ID POLG_SVM10 Reviewed; 2278 AA. AC Q6XDK8; DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 29-MAY-2024, entry version 98. DE RecName: Full=Genome polyprotein; DE Contains: DE RecName: Full=NS1; DE AltName: Full=Protein p11; DE Contains: DE RecName: Full=NS2; DE AltName: Full=Protein p28; DE Contains: DE RecName: Full=NTPase; DE EC=3.6.1.15 {ECO:0000250|UniProtKB:Q04544}; DE AltName: Full=NS3; DE AltName: Full=p35; DE Contains: DE RecName: Full=NS4; DE AltName: Full=Protein p32; DE Contains: DE RecName: Full=Viral genome-linked protein; DE Short=VPg; DE AltName: Full=NS5; DE AltName: Full=p14; DE Contains: DE RecName: Full=Protease-polymerase p70; DE Short=Pro-Pol; DE EC=2.7.7.48 {ECO:0000250|UniProtKB:Q69014}; DE EC=3.4.22.66 {ECO:0000269|PubMed:17459935}; DE AltName: Full=NS6-7; DE Contains: DE RecName: Full=Capsid protein; DE Short=CP; DE AltName: Full=VP1; DE AltName: Full=p60; GN ORFNames=ORF1; OS Sapporo virus (isolate GII/Human/Thailand/Mc10/2000) OS (Hu/SaV/Mc10/2000/Thailand). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Picornavirales; Caliciviridae; Sapovirus; Sapporo virus. OX NCBI_TaxID=234601; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEOLYTIC CLEAVAGE (GENOME RP POLYPROTEIN), AND MUTAGENESIS OF CYS-1171. RX PubMed=15919882; DOI=10.1128/jvi.79.12.7283-7290.2005; RA Oka T., Katayama K., Ogawa S., Hansman G.S., Kageyama T., Ushijima H., RA Miyamura T., Takeda N.; RT "Proteolytic processing of sapovirus ORF1 polyprotein."; RL J. Virol. 79:7283-7290(2005). RN [2] RP PROTEIN SEQUENCE OF 1056-1060, AND PROTEOLYTIC CLEAVAGE (GENOME RP POLYPROTEIN). RX PubMed=16052286; DOI=10.1007/s00705-005-0591-0; RA Oka T., Katayama K., Ogawa S., Hansman G.S., Kageyama T., Miyamura T., RA Takeda N.; RT "Cleavage activity of the sapovirus 3C-like protease in Escherichia coli."; RL Arch. Virol. 150:2539-2548(2005). RN [3] RP MUTAGENESIS OF HIS-1069; HIS-1075; HIS-1086; GLU-1107; HIS-1120; HIS-1136; RP GLU-1143; GLU-1147 AND HIS-1186, ACTIVE SITE (PROTEASE-POLYMERASE P70), AND RP CATALYTIC ACTIVITY (PROTEASE-POLYMERASE P70). RX PubMed=17459935; DOI=10.1128/jvi.02840-06; RA Oka T., Yamamoto M., Yokoyama M., Ogawa S., Hansman G.S., Katayama K., RA Miyashita K., Takagi H., Tohya Y., Sato H., Takeda N.; RT "Highly conserved configuration of catalytic amino acid residues among RT calicivirus-encoded proteases."; RL J. Virol. 81:6798-6806(2007). RN [4] RP PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN). RX PubMed=22973264; DOI=10.3389/fmicb.2012.00312; RA Yokoyama M., Oka T., Kojima H., Nagano T., Okabe T., Katayama K., RA Wakita T., Kanda T., Sato H.; RT "Structural basis for specific recognition of substrates by sapovirus RT protease."; RL Front. Microbiol. 3:312-312(2012). CC -!- FUNCTION: [NS2]: Together with NTPase and NS4, initiates the formation CC of the replication complex (By similarity). Induces the proliferation CC of the host smooth ER membranes forming long tubular structures (By CC similarity). These remodeled membranes probably form the viral CC factories that contain the replication complex (By similarity). CC {ECO:0000250|UniProtKB:P54634, ECO:0000250|UniProtKB:Q66914}. CC -!