ID GP_RVFV Reviewed; 1206 AA. AC P03518; Q86494; Q86495; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 24-JAN-2024, entry version 105. DE RecName: Full=Envelopment polyprotein; DE AltName: Full=M polyprotein; DE Contains: DE RecName: Full=NSm-Gn protein {ECO:0000250|UniProtKB:P21401}; DE Contains: DE RecName: Full=Glycoprotein N {ECO:0000250|UniProtKB:P21401}; DE Short=Gn; DE AltName: Full=Glycoprotein G1; DE Contains: DE RecName: Full=Glycoprotein C {ECO:0000250|UniProtKB:P21401}; DE Short=Gc; DE AltName: Full=Glycoprotein G2; DE Flags: Precursor; GN Name=GP; OS Rift valley fever virus (RVFV). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Ellioviricetes; Bunyavirales; Phenuiviridae; Phlebovirus; OC Phlebovirus riftense. OX NCBI_TaxID=11588; OH NCBI_TaxID=7158; Aedes. OH NCBI_TaxID=9913; Bos taurus (Bovine). OH NCBI_TaxID=297284; Bos taurus x Bison bison (beefalo). OH NCBI_TaxID=9837; Camelus bactrianus (Bactrian camel). OH NCBI_TaxID=9925; Capra hircus (Goat). OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9940; Ovis aries (Sheep). OH NCBI_TaxID=29031; Phlebotomus papatasi (Sandfly). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=2998042; DOI=10.1016/0042-6822(85)90320-4; RA Collett M.S., Purchio A.F., Keegan K., Frazier S., Hays W., Anderson D.K., RA Parker M.D., Schmaljohn C.S., Schmidt J., Dalrymple J.M.; RT "Complete nucleotide sequence of the M RNA segment of Rift Valley fever RT virus."; RL Virology 144:228-245(1985). RN [2] RP FUNCTION (ISOFORM NSM PROTEIN). RX PubMed=24551252; DOI=10.1371/journal.pntd.0002670; RA Kading R.C., Crabtree M.B., Bird B.H., Nichol S.T., Erickson B.R., RA Horiuchi K., Biggerstaff B.J., Miller B.R.; RT "Deletion of the NSm virulence gene of Rift Valley fever virus inhibits RT virus replication in and dissemination from the midgut of Aedes aegypti RT mosquitoes."; RL PLoS Negl. Trop. Dis. 8:e2670-e2670(2014). RN [3] RP STRUCTURE BY ELECTRON MICROSCOPY (22.0 ANGSTROMS) OF THE VIRAL PARTICLE, RP SUBUNIT (GLYCOPROTEIN N), SUBUNIT (GLYCOPROTEIN C), FUNCTION (GLYCOPROTEIN RP N), AND FUNCTION (GLYCOPROTEIN C). RC STRAIN=Clone 13 {ECO:0000305}; RX PubMed=19193794; DOI=10.1128/jvi.02483-08; RA Huiskonen J.T., Overby A.K., Weber F., Gruenewald K.; RT "Electron cryo-microscopy and single-particle averaging of Rift Valley RT fever virus: evidence for GN-GC glycoprotein heterodimers."; RL J. Virol. 83:3762-3769(2009). RN [4] {ECO:0007744|PDB:4HJ1, ECO:0007744|PDB:4HJC} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 691-1119, AND GLYCOSYLATION AT RP ASN-794 AND ASN-1035. RX PubMed=23319635; DOI=10.1073/pnas.1217780110; RA Dessau M., Modis Y.; RT "Crystal structure of glycoprotein C from Rift Valley fever virus."; RL Proc. Natl. Acad. Sci. U.S.A. 110:1696-1701(2013). RN [5] {ECO:0007744|PDB:5Y0W, ECO:0007744|PDB:5Y0Y} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 154-469, AND DISULFIDE BONDS. RX PubMed=28827346; DOI=10.1073/pnas.1705176114; RA Wu Y., Zhu Y., Gao F., Jiao Y., Oladejo B.O., Chai Y., Bi Y., Lu S., RA Dong M., Zhang C., Huang G., Wong G., Li N., Zhang Y., Li Y., Feng W.H., RA Shi Y., Liang M., Zhang R., Qi J., Gao G.F.; RT "Structures of phlebovirus glycoprotein Gn and identification of a RT neutralizing antibody epitope."; RL Proc. Natl. Acad. Sci. U.S.A. 114:E7564-E7573(2017). RN [6] {ECO:0007744|PDB:6EGT, ECO:0007744|PDB:6EGU} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 691-1158, FUNCTION (GLYCOPROTEIN RP C), AND SUBUNIT (GLYCOPROTEIN C). RX PubMed=29097548; DOI=10.1126/science.aal2712; RA Guardado-Calvo P., Atkovska