ID MYSS_CHICK Reviewed; 1939 AA. AC P13538; O13228; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 182. DE RecName: Full=Myosin heavy chain, skeletal muscle, adult; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=White leghorn; TISSUE=Pectoralis muscle; RX PubMed=9358064; DOI=10.1016/s0378-1119(97)00386-7; RA Chao T.H., Bandman E.; RT "Cloning, nucleotide sequence and characterization of a full-length cDNA RT encoding the myosin heavy chain from adult chicken pectoralis major RT muscle."; RL Gene 199:265-270(1997). RN [2] RP PROTEIN SEQUENCE OF 2-206. RC TISSUE=Pectoralis muscle; RX PubMed=1939027; DOI=10.1093/oxfordjournals.jbchem.a123543; RA Hayashida M., Maita T., Matsuda G.; RT "The primary structure of skeletal muscle myosin heavy chain: I. Sequence RT of the amino-terminal 23 kDa fragment."; RL J. Biochem. 110:54-59(1991). RN [3] RP PROTEIN SEQUENCE OF 207-637. RC TISSUE=Pectoralis muscle; RX PubMed=1939028; DOI=10.1093/oxfordjournals.jbchem.a123544; RA Komine Y., Maita T., Matsuda G.; RT "The primary structure of skeletal muscle myosin heavy chain: II. Sequence RT of the 50 kDa fragment of subfragment-1."; RL J. Biochem. 110:60-67(1991). RN [4] RP PROTEIN SEQUENCE OF 638-838. RC TISSUE=Pectoralis muscle; RX PubMed=1939029; DOI=10.1093/oxfordjournals.jbchem.a123545; RA Maita T., Miyanishi T., Matsuzono K., Tanioka Y., Matsuda G.; RT "The primary structure of skeletal muscle myosin heavy chain: III. Sequence RT of the 22 kDa fragment and the alignment of the 23 kDa, 50 kDa, and 22 kDa RT fragments."; RL J. Biochem. 110:68-74(1991). RN [5] RP PROTEIN SEQUENCE OF 839-1939. RC TISSUE=Pectoralis muscle; RX PubMed=1939030; DOI=10.1093/oxfordjournals.jbchem.a123546; RA Maita T., Yajima E., Nagata S., Miyanishi T., Nakayama S., Matsuda G.; RT "The primary structure of skeletal muscle myosin heavy chain: IV. Sequence RT of the rod, and the complete 1,938-residue sequence of the heavy chain."; RL J. Biochem. 110:75-87(1991). RN [6] RP PRELIMINARY PROTEIN SEQUENCE OF 2-809, ACETYLATION AT ALA-2, CLEAVAGE OF RP INITIATOR METHIONINE, AND METHYLATION AT LYS-36; LYS-131; LYS-552 AND RP HIS-756. RX PubMed=3467365; DOI=10.1073/pnas.84.2.416; RA Maita T., Hayashida M., Tanioka Y., Komine Y., Matsuda G.; RT "The primary structure of the myosin head."; RL Proc. Natl. Acad. Sci. U.S.A. 84:416-420(1987). RN [7] RP PROTEIN SEQUENCE OF 843-1271. RX PubMed=2610940; DOI=10.1515/bchm3.1989.370.2.1027; RA Watanabe B.; RT "Complete amino-acid sequence of subfragment-2 in adult chicken skeletal RT muscle myosin."; RL Biol. Chem. Hoppe-Seyler 370:1027-1034(1989). RN [8] RP PROTEIN SEQUENCE OF 853-1109. RX PubMed=2775482; DOI=10.1515/bchm3.1989.370.1.549; RA Watanabe B.; RT "Amino-acid sequence of the short subfragment-2 in adult chicken skeletal RT muscle myosin."; RL Biol. Chem. Hoppe-Seyler 370:549-558(1989). RN [9] RP PROTEIN SEQUENCE OF 1146-1271. RX PubMed=2713098; DOI=10.1515/bchm3.1989.370.1.55; RA Watanabe B.; RT "Amino-acid sequence of the hinge region in chicken myosin subfragment-2."; RL Biol. Chem. Hoppe-Seyler 370:55-61(1989). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1858-1939. RX PubMed=3034534; DOI=10.1089/dna.1987.6.91; RA Moriarity D.M., Barringer K.J., Dodgson J.B., Richter H.E., Young R.B.; RT "Genomic clones encoding chicken myosin heavy-chain genes."; RL DNA 6:91-99(1987). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-844. RX PubMed=8316857; DOI=10.1126/science.8316857; RA Rayment I., Rypniewski W.R., Schmidt-Base K., Smith R., Tomchick D.R., RA Benning M.M., Winkelmann D.A., Wesenberg G., Holden H.M.; RT "Three-dimensional structure of myosin subfragment-1: a molecular motor."; RL Science 261:50-58(1993). CC -!