- FUNCTION: [NTPase]: Displays NTPase activity, but no helicase activity CC (By similarity). Induces the formation of convoluted membranes derived CC from the host ER (By similarity). These remodeled membranes probably CC form the viral factories that contain the replication complex (By CC similarity). Together with NS2 and NS4, initiates the formation of the CC replication complex (By similarity). {ECO:0000250|UniProtKB:P54634, CC ECO:0000250|UniProtKB:Q04544, ECO:0000250|UniProtKB:Q66914}. CC -!- FUNCTION: [NS4]: Probable key protein responsible for the formation of CC membrane alterations by the virus (By similarity). Induces the CC formation of convoluted membranes derived from the host ER (By CC similarity). These remodeled membranes probably form the viral CC factories that contain the replication complex (By similarity). CC Together with NS2 and NTPase, initiates the formation of the CC replication complex (By similarity). {ECO:0000250|UniProtKB:P54634, CC ECO:0000250|UniProtKB:Q66914}. CC -!- FUNCTION: [Viral genome-linked protein]: Viral genome-linked protein is CC covalently linked to the 5'-end of the positive-strand, negative-strand CC genomic RNAs and subgenomic RNA. Acts as a genome-linked replication CC primer. May recruit ribosome to viral RNA thereby promoting viral CC proteins translation. Interacts with host translation initiation CC complex to allow the translation of viral proteins. CC {ECO:0000250|UniProtKB:P27409}. CC -!- FUNCTION: [Protease-polymerase p70]: Protease-polymerase p76 processes CC the polyprotein: Pro-Pol is first released by autocleavage, then all CC other proteins are cleaved (By similarity). Cleaves host translation CC initiation factor eIF4G1, eIF4G2 and PABP1 thereby inducing a shutdown CC of host protein synthesis (By similarity). This shutdown may not CC prevent viral mRNA from being translated since viral Vpg replaces the CC cap (By similarity). It is also an RNA-directed RNA polymerase which CC replicates genomic and antigenomic viral RNA by recognizing specific CC signals (By similarity). Transcribes also a subgenomic mRNA by CC initiating RNA synthesis internally on antigenomic RNA (By similarity). CC This sgRNA codes for structural proteins. Catalyzes the covalent CC attachment VPg with viral RNAs (By similarity). CC {ECO:0000250|UniProtKB:Q66914}. CC -!- FUNCTION: [Capsid protein]: Capsid protein self assembles to form an CC icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and CC consisting of 180 capsid proteins (By similarity). The capsid CC encapsulate the genomic RNA and VP2 proteins. Attaches virion to target CC cells, inducing endocytosis of the viral particle. Acidification of the CC endosome induces conformational change of capsid protein thereby CC injecting virus genomic RNA into host cytoplasm (By similarity). CC {ECO:0000250, ECO:0000250|UniProtKB:Q9QEJ5}. CC -!- CATALYTIC ACTIVITY: [NTPase]: CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; CC Evidence={ECO:0000250|UniProtKB:Q04544}; CC -!- CATALYTIC ACTIVITY: [Protease-polymerase p70]: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CC -!- CATALYTIC ACTIVITY: [Protease-polymerase p70]: CC Reaction=Endopeptidase with a preference for cleavage when the P1 CC position is occupied by Glu-|-Xaa and the P1' position is occupied by CC Gly-|-Yaa.; EC=3.4.22.66; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU01242, ECO:0000269|PubMed:17459935}; CC -!