ID POLG_DEN27 Reviewed; 3391 AA. AC P29991; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 24-NOV-2009, entry version 90. DE RecName: Full=Genome polyprotein; DE Contains: DE RecName: Full=Protein C; DE AltName: Full=Core protein; DE AltName: Full=Capsid protein; DE Contains: DE RecName: Full=prM; DE Contains: DE RecName: Full=Peptide pr; DE Contains: DE RecName: Full=Small envelope protein M; DE AltName: Full=Matrix protein; DE Contains: DE RecName: Full=Envelope protein E; DE Contains: DE RecName: Full=Non-structural protein 1; DE Short=NS1; DE Contains: DE RecName: Full=Non-structural protein 2A; DE Short=NS2A; DE Contains: DE RecName: Full=Non-structural protein 2A-alpha; DE Short=NS2A-alpha; DE Contains: DE RecName: Full=Serine protease subunit NS2B; DE AltName: Full=Non-structural protein 2B; DE Contains: DE RecName: Full=Serine protease subunit NS3; DE EC=3.4.21.91; DE AltName: Full=Non-structural protein 3; DE Contains: DE RecName: Full=Non-structural protein 4A; DE Short=NS4A; DE Contains: DE RecName: Full=Peptide 2k; DE Contains: DE RecName: Full=Non-structural protein 4B; DE Short=NS4B; DE Contains: DE RecName: Full=RNA-directed RNA polymerase NS5; DE EC=2.7.7.48; DE EC=2.1.1.56; DE AltName: Full=Non-structural protein 5; OS Dengue virus type 2 (strain 16681-PDK53) (DENV-2). OC Viruses; ssRNA positive-strand viruses, no DNA stage; Flaviviridae; OC Flavivirus; Dengue virus group. OX NCBI_TaxID=31635; OH NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti). OH NCBI_TaxID=299627; Aedes furcifer (Mosquito). OH NCBI_TaxID=299628; Aedes taylori (Mosquito). OH NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas). OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX MEDLINE=92188532; PubMed=1312269; DOI=10.1016/0042-6822(92)90460-7; RA Blok J., McWilliam S.M., Butler H.C., Gibbs A.J., Weiller G., RA Herring B.L., Hemsley A.C., Aaskov J.G., Yoksan S., Bhamarapravati N.; RT "Comparison of a dengue-2 virus and its candidate vaccine derivative: RT sequence relationships with the flaviviruses and other viruses."; RL Virology 187:573-590(1992). CC -!- FUNCTION: Protein C packages viral RNA to form a viral CC nucleocapsid, and promotes virion budding (By similarity). CC -!- FUNCTION: prM acts as a chaperone for envelope protein E during CC intracellular virion assembly by masking and inactivating envelope CC protein E fusion peptide. prM is matured in the last step of CC virion assembly, presumably to avoid catastrophic activation of CC the viral fusion peptide induced by the acidic pH of the trans- CC Golgi network. After cleavage by host furin, the pr peptide is CC released in the extracellular medium and small envelope protein M CC and envelope protein E homodimers are dissociated (By similarity). CC -!- FUNCTION: Envelope protein E binds cell surface receptor and is CC involved in membrane fusion between virion and target cell. CC Synthesized as an homodimer with prM which acts as a chaperone for CC envelope protein E. After cleavage of prM, envelope protein E CC dissociate from small envelope protein M and homodimerizes (By CC similarity). CC -!- FUNCTION: Non-structural protein 1 is slowly secreted from CC mammalian cells, but not from mosquito cells. Secreted form CC elicits protective immune response and plays an essential role in CC RNA replication. Soluble and membrane-associated NS1 may activate CC human complement and induce host vascular leakage. This effect CC might explain the clinical manifestations of dengue hemorrhagic CC fever and dengue shock syndrome (By similarity). CC -!