MYH9_RAT
ID MYH9_RAT Reviewed; 1961 AA.
AC Q62812;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Myosin-9;
DE AltName: Full=Cellular myosin heavy chain, type A;
DE AltName: Full=Myosin heavy chain 9;
DE AltName: Full=Myosin heavy chain, non-muscle IIa;
DE AltName: Full=Non-muscle myosin heavy chain A;
DE Short=NMMHC-A;
DE AltName: Full=Non-muscle myosin heavy chain IIa;
DE Short=NMMHC II-a;
DE Short=NMMHC-IIA;
GN Name=Myh9;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8740433; DOI=10.1007/bf00140325;
RA Choi O.H., Park C., Itoh K., Adelstein R.S., Beaven M.A.;
RT "Cloning of the cDNA encoding rat myosin heavy chain-A and evidence for the
RT absence of myosin heavy chain-B in cultured rat mast (RBL-2H3) cells.";
RL J. Muscle Res. Cell Motil. 17:69-77(1996).
RN [2]
RP PROTEIN SEQUENCE OF 181-199; 546-555; 618-639; 1241-1248; 1402-1411;
RP 1446-1455; 1474-1478; 1557-1567; 1605-1614; 1793-1803 AND 1925-1934, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP RETRACTED PAPER.
RX PubMed=12944413; DOI=10.1074/jbc.m306360200;
RA Ozaslan D., Wang S., Ahmed B.A., Kocabas A.M., McCastlain J.C., Bene A.,
RA Kilic F.;
RT "Glycosyl modification facilitates homo- and hetero-oligomerization of the
RT serotonin transporter. A specific role for sialic acid residues.";
RL J. Biol. Chem. 278:43991-44000(2003).
RN [4]
RP RETRACTION NOTICE OF PUBMED:12944413.
RX PubMed=31201245; DOI=10.1074/jbc.w119.009466;
RA Ozaslan D., Wang S., Ahmed B.A., Kocabas A.M., McCastlain J.C., Bene A.,
RA Kilic F.;
RT "Withdrawal: Glycosyl modification facilitates homo- and hetero-
RT oligomerization of the serotonin transporter: a specific role for sialic
RT acid residues.";
RL J. Biol. Chem. 294:9657-9657(2019).
RN [5]
RP INTERACTION WITH PDLIM2.
RX PubMed=15505042; DOI=10.1167/iovs.04-0721;
RA Torrado M., Senatorov V.V., Trivedi R., Fariss R.N., Tomarev S.I.;
RT "Pdlim2, a novel PDZ-LIM domain protein, interacts with alpha-actinins and
RT filamin A.";
RL Invest. Ophthalmol. Vis. Sci. 45:3955-3963(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-754; SER-1114; SER-1715 AND
RP SER-1944, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Cellular myosin that appears to play a role in cytokinesis,
CC cell shape, and specialized functions such as secretion and capping (By
CC similarity). Required for cortical actin clearance prior to oocyte
CC exocytosis (By similarity). Promotes cell motility in conjunction with
CC S100A4 (By similarity). During cell spreading, plays an important role
CC in cytoskeleton reorganization, focal contact formation (in the margins
CC but not the central part of spreading cells), and lamellipodial
CC retraction; this function is mechanically antagonized by MYH10 (By
CC similarity). {ECO:0000250|UniProtKB:P35579,
CC ECO:0000250|UniProtKB:Q8VDD5}.
CC -!- SUBUNIT: Myosin is a hexameric protein that consists of 2 heavy chain
CC subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory
CC light chain subunits (MLC-2). Interacts with RASIP1 (By similarity).
CC Interacts with DDR1 (By similarity). Interacts with PDLIM2
CC (PubMed:15505042). Interacts with SVIL (By similarity). Interacts with
CC HTRA3 (By similarity). Interacts with Myo7a (By similarity). Interacts
CC with CFAP95 (By similarity). Interacts with LIMCH1; independently of
CC the integration of MYH9 into the myosin complex (By similarity).
CC Interacts with RAB3A (By similarity). Interacts with ZBED4 (By
CC similarity). Interacts with S100A4; this interaction increases cell
CC motility (By similarity). {ECO:0000250|UniProtKB:P35579,
CC ECO:0000250|UniProtKB:Q8VDD5, ECO:0000269|PubMed:15505042}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8VDD5}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q8VDD5}. Cytoplasmic vesicle, secretory vesicle,
CC Cortical granule {ECO:0000250|UniProtKB:Q8VDD5}. Note=Colocalizes with
CC actin filaments at lamellipodia margins and at the leading edge of
CC migrating cells (By similarity). In retinal pigment epithelial cells,
CC predominantly localized to stress fiber-like structures with some
CC localization to cytoplasmic puncta (By similarity).
