ID SPIKE_SARS Reviewed; 1255 AA. AC P59594; Q6QU82; Q7T696; Q7TA19; Q7TFA2; Q7TFB1; Q80BV6; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 23-APR-2003, sequence version 1. DT 27-NOV-2024, entry version 159. DE RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099}; DE Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099}; DE AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04099}; DE AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04099}; DE Contains: DE RecName: Full=Spike protein S1 {ECO:0000255|HAMAP-Rule:MF_04099}; DE Contains: DE RecName: Full=Spike protein S2 {ECO:0000255|HAMAP-Rule:MF_04099}; DE Contains: DE RecName: Full=Spike protein S2' {ECO:0000255|HAMAP-Rule:MF_04099}; DE Flags: Precursor; GN Name=S {ECO:0000255|HAMAP-Rule:MF_04099}; ORFNames=2; OS Severe acute respiratory syndrome coronavirus (SARS-CoV). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae; OC Betacoronavirus; Sarbecovirus. OX NCBI_TaxID=694009; OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9675; Paguma larvata (Masked palm civet). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate Urbani; RX PubMed=12730500; DOI=10.1126/science.1085952; RA Rota P.A., Oberste M.S., Monroe S.S., Nix W.A., Campagnoli R., RA Icenogle J.P., Penaranda S., Bankamp B., Maher K., Chen M.-H., Tong S., RA Tamin A., Lowe L., Frace M., DeRisi J.L., Chen Q., Wang D., Erdman D.D., RA Peret T.C.T., Burns C., Ksiazek T.G., Rollin P.E., Sanchez A., Liffick S., RA Holloway B., Limor J., McCaustland K., Olsen-Rasmussen M., Fouchier R., RA Guenther S., Osterhaus A.D.M.E., Drosten C., Pallansch M.A., Anderson L.J., RA Bellini W.J.; RT "Characterization of a novel coronavirus associated with severe acute RT respiratory syndrome."; RL Science 300:1394-1399(2003). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate Tor2; RX PubMed=12730501; DOI=10.1126/science.1085953; RA Marra M.A., Jones S.J.M., Astell C.R., Holt R.A., Brooks-Wilson A., RA Butterfield Y.S.N., Khattra J., Asano J.K., Barber S.A., Chan S.Y., RA Cloutier A., Coughlin S.M., Freeman D., Girn N., Griffith O.L., Leach S.R., RA Mayo M., McDonald H., Montgomery S.B., Pandoh P.K., Petrescu A.S., RA Robertson A.G., Schein J.E., Siddiqui A., Smailus D.E., Stott J.M., RA Yang G.S., Plummer F., Andonov A., Artsob H., Bastien N., Bernard K., RA Booth T.F., Bowness D., Czub M., Drebot M., Fernando L., Flick R., RA Garbutt M., Gray M., Grolla A., Jones S., Feldmann H., Meyers A., RA Kabani A., Li Y., Normand S., Stroher U., Tipples G.A., Tyler S., RA Vogrig R., Ward D., Watson B., Brunham R.C., Krajden M., Petric M., RA Skowronski D.M., Upton C., Roper R.L.; RT "The genome sequence of the SARS-associated coronavirus."; RL Science 300:1399-1404(2003). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate CUHK-Su10, and Isolate CUHK-W1; RX PubMed=12853594; DOI=10.1056/nejm200307103490216; RA Tsui S.K.W., Chim S.S.C., Lo Y.M.D.; RT "Coronavirus genomic-sequence variations and the epidemiology of the severe RT acute respiratory syndrome."; RL N. Engl. J. Med. 349:187-188(2003). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate HKU-39849; RX PubMed=12876307; DOI=10.1177/15353702-0322807-13; RA Zeng F.Y., Chan C.W., Chan M.N., Chen J.D., Chow K.Y.C., Hon C.C.C., RA Hui R.K.H., Li J., Li V.Y.Y., Wang C.Y., Wang P.Y., Guan Y., Zheng B., RA Poon L.L.M., Chan K.H., Yuen K.Y., Peiris J.S.M., Leung F.C.; RT "The complete genome sequence of severe acute respiratory syndrome RT coronavirus strain HKU-39849 (HK-39)."; RL Exp. Biol. Med. 228:866-873(2003). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate GZ50, and Isolate HKU-36871; RX PubMed=12958366; DOI=10.1126/science.1087139; RA Guan Y., Zheng B.J., He Y.Q., Liu X.L., Zhuang Z.X., Cheung C.L., Luo S.W., RA Li P.H., Zhang L.J., Guan Y.J., Butt K.M., Wong K.L., Chan K.W., Lim W., RA Shortridge K.F., Yuen K.Y., Peiris J.S.M., Poon L.L.M.; RT "Isolation and characterization of viruses related to the SARS coronavirus RT from animals in southern China."; RL Science 302:276-278(2003). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04, and RC Isolate GD01; RA Qin E., Zhu Q., Yu M., Fan B., Chang G., Si B., Yang B., Peng W., Jiang T., RA Liu B., Deng Y., Liu H., Zhang Y., Wang C., Li Y., Gan Y., Li X., Lu F., RA Tan G., Yang R., Cao W.S., Wang J., Chen W., Cong L., Deng Y., Dong W., RA Han Y., Hu W., Lei M., Li C., Li G., Li G., Li H., Li S., Li S., Li W., RA Li W., Lin W., Liu J., Liu Z., Lu H., Ni P., Qi Q., Sun Y., Tang L., RA Tong Z., Wang J., Wang X., Wu Q., Xi Y., Xu Z., Yang L., Ye C., Ye J., RA Zhang B., Zhang F., Zhang J., Zhang X., Zhou J., Yang H.; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate Sin2500, Isolate Sin2677, Isolate Sin2679, Isolate Sin2748, RC and Isolate sin2774; RX PubMed=12781537; DOI=10.1016/s0140-6736(03)13414-9; RA Ruan Y., Wei C.L., Ling A.E., Vega V.B., Thoreau H., Se Thoe S.Y., RA Chia J.-M., Ng P., Chiu K.P., Lim L., Zhang T., Chan K.P., Oon L.E.L., RA Ng M.L., Leo S.Y., Ng L.F.P., Ren E.C., Stanton L.W., Long P.M., Liu E.T.; RT "Comparative full-length genome sequence analysis of 14 SARS coronavirus RT isolates and common mutations associated with putative origins of RT infection."; RL Lancet 361:1779-1785(2003). RN [8] RP ERRATUM OF PUBMED:12781537. RA Ruan Y., Wei C.L., Ling A.E., Vega V.B., Thoreau H., Se Thoe S.Y., RA Chia J.-M., Ng P., Chiu K.P., Lim L., Zhang T., Chan K.P., Oon L.E.L., RA Ng M.L., Leo S.Y., Ng L.F.P., Ren E.C., Stanton L.W., Long P.M., Liu E.T.; RL Lancet 361:1832-1832(2003). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate TW1; RA Yeh S.-H., Kao C.-L., Tsai C.-Y., Liu C.-J., Chen D.-S., Chen P.-J.; RT "The complete genome of SARS coronavirus clone TW1."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate FRA; RA Eickmann M., Becker S., Klenk H.-D., Doerr H.W., Stadler K., Censini S., RA Guidotti S., Masignani V., Scarselli M., Mora M., Donati C., Han J., RA Song H.C., Abrignani S., Covacci A., Rappuoli R.; RT "SARS virus is a close relative of type II coronaviruses."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate Frankfurt 1; RX PubMed=12917450; DOI=10.1099/vir.0.19424-0; RA Thiel V., Ivanov K.A., Putics A., Hertzig T., Schelle B., Bayer S., RA Weissbrich B., Snijder E.J., Rabenau H., Doerr H.W., Gorbalenya A.E., RA Ziebuhr J.; RT "Mechanisms and enzymes involved in SARS coronavirus genome expression."; RL J. Gen. Virol. 84:2305-2315(2003). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate TWC; RA Yang J.-Y., Lin J.-H., Chiu S.-C., Wang S.-F., Lee S.C., Lin Y.-C., RA Hsu C.-K., Chen H.-Y., Chang J.G., Chen P.-J., Su I.-J.; RT "Genomic sequence of SARS isolate from the first fatal case in Taiwan."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Isolate ZJ01; RA Cong L.-M., Ding G.