K., Jeffers S.A., Grau N., Backovic M., RA Perez-Vargas J., de Boer S.M., Tortorici M.A., Pehau-Arnaudet G., RA Lepault J., England P., Rottier P.J., Bosch B.J., Hub J.S., Rey F.A.; RT "A glycerophospholipid-specific pocket in the RVFV class II fusion protein RT drives target membrane insertion."; RL Science 358:663-667(2017). RN [7] {ECO:0007744|PDB:6IEA, ECO:0007744|PDB:6IEB, ECO:0007744|PDB:6IEC, ECO:0007744|PDB:6IEK} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 154-469. RX PubMed=30936489; DOI=10.1038/s41564-019-0411-z; RA Wang Q., Ma T., Wu Y., Chen Z., Zeng H., Tong Z., Gao F., Qi J., Zhao Z., RA Chai Y., Yang H., Wong G., Bi Y., Wu L., Shi R., Yang M., Song J., RA Jiang H., An Z., Wang J., Yilma T.D., Shi Y., Liu W.J., Liang M., Qin C., RA Gao G.F., Yan J.; RT "Neutralization mechanism of human monoclonal antibodies against Rift RT Valley fever virus."; RL Nat. Microbiol. 4:1231-1241(2019). CC -!- FUNCTION: [Glycoprotein N]: Structural component of the virion that CC interacts with glycoprotein C (By similarity). It shields the CC hydrophobic fusion loops of the glycoprotein C, preventing premature CC fusion (By similarity). The glycoprotein protrusions are arranged on an CC icosahedral lattice, with T=12 triangulation (PubMed:19193794, CC PubMed:23319635). They are able to attach the virion to the host cell CC receptor CD209/DC-SIGN and to promote fusion of membranes with the late CC endosome after endocytosis of the virion (By similarity). Plays a role CC in the packaging of ribonucleoproteins and polymerase during virus CC assembly (By similarity). {ECO:0000250|UniProtKB:P09613, CC ECO:0000250|UniProtKB:P21401, ECO:0000269|PubMed:19193794, CC ECO:0000269|PubMed:23319635}. CC -!- FUNCTION: [Glycoprotein C]: Structural component of the virion that CC interacts with glycoprotein N (By similarity). Acts as a class II CC fusion protein that is activated upon acidification and subsequent CC repositioning of the glycoprotein N (PubMed:23319635, PubMed:29097548). CC The glycoprotein protrusions are arranged on an icosahedral lattice, CC with T=12 triangulation (PubMed:19193794, PubMed:23319635). They are CC able to attach the virion to the host cell receptor CD209/DC-SIGN and CC to promote fusion of membranes with the late endosome after endocytosis CC of the virion (By similarity). {ECO:0000250|UniProtKB:P09613, CC ECO:0000269|PubMed:19193794, ECO:0000269|PubMed:23319635, CC ECO:0000269|PubMed:29097548}. CC -!- FUNCTION: [Isoform NSm protein]: Plays a role for virus dissemination CC in the mosquito. {ECO:0000250|UniProtKB:P21401, CC ECO:0000269|PubMed:24551252}. CC -!- FUNCTION: [NSm-Gn protein]: Plays a role for virus dissemination in CC mosquitoes. {ECO:0000250|UniProtKB:P21401}. CC -!- SUBUNIT: [Glycoprotein N]: Heterodimer with glycoprotein C CC (PubMed:19193794, PubMed:28827346). Interacts with nucleocapsid protein CC N and with the polymerase L in order to package them into virus CC particles (By similarity). {ECO:0000250|UniProtKB:P21401, CC ECO:0000269|PubMed:19193794, ECO:0000269|PubMed:28827346}. CC -!