciding with the tracks of fast organelles.
CC {ECO:0000269|PubMed:17500056, ECO:0000269|PubMed:18598361}.
CC -!- DOMAIN: IQ domain mediates interaction with calmodulin. {ECO:0000250}.
CC -!- DOMAIN: The tail domain is a globular cargo-binding domain.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Impaired growth of root hair cells
CC (PubMed:18178669). No visible phenotype (PubMed:15792961).
CC {ECO:0000269|PubMed:15792961, ECO:0000269|PubMed:18178669,
CC ECO:0000269|PubMed:19060218}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. Plant myosin class XI subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA84066.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z34293; CAA84066.1; ALT_FRAME; mRNA.
DR EMBL; AP000368; BAA98070.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95022.1; -; Genomic_DNA.
DR EMBL; AK229124; BAF00999.1; -; mRNA.
DR PIR; S51824; S51824.
DR RefSeq; NP_199203.1; NM_123757.5. [Q9LKB9-1]
DR PDB; 7DHW; X-ray; 2.84 A; A=1-738.
DR PDBsum; 7DHW; -.
DR AlphaFoldDB; Q9LKB9; -.
DR SMR; Q9LKB9; -.
DR BioGRID; 19662; 3.
DR IntAct; Q9LKB9; 2.
DR STRING; 3702.AT5G43900.3; -.
DR iPTMnet; Q9LKB9; -.
DR PaxDb; Q9LKB9; -.
DR PRIDE; Q9LKB9; -.
DR ProteomicsDB; 251405; -. [Q9LKB9-1]
DR EnsemblPlants; AT5G43900.1; AT5G43900.1; AT5G43900. [Q9LKB9-1]
DR GeneID; 834412; -.
DR Gramene; AT5G43900.1; AT5G43900.1; AT5G43900. [Q9LKB9-1]
DR KEGG; ath:AT5G43900; -.
DR Araport; AT5G43900; -.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_3_1_1; -.
DR OMA; NQDNNDH; -.
DR PhylomeDB; Q9LKB9; -.
DR PRO; PR:Q9LKB9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LKB9; baseline and differential.
DR Genevisible; Q9LKB9; AT.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0048767; P:root hair elongation; IBA:GO_Central.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd15475; MyosinXI_CBD; 1.
DR CDD; cd01384; MYSc_Myo11; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR037975; MyosinXI_CBD.
DR InterPro; IPR036018; MYSc_Myo11.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 6.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 6.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; ATP-binding;
KW Calmodulin-binding; Coiled coil; Cytoplasm; Motor protein; Myosin;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1505
FT /note="Myosin-6"
FT /id="PRO_0000422861"
FT DOMAIN 8..57
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 62..731
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 734..763
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 757..786
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 782..811
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 805..834
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 830..859
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 853..882
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1148..1452
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 495..529
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 531..554
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 589..612
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 612..634
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT COILED 883..1048
FT /evidence="ECO:0000255"
FT BINDING 156..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 209..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 136
FT /note="A -> P (in Ref. 1; CAA84066)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="P -> S (in Ref. 1; CAA84066)"
FT /evidence="ECO:0000305"
FT CONFLICT 1442
FT /note="V -> A (in Ref. 4; BAF00999)"
FT /evidence="ECO:0000305"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 18..30
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:7DHW"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:7DHW"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 132..146