-Q., Lu Y.-Y., Weng J.-Q., Yan J.-Y., Hu N.-P., RA Wo J.-E., Chen S.-Y., Zhang Y.-J., Mei L.-L., Wang Z.-G., Yao J., RA Zhu H.-P., Lu Q.-Y., Li M.-H., Gong L.-M., Shi W., Li L.-J.; RT "SARS coronavirus ZJ01 isolate spike glycoprotein."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate Shanghai LY; RA Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate Taiwan TC1, Isolate Taiwan TC2, and Isolate Taiwan TC3; RA Chang J.-G.C., Lin T.-H., Chen C.-M., Lin C.-S., Chan W.-L., Shih M.-C.; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate TWH, Isolate TWJ, Isolate TWK, Isolate TWS, and Isolate TWY; RA Shu H.Y., Wu K.M., Tsai S.F.; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate HSR 1; RA Canducci F., Clementi M., Poli G., Vicenzi E.; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [18] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate TWC2, and Isolate TWC3; RA Yang J.-Y., Lin J.-H., Chiu S.-C., Wang S.-F., Lee H.-C., Lin Y.-C., RA Hsu C.-K., Chen H.-Y., Chen P.-J., Su I.-J.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [19] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate AS; RA Balotta C., Corvasce S., Violin M., Galli M., Moroni M., Vigevani G.M., RA Ruan Y.J., Salemi M.; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [20] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate Shanghai QXC1; RA Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.; RT "Analysis of SARS coronavirus genome in Shanghai isolates."; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [21] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate GD03; 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). RN [22] RP INTERACTION WITH HUMAN ACE2, AND CHARACTERIZATION OF CELLULAR RECEPTOR. RX PubMed=14647384; DOI=10.1038/nature02145; RA Li W., Moore M.J., Vasilieva N., Sui J., Wong S.-K., Berne M.A., RA Somasundaran M., Sullivan J.L., Luzuriaga K., Greenough T.C., Choe H., RA Farzan M.; RT "Angiotensin-converting enzyme 2 is a functional receptor for the SARS RT coronavirus."; RL Nature 426:450-454(2003). RN [23] RP FUNCTION, INTERACTION WITH HUMAN ACE2, AND MUTAGENESIS OF CYS-323; CYS-348; RP GLU-452; ASP-454; ASP-463; CYS-467; CYS-474 AND ASP-480. RX PubMed=14670965; DOI=10.1074/jbc.c300520200; RA Wong S.K., Li W., Moore M.J., Choe H., Farzan M.; RT "A 193-amino acid fragment of the SARS coronavirus S protein efficiently RT binds angiotensin-converting enzyme 2."; RL J. Biol. Chem. 279:3197-3201(2004). RN [24] RP CHARACTERIZATION OF HEPTAD REPEAT REGIONS. RX PubMed=15518555; DOI=10.1021/bi049101q; RA Xu Y., Zhu J., Liu Y., Lou Z., Yuan F., Liu Y., Cole D.K., Ni L., Su N., RA Qin L., Li X., Bai Z., Bell J.I., Pang H., Tien P., Gao G.F., Rao Z.; RT "Characterization of the heptad repeat regions, HR1 and HR2, and design of RT a fusion core structure model of the spike protein from severe acute RT respiratory syndrome (SARS) coronavirus."; RL Biochemistry 43:14064-14071(2004). RN [25] RP CLEAVAGE. RX PubMed=15450134; DOI=10.1038/sj.cr.7290240; RA Wu X.D., Shang B., Yang R.F., Yu H., Ma Z.H., Shen X., Ji Y.Y., Lin Y., RA Wu Y.D., Lin G.M., Tian L., Gan X.Q., Yang S., Jiang W.H., Dai E.H., RA Wang X.Y., Jiang H.L., Xie Y.H., Zhu X.L., Pei G., Li L., Wu J.R., Sun B.; RT "The spike protein of severe acute respiratory syndrome (SARS) is cleaved RT in virus infected Vero-E6 cells."; RL Cell Res. 14:400-406(2004). RN [26] RP FUNCTION, AND INTERACTION WITH HUMAN CLEC4M/DC-SIGNR. RX PubMed=15496474; DOI=10.1073/pnas.0403812101; RA Jeffers S.A., Tusell S.M., Gillim-Ross L., Hemmila E.M., Achenbach J.E., RA Babcock G.J., Thomas W.D. Jr., Thackray L.B., Young M.D., Mason R.J., RA Ambrosino D.M., Wentworth D.E., Demartini J.C., Holmes K.V.; RT "CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome RT coronavirus."