- SUBUNIT: [Glycoprotein C]: Heterodimer with glycoprotein C CC (PubMed:19193794, PubMed:28827346). Homotrimer (postfusion) CC (PubMed:29097548). Interacts with nucleocapsid protein N and with the CC polymerase L in order to package them into virus particles (By CC similarity). Interacts with host E3 ubiquitin-protein ligase UBR4; this CC interaction is important for viral RNA production (By similarity). CC Interacts with host LRP1; this interaction facilitates virus entry into CC the host cell (By similarity). {ECO:0000250|UniProtKB:P09613, CC ECO:0000250|UniProtKB:P21401, ECO:0000269|PubMed:19193794, CC ECO:0000269|PubMed:28827346, ECO:0000269|PubMed:29097548}. CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:P09613}. Host endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:P09613}. Note=Interaction between Glycoprotein N CC and Glycoprotein C is essential for proper targeting of Glycoprotein C CC to the Golgi complex, where virion budding occurs. CC {ECO:0000250|UniProtKB:P09613}. CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:P09613}. Note=Interaction between Glycoprotein N CC and Glycoprotein C is essential for proper targeting of Glycoprotein C CC to the Golgi complex, where virion budding occurs. CC {ECO:0000250|UniProtKB:P09613}. CC -!- SUBCELLULAR LOCATION: [Isoform NSm protein]: Host mitochondrion outer CC membrane {ECO:0000250|UniProtKB:P09613}; Single-pass type II membrane CC protein {ECO:0000250|UniProtKB:P09613}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=3; CC Name=1; CC IsoId=P03518-1; Sequence=Displayed; CC Name=NSm protein {ECO:0000250|UniProtKB:P21401}; Synonyms=P14; CC IsoId=P03518-2; Sequence=VSP_057986, VSP_057987; CC Name=NSm' protein {ECO:0000250|UniProtKB:P21401}; Synonyms=P13; CC IsoId=P03518-3; Sequence=VSP_057985, VSP_057987; CC -!- DOMAIN: [Glycoprotein N]: Contains a Golgi retention signal on its C- CC terminus (By similarity). The cytoplasmic tail specifically interacts CC with the ribonucleoproteins and is critical for genome packaging (By CC similarity). {ECO:0000250|UniProtKB:P09613}. CC -!- PTM: [Envelopment polyprotein]: Specific enzymatic cleavages in vivo CC yield mature proteins including NSm protein, Glycoprotein C, and CC Glycoprotein N. {ECO:0000250|UniProtKB:P21401}. CC -!- PTM: [Glycoprotein N]: Glycosylated (By similarity). The glycans can CC attach to host CD209/DC-SIGN, and may play a role in virus entry into CC dendritic cells (By similarity). {ECO:0000250|UniProtKB:P21401}. CC -!- PTM: [Glycoprotein C]: Glycosylated (By similarity). The glycans can CC attach to host CD209/DC-SIGN, and may play a role in virus entry into CC dendritic cells (By similarity). {ECO:0000250|UniProtKB:P21401}. CC -!- PTM: [Glycoprotein C]: Palmitoylated. {ECO:0000250|UniProtKB:P09613}. CC -!- SIMILARITY: Belongs to the phlebovirus envelope glycoprotein family. CC {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; M11157; AAA47450.1; -; Genomic_RNA. DR PIR; A04110; VGVURV. DR PDB; 4HJ1; X-ray; 1.90 A; A/B/C/D=691-1119. DR PDB; 4HJC; X-ray; 4.15 A; A=691-1118. DR PDB; 5Y0W; X-ray; 2.50 A; A=154-469. DR PDB; 5Y0Y; X-ray; 3.40 A; A=154-469. DR PDB; 6EGT; X-ray; 2.50 A; A/B/C=691-1158. DR PDB; 6EGU; X-ray; 2.30 A; A/B/C=691-1158. DR PDB; 6F9F; EM; 13.30 A; A/C/E/G/I=154-469. DR PDB; 6IEA; X-ray; 2.00 A; A=154-469. DR PDB; 6IEB; X-ray; 2.41 A; A/B=154-469. DR PDB; 6IEC; X-ray; 3.20 A; A/B/E/I=154-469. DR PDB; 6IEK; X-ray; 2.70 A; A/D=154-469. DR PDBsum; 4HJ1; -. DR PDBsum; 4HJC; -. DR PDBsum; 5Y0W; -. DR PDBsum; 5Y0Y; -. DR PDBsum; 6EGT; -. DR PDBsum; 6EGU; -. DR PDBsum; 6F9F; -. DR PDBsum; 6IEA; -. DR PDBsum; 6IEB; -. DR PDBsum; 6IEC; -. DR PDBsum; 6IEK; -. DR EMDB; EMD-4201; -. DR SMR; P03518; -. DR GlyCosmos; P03518; 3 sites, No reported glycans. DR ABCD; P03518; 10 sequenced antibodies. DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044193; C:host cell mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW. DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW. DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.3770; -; 