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 162..177
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 187..202
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 212..223
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 255..261
FT /evidence="ECO:0007829|PDB:7DHW"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:7DHW"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 295..309
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 313..330
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 348..360
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 365..373
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 390..420
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 427..434
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 446..466
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 468..476
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 490..497
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 503..512
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 518..528
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 533..536
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 542..549
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 552..557
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 561..565
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 571..578
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 583..586
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 604..619
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 622..630
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 643..652
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 655..664
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 668..671
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 672..679
FT /evidence="ECO:0007829|PDB:7DHW"
FT TURN 680..682
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 694..704
FT /evidence="ECO:0007829|PDB:7DHW"
FT STRAND 713..718
FT /evidence="ECO:0007829|PDB:7DHW"
FT HELIX 722..735
FT /evidence="ECO:0007829|PDB:7DHW"
SQ SEQUENCE 1505 AA; 169931 MW; B344E4668DEC6A8D CRC64;
MVANFNPSVG SFVWVEDPDE AWIDGEVVQV NGDEIKVLCT SGKHVVTKIS NAYPKDVEAP
ASGVDDMTRL AYLHEPGVLQ NLHSRYDINE IYTYTGSILI AVNPFRRLPH LYSSHMMAQY
KGASLGELSP HPFAVADAAY RQMINDGVSQ SILVSGESGA GKTESTKLLM RYLAYMGGRA
AAEGRSVEQK VLESNPVLEA FGNAKTVRNN NSSRFGKFVE IQFDEKGRIS GAAIRTYLLE
RSRVCQVSDP ERNYHCFYML CAAPQEDVKK FKLEEPKKYH YLNQSKCLEL DSINDAEEYH
ATRRAMDVVG ISTEEQDAIF SVVAAILHIG NIEFAKGEEI DSSIPKDDKS LFHLKTAAEL
LSCDEKALED SLCKRIMVTR DETITKTLDP EAATLSRDAL AKVMYSRLFD WLVDKINSSI
GQDHDSKYLI GVLDIYGFES FKTNSFEQFC INLTNEKLQQ HFNQHVFKME QEEYKKEEIN
WSYIEFVDNQ DILDLIEKKP GGIIALLDEA CMFPRSTHET FAQKLYQTFK THKRFTKPKL
ARSDFTICHY AGDVTYQTEL FLDKNKDYVI AEHQALLNSS SCSFVASLFP PMSDDSKQSK
FSSIGTRFKQ QLVSLLEILN TTEPHYIRCI KPNNLLKPGI FENENILQQL RCGGVMEAIR
ISCAGYPTRK HFDEFLARFG ILAPEVLVKN SDDPAACKKL LDKVGLEGYQ IGKTKVFLRA
GQMADLDTRR TEVLGRSASI IQRKVRSYLA KKSFIVLRNS AKQIQSVCRG YLARSVYEGM
RREAAALKIQ RDLRRFLARK AYTELYSAAV SVQAGMRGMV ARKELCFRRQ TKAAIIIQTW
CRGYLARLHY RKLKKAAITT QCAWRSKVAR GELRKLKMAA RETGALQAAK NKLEKQVEEL
TWRLQLEKRI RTDLEEAKKQ ESAKAQSSLE ELQLKCKETE ALLIKEREAA KKIAETAPII
KEIPVVDQEL MDKITNENEK LKSMVSSLEM KIGETEKKLQ ETTKISQDRL NQALEAESKL
VKLKTAMQRL EEKILDMEAE KKIMHQQTIS TPVRTNLGHP PTAPVKNLEN GHQTNLEKEF
NEAEFTTPVD GKAGKSAAER QIMNVDALID CVKDNIGFSN GKPVAAFTIY KCLLHWKCFE
SEKTNVFDRL IQMIGSAIEN EDDNSHLAYW LTSTSALLFL LQKSLKTNGS GATQSKKPPA
STSLFGRMAM SFRSSPASGN LAAAAEAAAL AVVRPVEAKY PALLFKQQLA AYVEKMFGMV
RDNLKRELST LLSLCIQAPR SSKGGMLRSG RSFGKDSPAV HWQSIIDGLN SLLVTLKENH
VPLVLIQKIY SQTFSYINVQ LFNSLLLRKE CCTFSNGEFV KSGLAELELW CCQAKEYSGP
SWEELKHIRQ AVGFLVIHQK YRISYDEIAN DLCPVLSVQQ LYRICTLYWD DSYNTRSVSQ
EVISSMRTLM TEESNDADSD SFLLDDDSSI PFSIDDISSS MEEKDFVGIK PAEELLENPA
FVFLH
