ID Q5GDB7_CVHSA Unreviewed; 1255 AA. AC Q5GDB7; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 12-AUG-2020, entry version 37. DE RecName: Full=Spike glycoprotein {ECO:0000256|HAMAP-Rule:MF_04099}; DE Short=S glycoprotein {ECO:0000256|HAMAP-Rule:MF_04099}; DE AltName: Full=E2 {ECO:0000256|HAMAP-Rule:MF_04099}; DE AltName: Full=Peplomer protein {ECO:0000256|HAMAP-Rule:MF_04099}; DE Contains: DE RecName: Full=Spike protein S1 {ECO:0000256|HAMAP-Rule:MF_04099}; DE Contains: DE RecName: Full=Spike protein S2 {ECO:0000256|HAMAP-Rule:MF_04099}; DE Contains: DE RecName: Full=Spike protein S2' {ECO:0000256|HAMAP-Rule:MF_04099}; GN Name=S {ECO:0000256|HAMAP-Rule:MF_04099}; OS SARS coronavirus PC4-115. OC Viruses; Riboviria; Nidovirales; Cornidovirineae; Coronaviridae; OC Orthocoronavirinae; Betacoronavirus; Sarbecovirus. OX NCBI_TaxID=296837 {ECO:0000313|EMBL:AAV49719.1}; RN [1] {ECO:0000313|EMBL:AAV49719.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=15695582; DOI=10.1073/pnas.0409608102; RA Song H.D., Tu C.C., Zhang G.W., Wang S.Y., Zheng K., Lei L.C., Chen Q.X., RA Gao Y.W., Zhou H.Q., Xiang H., Zheng H.J., Chern S.W., Cheng F., Pan C.M., RA Xuan H., Chen S.J., Luo H.M., Zhou D.H., Liu Y.F., He J.F., Qin P.Z., RA Li L.H., Ren Y.Q., Liang W.J., Yu Y.D., Anderson L., Wang M., Xu R.H., RA Wu X.W., Zheng H.Y., Chen J.D., Liang G., Gao Y., Liao M., Fang L., RA Jiang L.Y., Li H., Chen F., Di B., He L.J., Lin J.Y., Tong S., Kong X., RA Du L., Hao P., Tang H., Bernini A., Yu X.J., Spiga O., Guo Z.M., Pan H.Y., RA He W.Z., Manuguerra J.C., Fontanet A., Danchin A., Niccolai N., Li Y.X., RA Wu C.I., Zhao G.P.; RT "Cross-host evolution of severe acute respiratory syndrome coronavirus in RT palm civet and human."; RL Proc. Natl. Acad. Sci. U.S.A. 102:2430-2435(2005). CC -!- FUNCTION: Spike protein S1: attaches the virion to the cell membrane by CC interacting with host receptor, initiating the infection. CC {ECO:0000256|HAMAP-Rule:MF_04099}. CC -!- FUNCTION: Spike protein S2': Acts as a viral fusion peptide which is CC unmasked following S2 cleavage occurring upon virus endocytosis. CC {ECO:0000256|HAMAP-Rule:MF_04099}. CC -!- FUNCTION: Spike protein S2: mediates fusion of the virion and cellular CC membranes by acting as a class I viral fusion protein. Under the CC current model, the protein has at least three conformational states: CC pre-fusion native state, pre-hairpin intermediate state, and post- CC fusion hairpin state. During viral and target cell membrane fusion, the CC coiled coil regions (heptad repeats) assume a trimer-of-hairpins CC structure, positioning the fusion peptide in close proximity to the C- CC terminal region of the ectodomain. The formation of this structure CC appears to drive apposition and subsequent fusion of viral and target CC cell membranes. {ECO:0000256|HAMAP-Rule:MF_04099}. CC -!- SUBUNIT: Homotrimer; each monomer consists of a S1 and a S2 subunit. CC The resulting peplomers protrude from the virus surface as spikes. CC {ECO:0000256|HAMAP-Rule:MF_04099}. CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000256|HAMAP- CC Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000256|HAMAP- CC Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate CC compartment membrane {ECO:0000256|HAMAP-Rule:MF_04099}; Single-pass CC type I membrane protein {ECO:0000256|HAMAP-Rule:MF_04099}. Host cell CC membrane {ECO:0000256|HAMAP-Rule:MF_04099}; Single-pass type I membrane CC