1. DR Gene3D; 2.60.98.50; -; 3. DR InterPro; IPR016404; M_polyprot_prcur_phlebovir. DR InterPro; IPR043603; Phlebo_G2_C. DR InterPro; IPR010826; Phlebovirus_G1. DR InterPro; IPR009878; Phlebovirus_G2_fusion. DR InterPro; IPR009879; Phlebovirus_NSM. DR Pfam; PF19019; Phlebo_G2_C; 1. DR Pfam; PF07243; Phlebovirus_G1; 1. DR Pfam; PF07245; Phlebovirus_G2; 1. DR Pfam; PF07246; Phlebovirus_NSM; 2. DR PIRSF; PIRSF003961; M_poly_PhleboV; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; Disulfide bond; KW Fusion of virus membrane with host endosomal membrane; KW Fusion of virus membrane with host membrane; Glycoprotein; KW Host endoplasmic reticulum; Host Golgi apparatus; Host membrane; KW Host mitochondrion; Host mitochondrion outer membrane; KW Host-virus interaction; Membrane; Signal; Transmembrane; KW Transmembrane helix; Viral attachment to host cell; KW Viral attachment to host entry receptor; KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell. FT SIGNAL 1..16 FT /evidence="ECO:0000255" FT CHAIN 17..1206 FT /note="Envelopment polyprotein" FT /id="PRO_0000247009" FT CHAIN 17..690 FT /note="NSm-Gn protein" FT /id="PRO_0000036847" FT CHAIN 154..690 FT /note="Glycoprotein N" FT /evidence="ECO:0000255" FT /id="PRO_0000036848" FT CHAIN 691..1206 FT /note="Glycoprotein C" FT /evidence="ECO:0000255" FT /id="PRO_0000036849" FT TOPO_DOM 17..130 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TOPO_DOM 154..582 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 583..603 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 604..673 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TOPO_DOM 691..1159 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 1160..1180 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1181..1206 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 131..153 FT /note="Internal signal sequence for glycoprotein N" FT /evidence="ECO:0000250|UniProtKB:P09613" FT REGION 608..650 FT /note="Golgi retention signal" FT /evidence="ECO:0000250|UniProtKB:P09613" FT REGION 646..650 FT /note="Important for correct targeting of the glycoproteins FT to the Golgi complex but not for heterodimerization" FT /evidence="ECO:0000250|UniProtKB:P09613" FT REGION 675..690 FT /note="Internal signal sequence for glycoprotein C" FT /evidence="ECO:0000250|UniProtKB:P09613" FT REGION 777..783 FT /note="Fusion loop" FT /evidence="ECO:0000250|UniProtKB:R4V2Q5" FT REGION 819..830 FT /note="Fusion loop" FT /evidence="ECO:0000250|UniProtKB:P21401" FT SITE 153..154 FT /note="Cleavage; by host signal peptidase" FT /evidence="ECO:0000250|UniProtKB:P21401" FT SITE 690..691 FT /note="Cleavage; by host signal peptidase" FT /evidence="ECO:0000250|UniProtKB:P21401" FT CARBOHYD 794 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000269|PubMed:23319635" FT CARBOHYD 1035 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000269|PubMed:23319635" FT CARBOHYD 1077 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT DISULFID 179..188 FT /evidence="ECO:0000269|PubMed:28827346" FT DISULFID 229..239 FT /evidence="ECO:0000269|PubMed:28827346" FT DISULFID 250..281 FT /evidence="ECO:0000269|PubMed:28827346" FT DISULFID 271..284 FT /evidence="ECO:0000269|PubMed:28827346" FT DISULFID 304..456 FT /evidence="ECO:0000269|PubMed:28827346" FT DISULFID 322..332 FT /evidence="ECO:0000269|PubMed:28827346" FT DISULFID 374..434 FT /evidence="ECO:0000269|PubMed:28827346" FT DISULFID 402..413 FT /evidence="ECO:0000269|PubMed:28827346" FT DISULFID 420..425 FT /evidence="ECO:0000269|PubMed:28827346" FT