- FUNCTION: Non-structural protein 2B is a required cofactor for the CC serine protease function of NS3 (By similarity). CC -!- FUNCTION: Serine protease NS3 displays three enzymatic activities: CC serine protease, NTPase and RNA helicase. NS3 serine protease, in CC association with NS2B, cleaves the polyprotein at dibasic sites in CC the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and CC NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' CC to 5' direction (By similarity). CC -!- FUNCTION: Non-structural protein 4A plays a role in RNA CC replication. Enhances inhibition of cell antiviral response by CC non-structural protein 4B (By similarity). CC -!- FUNCTION: Non-structural protein 4B prevent the establishment of CC cellular antiviral state by blocking the interferon-alpha/beta CC (IFN-alpha/beta) and IFN-gamma signaling pathways (By similarity). CC -!- FUNCTION: RNA-directed RNA polymerase NS5 replicates the viral (+) CC and (-) genome, and assure the capping of genomes in the CC cytoplasm. May be involved in methylation of 5'RNA cap structure CC (By similarity). CC -!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds CC in which each of the Xaa can be either Arg or Lys and Yaa can be CC either Ser or Ala. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S- CC adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. CC -!- SUBUNIT: prM and envelope protein E form heterodimers in the CC endoplasmic reticulum and Golgi. Envelope protein E forms CC homodimers. NS1 forms homodimers as well as homohexamers when CC secreted. NS1 may interact with NS4A. NS3 and NS2B form an CC heterodimer. NS3 interacts with unphosphorylated NS5 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Protein C: Virion (By similarity). CC -!- SUBCELLULAR LOCATION: Peptide pr: Secreted (By similarity). CC -!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane; CC Single-pass type I membrane protein (By similarity). CC -!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane; Single- CC pass type I membrane protein (By similarity). CC -!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted. Host CC endoplasmic reticulum membrane; Peripheral membrane protein; CC Lumenal side (By similarity). CC -!- SUBCELLULAR LOCATION: Non-structural protein 2A-alpha: Host CC endoplasmic reticulum membrane (By similarity). CC -!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic CC reticulum membrane (By similarity). CC -!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host CC endoplasmic reticulum membrane; Peripheral membrane protein; CC Cytoplasmic side (By similarity). CC -!- SUBCELLULAR LOCATION: Serine protease subunit NS3: Host CC endoplasmic reticulum membrane; Peripheral membrane protein; CC Cytoplasmic side (By similarity). CC -!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic CC reticulum membrane; Peripheral membrane protein; Cytoplasmic side CC (By similarity). CC -!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic CC reticulum membrane; Multi-pass membrane protein (By similarity). CC Note=The C-terminal transmembrane domain of non-structural protein CC 4B is presumably reoriented after cleavage on the lumenal side (By CC similarity). CC -!