protein {ECO:0000256|HAMAP-Rule:MF_04099}. Note=Accumulates in the CC endoplasmic reticulum-Golgi intermediate compartment, where it CC participates in virus particle assembly. Some S oligomers are CC transported to the host plasma membrane, where they may mediate cell- CC cell fusion. {ECO:0000256|HAMAP-Rule:MF_04099}. CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The CC precursor is processed into S1 and S2 by host cell furin or another CC cellular protease to yield the mature S1 and S2 proteins. Additionally, CC a second cleavage leads to the release of a fusion peptide after viral CC attachment to host cell receptor. {ECO:0000256|HAMAP-Rule:MF_04099}. CC -!- PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike CC glycoprotein is digested within host endosomes. {ECO:0000256|HAMAP- CC Rule:MF_04099}. CC -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family. CC {ECO:0000256|HAMAP-Rule:MF_04099}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04099}. 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; AY627044; AAV49719.1; -; Genomic_RNA. DR GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; 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-UniRule. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-UniRule. DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule. DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:UniProtKB-UniRule. DR Gene3D; 1.20.5.790; -; 1. DR HAMAP; MF_04099; BETA_CORONA_SPIKE; 1. DR InterPro; IPR042578; BETA_CORONA_SPIKE. DR InterPro; IPR043473; S2_sf_CoV. DR InterPro; IPR027400; S_HR2_CoV. DR InterPro; IPR032500; Spike_N. DR InterPro; IPR018548; Spike_rcpt-bd_bCoV. DR InterPro; IPR036326; Spike_rcpt-bd_sf_CoV. DR InterPro; IPR002552; Spike_S2_CoV. DR Pfam; PF01601; Corona_S2; 1. DR Pfam; PF16451; Spike_NTD; 1. DR Pfam; PF09408; Spike_rec_bind; 1. DR SUPFAM; SSF111474; SSF111474; 2. DR SUPFAM; SSF143587; SSF143587; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP- KW Rule:MF_04099}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP- KW Rule:MF_04099}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|ARBA:ARBA00022510, ECO:0000256|HAMAP-Rule:MF_04099}; KW Fusion of virus membrane with host membrane {ECO:0000256|ARBA:ARBA00022506, KW ECO:0000256|HAMAP-Rule:MF_04099}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|HAMAP- KW Rule:MF_04099}; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511, ECO:0000256|HAMAP- KW Rule:MF_04099}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870, ECO:0000256|HAMAP- KW Rule:MF_04099}; Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04099}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP- KW Rule:MF_04099}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04099, KW ECO:0000256|SAM:Phobius}; KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_04099}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_04099}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_04099, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04099, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804, KW ECO:0000256|HAMAP-Rule:MF_04099}; KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879, ECO:0000256|HAMAP- KW Rule:MF_04099}; KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595, KW ECO:0000256|HAMAP-Rule:MF_04099}; KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04099}; KW Virulence {ECO:0000256|ARBA:ARBA00023026, ECO:0000256|HAMAP-Rule:MF_04099}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296, KW