DISULFID 479..482 FT /evidence="ECO:0000303|PubMed:28827346" FT DISULFID 486..556 FT /evidence="ECO:0000303|PubMed:28827346" FT DISULFID 506..511 FT /evidence="ECO:0000303|PubMed:28827346" FT DISULFID 691..731 FT /evidence="ECO:0000250|UniProtKB:P21401" FT DISULFID 704..713 FT /evidence="ECO:0000250|UniProtKB:P21401" FT DISULFID 756..852 FT /evidence="ECO:0000250|UniProtKB:P21401" FT DISULFID 771..965 FT /evidence="ECO:0000250|UniProtKB:P21401" FT DISULFID 777..825 FT /evidence="ECO:0000250|UniProtKB:P21401" FT DISULFID 783..832 FT /evidence="ECO:0000250|UniProtKB:P21401" FT DISULFID 788..814 FT /evidence="ECO:0000250|UniProtKB:P21401" FT DISULFID 818..823 FT /evidence="ECO:0000250|UniProtKB:P21401" FT DISULFID 934..947 FT /evidence="ECO:0000250|UniProtKB:P21401" FT DISULFID 1029..1101 FT /evidence="ECO:0000250|UniProtKB:P21401" FT DISULFID 1039..1042 FT /evidence="ECO:0000250|UniProtKB:P21401" FT DISULFID 1049..1083 FT /evidence="ECO:0000250|UniProtKB:P21401" FT VAR_SEQ 1..51 FT /note="Missing (in isoform NSm' protein)" FT /id="VSP_057985" FT VAR_SEQ 1..38 FT /note="Missing (in isoform NSm protein)" FT /id="VSP_057986" FT VAR_SEQ 154..1197 FT /note="Missing (in isoform NSm protein and isoform NSm' FT protein)" FT /id="VSP_057987" FT TURN 156..159 FT /evidence="ECO:0007829|PDB:6IEB" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:5Y0Y" FT HELIX 176..179 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:6IEA" FT TURN 189..191 FT /evidence="ECO:0007829|PDB:6IEA" FT HELIX 192..195 FT /evidence="ECO:0007829|PDB:6IEA" FT TURN 197..199 FT /evidence="ECO:0007829|PDB:6IEB" FT HELIX 201..205 FT /evidence="ECO:0007829|PDB:6IEA" FT TURN 206..208 FT /evidence="ECO:0007829|PDB:6IEA" FT HELIX 212..217 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 225..230 FT /evidence="ECO:0007829|PDB:6IEA" FT HELIX 240..244 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 255..260 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 264..270 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 275..277 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 284..286 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 288..291 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 294..298 FT /evidence="ECO:0007829|PDB:5Y0W" FT STRAND 300..304 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 321..324 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 336..347 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 354..358 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 361..364 FT /evidence="ECO:0007829|PDB:6IEA" FT HELIX 369..371 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 372..376 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 394..397 FT /evidence="ECO:0007829|PDB:5Y0W" FT HELIX 399..401 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 404..407 FT /evidence="ECO:0007829|PDB:6IEB" FT STRAND 413..415 FT /evidence="ECO:0007829|PDB:6IEA" FT HELIX 417..420 FT /evidence="ECO:0007829|PDB:6IEA" FT HELIX 427..429 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 431..436 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 441..447 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 450..452 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 455..467 FT /evidence="ECO:0007829|PDB:6IEA" FT STRAND 691..696 FT /evidence="ECO:0007829|PDB:4HJ1" FT HELIX 699..701 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 702..709 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 711..722 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 728..735 