ID POLS_SAGV Reviewed; 1253 AA. AC Q9JGK8; Q80S33; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 29-SEP-2021, entry version 105. DE RecName: Full=Structural polyprotein; DE AltName: Full=p130; DE Contains: DE RecName: Full=Capsid protein; DE EC=3.4.21.90 {ECO:0000250|UniProtKB:P03315}; DE AltName: Full=Coat protein; DE Short=C; DE Contains: DE RecName: Full=Precursor of protein E3/E2; DE AltName: Full=p62; DE AltName: Full=pE2; DE Contains: DE RecName: Full=Assembly protein E3; DE Contains: DE RecName: Full=Spike glycoprotein E2; DE AltName: Full=E2 envelope glycoprotein; DE Contains: DE RecName: Full=6K protein; DE Contains: DE RecName: Full=Spike glycoprotein E1; DE AltName: Full=E1 envelope glycoprotein; OS Sagiyama virus (SAGV). OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes; OC Martellivirales; Togaviridae; Alphavirus. OX NCBI_TaxID=59303; OH NCBI_TaxID=7163; Aedes vexans (Inland floodwater mosquito) (Culex vexans). OH NCBI_TaxID=7178; Culex tritaeniorhynchus (Mosquito). OH NCBI_TaxID=9796; Equus caballus (Horse). OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9823; Sus scrofa (Pig). OH NCBI_TaxID=9627; Vulpes vulpes (Red fox). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=10769079; DOI=10.1099/0022-1317-81-5-1353; RA Shirako Y., Yamaguchi Y.; RT "Genome structure of Sagiyama virus and its relatedness to other RT alphaviruses."; RL J. Gen. Virol. 81:1353-1360(2000). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RA Kinney R.M., Pfeffer M.; RT "Nucleotide sequence analyses of the 26S mRNAs of viruses of the genus RT Alphavirus."; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: [Capsid protein]: Forms an icosahedral capsid with a T=4 CC symmetry composed of 240 copies of the capsid protein surrounded by a CC lipid membrane through which penetrate 80 spikes composed of trimers of CC E1-E2 heterodimers (By similarity). The capsid protein binds to the CC viral RNA genome at a site adjacent to a ribosome binding site for CC viral genome translation following genome release (By similarity). CC Possesses a protease activity that results in its autocatalytic CC cleavage from the nascent structural protein (By similarity). Following CC its self-cleavage, the capsid protein transiently associates with CC ribosomes, and within several minutes the protein binds to viral RNA CC and rapidly assembles into icosahedric core particles (By similarity). CC The resulting nucleocapsid eventually associates with the cytoplasmic CC domain of the spike glycoprotein E2 at the cell membrane, leading to CC budding and formation of mature virions (By similarity). In case of CC infection, new virions attach to target cells and after clathrin- CC mediated endocytosis their membrane fuses with the host endosomal CC membrane (By similarity). This leads to the release of the nucleocapsid CC into the cytoplasm, followed by an uncoating event necessary for the CC genomic RNA to become accessible (By similarity). The uncoating might CC be triggered by the interaction of capsid proteins with ribosomes (By CC similarity). Binding of ribosomes would release the genomic RNA since CC the same region is genomic RNA-binding and ribosome-binding (By CC similarity). Specifically inhibits interleukin-1 receptor-associated CC kinase 1/IRAK1-dependent signaling during viral entry, representing a CC means by which the alphaviruses may evade innate immune detection and CC activation prior to viral gene expression (By similarity). CC {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:P03316, CC ECO:0000250|UniProtKB:P27284}. CC -!- FUNCTION: [Assembly protein E3]: Provides the signal sequence for the CC translocation of the precursor of protein E3/E2 to the host endoplasmic CC reticulum. Furin-cleaved E3 remains associated with spike glycoprotein CC E1 and mediates pH protection of the latter during the transport via CC the secretory pathway. After virion release from the host cell, the CC assembly protein E3 is gradually released in the extracellular space. CC {ECO:0000250|UniProtKB:P03315}. CC -!