CC {ECO:0000250|UniProtKB:P35579}.
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 -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P35579,
CC ECO:0000250|UniProtKB:Q8VDD5}.
CC -!- PTM: Ubiquitination. {ECO:0000250|UniProtKB:P35579,
CC ECO:0000250|UniProtKB:Q8VDD5}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Reported to interact with SLC6A4 in its sialylated form.
CC However, this publication was retracted due to image duplication in the
CC figures. {ECO:0000305|PubMed:12944413, ECO:0000305|PubMed:31201245}.
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DR EMBL; U31463; AAA74950.1; -; mRNA.
DR AlphaFoldDB; Q62812; -.
DR SMR; Q62812; -.
DR BioGRID; 247773; 10.
DR CORUM; Q62812; -.
DR IntAct; Q62812; 5.
DR MINT; Q62812; -.
DR STRING; 10116.ENSRNOP00000007398; -.
DR CarbonylDB; Q62812; -.
DR iPTMnet; Q62812; -.
DR PhosphoSitePlus; Q62812; -.
DR SwissPalm; Q62812; -.
DR jPOST; Q62812; -.
DR PaxDb; Q62812; -.
DR PRIDE; Q62812; -.
DR UCSC; RGD:3140; rat.
DR RGD; 3140; Myh9.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; Q62812; -.
DR PhylomeDB; Q62812; -.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-5627123; RHO GTPases activate PAKs.
DR PRO; PR:Q62812; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005884; C:actin filament; IDA:RGD.
DR GO; GO:0042641; C:actomyosin; ISO:RGD.
DR GO; GO:0005826; C:actomyosin contractile ring; ISS:UniProtKB.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0005903; C:brush border; IDA:RGD.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0030863; C:cortical cytoskeleton; ISO:RGD.
DR GO; GO:0060473; C:cortical granule; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0001772; C:immunological synapse; ISO:RGD.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0016459; C:myosin complex; ISO:RGD.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; ISO:RGD.
DR GO; GO:0097513; C:myosin II filament; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISO:RGD.
DR GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0001931; C:uropod; ISO:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0043531; F:ADP binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0031762; F:follicle-stimulating hormone receptor binding; IDA:RGD.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; ISS:UniProtKB.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0043495; F:protein-membrane adaptor activity; ISS:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; IDA:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:RGD.
DR GO; GO:0051017; P:actin filament bundle assembly; IMP:RGD.
DR GO; GO:0070650; P:actin filament bundle distribution; IMP:RGD.
DR GO; GO:0030048; P:actin filament-based movement; ISS:UniProtKB.
DR GO; GO:0031032; P:actomyosin structure organization; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0000904; P:cell morphogenesis involved in differentiation; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEP:RGD.
DR GO; GO:0060471; P:cortical granule exocytosis; ISS:UniProtKB.
DR GO; GO:0032506; P:cytokinetic process; ISS:UniProtKB.
DR GO; GO:0051295; P:establishment of meiotic spindle localization; ISO:RGD.
DR GO; GO:0001768; P:establishment of T cell polarity; ISO:RGD.
DR GO; GO:0042699; P:follicle-stimulating hormone signaling pathway; IMP:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0032418; P:lysosome localization; ISO:RGD.
DR GO; GO:0000212; P:meiotic spindle organization; ISO:RGD.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:UniProtKB.
DR GO; GO:0030224; P:monocyte differentiation; ISS:UniProtKB.
DR GO; GO:0007520; P:myoblast fusion; ISO:RGD.
DR GO; GO:1903919; P:negative regulation of actin filament severing; ISO:RGD.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IMP:RGD.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISO:RGD.
DR GO; GO:0001778; P:plasma membrane repair; ISO:RGD.
DR GO; GO:0030220; P:platelet formation; ISS:UniProtKB.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IMP:RGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:RGD.
DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; IMP:RGD.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:RGD.
DR GO; GO:1903923; P:positive regulation of protein processing in phagocytic vesicle; ISO:RGD.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR GO; GO:0045055; P:regulated exocytosis; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:1905684; P:regulation of plasma membrane repair; ISO:RGD.
DR GO; GO:0032796; P:uropod organization; ISO:RGD.