- SUBUNIT: [Capsid protein]: Homodimer. Homomultimer. CC {ECO:0000250|UniProtKB:Q9QEJ5}. CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion. Host cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage; Named isoforms=2; CC Name=Genome polyprotein; CC IsoId=Q6XDK8-1; Sequence=Displayed; CC Name=Subgenomic capsid protein; Synonyms=VP1; CC IsoId=Q6XDK8-2; Sequence=VSP_034390; CC -!- DOMAIN: [Protease-polymerase p70]: Protease-polymerase is composed of CC two domains displaying two different catalytic activity. These CC activities may act independently. {ECO:0000305}. CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield CC mature proteins (PubMed:15919882, PubMed:16052286, PubMed:22973264). CC Pro-Pol is first autocatalytically cleaved, then processes the whole CC polyprotein (By similarity). {ECO:0000250|UniProtKB:Q66914, CC ECO:0000269|PubMed:15919882, ECO:0000269|PubMed:16052286, CC ECO:0000269|PubMed:22973264}. CC -!- PTM: [Viral genome-linked protein]: VPg is uridylylated by the CC polymerase and is covalently attached to the 5'-end of the CC polyadenylated genomic and subgenomic RNAs. This uridylylated form acts CC as a nucleotide-peptide primer for the polymerase. CC {ECO:0000250|UniProtKB:Q66914}. CC -!- MISCELLANEOUS: Two different RNAs lead the expression of the capsid CC protein. One arises from the cleavage of the polyprotein translated CC from the genomic RNA and the other from the translation of a subgenomic CC RNA derived from the (-)RNA template. Capsid protein expressed from the CC subgenomic mRNA is produced in much larger amounts than the cleaved one CC (By similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: [Isoform Genome polyprotein]: Produced from the genomic CC RNA. CC -!- MISCELLANEOUS: [Isoform Subgenomic capsid protein]: Produced from the CC subgenomic RNA. {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; AY237420; AAQ17058.2; -; mRNA. DR RefSeq; YP_022762.1; NC_010624.1. [Q6XDK8-1] DR SMR; Q6XDK8; -. DR MEROPS; C24.003; -. DR GeneID; 2943313; -. DR KEGG; vg:2943313; -. DR Proteomes; UP000112655; Genome. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR CDD; cd00009; AAA; 1. DR CDD; cd23192; Caliciviridae_RdRp; 1. DR CDD; cd00205; rhv_like; 1. DR Gene3D; 1.10.260.110; -; 1. DR Gene3D; 1.20.960.20; -; 1. DR Gene3D; 2.60.120.20; -; 1. DR Gene3D; 3.30.70.270; -; 2. DR Gene3D; 6.10.250.3230; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR004005; Calicivirus_coat. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ. DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir. DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000317; Peptidase_C24. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase. DR InterPro; IPR033703; Rhv-like. DR InterPro; IPR001205; RNA-dir_pol_C. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR029053; Viral_coat. DR InterPro; IPR049434; VPg. DR Pfam; PF00915; Calici_coat; 1. DR Pfam; PF03510; Peptidase_C24; 1. DR Pfam; PF00680; RdRP_1; 1. DR Pfam; PF00910; RNA_helicase; 1. DR Pfam; PF20915; VPg; 1. DR PRINTS; PR00916; 2CENDOPTASE. DR PRINTS; PR00918; CALICVIRUSNS. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF88633; Positive stranded ssRNA viruses; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS51894; CV_3CL_PRO; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51218; SF3_HELICASE_2; 1. PE 1: Evidence at protein level; KW Alternative promoter usage; ATP-binding; Capsid protein; KW Covalent protein-RNA linkage; Direct protein sequencing; DNA replication; KW Host cytoplasm; Hydrolase; Nucleotide-binding; Nucleotidyltransferase; KW Phosphoprotein; Protease; RNA-directed RNA polymerase; Thiol protease; KW Transferase; Viral RNA replication; Virion. FT CHAIN 1..2278 FT /note="Genome polyprotein" FT /id="PRO_0000342101" FT CHAIN 1..69 FT /note="NS1" FT /id="PRO_0000342102" FT CHAIN 70..325 FT /note="NS2" FT /id="PRO_0000342103" FT CHAIN 326..666 FT /note="NTPase" FT /id="PRO_0000342104" FT CHAIN 667..940 FT /note="NS4" FT /id="PRO_0000342105" FT CHAIN 941..1055 FT /note="Viral genome-linked protein" FT /id="PRO_0000342106" FT CHAIN 1056..1722 FT /note="Protease-polymerase p70" FT /id="PRO_0000342107" FT CHAIN 1723..2278 FT /note="Capsid protein" FT /id="PRO_5000090469" FT DOMAIN 454..609 FT /note="SF3 helicase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551" FT DOMAIN 1056..1204 FT /note="Peptidase C24" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242" FT DOMAIN 1443..1568 FT /note="RdRp catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539" FT REGION 939..958 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1086 FT /note="For 3CLpro activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242, FT ECO:0000269|PubMed:17459935" FT ACT_SITE 1107 FT /note="For 3CLpro activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242, FT ECO:0000269|PubMed:17459935" FT ACT_SITE 1171 FT /note="For 3CLpro activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242, FT ECO:0000269|PubMed:17459935" FT BINDING 481..488 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551" FT SITE 69..70 FT /note="Cleavage; by Pro-Pol" FT /evidence="ECO:0000269|PubMed:22973264" FT SITE 325..326 FT /note="Cleavage; by Pro-Pol" FT /evidence="ECO:0000269|PubMed:22973264" FT SITE 666..667 FT /note="Cleavage; by Pro-Pol" FT /evidence="ECO:0000269|PubMed:22973264" FT SITE 940..941 FT /note="Cleavage; by Pro-Pol" FT /evidence="ECO:0000269|PubMed:15919882, FT ECO:0000269|PubMed:22973264" FT SITE 1055..1056 FT /note="Cleavage; by Pro-Pol" FT /evidence="ECO:0000269|PubMed:15919882, FT ECO:0000269|PubMed:16052286, ECO:0000269|PubMed:22973264" FT SITE 1722..1723 FT /note="Cleavage; by Pro-Pol" FT /evidence="ECO:0000269|PubMed:22973264" FT MOD_RES 966 FT /note="O-(5'-phospho-RNA)-tyrosine" FT /evidence="ECO:0000250|UniProtKB:P27409" FT VAR_SEQ 1..1720 FT /note="Missing (in isoform Subgenomic capsid protein)" FT /evidence="ECO:0000305" FT /id="VSP_034390" FT MUTAGEN 1069 FT /note="H->A: No effect on protease activity in vitro." FT /evidence="ECO:0000269|PubMed:17459935" FT MUTAGEN 1075 FT /note="H->A: No effect on protease activity in vitro." FT /evidence="ECO:0000269|PubMed:17459935" FT MUTAGEN 1086 FT /note="H->A: Complete loss of protease activity in vitro." FT /evidence="ECO:0000269|PubMed:17459935" FT MUTAGEN 1107 FT /note="E->A: Complete loss of protease activity in vitro." FT /evidence="ECO:0000269|PubMed:17459935" FT MUTAGEN 