- FUNCTION: [Spike glycoprotein E2]: Plays a role in viral attachment to CC target host cell, by binding to the cell receptor. Synthesized as a p62 CC precursor which is processed by furin at the cell membrane just before CC virion budding, giving rise to E2-E1 heterodimer. The p62-E1 CC heterodimer is stable, whereas E2-E1 is unstable and dissociate at low CC pH. p62 is processed at the last step, presumably to avoid E1 fusion CC activation before its final export to cell surface. E2 C-terminus CC contains a transitory transmembrane that would be disrupted by CC palmitoylation, resulting in reorientation of the C-terminal tail from CC lumenal to cytoplasmic side. This step is critical since E2 C-terminus CC is involved in budding by interacting with capsid proteins. This CC release of E2 C-terminus in cytoplasm occurs lately in protein export, CC and precludes premature assembly of particles at the endoplasmic CC reticulum membrane. {ECO:0000250|UniProtKB:P03315}. CC -!- FUNCTION: [6K protein]: Constitutive membrane protein involved in virus CC glycoprotein processing, cell permeabilization, and the budding of CC viral particles. Disrupts the calcium homeostasis of the cell, probably CC at the endoplasmic reticulum level. This leads to cytoplasmic calcium CC elevation. Because of its lipophilic properties, the 6K protein is CC postulated to influence the selection of lipids that interact with the CC transmembrane domains of the glycoproteins, which, in turn, affects the CC deformability of the bilayer required for the extreme curvature that CC occurs as budding proceeds. Present in low amount in virions, about 3% CC compared to viral glycoproteins. {ECO:0000250|UniProtKB:P03315}. CC -!- FUNCTION: [Spike glycoprotein E1]: Class II viral fusion protein. CC Fusion activity is inactive as long as E1 is bound to E2 in mature CC virion. After virus attachment to target cell and endocytosis, CC acidification of the endosome would induce dissociation of E1/E2 CC heterodimer and concomitant trimerization of the E1 subunits. This E1 CC trimer is fusion active, and promotes release of viral nucleocapsid in CC cytoplasm after endosome and viral membrane fusion. Efficient fusion CC requires the presence of cholesterol and sphingolipid in the target CC membrane. Fusion is optimal at levels of about 1 molecule of CC cholesterol per 2 molecules of phospholipids, and is specific for CC sterols containing a 3-beta-hydroxyl group. CC {ECO:0000250|UniProtKB:P03315}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Autocatalytic release of the core protein from the N-terminus CC of the togavirus structural polyprotein by hydrolysis of a -Trp-|- CC Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000250|UniProtKB:P03315}; CC -!- SUBUNIT: [Capsid protein]: Homodimer (By similarity). Homomultimer CC (Probable). Interacts with host karyopherin KPNA4; this interaction CC allows the nuclear import of the viral capsid protein (By similarity). CC Interacts with spike glycoprotein E2 (By similarity). Interacts with CC host IRAK1; the interaction leads to inhibition of IRAK1-dependent CC signaling (By similarity). {ECO:0000250|UniProtKB:P03315, CC ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P0DOK1, CC ECO:0000250|UniProtKB:Q8JUX5, ECO:0000305}. CC -!- SUBUNIT: [Precursor of protein E3/E2]: The precursor of protein E3/E2 CC and E1 form a heterodimer shortly after synthesis (By similarity). CC {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:P03316, CC ECO:0000250|UniProtKB:P0DOK1, ECO:0000250|UniProtKB:Q8JUX5}. CC -!- SUBUNIT: [Spike glycoprotein E1]: The precursor of protein E3/E2 and E1 CC form a heterodimer shortly after synthesis (By similarity). Processing CC of the precursor of protein E3/E2 into E2 and E3 results in a CC heterodimer of the spike glycoproteins E2 and E1 (By similarity). Spike CC at virion surface are constituted of three E2-E1 heterodimers (By CC similarity). After target cell attachment and endocytosis, E1 change CC conformation to form homotrimers (By similarity). Interacts with 6K CC protein (By similarity). {ECO:0000250|UniProtKB:P03315, CC ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P0DOK1, CC ECO:0000250|UniProtKB:Q8JUX5}. CC -!