- FUNCTION: Muscle contraction. Myosin is a protein that binds to F-actin CC and has ATPase activity that is activated by F-actin. CC -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy CC chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 CC regulatory light chain subunits (MLC-2). CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the CC myofibrils. CC -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles CC of a 28-residue repeat pattern composed of 4 heptapeptides, CC characteristic for alpha-helical coiled coils. CC -!- DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light CC meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further CC cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment CC (S2). {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Myosin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U87231; AAB47555.1; -; mRNA. DR EMBL; M16557; AAA48970.1; -; Genomic_DNA. DR RefSeq; NP_001013415.1; NM_001013397.2. DR PDB; 1M8Q; EM; 70.00 A; A/D/G/P=5-844. DR PDB; 1MVW; EM; 70.00 A; A/D/G/J/M/P=5-844. DR PDB; 1O18; EM; 70.00 A; A/D/G/J/M/P=5-844. DR PDB; 1O19; EM; 70.00 A; A/D/G/J/M/S=5-844. DR PDB; 1O1A; EM; 70.00 A; A/D/G/J/M/P=5-844. DR PDB; 1O1B; EM; 70.00 A; A/D/G/J=5-844. DR PDB; 1O1C; EM; 70.00 A; A/D/G/J/P=5-844. DR PDB; 1O1D; EM; 70.00 A; A/D/G/J/M/P=5-844. DR PDB; 1O1E; EM; 70.00 A; A/D/G/J/M/P=5-844. DR PDB; 1O1F; EM; 70.00 A; A/D/G/J=5-844. DR PDB; 1O1G; EM; 70.00 A; A/D/G/J/M/P=5-844. DR PDB; 2MYS; X-ray; 2.80 A; A=2-844. DR PDB; 2W4A; EM; 35.00 A; M=5-844. DR PDB; 2W4G; EM; 35.00 A; M=5-844. DR PDB; 2W4H; EM; 35.00 A; M=5-844. DR PDBsum; 1M8Q; -. DR PDBsum; 1MVW; -. DR PDBsum; 1O18; -. DR PDBsum; 1O19; -. DR PDBsum; 1O1A; -. DR PDBsum; 1O1B; -. DR PDBsum; 1O1C; -. DR PDBsum; 1O1D; -. DR PDBsum; 1O1E; -. DR PDBsum; 1O1F; -. DR PDBsum; 1O1G; -. DR PDBsum; 2MYS; -. DR PDBsum; 2W4A; -. DR PDBsum; 2W4G; -. DR PDBsum; 2W4H; -. DR AlphaFoldDB; P13538; -. DR SMR; P13538; -. DR STRING; 9031.ENSGALP00000045379; -. DR iPTMnet; P13538; -. DR PaxDb; 9031-ENSGALP00000043474; -. DR KEGG; gga:427788; -. DR VEuPathDB; HostDB:geneid_427788; -. DR eggNOG; KOG0161; Eukaryota. DR InParanoid; P13538; -. DR BRENDA; 5.6.1.8; 1306. DR EvolutionaryTrace; P13538; -. DR PRO; PR:P13538; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell. DR GO; GO:0032982; C:myosin filament; IBA:GO_Central. DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central. 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:0006936; P:muscle contraction; IBA:GO_Central. DR CDD; cd01377; MYSc_class_II; 1. DR Gene3D; 1.10.10.820; -; 1. DR Gene3D; 1.20.5.340; -; 4. DR Gene3D; 1.20.5.370; -; 4. DR Gene3D; 1.20.5.4820; -; 1. DR Gene3D; 1.20.58.530; -; 1. DR Gene3D; 6.10.250.2420; -; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1. DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1. 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; IPR008989; Myosin_S1_N. DR InterPro; IPR002928; Myosin_tail. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014751; XRCC4-like_C. DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1. DR PANTHER; PTHR45615:SF74; MYOSIN HEAVY CHAIN, SKELETAL MUSCLE, ADULT; 1. DR Pfam; PF00063; Myosin_head; 1. DR Pfam; PF02736; Myosin_N; 1. DR Pfam; PF01576; Myosin_tail_1; 1. DR PRINTS; PR00193; MYOSINHEAVY. DR SMART; SM00015; IQ; 1. DR SMART; SM00242; MYSc; 1. DR SUPFAM; SSF90257; Myosin rod fragments; 5. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS50096; IQ; 1. DR PROSITE; PS51456; MYOSIN_MOTOR; 1. DR PROSITE; PS51844; SH3_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; ATP-binding; Calmodulin-binding; KW Coiled coil; Cytoplasm; Direct protein sequencing; Methylation; KW Motor protein; Muscle protein; Myosin; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Thick filament. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1939027, FT ECO:0000269|PubMed:3467365" FT CHAIN 2..1939 FT /note="Myosin heavy chain, skeletal muscle, adult" FT /id="PRO_0000123434" FT DOMAIN 34..83 FT /note="Myosin N-terminal SH3-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190" FT DOMAIN 87..781 FT /note="Myosin motor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782" FT DOMAIN 784..813 FT /note="IQ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT REGION 658..680 FT /note="Actin-binding" FT REGION 760..774 FT /note="Actin-binding" FT REGION 839..841 FT /note="Hinge" FT COILED 842..1939 FT /evidence="ECO:0000255" FT BINDING 180..187 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:3467365" FT MOD_RES 36 FT /note="N6-methyllysine" FT /evidence="ECO:0000269|PubMed:3467365" FT MOD_RES 131 FT /note="N6,N6,N6-trimethyllysine" FT /evidence="ECO:0000269|PubMed:3467365" FT MOD_RES 552 FT /note="N6,N6,N6-trimethyllysine" FT /evidence="ECO:0000269|PubMed:3467365" FT MOD_RES 756 FT /note="Pros-methylhistidine" FT /evidence="ECO:0000269|PubMed:3467365" FT CONFLICT 908 FT /note="C -> Q (in Ref. 7; AA sequence and 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 981 FT /note="L -> F (in Ref. 1; AAB47555)" FT /evidence="ECO:0000305" FT CONFLICT 1344 FT /note="E -> D (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1546 FT /note="S -> A (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1797..1798 FT /note="HV -> QL (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1831 FT /note="S -> A (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1864 FT /note="I -> V (in Ref. 10; AAA48970)" FT /evidence="ECO:0000305" FT CONFLICT 1930..1932 FT /note="IHG -> FH (in Ref. 10; AAA48970)" FT /evidence="ECO:0000305" FT HELIX 15..18 FT /evidence="ECO:0007829|PDB:2MYS" FT TURN 22..25 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 26..29 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 44..49 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 51..55 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 62..65 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 75..77 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 92..94 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 100..107 FT /evidence="ECO:0007829|PDB:2MYS" FT TURN 111..114 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 117..119 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 124..127 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 134..136 FT /evidence="ECO:0007829|PDB:2MYS" FT TURN 141..146 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 156..170 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 174..180 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 186..190 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 193..200 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 219..234 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 242..245 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 247..255 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 257..263 FT /evidence="ECO:0007829|PDB:2MYS" FT TURN 275..277 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 287..292 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 299..304 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 310..312 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 314..316 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 328..341 FT /evidence="ECO:0007829|PDB:2MYS" FT TURN 346..348 FT /evidence="ECO:0007829|PDB:2MYS" FT TURN 351..353 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 358..362 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 367..370 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 375..379 FT /evidence="ECO:0007829|PDB:2MYS" FT TURN 383..385 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 388..391 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 395..403 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 410..412 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 420..431 FT /evidence="ECO:0007829|PDB:2MYS" FT TURN 434..436 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 439..449 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 458..466 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 