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15748-15753(2004). RN [27] RP HOMOTRIMERIZATION. RX PubMed=15313178; DOI=10.1016/j.bbrc.2004.07.084; RA Xiao X., Feng Y., Chakraborti S., Dimitrov D.S.; RT "Oligomerization of the SARS-CoV S glycoprotein: dimerization of the N- RT terminus and trimerization of the ectodomain."; RL Biochem. Biophys. Res. Commun. 322:93-99(2004). RN [28] RP CHARACTERIZATION OF FUSION PEPTIDE. RX PubMed=15890958; DOI=10.1128/jvi.79.11.7195-7206.2005; RA Sainz B. Jr., Rausch J.M., Gallaher W.R., Garry R.F., Wimley W.C.; RT "Identification and characterization of the putative fusion peptide of the RT severe acute respiratory syndrome-associated coronavirus spike protein."; RL J. Virol. 79:7195-7206(2005). RN [29] RP SUBCELLULAR LOCATION. RX PubMed=15831954; DOI=10.1099/vir.0.80671-0; RA Nal B., Chan C., Kien F., Siu L., Tse J., Chu K., Kam J., Staropoli I., RA Crescenzo-Chaigne B., Escriou N., van der Werf S., Yuen K.Y., Altmeyer R.; RT "Differential maturation and subcellular localization of severe acute RT respiratory syndrome coronavirus surface proteins S, M and E."; RL J. Gen. Virol. 86:1423-1434(2005). RN [30] RP CHARACTERIZATION OF VARIANTS ARG-344; SER-360; LYS-479 AND SER-487. RX PubMed=15791205; DOI=10.1038/sj.emboj.7600640; RA Li W., Zhang C., Sui J., Kuhn J.H., Moore M.J., Luo S., Wong S.-K., RA Huang I.-C., Xu K., Vasilieva N., Murakami A., He Y., Marasco W.A., RA Guan Y., Choe H., Farzan M.; RT "Receptor and viral determinants of SARS-coronavirus adaptation to human RT ACE2."; RL EMBO J. 24:1634-1643(2005). RN [31] RP PROTEOLYSIS BY HUMAN CTSL. RX PubMed=16081529; DOI=10.1073/pnas.0505577102; RA Simmons G., Gosalia D.N., Rennekamp A.J., Reeves J.D., Diamond S.L., RA Bates P.; RT "Inhibitors of cathepsin L prevent severe acute respiratory syndrome RT coronavirus entry."; RL Proc. Natl. Acad. Sci. U.S.A. 102:11876-11881(2005). RN [32] RP INTERACTION WITH ACCESSORY PROTEIN 3A. RX PubMed=15194747; DOI=10.1128/jvi.78.13.6723-6734.2004; RA Tan Y.-J., Teng E., Shen S., Tan T.H.P., Goh P.-Y., Fielding B.C., RA Ooi E.-E., Tan H.-C., Lim S.G., Hong W.; RT "A novel severe acute respiratory syndrome coronavirus protein, U274, is RT transported to the cell surface and undergoes endocytosis."; RL J. Virol. 78:6723-6734(2004). RN [33] RP INTERACTION WITH ACCESSORY PROTEIN 7A. RX PubMed=16840309; DOI=10.1128/jvi.00414-06; RA Huang C., Ito N., Tseng C.-T.K., Makino S.; RT "Severe acute respiratory syndrome coronavirus 7a accessory protein is a RT viral structural protein."; RL J. Virol. 