1120 FT /note="H->A: No effect on protease activity in vitro." FT /evidence="ECO:0000269|PubMed:17459935" FT MUTAGEN 1136 FT /note="H->A: No effect on protease activity in vitro." FT /evidence="ECO:0000269|PubMed:17459935" FT MUTAGEN 1143 FT /note="E->A: No effect on protease activity in vitro." FT /evidence="ECO:0000269|PubMed:17459935" FT MUTAGEN 1147 FT /note="E->A: No effect on protease activity in vitro." FT /evidence="ECO:0000269|PubMed:17459935" FT MUTAGEN 1171 FT /note="C->A: Complete loss of protease activity in vitro." FT /evidence="ECO:0000269|PubMed:15919882" FT MUTAGEN 1186 FT /note="H->A: No effect on protease activity in vitro." FT /evidence="ECO:0000269|PubMed:17459935" SQ SEQUENCE 2278 AA; 250097 MW; DE7386F8EE49AD11 CRC64; MASKPFYPIE FNPSVELQVL RSAHLRVGGR EQMFETINDL NDHVRGVVAK LWCKHLHRSL AAAPTFTEEG LLDSFLSKPP VDINPDTTFR ELFGINPHEQ FPLSIHDLAK LQGELVDAAR NPGHVLRRHY STDSLTALIN KITKFVPVHA TLQEMQARRA FERERAELFR ELPHADLDVS RQQKSYFYAM WRQVVKKSKE FFIPLVKCTS WRKKFTEPAE IVRQVLVHFC EGMRSQFSTN ANYINLSLIA KLRPTVLTMI LQQHKNTYRG WLATVTALVE VYSNLFQDMR DTAVSAVSAI TLVFETIKDF VVNVIDLVKS TFQSQGPTSC GWAAIIAGAL LILMKLSGCS NTTSYWHRLL KVCGGVTTIA AAARAVVWVR DIIAEADGKA RLKKYMARTA ALLELAASRD VTGTDELKRL LDCFTQLIEE GTELIQEFGT SPLAGLTRSY VSELESTANS IRSTILLDTP RKTPVAIILT GPPGIGKTRL AQHLAAGFGK VSNFSVTLDH HDSYTGNEVA IWDEFDVDTQ GKFVETMIGV VNTAPYPLNC DRVENKGKVF TSDYIICTSN YPTSVLPDNP RAGAFYRRVT TIDVSSPTIE DWKKKNPGKK PPPDLYKNDF THLRLSVRPF LGYNPEGDTL DGVRVKPVLT SVDGLSRLME TKFKEQGNEH RNLWITCPRD LVAPAASGLK AYMAANRALA QVFQEPSSQD IGETCTSRVY VSCNNPPPTY SGRVVKITAI NPWDASLANS MLSMFETTSH IPASIQREIM YRVWDPLVHL QTREPNTQML PYINRVVPVS SAFDFIRGLR HHLGLCSVKG MWRAYQGWNS SSSILEFLSK HMADVAFPHN PECTVFRAPD GDVIFYTFGS YACFVSPARV PFVGEPPKNV HSNITRNMTW AETLRLLAET ITESLVHFGP FLLMMHNVSY LATRSGREEE AKGKTKHGRG AKHARRGGVS LSDDEYDEWR DLVRDWRQDM TVGEFVELRE RYALGMDSED VQRYRAWLEL RAMRMGAGAY QHATIIGRGG VQDTIIRTQP MRAPRAPRNQ GYDEEAPTPI VTFTSGGDHI GYGCHMGNGV VVTVTHVASA SDQVEGQDFA IRKTEGETTW VNTNLGHLPH YQIGDGAPVY YSARLHPVTT LAEGTYETPN ITVQGYHLRI INGYPTKRGD CGTPYFDSCR RLVGLHAATS TNGETKLAQR VTKTSKVENA FAWKGLPVVR GPDCGGMPTG TRYHRSPAWP NPVEGETHAP APFGSGDERY KFSQVEMLVN GLKPYSEPTP GIPPALLQRA ATHTRTYLET IIGTHRSPNL SFSEACSLLE KSTSCGPFVA GQKGDYWDED KQCYTGVLAE HLAKAWDAAN RGVAPQNAYK LALKDELRPI EKNAQGKRRL LWGCDAGATL VATAAFKGVA TRLQAVAPMT PVSVGINMDS YQVEVLNESL KGGVLYCLDY SKWDSTQHPA VTAASLGILE RLSEATPITT SAVELLSSPA RGHLNDIVFI TKSGLPSGMP FTSVINSLNH MTYFAAAVLK AYEQHGAPYT GNVFQVETVH TYGDDCLYSV CPATASIFQT VLANLTSFGL KPTAADKSET IAPTHTPVFL KRTLTCTPRG VRGLLDITSI KRQFLWIKAN RTVDINSPPA YDRDARGIQL ENALAYASQH GHAVFEEVAE LARHTAKAEG LVLTNVNYDQ ALATYESWFI GGTGLVQGSP SEETTKLVFE MEGLGQPQPQ GGEKTSPQPV TPQDTIGPTA ALLLPTQIET PNASAQRLEL AMATGAVTSN VPNCIRECFA SVTTIPWTTR QAANTFLGAI HLGPRINPYT AHLSAMFAGW GGGFQVRVTI SGSGLFAGRA VTAILPPGVN PASVQNPGVF PHAFIDARTT EPILINLPDI RPVDFHRVDG DDATASVGLW VAQPLINPFQ TGPVSTCWLS FETRPGPDFD FCLLKAPEQQ MDNGISPASL LPRRLGRSRG NRMGGRIVGL VVVAAAEQVN HHFDARSTTL GWSTLPVEPI AGDISWYGDA GNKSIRGLVS AQGKGIIFPN IVNHWTDVAL SSKTSNTTTI PTDTSTLGNL PGASGPLVTF ADNGDVNESS AQNAILTAAN QNFTSFSPTF DAAGIWVWMP WATDRPGASD SNIYISPTWV NGNPSHPIHE KCTNMIGTNF QFGGTGTNNI MLWQEQHFTS WPGAAEVYCS QLESTAEIFQ NNIVNIPMNQ MAVFNVETAG NSFQIAILPN GYCVTNAPVG THQLLDYETS FKFVGLFPQS TSLQGPHGNS GRAVRFLE //