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Host CC endoplasmic reticulum membrane; Peripheral membrane protein; CC Cytoplasmic side. Host nucleus (By similarity). CC -!- DOMAIN: Transmembrane domains of the small envelope protein M and CC envelope protein E contains an endoplasmic reticulum retention CC signals (By similarity). CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. CC The nascent protein C contains a C-terminal hydrophobic domain CC that act as a signal sequence for translocation of prM into the CC lumen of the ER. Mature protein C is cleaved at a site upstream of CC this hydrophobic domain by NS3. prM is cleaved in post-Golgi CC vesicles by a host furin, releasing the mature small envelope CC protein M, and peptide pr. Non-structural protein 2A-alpha, a C- CC terminally truncated form of non-structural protein 2A, results CC from partial cleavage by NS3 (By similarity). CC -!- PTM: RNA-directed RNA polymerase NS5 is phosphorylated on serines CC residues. This phosphorylation may trigger NS5 nuclear CC localization (By similarity). CC -!- PTM: Envelope protein E and non-structural protein 1 are N- CC glycosylated (By similarity). CC -!- MISCELLANEOUS: The virion is assembled in the endoplasmic CC reticulum lumen, transported by vesicles to the Golgi, then CC transported again to the cell membrane where it is released CC outside the cell. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC -!- SIMILARITY: Contains 1 peptidase S7 domain. CC -!- SIMILARITY: Contains 1 RdRp catalytic domain. 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; M84728; AAA73186.1; -; Genomic_RNA. DR EMBL; M84727; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR PIR; B42451; GNWV26. DR PDB; 2R29; X-ray; 3.00 A; A=578-674. DR PDB; 3EVG; X-ray; 2.20 A; A=2493-2757. DR PDBsum; 2R29; -. DR PDBsum; 3EVG; -. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW. DR GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:EC. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed RNA polymerase activity; 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:0032259; P:methylation; IEA:InterPro. DR GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW. DR GO; GO:0016070; P:RNA metabolic process; IEA:InterPro. DR GO; GO:0006410; P:transcription, RNA-dependent; IEA:UniProtKB-KW. DR GO; GO:0019079; P:viral genome replication; IEA:InterPro. DR InterPro; IPR014001; DEAD-like_N. DR InterPro; IPR011492; DEAD_Flavivir. DR InterPro; IPR001650; DNA/RNA_helicase_C. DR InterPro; IPR000069; Env_glycoprot_M_flavivir. DR InterPro; IPR013754; Flav_glyE_dim. DR InterPro; IPR001122; Flavi_capsidC. DR InterPro; IPR001157; Flavi_NS1. DR InterPro; IPR000752; Flavi_NS2A. DR InterPro; IPR000487; Flavi_NS2B. DR InterPro; IPR000404; Flavi_NS4A. DR InterPro; IPR001528; Flavi_NS4B. DR InterPro; IPR002535; Flavi_propep. DR InterPro; IPR000336; Flv_glyE_Ig-like. DR InterPro; IPR014412; Gen_Poly_FLV. DR InterPro; IPR011999; GlycoprotE_cen/dimer_Flavivir. DR InterPro; IPR011998; GlycoprotE_cen/dimer_vir. DR InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR001850; Peptidase_S7. DR InterPro; IPR000208; RNA-dir_pol_flavivirus. