MYH4_RABIT
ID MYH4_RABIT Reviewed; 1938 AA.
AC Q28641; G1TKS9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Myosin-4;
DE AltName: Full=Myosin heavy chain 2b;
DE Short=MyHC-2b;
DE AltName: Full=Myosin heavy chain 4;
DE AltName: Full=Myosin heavy chain, skeletal muscle, juvenile;
GN Name=MYH4;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Skeletal muscle;
RA Maeda K., Hostinova E., Roesch-Kleinkauf A., Schuster H., Gasperik J.,
RA Wittinghofer A.;
RT "Isolation, sequencing of myosin heavy chain cDNA from rabbit skeletal
RT muscle and a novel cosynthesis of S-1 fragment with the essential and
RT regulatory light chains.";
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000312|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [3]
RP PROTEIN SEQUENCE OF 748-760, AND METHYLATION AT HIS-756.
RC TISSUE=Skeletal muscle;
RX PubMed=5539225; DOI=10.1021/bi00778a006;
RA Huszar G., Elzinga M.;
RT "Amino acid sequence around the single 3-methylhistidine residue in rabbit
RT skeletal muscle myosin.";
RL Biochemistry 10:229-236(1971).
CC -!- FUNCTION: Muscle contraction.
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:0000255|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: Represents a conventional myosin. This protein should not be
CC confused with the unconventional myosin-4 (MYO4). {ECO:0000305}.
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DR EMBL; U32574; AAA74199.1; -; mRNA.
DR EMBL; AAGW02049470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A35557; A35557.
DR PIR; A59293; A59293.
DR RefSeq; NP_001103286.1; NM_001109816.1.
DR PDB; 6YSY; X-ray; 3.25 A; A=1-1938.
DR PDBsum; 6YSY; -.
DR AlphaFoldDB; Q28641; -.
DR SMR; Q28641; -.
DR STRING; 9986.ENSOCUP00000017571; -.
DR ChEMBL; CHEMBL4295837; -.
DR PRIDE; Q28641; -.
DR ABCD; Q28641; 1 sequenced antibody.
DR Ensembl; ENSOCUT00000022103; ENSOCUP00000017571; ENSOCUG00000026636.
DR GeneID; 100125991; -.
DR KEGG; ocu:100125991; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000154760; -.
DR HOGENOM; CLU_000192_8_0_1; -.
DR InParanoid; Q28641; -.
DR OrthoDB; 47111at2759; -.
DR TreeFam; TF314375; -.
DR Proteomes; UP000001811; Chromosome 19.
DR Bgee; ENSOCUG00000026636; Expressed in skeletal muscle tissue and 13 other tissues.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
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; 2.
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; Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil;
KW Cytoplasm; Direct protein sequencing; Methylation; Motor protein;
KW Muscle protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Thick filament.
FT CHAIN 1..1938
FT /note="Myosin-4"
FT /id="PRO_0000123400"
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 86..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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 760..774
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT COILED 845..1926
FT /evidence="ECO:0000255"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 389
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 419
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 424
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 756
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000269|PubMed:5539225"
FT MOD_RES 1091
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1095
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1240
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1254
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1264
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1285
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1463
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1466
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1491
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1500
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1516
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1599
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1713
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1725
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1729
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1735
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1738
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT CONFLICT 2..3
FT /note="SS -> RK (in Ref. 1; AAA74199)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="G -> A (in Ref. 1; AAA74199)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="G -> R (in Ref. 1; AAA74199)"
FT /evidence="ECO:0000305"
FT CONFLICT 667..669