80:7287-7294(2006). RN [34] RP MUTAGENESIS OF ARG-667 AND LYS-672. RX PubMed=16519916; DOI=10.1016/j.virol.2006.02.003; RA Follis K.E., York J., Nunberg J.H.; RT "Furin cleavage of the SARS coronavirus spike glycoprotein enhances cell- RT cell fusion but does not affect virion entry."; RL Virology 350:358-369(2006). RN [35] RP PALMITOYLATION. RX PubMed=17134730; DOI=10.1016/j.virol.2006.10.034; RA Petit C.M., Chouljenko V.N., Iyer A., Colgrove R., Farzan M., Knipe D.M., RA Kousoulas K.G.; RT "Palmitoylation of the cysteine-rich endodomain of the SARS-coronavirus RT spike glycoprotein is important for spike-mediated cell fusion."; RL Virology 360:264-274(2007). RN [36] RP ENDOPLASMIC RETICULUM RETENTION MOTIF, AND MUTAGENESIS OF LYS-1251 AND RP HIS-1253. RX PubMed=17166901; DOI=10.1128/jvi.02146-06; RA McBride C.E., Li J., Machamer C.E.; RT "The cytoplasmic tail of the severe acute respiratory syndrome coronavirus RT spike protein contains a novel endoplasmic reticulum retrieval signal that RT binds COPI and promotes interaction with membrane protein."; RL J. Virol. 81:2418-2428(2007). RN [37] RP CLEAVAGE, AND FUNCTION. RX PubMed=19321428; DOI=10.1073/pnas.0809524106; RA Belouzard S., Chu V.C., Whittaker G.R.; RT "Activation of the SARS coronavirus spike protein via sequential RT proteolytic cleavage at two distinct sites."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5871-5876(2009). RN [38] RP SUBCELLULAR LOCATION. RX PubMed=20861307; DOI=10.1091/mbc.e10-04-0338; RA Teoh K.T., Siu Y.L., Chan W.L., Schlueter M.A., Liu C.J., Peiris J.S., RA Bruzzone R., Margolis B., Nal B.; RT "The SARS coronavirus E protein interacts with PALS1 and alters tight RT junction formation and epithelial morphogenesis."; RL Mol. Biol. Cell 21:3838-3852(2010). RN [39] RP CHARACTERIZATION OF FUSION PEPTIDE. RX PubMed=29056462; DOI=10.1016/j.jmb.2017.10.017; RA Lai A.L., Millet J.K., Daniel S., Freed J.H., Whittaker G.R.; RT "The SARS-CoV fusion peptide forms an extended bipartite fusion platform RT that perturbs membrane order in a calcium-dependent manner."; RL J. Mol. Biol. 429:3875-3892(2017). RN [40] RP FUNCTION. RX PubMed=31199522; DOI=10.1002/jmv.25518; RA Wang S.M., Huang K.J., Wang C.T.; RT "Severe acute respiratory syndrome coronavirus spike protein counteracts RT BST2-mediated restriction of virus-like particle release."; RL J. Med. Virol. 91:1743-1750(2019). RN [41] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 900-948. RX PubMed=15345712; DOI=10.1074/jbc.m408782200; RA Xu Y., Lou Z., Liu Y., Pang H., Tien P., Gao G.F., Rao Z.; RT "Crystal structure of severe acute respiratory syndrome coronavirus spike RT protein fusion core."; RL J. Biol. Chem. 279:49414-49419(2004). RN [42] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 895-972 AND 1142-1180. RX PubMed=15604146; DOI=10.1073/pnas.0406128102; RA Supekar V.M., Bruckmann C., Ingallinella P., Bianchi E., Pessi A., RA Carfi A.; RT "Structure of a proteolytically resistant core from the severe acute RT respiratory syndrome coronavirus S2 fusion protein."; RL Proc. Natl. Acad. Sci. U.S.A. 101:17958-17963(2004). RN [43] RP 3D-STRUCTURE MODELING OF 17-680. RX PubMed=14511651; DOI=10.1016/j.bbrc.2003.08.122; RA Spiga O., Bernini A., Ciutti A., Chiellini S., Menciassi N., Finetti F., RA Causarono V., Anselmi F., Prischi F., Niccolai N.; RT "Molecular modelling of S1 and S2 subunits of SARS coronavirus spike RT glycoprotein."; RL Biochem. Biophys. Res. Commun. 310:78-83(2003). RN [44] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 323-502 IN COMPLEX WITH HUMAN RP ACE2. RX PubMed=16166518; DOI=10.1126/science.1116480; RA Li F., Li W., Farzan M., Harrison S.C.; RT "Structure of SARS coronavirus spike receptor-binding domain complexed with RT receptor."; RL Science 309:1864-1868(2005). RN [45] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1150-1193. RX PubMed=16698550; DOI=10.1016/j.str.2006.03.007; RA Deng Y., Liu J., Zheng Q., Yong W., Lu M.; RT "Structures and polymorphic interactions of two heptad-repeat regions of RT the SARS virus S2 protein."; RL Structure 14:889-899(2006). CC -!