MYSS_CHICK
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 03-AUG-2022, entry version 174.
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}.
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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.ENSGALP00000043474; -.
DR iPTMnet; P13538; -.
DR PaxDb; P13538; -.
DR PRIDE; P13538; -.
DR GeneID; 427788; -.
DR KEGG; gga:427788; -.
DR CTD; 427788; -.
DR VEuPathDB; HostDB:geneid_427788; -.
DR eggNOG; KOG0161; Eukaryota.
DR OrthoDB; 47111at2759; -.
DR BRENDA; 5.6.1.8; 1306.
DR EvolutionaryTrace; P13538; -.
DR PRO; PR:P13538; -.
DR Proteomes; UP000000539; Unplaced.
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 Gene3D; 1.20.5.370; -; 4.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 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 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; SSF52540; SSF52540; 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
