ID L7QI57_9MONO Unreviewed; 676 AA. AC L7QI57; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 16-MAR-2016, entry version 16. DE SubName: Full=Virion spike glycoprotein {ECO:0000313|EMBL:AGB56830.1}; GN Name=GP {ECO:0000313|EMBL:AGB56830.1}; OS Zaire ebolavirus. OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Mononegavirales; Filoviridae; Ebolavirus. OX NCBI_TaxID=186538 {ECO:0000313|EMBL:AGB56830.1}; RN [1] {ECO:0000313|EMBL:AGB56830.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=EBOV/H.sapiens-tc/GAB/2002/Ilembe RC {ECO:0000313|EMBL:AGB56830.1}; RX PubMed=23255795; DOI=10.1128/JVI.03118-12; RA Carroll S.A., Towner J.S., Sealy T.K., McMullan L.K., Khristova M.L., RA Burt F.J., Swanepoel R., Rollin P.E., Nichol S.T.; RT "Molecular evolution of viruses of the family filoviridae based on 97 RT whole-genome sequences."; RL J. Virol. 87:2608-2616(2013). RN [2] {ECO:0000213|PDB:2MB1} RP STRUCTURE BY NMR OF 507-560, AND DISULFIDE BONDS. RX PubMed=24696482; DOI=10.1128/JVI.00396-14; RA Gregory S.M., Larsson P., Nelson E.A., Kasson P.M., White J.M., RA Tamm L.K.; RT "Ebolavirus entry requires a compact hydrophobic fist at the tip of RT the fusion loop."; RL J. Virol. 88:6636-6649(2014). 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; KC242800; AGB56830.1; -; Viral_cRNA. DR PDB; 2MB1; NMR; -; A=507-560. DR PDBsum; 2MB1; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR014625; GPC_FiloV. DR InterPro; IPR002561; GPC_filovir-type_extra_dom. DR Pfam; PF01611; Filo_glycop; 1. DR PIRSF; PIRSF036874; GPC_FiloV; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2MB1}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR036874-50}; KW Lipoprotein {ECO:0000256|PIRSR:PIRSR036874-51}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Palmitate {ECO:0000256|PIRSR:PIRSR036874-51}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 651 675 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 15 348 Filo_glycop. {ECO:0000259|Pfam:PF01611}. FT LIPID 670 670 S-palmitoyl cysteine; by host. FT {ECO:0000256|PIRSR:PIRSR036874-51}. FT LIPID 672 672 S-palmitoyl cysteine; by host. FT {ECO:0000256|PIRSR:PIRSR036874-51}. FT DISULFID 53 609 Interchain (between GP1 and GP2 chains). FT {ECO:0000256|PIRSR:PIRSR036874-50}. FT DISULFID 108 135 {ECO:0000256|PIRSR:PIRSR036874-50}. FT DISULFID 121 147 {ECO:0000256|PIRSR:PIRSR036874-50}. FT DISULFID 511 556 {ECO:0000213|PDB:2MB1, ECO:0000256|PIRSR: FT PIRSR036874-50}. FT DISULFID 601 608 {ECO:0000256|PIRSR:PIRSR036874-50}. SQ SEQUENCE 676 AA; 74482 MW; C15173F529AF4C42 CRC64; MGITGILQLP RDRFKRTSFF LWVIILFQRT FSIPLGVIHN STLQVSDVDK LVCRDKLSST NQLRSVGLNL EGNGVATDVP SATKRWGFRS GVPPKVVNYE AGEWAENCYN LEIKKPDGSE CLPAAPDGIR GFPRCRYVHK VSGTGPCAGD FAFHKEGAFF LYDRLASTVI YRGTTFAEGV VAFLILPQAK KDFFSSHPLR EPVNATEDPS SGYYSTTIRY QATGFGTNET EYLFEVDNLT YVQLESRFTP QFLLQLNETI YASGKRSNTT GKLIWKVNPE IDTTIGEWAF WETKKNLTRK IRSEELSFTA VSNGAKDISG QSPARTSSDP ETYTTTEDHK IMASENSSAM VQVHNQGREA AVSHLITLAT ISTSPQSPTT KPGQDNSTHN TPVYKLDISE ATQVEQHHRR TDNDSTASDT PPATTAAGPP KAENINTSKS ADSLDPATTT SPQNYSETAG NNNTHHQDTG EESAGSGKLG LIANTIAGVA GLITGGRRTR REAIVNAQPK CNPNLHYWTT QDEGAAIGLA WIPYFGPAAE GIYTEGLMHN QDGLICGLRQ LANETTQALQ LFLRATTELR TFSILNRKAI DFLLQRWGGT CHILGPDCCI EPHDWTKNIT DKIDQIIHDF VDKTLPDQGD NDNWWTGWRQ WIPAGIGVTG VIIAVIALFC ICKFVF //