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 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 Acetylation; Actin-binding; ATP-binding; Calmodulin-binding; Cell adhesion;
KW Cell shape; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Direct protein sequencing; Methylation; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT CHAIN 2..1961
FT /note="Myosin-9"
FT /id="PRO_0000123418"
FT DOMAIN 27..77
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 81..776
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 779..808
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 2..838
FT /note="Mediates interaction with LIMCH1"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT REGION 654..676
FT /note="Actin-binding"
FT REGION 1035..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1878..1910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1938..1961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 841..1927
FT /evidence="ECO:0000255"
FT COMPBIAS 1878..1909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 11
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 435
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 613
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 754
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 850
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 860
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 975
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1024
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61879"
FT MOD_RES 1249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1358
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1393
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1405
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1411
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1460
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1639
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1670
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1715
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1794
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1803
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1846
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1924
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61879"
FT MOD_RES 1944
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1961 AA; 226338 MW; 9B9876D9681FB19E CRC64;
MAQQAADKYL YVDKNFINNP LAQADCGAKK LVWVPSTKNG FEPASLKEEV GEEAIVELVE
NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN LKERYYSGLI YTYSGLFCVV
INPYKNLPIY SEEIVDMYKG KKRHEMPPHI YAITDTAYRS MMQDREDQSI LCTGESGAGK
TENTKKVIQY LAHVASSHKS KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR
INFDVNGYIV GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY
RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPEDEQMGLL RVISGVLQLG NIVFKKERNT
DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY VQKAQTKEQA DFAIEALAKA
TYERMFRWLV LRINKALDKT KRQGASFIGI LDIAGFEIFD LNSFEQLCIN YTNEKLQQLF
NHTMFILEQE EYQREGIEWN FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK
SFVEKVVQEQ GTHPKFQKPK QLKDKADFCI IHYAGKVDYK ADEWLMKNMD PLNDNIATLL
HQSSDKFVSE LWKDVDRIIG LDQVAGMSET ALPGAFKTRK GMFRTVGQLY KEQLAKLMAT
LRNTNPNFVC CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG IRICRQGFPN RVVFQEFRQR
YEILTPNSIP KGFMDGKQAC VLMIKALELD SNLYRIGQSK VFFRSGVLAH LEEERDLKIT
DVIIGFQACC RGYLARKAFA KRQQQLTAMK VLQRNCAAYL RLRNWQWWRL FTKVKPLLNS
IRHEDELLAK EAELTKVREK HLAAENRLTE METMQSQLMA EKLQLQEQLQ AKTELCAEAE
ELRARLTAKK QELEEICHDL EARVEEEEER CQYLQAEKKK MQQNIQELEE QLEEEESARQ
KLQLEKVTTE AKLKKLEEDQ IIMEDQNCKL AKEKKLLEDR VAEFTTDLME EEEKSKSLAK
LKNKHEAMIT DLEERLRREE KQRQELEKTR RKLEGDSTDL SDQIAELQAQ IAELKMQLAK
KEEELQAALA RVEEEAAQKN MALKKIRELE TQISELQEDL ESERACRNKA EKQKRDLGEE
LEALKTELED TLDSTAAQQE LRSKREQEVS ILKKTLEDEA KTHEAQIQEM RQKHSQAVEE
LAEQLEQTKR VKATLEKAKQ TLENERGELA NEVKALLQGK GDSEHKRKKV EAQLQELQVK
FSEGERVRTE LADKVSKLQV ELDSVTGLLN QSDSKSSKLT KDFSALESQL QDTQELLQEE
NRQKLSLSTK LKQMEDEKNS FREQLEEEEE EAKRNLEKQI ATLHAQVTDM KKKMEDGVGC
LETAEEAKRR LQKDLEGLSQ RLEEKVAAYD KLEKTKTRLQ QELDDLLVDL DHQRQSVSNL
EKKQKKFDQL LAEEKTISAK YAEERDRAEA EAREKETKAL SLARALEEAM EQKAELERLN
KQFRTEMEDL MSSKDDVGKS VHELEKSNRA LEQQVEEMKT QLEELEDELQ ATEDAKLRLE
VNLQAMKAQF ERDLQGRDEQ SEEKKKQLVR QVREMEAELE DERKQRSIAM AARKKLEMDL
KDLEAHIDTA NKNREEAIKQ LRKLQAQMKD CMRDVDDTRA SREEILAQAK ENEKKLKSME
AEMIQLQEEL AAAERAKRQA QQERDELADE IANSSGKGAL ALEEKRRLEA LIALLEEELE
EEQGNTELIN DRLKKANLQI DQINTDLNLE RSHAQKNENA RQQLERQNKE LKAKLQEMES
AVKSKYKASI AALEAKIAQL EEQLDNETKE RQAASKQVRR AEKKLKDVLL QVEDERRNAE
QFKDQADKAS TRLKQLKRQL EEAEEEAQRA NASRRKLQRE LEDATETADA MNREVSSLKN
KLRRGDMPFV VTRRIVRKGT GDCSDEEVDG KADGADAKAT E