ECO:0000256|HAMAP-Rule:MF_04099}. FT CHAIN 14..667 FT /note="Spike protein S1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04099" FT /id="PRO_5023370372" FT CHAIN 668..1255 FT /note="Spike protein S2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04099" FT /id="PRO_5023370373" FT CHAIN 798..1255 FT /note="Spike protein S2'" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04099" FT /id="PRO_5023370374" FT TOPO_DOM 14..1195 FT /note="Extracellular" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04099" FT TRANSMEM 1196..1218 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TOPO_DOM 1217..1255 FT /note="Cytoplasmic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04099" FT DOMAIN 100..280 FT /note="Spike_NTD" FT /evidence="ECO:0000259|Pfam:PF16451" FT DOMAIN 317..568 FT /note="Spike_rec_bind" FT /evidence="ECO:0000259|Pfam:PF09408" FT DOMAIN 658..1252 FT /note="Corona_S2" FT /evidence="ECO:0000259|Pfam:PF01601" FT REGION 306..527 FT /note="Receptor-binding domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04099" FT REGION 770..788 FT /note="Fusion peptide" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04099" FT REGION 902..952 FT /note="Heptad repeat 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04099" FT REGION 1145..1184 FT /note="Heptad repeat 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04099" FT COILED 931..975 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04099" FT COILED 1157..1185 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04099" FT MOTIF 1251..1255 FT /note="KxHxx" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04099" FT SITE 667..668 FT /note="Cleavage" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04099" FT SITE 797..798 FT /note="Cleavage" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04099" FT DISULFID 323..348 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04099" FT DISULFID 366..419 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04099" SQ SEQUENCE 1255 AA; 139173 MW; 696C5EA96FB5426F CRC64; MFIFLLFLTL TSGSDLDRCT TFDDVQAPNY TQHTSSMRGV YYPDEIFRSD TLYLTQDLFL PFYSNVTGFH TINHTFDNPV IPFKDGIYFA ATEKSNVVRG WVFGSTMNNK SQSVIIINNS TNVVIRACNF ELCDNPFFVV SKPMGTRTHT MIFDNAFNCT FEYISDAFSL DVSEKSGNFK HLREFVFKNK DGFLYVYKGY QPIDVVRDLP SGFNTLKPIF KLPLGINITN FRAILTAFSP AQDTWGTSAA AYFVGYLKPT TFMLKYDENG TITDAVDCSQ NPLAELKCSV KSFEIDKGIY QTSNFRVVPS GDVVRFPNIT NLCPFGEVFN ATKFPSVYAW ERKRISNCVA DYSVLYNSTS FSTFKCYGVS ATKLNDLCFS NVYADSFVVK GDDVRQIAPG QTGVIADYNY KLPDDFMGCV LAWNTRNIDA TSTGNYNYKY RYLRHGKLRP FERDISNVPF SPDGKPCTPP APNCYWPLNG YGFYTTSGIG YQPYRVVVLS FELLNAPATV CGPKLSTDLI KNQCVNFNFN GLTGTGVLTP SSKRFQPFQQ FGRDVSDFTD SVRDPKTSEI LDISPCSFGG VSVITPGTNA SSEVAVLYQD VNCTDVSTLI HAEQLTPAWR IYSTGNNVFQ TQAGCLIGAE HVDTSYECDI PIGAGICASY HTVSSLRSTS QKSIVAYTMS LGADSSIAYS NNTIAIPTNF SISITTEVMP VSMAKTSVDC NMYICGDSTE CANLLLQYGS FCRQLNRALS GIAAEQDRNT REVFVQVKQM YKTPTLKDFG GFNFSQILPD PLKPTKRSFI EDLLFNKVTL ADAGFMKQYG ECLGDINARD LICAQKFNGL TVLPPLLTDD MIAAYTAALV SGTATAGWTF GAGAALQIPF AMQMAYRFNG IGVTQNVLYE NQKQIANQFN KAISQIQESL TTTSTALGKL QDVVNQNAQA LNTLVKQLSS NFGAISSVLN DILSRLDKVE AEVQIDRLIT GRLQSLQTYV TQQLIRAAEI RASANLAATK MSECVLGQSK RVDFCGKGYH LMSFPQAAPH GVVFLHVTYV PSQERNFTTA PAICHEGKAY FPREGVFVFN GTSWFITQRN FFSPQIITTD NTFVSGNCDV VIGIINNTVY DPLQPELDSF KEELDKYFKN HTSPDVDLGD ISGINASVVN IQEEIDRLNE VAKNLNESLI DLQELGKYEQ YIKWPWYVWL GFIAGLIAIV MVTILLCCMT SCCSCLKGAC SCGSCCKFDE DDSEPVLKGV KLHYT //