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR002877; rRNA_MeTrfase_RrmJ/FtsJ. DR InterPro; IPR009003; Ser/Cys_Pept_Trypsin-like. DR Gene3D; G3DSA:2.60.98.10; Flav_glyE_dim; 1. DR Gene3D; G3DSA:2.60.40.350; Flv_glyE_Ig-like; 1. DR Pfam; PF01003; Flavi_capsid; 1. DR Pfam; PF07652; Flavi_DEAD; 1. DR Pfam; PF02832; Flavi_glycop_C; 1. DR Pfam; PF00869; Flavi_glycoprot; 1. DR Pfam; PF01004; Flavi_M; 1. DR Pfam; PF00948; Flavi_NS1; 1. DR Pfam; PF01005; Flavi_NS2A; 1. DR Pfam; PF01002; Flavi_NS2B; 1. DR Pfam; PF01350; Flavi_NS4A; 1. DR Pfam; PF01349; Flavi_NS4B; 1. DR Pfam; PF00972; Flavi_NS5; 1. DR Pfam; PF01570; Flavi_propep; 1. DR Pfam; PF01728; FtsJ; 1. DR Pfam; PF00949; Peptidase_S7; 1. DR PIRSF; PIRSF003817; Gen_Poly_FLV; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR PROSITE; PS00690; DEAH_ATP_HELICASE; FALSE_NEG. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; FALSE_NEG. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Capsid protein; KW Cleavage on pair of basic residues; Complete proteome; Disulfide bond; KW Envelope protein; Glycoprotein; Helicase; Host endoplasmic reticulum; KW Host membrane; Host nucleus; Hydrolase; Membrane; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; KW Phosphoprotein; Protease; Ribonucleoprotein; RNA replication; KW RNA-binding; RNA-directed RNA polymerase; Secreted; Serine protease; KW Transcription; Transcription regulation; Transferase; Transmembrane; KW Viral nucleoprotein; Virion. FT CHAIN 1 100 Protein C (By similarity). FT /FTId=PRO_0000037936. FT PROPEP 101 114 ER anchor for the protein C, removed in FT mature form by serine protease NS3 (By FT similarity). FT /FTId=PRO_0000037937. FT CHAIN 115 280 prM (By similarity). FT /FTId=PRO_0000308279. FT CHAIN 115 205 Peptide pr (By similarity). FT /FTId=PRO_0000308280. FT CHAIN 206 280 Small envelope protein M (By similarity). FT /FTId=PRO_0000037938. FT CHAIN 281 775 Envelope protein E (By similarity). FT /FTId=PRO_0000037939. FT CHAIN 776 1127 Non-structural protein 1 (By similarity). FT /FTId=PRO_0000037940. FT CHAIN 1128 1345 Non-structural protein 2A (By FT similarity). FT /FTId=PRO_0000037941. FT CHAIN 1128 1315 Non-structural protein 2A-alpha (By FT similarity). FT /FTId=PRO_0000037942. FT CHAIN 1346 1475 Serine protease subunit NS2B (By FT similarity). FT /FTId=PRO_0000037943. FT CHAIN 1476 2093 Serine protease subunit NS3 (By FT similarity). FT /FTId=PRO_0000308465. FT CHAIN 2094 2220 Non-structural protein 4A (By FT similarity). FT /FTId=PRO_0000037944. FT PEPTIDE 2221 2243 Peptide 2k (By similarity). FT /FTId=PRO_0000308281. FT CHAIN 2244 2491 Non-structural protein 4B (By FT similarity). FT /FTId=PRO_0000037945. FT CHAIN 2492 3391 RNA-directed RNA polymerase NS5 (By FT similarity). FT /FTId=PRO_0000037946. FT TOPO_DOM 1 101 Cytoplasmic (Potential). FT TRANSMEM 102 122 Potential. FT TOPO_DOM 123 238 Extracellular (Potential). FT TRANSMEM 239 259 Potential. FT TOPO_DOM 260 265 Cytoplasmic (Potential). FT TRANSMEM 266 286 Potential. FT TOPO_DOM 287 725 Extracellular (Potential). FT TRANSMEM 726 746 Potential. FT TOPO_DOM 747 752 Cytoplasmic (Potential). FT TRANSMEM 753 773 Potential. FT TOPO_DOM 774 1156 Extracellular (Potential). FT TRANSMEM 1157 1177 Potential. FT TOPO_DOM 1178 1447 Cytoplasmic (Potential). FT TRANSMEM 1448 1468 Potential. FT TOPO_DOM 1469 2192 Lumenal (Potential). FT TRANSMEM 2193 2213 Potential. FT TOPO_DOM 2214 2220 Cytoplasmic (Potential). FT TRANSMEM 2221 2240 Potential. FT