- SUBUNIT: [Spike glycoprotein E2]: Processing of the precursor of CC protein E3/E2 into E2 and E3 results in a heterodimer of the spike CC glycoproteins E2 and E1 (By similarity). Spike at virion surface are CC constituted of three E2-E1 heterodimers (By similarity). Interacts with CC 6K protein (By similarity). Interacts with host MXRA8; this interaction CC mediates virus entry (By similarity). {ECO:0000250|UniProtKB:P03315, CC ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P0DOK1, CC ECO:0000250|UniProtKB:Q8JUX5}. CC -!- SUBUNIT: [6K protein]: Interacts with spike glycoprotein E1 (By CC similarity). Interacts with spike glycoprotein E2 (By similarity). CC {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:P03316, CC ECO:0000250|UniProtKB:P0DOK1, ECO:0000250|UniProtKB:Q8JUX5}. CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion CC {ECO:0000250|UniProtKB:P03316}. Host cytoplasm CC {ECO:0000250|UniProtKB:Q8JUX5}. Host cell membrane CC {ECO:0000250|UniProtKB:P03316}. Host nucleus CC {ECO:0000250|UniProtKB:Q8JUX5}. Note=Shuttles between the cytoplasm and CC the nucleus. {ECO:0000250|UniProtKB:Q8JUX5}. CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane CC {ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein CC {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:P03316}; CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8JUX5}. CC -!- SUBCELLULAR LOCATION: [6K protein]: Host cell membrane CC {ECO:0000250|UniProtKB:P03316}; Multi-pass membrane protein CC {ECO:0000255}. Virion membrane {ECO:0000250|UniProtKB:P03316}; Multi- CC pass membrane protein {ECO:0000255}. CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E1]: Virion membrane CC {ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein CC {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:P03316, CC ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein CC {ECO:0000255}. CC -!- DOMAIN: [Capsid protein]: The very N-terminus also plays a role in the CC particle assembly process (By similarity). The N-terminus also contains CC a nuclear localization signal and a supra nuclear export signal CC (supraNES), which is an unusually strong NES that mediates host CRM1 CC binding in the absence of RanGTP and thus can bind CRM1, not only in CC the nucleus, but also in the cytoplasm (By similarity). The C-terminus CC functions as a protease during translation to cleave itself from the CC translating structural polyprotein (By similarity). CC {ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:P09592}. CC -!- DOMAIN: Structural polyprotein: As soon as the capsid protein has been CC autocleaved, an internal uncleaved signal peptide directs the remaining CC polyprotein to the endoplasmic reticulum. CC {ECO:0000250|UniProtKB:P03315}. CC -!- PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield CC mature proteins. Capsid protein is auto-cleaved during polyprotein CC translation, unmasking a signal peptide at the N-terminus of the CC precursor of E3/E2 (By similarity). The remaining polyprotein is then CC targeted to the host endoplasmic reticulum, where host signal peptidase CC cleaves it into pE2, 6K and E1 proteins. pE2 is further processed to CC mature E3 and E2 by host furin in trans-Golgi vesicle (By similarity). CC {ECO:0000250|UniProtKB:P03315}. CC -!- PTM: [Spike glycoprotein E2]: Palmitoylated via thioester bonds. These CC palmitoylations may induce disruption of the C-terminus transmembrane. CC This would result in the reorientation of E2 C-terminus from lumenal to CC cytoplasmic side. {ECO:0000250|UniProtKB:P03315}. CC -!- PTM: [Spike glycoprotein E1]: N-glycosylated. CC {ECO:0000250|UniProtKB:P03315}. CC -!- PTM: [Spike glycoprotein E2]: N-glycosylated. CC {ECO:0000250|UniProtKB:P03315}. CC -!- PTM: [Assembly protein E3]: N-glycosylated. CC {ECO:0000250|UniProtKB:P03315}. CC -!- PTM: [6K protein]: Palmitoylated via thioester bonds. CC {ECO:0000250|UniProtKB:P03315}. CC -!- MISCELLANEOUS: Structural polyprotein: Translated from a subgenomic RNA CC synthesized during togavirus replication. CC {ECO:0000250|UniProtKB:Q86925}. 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; AB032553; BAA92847.1; -; Genomic_RNA. DR EMBL; AF339483; AAO33337.1; -; Genomic_RNA. DR SMR; Q9JGK8; -. DR MEROPS; S03.001; -. DR Proteomes; UP000007138; Genome. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW. DR GO; GO:0039722; P:suppression by virus of host toll-like receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR Gene3D; 2.40.10.10; -; 2. DR Gene3D; 2.60.40.2400; -; 1. DR Gene3D; 2.60.40.3200; -; 1. DR Gene3D; 2.60.40.350; -; 1. DR Gene3D; 2.60.40.4310; -; 1. DR Gene3D; 2.60.98.10; -; 3. DR InterPro; IPR002548; Alpha_E1_glycop. DR InterPro; IPR000936; Alpha_E2_glycop. DR InterPro; IPR002533; Alpha_E3_glycop. DR InterPro; IPR042304; Alphavir_E2_A. DR InterPro; IPR042305; Alphavir_E2_B. DR InterPro; IPR042306; Alphavir_E2_C. DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf. DR InterPro; IPR036253; Glycoprot_cen/dimer_sf. DR InterPro; IPR038055; Glycoprot_E_dimer_dom. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR000930; Peptidase_S3. DR Pfam; PF01589; Alpha_E1_glycop; 1. DR Pfam; PF00943; Alpha_E2_glycop; 1. DR Pfam; PF01563; Alpha_E3_glycop; 1. DR Pfam; PF00944; Peptidase_S3; 1. DR PRINTS; PR00798; TOGAVIRIN. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF56983; SSF56983; 1. DR SUPFAM; SSF81296; SSF81296; 1. DR PROSITE; PS51690; ALPHAVIRUS_CP; 1. PE 3: Inferred from homology; KW Capsid protein; Cleavage on pair of basic residues; Disulfide bond; KW Fusion of virus membrane with host endosomal membrane; KW Fusion of virus membrane with host membrane; Glycoprotein; KW Host cell membrane; Host cytoplasm; Host membrane; Host nucleus; KW Host-virus interaction; Hydrolase; Lipoprotein; Membrane; Palmitate; KW Protease; RNA-binding; Serine protease; T=4 icosahedral capsid protein; KW Transmembrane; Transmembrane helix; Viral attachment to host cell; KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell. FT CHAIN 1..268 FT /note="Capsid protein" FT /evidence="ECO:0000250" FT /id="PRO_0000238766" FT CHAIN 269..754 FT /note="Precursor of protein E3/E2" FT /evidence="ECO:0000250" FT /id="PRO_0000238767" FT CHAIN 269..332 FT /note="Assembly protein E3" FT /evidence="ECO:0000250" FT /id="PRO_0000238768" FT CHAIN 333..754 FT /note="Spike glycoprotein E2" FT /evidence="ECO:0000250" FT /id="PRO_0000238769" FT CHAIN 755..815 FT /note="6K protein" FT /evidence="ECO:0000250" FT /id="PRO_0000238770" FT CHAIN 816..1253 FT /note="Spike glycoprotein E1" FT /evidence="ECO:0000250" FT /id="PRO_0000238771" FT TOPO_DOM 333..694 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 695..715 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 716..754 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TOPO_DOM 755..769 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 770..790 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 791..792 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 793..813 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 814..1227 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1228..1248 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1249..1253 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 120..268 FT /note="Peptidase S3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027" FT REGION 43..77 FT /note="Host transcription inhibition" FT /evidence="ECO:0000250|UniProtKB:P09592" FT REGION 58..109 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 90..121 FT /note="Binding to the viral RNA" FT /evidence="ECO:0000250|UniProtKB:P27284" FT REGION 106..120 FT /note="Ribosome-binding" FT /evidence="ECO:0000250|UniProtKB:P27284" FT REGION 190..200 FT /note="Dimerization of the