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 742..764 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 767..776 FT /evidence="ECO:0007829|PDB:4HJ1" FT TURN 785..790 FT /evidence="ECO:0007829|PDB:4HJ1" FT HELIX 798..803 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 810..817 FT /evidence="ECO:0007829|PDB:4HJ1" FT HELIX 821..823 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 826..829 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 831..844 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 847..864 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 870..875 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 880..883 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 886..893 FT /evidence="ECO:0007829|PDB:4HJ1" FT HELIX 900..902 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 904..908 FT /evidence="ECO:0007829|PDB:4HJ1" FT TURN 909..911 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 912..918 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 931..936 FT /evidence="ECO:0007829|PDB:4HJ1" FT HELIX 937..941 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 947..949 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 954..959 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 962..967 FT /evidence="ECO:0007829|PDB:4HJ1" FT HELIX 972..978 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 980..985 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 988..992 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 994..996 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 999..1003 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 1009..1021 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 1030..1044 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 1046..1056 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 1058..1064 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 1070..1075 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 1077..1086 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 1089..1103 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 1106..1113 FT /evidence="ECO:0007829|PDB:4HJ1" FT STRAND 1123..1129 FT /evidence="ECO:0007829|PDB:6EGU" SQ SEQUENCE 1206 AA; 132053 MW; D2E8017179285924 CRC64; MYVLLTILIS VLVCEAVIRV SLSSTREETC FGDSTNPEMI EGAWDSLREE EMPEELSCSI SGIREVKTSS QELYRALKAI IAADGLNNIT CHGKDPEDKI SLIKGPPHKK RVGIVRCERR RDAKQIGRET MAGIAMTVLP ALAVFALAPV VFAEDPHLRN RPGKGHNYID GMTQEDATCK PVTYAGACSS FDVLLEKGKF PLFQSYAHHR TLLEAVHDTI IAKADPPSCD LQSAHGNPCM KEKLVMKTHC PNDYQSAHYL NNDGKMASVK CPPKYGLTED CNFCRQMTGA SLKKGSYPLQ DLFCQSSEDD GSKLKTKMKG VCEVGVQAHK KCDGQLSTAH EVVPFAVFKN SKKVYLDKLD LKTEENLLPD SFVCFEHKGQ YKGTMDSGQT KRELKSFDIS QCPKIGGHGS KKCTGDAAFC SAYECTAQYA NAYCSHANGS GIVQIQVSGV WKKPLCVGYE RVVVKRELSA KPIQRVEPCT TCITKCEPHG LVVRSTGFKI SSAVACASGV CVTGSQSPST EITLKYPGIS QSSGGDIGVH MAHDDQSVSS KIVAHCPPQD PCLVHGCIVC AHGLINYQCH TALSAFVVVF VFSSIAIICL AVLYRVLKCL KIAPRKVLNP LMWITAFIRW IYKKMVARVA HNINQVNREI GWMEGGQLVL GNPAPIPRHA PIPRYSTYLM LLLIVSYASA CSELIQASSR ITTCSTEGVN TKCRLSGTAL IRAGSVGAEA CLMLKGVKED QTKFLKIKTV SSELSCREGQ SYWTGSISPK CLSSRRCHLV GECHVNRCLS WRDNETSAEF SFVGESTTMR ENKCFEQCGG WGCGCFNVNP SCLFVHTYLQ SVRKEALRVF NCIDWVHKLT LEITDFDGSV STIDLGASSS RFTNWGSVSL SLDAEGISGS NSFSFIESPS KGYAIVDEPF SEIPRQGFLG EIRCNSESSV LSAHESCLRA PNLISYKPMI DQLECTTNLI DPFVVFERGS LPQTRNDKTF AASKGNRGVQ AFSKGSVQAD LTLMFDNFEV DFVGAAVSCD AAFLNLTGCY SCNAGARVCL SITSTGTGSL SAHNKDGSLH IVLPSENGTK DQCQILHFTV PEVEEEFMYS CDGDERPLLV KGTLIAIDPF DDRREAGGES TVVNPKSGSW NFFDWFSGLM SWFGGPLKLY SSFACMLHYQ LGSFSSLYIL EEQASLKCGL LPLRRPHRSV RVKVIC //