ID Q5GDB7_CVHSA Unreviewed; 1255 AA. AC Q5GDB7; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 16-OCT-2019, entry version 35. 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., RA Chen Q.X., Gao Y.W., Zhou H.Q., Xiang H., Zheng H.J., Chern S.W., RA Cheng F., Pan C.M., Xuan H., Chen S.J., Luo H.M., Zhou D.H., Liu Y.F., RA He J.F., Qin P.Z., Li L.H., Ren Y.Q., Liang W.J., Yu Y.D., RA Anderson L., Wang M., Xu R.H., Wu X.W., Zheng H.Y., Chen J.D., RA Liang G., Gao Y., Liao M., Fang L., Jiang L.Y., Li H., Chen F., Di B., RA He L.J., Lin J.Y., Tong S., Kong X., Du L., Hao P., Tang H., RA Bernini A., Yu X.J., Spiga O., Guo Z.M., Pan H.Y., He W.Z., RA 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 RT in 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 CC membrane by interacting with host receptor, initiating the CC infection. {ECO:0000256|HAMAP-Rule:MF_04099}. CC -!- FUNCTION: Spike protein S2': Acts as a viral fusion peptide which CC is unmasked following S2 cleavage occurring upon virus CC endocytosis. {ECO:0000256|HAMAP-Rule:MF_04099}. CC -!- FUNCTION: Spike protein S2: mediates fusion of the virion and CC cellular membranes by acting as a class I viral fusion protein. CC Under the current model, the protein has at least three CC conformational states: pre-fusion native state, pre-hairpin CC intermediate state, and post-fusion hairpin state. During viral CC and target cell membrane fusion, the coiled coil regions (heptad CC repeats) assume a trimer-of-hairpins structure, positioning the CC fusion peptide in close proximity to the C-terminal region of the CC ectodomain. The formation of this structure appears to drive CC apposition and subsequent fusion of viral and target cell CC membranes. {ECO:0000256|HAMAP-Rule:MF_04099}. CC -!- SUBUNIT: Homotrimer; each monomer consists of a S1 and a S2 CC subunit. The resulting peplomers protrude from the virus surface CC as spikes. {ECO:0000256|HAMAP-Rule:MF_04099}. CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000256|HAMAP- CC Rule:MF_04099}; Single-pass type I membrane protein CC {ECO:0000256|HAMAP-Rule:MF_04099}. Host endoplasmic reticulum- CC Golgi intermediate compartment membrane {ECO:0000256|HAMAP- CC Rule:MF_04099}; Single-pass type I membrane protein CC {ECO:0000256|HAMAP-Rule:MF_04099}. Host cell membrane CC {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 CC cell-cell fusion. {ECO:0000256|HAMAP-Rule:MF_04099}. CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. CC The precursor is processed into S1 and S2 by host cell furin or CC another cellular protease to yield the mature S1 and S2 proteins. CC Additionally, a second cleavage leads to the release of a fusion CC peptide after viral attachment to host cell receptor. CC {ECO:0000256|HAMAP-Rule:MF_04099}. CC -!- PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike CC glycoprotein is digested within host endosomes. CC {ECO:0000256|HAMAP-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 CC of 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; IPR002552; Corona_S2. DR InterPro; IPR027400; S_HR2. DR InterPro; IPR032500; Spike_N. DR InterPro; IPR018548; Spike_rcpt-bd. DR InterPro; IPR036326; Spike_rcpt-bd_sf. DR Pfam; PF01601; Corona_S2; 1. DR Pfam; PF16451; Spike_NTD; 1. DR Pfam; PF09408; Spike_rec_bind; 1. DR SUPFAM; SSF143587; SSF143587; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_04099}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04099}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|HAMAP-Rule:MF_04099}; KW Fusion of virus membrane with host membrane {ECO:0000256|HAMAP- KW Rule:MF_04099}; Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04099}; KW Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04099}; KW Host membrane {ECO:0000256|HAMAP-Rule:MF_04099}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04099}; KW Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04099}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_04099, ECO:0000256|SAM:Phobius}; KW Palmitate {ECO:0000256|HAMAP-Rule:MF_04099}; KW Signal {ECO:0000256|HAMAP-Rule:MF_04099}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_04099, KW 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|HAMAP-Rule:MF_04099}; KW Viral envelope protein {ECO:0000256|HAMAP-Rule:MF_04099}; KW Viral penetration into host cytoplasm {ECO:0000256|HAMAP- KW Rule:MF_04099}; Virion {ECO:0000256|HAMAP-Rule:MF_04099}; KW Virulence {ECO:0000256|HAMAP-Rule:MF_04099}; KW Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04099}. FT TOPO_DOM 14 1195 Extracellular. {ECO:0000256|HAMAP-Rule: FT MF_04099}. FT TRANSMEM 1196 1218 Helical. {ECO:0000256|SAM:Phobius}. FT TOPO_DOM 1217 1255 Cytoplasmic. {ECO:0000256|HAMAP-Rule: FT MF_04099}. FT DOMAIN 100 280 Spike_NTD. {ECO:0000259|Pfam:PF16451}. FT DOMAIN 317 568 Spike_rec_bind. {ECO:0000259|Pfam: FT PF09408}. FT DOMAIN 658 1252 Corona_S2. {ECO:0000259|Pfam:PF01601}. FT REGION 306 527 Receptor-binding domain. FT {ECO:0000256|HAMAP-Rule:MF_04099}. FT REGION 770 788 Fusion peptide. {ECO:0000256|HAMAP-Rule: FT MF_04099}. FT REGION 902 952 Heptad repeat 1. {ECO:0000256|HAMAP-Rule: FT MF_04099}. FT REGION 1145 1184 Heptad repeat 2. {ECO:0000256|HAMAP-Rule: FT MF_04099}. FT COILED 931 975 {ECO:0000256|HAMAP-Rule:MF_04099}. FT COILED 1157 1185 {ECO:0000256|HAMAP-Rule:MF_04099}. FT MOTIF 1251 1255 KxHxx. {ECO:0000256|HAMAP-Rule:MF_04099}. FT SITE 667 668 Cleavage. {ECO:0000256|HAMAP-Rule: FT MF_04099}. FT SITE 797 798 Cleavage. {ECO:0000256|HAMAP-Rule: FT MF_04099}. FT DISULFID 323 348 {ECO:0000256|HAMAP-Rule:MF_04099}. FT DISULFID 366 419 {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 //