TRANSMEM 2348 2368 Potential. FT TOPO_DOM 2369 2413 Cytoplasmic (Potential). FT TRANSMEM 2414 2434 Potential. FT TOPO_DOM 2435 2459 Lumenal (Potential). FT TRANSMEM 2460 2480 Potential. FT TOPO_DOM 2481 3391 Cytoplasmic (Potential). FT DOMAIN 1655 1811 Helicase ATP-binding. FT DOMAIN 1821 1988 Helicase C-terminal. FT DOMAIN 3020 3169 RdRp catalytic. FT NP_BIND 1668 1675 ATP (Potential). FT MOTIF 1759 1762 DEAH box (By similarity). FT ACT_SITE 1526 1526 Charge relay system; for serine protease FT NS3 activity (By similarity). FT ACT_SITE 1550 1550 Charge relay system; for serine protease FT NS3 activity (By similarity). FT ACT_SITE 1610 1610 Charge relay system; for serine protease FT NS3 activity (By similarity). FT SITE 100 101 Cleavage; by serine protease NS3 (By FT similarity). FT SITE 114 115 Cleavage; by host signal peptidase (By FT similarity). FT SITE 205 206 Cleavage; by host furin (By similarity). FT SITE 280 281 Cleavage; by host signal peptidase (By FT similarity). FT SITE 775 776 Cleavage; by host signal peptidase (By FT similarity). FT SITE 1127 1128 Cleavage; by host (By similarity). FT SITE 1315 1316 Cleavage; by serine protease NS3 (By FT similarity). FT SITE 1345 1346 Cleavage; by serine protease NS3 (By FT similarity). FT SITE 1475 1476 Cleavage; by serine protease NS3 (By FT similarity). FT SITE 2093 2094 Cleavage; by serine protease NS3 (By FT similarity). FT SITE 2220 2221 Cleavage; by host signal peptidase (By FT similarity). FT SITE 2243 2244 Cleavage; by serine protease NS3 (By FT similarity). FT SITE 2491 2492 Cleavage; by serine protease NS3 (By FT similarity). FT CARBOHYD 183 183 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 347 347 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 433 433 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 905 905 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 982 982 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 1134 1134 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 2301 2301 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 2305 2305 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 2457 2457 N-linked (GlcNAc...); by host FT (Potential). FT DISULFID 283 310 By similarity. FT DISULFID 340 401 By similarity. FT DISULFID 354 385 By similarity. FT DISULFID 372 396 By similarity. FT DISULFID 465 565 By similarity. FT DISULFID 582 613 By similarity. FT HELIX 2503 2509 FT HELIX 2514 2521 FT STRAND 2525 2528 FT HELIX 2530 2533 FT HELIX 2551 2557 FT TURN 2558 2560 FT STRAND 2568 2571 FT TURN 2579 2581 FT HELIX 2623 2625 FT STRAND 2632 2636 FT HELIX 2645 2648 FT HELIX 2652 2662 FT STRAND 2668 2674 FT HELIX 2680 2691 FT STRAND 2709 2712 FT HELIX 2719 2732 FT HELIX 2733 2735 FT STRAND 2742 2745 SQ SEQUENCE 3391 AA; 379884 MW; 5EE11A74081C5177 CRC64; MNDQRKEAKN TPFNMLKRER NRVSTVQQLT KRFSLGMLQG RGPLKLYMAL VAFLRFLTIP PTAGILKRWG TIKKSKAINV LRGFRKEIGR MLNILNRRRR SAGMIIMLIP TVMAFHLTTR NGEPHMIVSR QEKGKSLLFK TEVGVNMCTL MAMDLGELCE DTITYKCPLL RQNEPEDIDC WCNSTSTWVT YGTCTTMGEH RREKRSVALV PHVGMGLETR TETWMSSEGA WKHVQRIETW ILRHPGFTMM AAILAYTIGT THFQRALILI LLTAVTPSMT MRCIGMSNRD FVEGVSGGSW VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC IEAKLTNTTT ESRCPTQGEP SLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFR CKKNMEGKVV QPENLEYTIV ITPHSGEEHA VGNDTGKHGK EIKITPQSSI TEAELTGYGT ITMECSPRTG LDFNEIVLLQ MENKAWLVHR QWFLDLPLPW LPGADTQGSN WIQKETLVTF KNPHAKKQDV VVLGSQEGAM HTALTGATEI QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS MCTGKFKVVK EIAETQHGTI VIRVQYEGDG SPCKIPFEIM DLEKRHVLGR LITVNPIVTE KDSPVNIEAE PPFGDSYIII GVEPGQLKLN WFKKGSSIGQ MFETTMRGAK RMAILGDTAW DFGSLGGVFT SIGKALHQVF GAIYGAAFSG VSWTMKILIG VIITWIGMNS RSTSLSVTLV LVGIVTLYLG VMVQADSGCV VSWKNKELKC GSGIFITDNV HTWTEQYKFQ PESPSKLASA IQKAHEEDIC GIRSVTRLEN LMWKQITPEL NHILSENEVK LTIMTGDIKG IMQAGKRSLR PQPTELKYSW KTWGKAKMLS TESHNQTFFI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLKLKEKQ DVFCDSKLMS AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKNCHW PKSHTLWSNG VLESEMIIPK NLAGPVSKHN YRPGYHTQIT GPWHLGKLEM DFDFCDGTTV VVTEDCGNRG PSLRTTTASG KLITEWCCRS CTLPPLRYRG EDGCWYGMEI RPLKEKEENL VNSLVTAGHG QVDNFSLGVL GMALFLEEML RTRVGTKHAI LLVAVSFVTL IIGNRSFRDL GRVMVMVGAT MTDDIGMGVT YLALLAAFKV RPTFAAGLLL RKLTSKELMM TTIGIVLSSQ STIPETILEL TDALALGMMV LKMVRNMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA VVSVSPLFLT SSQQKTDWIP LALTIKGLNP TAIFLTTLSR TSKKRSWPLN EAIMAVGMVS ILASSLLKND IPMTGPLVAG GLLTVCYVLT GRSADLELER AADVKWEDQA EISGSSPILS ITISEDGSMS IKNEEEEQTL TILIRRGLLV ISGLFPVSIP ITAAAWYLWE VKKQRAGVLW DVPSPPPMGK AELEDGAYRI KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD LISYGGGWKL EGEWKEGEEV QVLALDPGKN PRAVQTKPGL FKTNAGTIGA VSLDFSPGTS GSPIIDKKGK VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN PEIEDDIFRK RRLTIMDLHP GAGKTKRYLP AIVREAIKRG LRTLILAPTR VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE IVDLMCHATF TMRLLSPVRV PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF PQSNAPIIDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KAGNDIAACL RKNGKKVIQL SRKTFDSEYV KTRTNDWDFV VTTDISEMGA NFKAERVIDP RRCMKPVILT DGEERVILAG PMPVTHSSAA QRRGRIGRNP KNENDQYIYM GEPLENDEDC AHWKEAKMLL DNINTPEGII PSMFEPEREK VDAIDGEYRL RGEARTTFVD LMRRGDLPVW LAYRVAAEGI NYADRRWCFD GVKNNQILEE NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFKEFAA GRKSLTLNLI TEMGRLPTFM TQKARNALDN LAVLHTAEAG GRAYNHALSE LPETLETLLL LTLLATVTGG IFLFLMSARG IGKMTLGMCC IITASILLWY AQIQPHWIAA SIILEFFLIV LLIPEPEKQR TPQDNQLTYV VIAILTVVAA TMANEMGFLE KTKKDLGLGS IATQQPESNI LDIDLRPASA WTLYAVATTF VTPMLRHSIE NSSVNVSLTA IANQATVLMG LGKGWPLSKM DIGVPLLAIG CYSQVNPTTL TAALFLLVAH YAIIGPALQA KASREAQKRA AAGIMKNPTV DGITVIDLDP IPYDPKFEKQ LGQVMLLVLC VTQVLMMRTT WALCEALTLA TGPISTLSEG NPGRFWNTTI AVSMANIFRG SYLAGAGLLF SIMKNTTNTR RVTGNIGETL GEKWKSRLNA LGKSEFQIYK KSGIQEVDRT LAKEGIKRGE TDHHAVSRGS AKLRWFVERN MVTPEGKVVD LGCGRGGWSY YCGGLKNVRE VKGLTKGGPG HEEPIPMSTY GWNLVRLQSG VDVFFIPPEK CDTLLCDIGE SSPNPTVEAG RTLRVLNLVE NWLNNNTQFC IKVLNPYMPS VIEKMEALQR KYGGALVRNP LSRNSTHEMY WVSNASGNIV SSVNMISRML INRFTMRYKK ATYEPDVDLG SGTRNIGIES EIPNLDIIGK RIEKIKQEHE TSWHYDQDHP YKTWAYHGSY ETKQTGSASS MVNGVFRLLT KPWDVVPMVT QMAMTDTTPF GQQRVFKEKV DTRTQEPKEG TKKLMKITAE WLWKELGKKK TPRMCTREEF TRKVRSNAAL GAIFTDENKW KSAREAVEDS RFWELVDKER NLHLEGKCET CVYNIMGKRE KKLGEFGKAK GSRAIWYMWL GARFLEFEAL GFLNEDHWFS RENSLSGVEG EGLHKLGYIL RDVSKKEGGA MYADDTAGWD TRITLEDLKN EEMVTNHMEG EHKKLAEAIF KLTYQNKVVR VQRPTPRGTV MDIISRRDQR GSGQVGTYGL NTFTNMEAQL IRQMEGEGVF KSIQHLTITE EIAVQNWLAR VGRERLSRMA ISGDDCVVKP LDDRLPSALT ALNDMGKIRK DIQQWEPSRG WNDWTQVPFC SHHFHELIMK DGRVLVVPCR NQDELIGRAR ISQGAGWSLR ETACLGKSYA QMWSLMYFHR RDLRLAANAI CSAVPSHWVP TSRTTWSIHA KHEWMTTEDM LTVWNRVWIQ ENPWMEDKTP VESWEEIPYL GKREDQWCGS LIGLTSRATW AKNIQAAINQ VRSLIGNEEY TDYMPSMKRF RREEEEAGVL W //