472..474 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 476..486 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 489..503 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 518..528 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 533..540 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 548..551 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 556..559 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 563..567 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 579..583 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 588..591 FT /evidence="ECO:0007829|PDB:2MYS" FT TURN 596..598 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 606..613 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 620..623 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 651..659 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 662..666 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 668..676 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 689..699 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 701..708 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 718..725 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 726..728 FT /evidence="ECO:0007829|PDB:2MYS" FT TURN 729..731 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 743..748 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 751..753 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 756..762 FT /evidence="ECO:0007829|PDB:2MYS" FT STRAND 765..768 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 772..782 FT /evidence="ECO:0007829|PDB:2MYS" FT HELIX 785..827 FT /evidence="ECO:0007829|PDB:2MYS" FT TURN 831..833 FT /evidence="ECO:0007829|PDB:2MYS" SQ SEQUENCE 1939 AA; 223145 MW; F6DAD73CABD82BFD CRC64; MASPDAEMAA FGEAAPYLRK SEKERIEAQN KPFDAKSSVF VVHPKESFVK GTIQSKEGGK VTVKTEGGET LTVKEDQVFS MNPPKYDKIE DMAMMTHLHE PAVLYNLKER YAAWMIYTYS GLFCVTVNPY KWLPVYNPEV VLAYRGKKRQ EAPPHIFSIS DNAYQFMLTD RENQSILITG ESGAGKTVNT KRVIQYFATI AASGEKKKEE QSGKMQGTLE DQIISANPLL EAFGNAKTVR NDNSSRFGKF IRIHFGATGK LASADIETYL LEKSRVTFQL PAERSYHIFY QIMSNKKPEL IDMLLITTNP YDYHYVSQGE ITVPSIDDQE ELMATDSAID ILGFSADEKT AIYKLTGAVM HYGNLKFKQK QREEQAEPDG TEVADKAAYL MGLNSAELLK ALCYPRVKVG NEFVTKGQTV SQVHNSVGAL AKAVYEKMFL WMVIRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSFEQLC INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE CMFPKATDTS FKNKLYDQHL GKSNNFQKPK PAKGKAEAHF SLVHYAGTVD YNISGWLEKN KDPLNETVIG LYQKSSVKTL ALLFATYGGE AEGGGGKKGG KKKGSSFQTV SALFRENLNK LMANLRSTHP HFVRCIIPNE TKTPGAMEHE LVLHQLRCNG VLEGIRICRK GFPSRVLYAD FKQRYRVLNA SAIPEGQFMD SKKASEKLLG SIDVDHTQYR FGHTKVFFKA GLLGLLEEMR DDKLAEIITR TQARCRGFLM RVEYRRMVER RESIFCIQYN VRSFMNVKHW PWMKLFFKIK PLLKSAESEK EMANMKEEFE KTKEELAKSE AKRKELEEKM VVLLQEKNDL QLQVQAEADS LADAEERCDQ LIKTKIQLEA KIKEVTERAE DEEEINAELT AKKRKLEDEC SELKKDIDDL ELTLAKVEKE KHATENKVKN LTEEMAVLDE TIAKLTKEKK ALQEAHQQTL DDLQVEEDKV NTLTKAKTKL EQQVDDLEGS LEQEKKLRMD LERAKRKLEG DLKLAHDSIM DLENDKQQLD EKLKKKDFEI SQIQSKIEDE QALGMQLQKK IKELQARIEE LEEEIEAERT SRAKAEKHRA DLSRELEEIS ERLEEAGGAT AAQIEMNKKR EAEFQKMRRD LEEATLQHEA TAAALRKKHA DSTAELGEQI DNLQRVKQKL EKEKSELKME IDDLASNMES VSKAKANLEK MCRTLEDQLS EIKTKEEQNQ RMINDLNTQR ARLQTETGEY SRQAEEKDAL ISQLSRGKQG FTQQIEELKR HLEEEIKAKN ALAHALQSAR HDCELLREQY EEEQEAKGEL QRALSKANSE VAQWRTKYET DAIQRTEELE EAKKKLAQRL QDAEEHVEAV NAKCASLEKT KQRLQNEVED LMVDVERSNA ACAALDKKQK NFDKILAEWK QKYEETQTEL EASQKESRSL STELFKMKNA YEESLDHLET LKRENKNLQQ EIADLTEQIA EGGKAVHELE KVKKHVEQEK SELQASLEEA EASLEHEEGK ILRLQLELNQ IKSEIDRKIA EKDEEIDQLK RNHLRIVESM QSTLDAEIRS RNEALRLKKK MEGDLNEMEI QLSHANRMAA EAQKNLRNTQ GTLKDTQIHL DDALRTQEDL KEQVAMVERR ANLLQAEVEE LRGALEQTER SRKVAEQELL DATERVQLLH TQNTSLINTK KKLETDIVQI QSEMEDTIQE ARNAEEKAKK AITDAAMMAE ELKKEQDTSA HLERMKKNMD QTVKDLHVRL DEAEQLALKG GKKQLQKLEA RVRELEGEVD SEQKRSAEAV KGVRKYERRV KELTYQCEED RKNILRLQDL VDKLQMKVKS YKRQAEEAEE LSNVNLSKFR KIQHELEEAE ERADIAESQV NKLRVKSREI HGKKIEEEE //