capsid protein" FT /evidence="ECO:0000250|UniProtKB:P0DOK1" FT REGION 226..230 FT /note="Dimerization of the capsid protein" FT /evidence="ECO:0000250|UniProtKB:P0DOK1" FT REGION 269..280 FT /note="Functions as an uncleaved signal peptide for the FT precursor of protein E3/E2" FT /evidence="ECO:0000250|UniProtKB:P03315" FT REGION 727..747 FT /note="Transient transmembrane before p62-6K protein FT processing" FT /evidence="ECO:0000255" FT REGION 899..916 FT /note="E1 fusion peptide loop" FT /evidence="ECO:0000250|UniProtKB:Q8JUX5" FT MOTIF 70..106 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250|UniProtKB:P09592" FT MOTIF 151..161 FT /note="Nuclear export signal" FT /evidence="ECO:0000250|UniProtKB:P09592" FT COMPBIAS 65..80 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 81..96 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 146 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027" FT ACT_SITE 168 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027" FT ACT_SITE 220 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027" FT SITE 194 FT /note="Involved in dimerization of the capsid protein" FT /evidence="ECO:0000250|UniProtKB:Q86925" FT SITE 227 FT /note="Involved in dimerization of the capsid protein" FT /evidence="ECO:0000250|UniProtKB:Q86925" FT SITE 268..269 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000250|UniProtKB:P03315" FT SITE 332..333 FT /note="Cleavage; by host furin" FT /evidence="ECO:0000250" FT SITE 754..755 FT /note="Cleavage; by host signal peptidase" FT /evidence="ECO:0000250" FT SITE 815..816 FT /note="Cleavage; by host signal peptidase" FT /evidence="ECO:0000250" FT LIPID 727 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000250" FT LIPID 747 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000250" FT LIPID 748 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000250" FT CARBOHYD 279 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 594 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 956 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT DISULFID 864..929 FT /evidence="ECO:0000250" FT DISULFID 877..909 FT /evidence="ECO:0000250" FT DISULFID 878..911 FT /evidence="ECO:0000250" FT DISULFID 883..893 FT /evidence="ECO:0000250" FT DISULFID 1074..1086 FT /evidence="ECO:0000250" FT DISULFID 1116..1191 FT /evidence="ECO:0000250" FT DISULFID 1121..1195 FT /evidence="ECO:0000250" FT DISULFID 1143..1185 FT /evidence="ECO:0000250" FT VARIANT 403 FT /note="V -> A" FT VARIANT 519 FT /note="D -> N" FT VARIANT 872 FT /note="P -> S" FT VARIANT 1242 FT /note="A -> V" SQ SEQUENCE 1253 AA; 138060 MW; D8F11776CF2152F2 CRC64; MNYIPTQTFY GRRWRPRPAF RPWRVPMQPA PPMVIPELQT PIVQAQQMQQ LISAVSALTT KQNGKAPKKP KKKPQKAKAK KNEQQKKNEN KKPPPKQKNL AKKKKPGKRE RMCMKIENDC IFEVKLDGKV TGYACLVGDK VMKPAHVKGV IDNPDLAKLT YKKSSKYDLE CAQIPVHMKS DASKYTHEKP EGHYNWHHGA VQYSGGRFTI PTGAGKPGDS GRPIFDNKGR VVAIVLGGAN EGARTALSVV TWTKDMVTRY TPEGTEEWSA ALMMCVLANV TFPCSEPACA PCCYEKQPEQ TLRMLEDNVD RPGYYDLLEA TMTCNNSARH RRSVTEHFNV YKATKPYLAY CADCGDGQFC YSPVAIEKIR DEASDGMIKI QVAAQIGINK RGTHEHNKIR YIVGHYMKEA NRDSLQVHTS GVCAIRGTMG HFIVAYCPPG DELKVQFQDA ESHTQACKVQ YKHDPAPVGR EKFTVRPHFG IEVPCTTYQL TTAPTEEEID MHTPPDIPDI TLLSQQSGDV KITAGGKTIR YNCTCGSGNV GTTSSDKTIN SCKIAQCHAA VTNHDKWQYT SSFVPRADQL PRKGKVHVPF PLTNSTCRVP LARAPGVTYG KRELTVKLHP DHPTLLTYRS LGADPRPYEE WIDRYVERTI PVTEDGIEYR WGNNPPVRLW AQLTTEGKPH GWPHEIILYY YGLYPAATIA AVSAAGLAVV LSLLASCYMF ATARRKCLTP YALTPGAVVP VTLGVLCCAP RAHAASFAES MAYLWDENQT LFWLELATPL AAIIILVCCL KNLLCCCQPL SFLVLVSLGT PVVKSYEHTA TIPNVVGFPY KAHIERNGFS PMTLQLEVLG TSLEPTLNLE YITCEYKTVV PPPYIKCCGA SECRSMERPD YQCQVYTGVY PFMWGGAYCF CDTENTQLSE AYVDRSDVCK HDHAAAYKAH TAAMKATIRI SYGNLNQTTT AFVNGEHTVT VGGSRFTFGP ISTAWTPFDN KIVVYKNDVY NQDFPPYGSG QPGRFGDVQS RTVESKDLYA NTALKLSRPS SGTVHVPYTQ TPSGFKYWIK ERGTSLNDKA PFGCVIKTNP VRAENCAVGN IPVSMDIPDS AFTRVIDAPA VTNLECQVAV CTHSSDFGGI ATLTFKTDKP GKCAVHSHSN VATIQEAAVD IKTDGKITLH FSTASASPAF MVSVCSAKTT CMAACEPPKD HIVPYGASHN NQVFPDMSGT AMTWVQRVAG GLGGLTLAAV AALILVTCVT MRR //