FT /note="STH -> THS (in Ref. 1; AAA74199)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="C -> S (in Ref. 1; AAA74199)"
FT /evidence="ECO:0000305"
FT CONFLICT 757..758
FT /note="TQ -> QT (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="R -> E (in Ref. 1; AAA74199)"
FT /evidence="ECO:0000305"
FT CONFLICT 1484
FT /note="L -> V (in Ref. 1; AAA74199)"
FT /evidence="ECO:0000305"
FT CONFLICT 1892..1894
FT /note="SNV -> CNI (in Ref. 1; AAA74199)"
FT /evidence="ECO:0000305"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:6YSY"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:6YSY"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 46..56
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:6YSY"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 219..234
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:6YSY"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 328..342
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 346..362
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 382..390
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 395..403
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 420..450
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 458..464
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 476..497
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 499..506
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 521..528
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 533..541
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 548..559
FT /evidence="ECO:0007829|PDB:6YSY"
FT TURN 560..562
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 579..584
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 596..599
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 606..613
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 618..623
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 650..666
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 668..676
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 689..699
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 701..710
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 714..717
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 718..725
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 726..732
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 741..749
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 758..761
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 763..768
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 772..808
FT /evidence="ECO:0007829|PDB:6YSY"
SQ SEQUENCE 1938 AA; 222876 MW; 20512FD30FE1282C CRC64;
MSSDADMAIF GEAAPYLRKS EKERIEAQNK PFDAKSSVFV ADPKESFVKA TVQSREGGKV
TAKTEAGATV TVKEDQVFPM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNAEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA VTGDKKKEEA TSGKMQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QIMSNKKPDL
IEMLLITTNP YDYAFVSQGE ITVPSIDDQE ELMATDSAID ILGFTSDERV SIYKLTGAVM
HYGNMKFKQK QREEQAEPDG TEVADKAAYL QSLNSADLLK ALCYPRVKVG NEYVTKGQTV
QQVYNAVGAL AKAVYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDTS FKNKLYEQHL GKSNNFQKPK PAKGKVEAHF SLVHYAGTVD YNITGWLDKN
KDPLNETVVG LYQKSAMKTL AFLFTGTAAA EAEGGGKKGG KKKGSSFQTV SALFRENLNK
LMTNLRSTHP HFVRCIIPNE TKTPGAMEHE LVLHQLRCNG VLEGIRICRK GFPSRILYAD
FKQRYKVLNA SAIPEGQFID SKKASEKLLG SIDVDHTQYK FGHTKVFFKA GLLGLLEEMR
DDKLAQLITR TQAMCRGFLA RVEYKKMVER RESIFCIQYN IRAFMNVKHW PWMKLYFKIK
PLLKSAETEK EMANMKEEFE KTKESLAKAE AKRKELEEKM VALMQEKNDL QLQVQAEADS
LADAEERCDQ LIKTKIQLEA KIKEVTERAE DEEEINAELT AKKRKLEDEC SELKKDIDDL
ELTLAKVEKE KHATENKVKN LTEEMAGLDE TIAKLTKEKK ALQEAHQQTL DDLQAEEDKV
NTLTKAKTKL EQQVDDLEGS LEQEKKIRMD LERAKRKLEG DLKLAQESTM DIENDKQQLD
EKLKKKEFEM SNLQSKIEDE QALAMQLQKK IKELQARIEE LEEEIEAERA SRAKAEKQRS
DLSRELEEIS ERLEEAGGAT SAQIEMNKKR EAEFQKMRRD LEEATLQHEA TAATLRKKHA
DSVAELGEQI DNLQRVKQKL EKEKSELKME IDDLASNMET VSKAKGNLEK MCRTLEDQVS
ELKTKEEEHQ RLINDLSAQR ARLQTESGEF SRQLDEKDSL VSQLSRGKQA FTQQIEELKR
QLEEEIKAKS ALAHALQSAR HDCDLLREQY EEEQEAKAEL QRAMSKANSE VAQWRTKYET
DAIQRTEELE EAKKKLAQRL QDAEEHVEAV NAKCASLEKT KQRLQNEVED LMIDVERTNA
ACAALDKKQR NFDKILAEWK HKYEETHAEL EASQKESRSL STELFKVKNA YEESLDQLET
LKRENKNLQQ EISDLTEQIA EGGKRIHELE KVKKQVEQEK SELQAALEEA EASLEHEEGK
ILRIQLELNQ VKSEIDRKIA EKDEEIDQLK RNHIRVVESM QSTLDAEIRS RNDAIRIKKK
MEGDLNEMEI QLNHANRMAA EALRNYRNTQ GILKDTQLHL DDALRGQEDL KEQLAMVERR
ANLLQAEIEE LRATLEQTER SRKVAEQELL DASERVQLLH TQNTSLINTK KKLETDISQI
QGEMEDIVQE ARNAEEKAKK AITDAAMMAE ELKKEQDTSA HLERMKKNME QTVKDLQHRL
DEAEQLALKG GKKQIQKLEA RVRELEAEVE SEQKRNVEAV KGLRKHERRV KELTYQTEED
RKNVLRLQDL VDKLQAKVKS YKRQAEEAEE QSNVNLSKFR KLQHELEEAE ERADIAESQV
NKLRVKSREV HTKVISEE