- FUNCTION: [Spike glycoprotein]: May down-regulate host tetherin (BST2) CC by lysosomal degradation, thereby counteracting its antiviral activity. CC {ECO:0000269|PubMed:31199522}. CC -!- FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane CC by interacting with host receptor, initiating the infection (By CC similarity). Binding to human ACE2 and CLEC4M/DC-SIGNR receptors and CC internalization of the virus into the endosomes of the host cell CC induces conformational changes in the S glycoprotein. Proteolysis by CC cathepsin CTSL may unmask the fusion peptide of S2 and activate CC membrane fusion within endosomes. {ECO:0000255|HAMAP-Rule:MF_04099, CC ECO:0000269|PubMed:14670965, ECO:0000269|PubMed:15496474}. CC -!- FUNCTION: [Spike protein S2]: Mediates fusion of the virion and CC cellular membranes by acting as a class I viral fusion protein. Under CC the current model, the protein has at least three conformational CC states: pre-fusion native state, pre-hairpin intermediate state, and CC post-fusion hairpin state. During viral and target cell membrane CC fusion, the coiled coil regions (heptad repeats) assume a trimer-of- CC hairpins structure, positioning the fusion peptide in close proximity CC to the C-terminal region of the ectodomain. The formation of this CC structure appears to drive apposition and subsequent fusion of viral CC and target cell membranes. {ECO:0000255|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:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:19321428}. CC -!- SUBUNIT: Homotrimer; each monomer consists of a S1 and a S2 subunit. CC The resulting peplomers protrude from the virus surface as spikes (By CC similarity). Binds to human and palm civet ACE2 and human CLEC4M/DC- CC SIGNR. Interacts with the accessory proteins 3a and 7a. CC {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:14647384, CC ECO:0000269|PubMed:14670965, ECO:0000269|PubMed:15194747, CC ECO:0000269|PubMed:15496474, ECO:0000269|PubMed:16166518, CC ECO:0000269|PubMed:16840309}. CC -!- INTERACTION: CC P59594; P59635: 7a; NbExp=3; IntAct=EBI-15582614, EBI-25492879; CC P59594; P59594: S; NbExp=22; IntAct=EBI-15582614, EBI-15582614; CC P59594; Q56NL1: ACE2; Xeno; NbExp=4; IntAct=EBI-15582614, EBI-25498790; CC P59594; Q5EGZ1: Ace2; Xeno; NbExp=2; IntAct=EBI-15582614, EBI-25503774; CC P59594; Q9BYF1: ACE2; Xeno; NbExp=57; IntAct=EBI-15582614, EBI-7730807; CC P59594; P07711: CTSL; Xeno; NbExp=2; IntAct=EBI-15582614, EBI-1220160; CC P59594; O00303: EIF3F; Xeno; NbExp=5; IntAct=EBI-15582614, EBI-711990; CC PRO_0000037209; Q9BYF1: ACE2; Xeno; NbExp=3; IntAct=EBI-25475261, EBI-7730807; CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04099, CC ECO:0000269|PubMed:15831954}; Single-pass type I membrane protein CC {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:15831954}. Host CC endoplasmic reticulum-Golgi intermediate compartment membrane CC {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:20861307}; Single- CC pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099, CC ECO:0000269|PubMed:15831954}. Host cell membrane {ECO:0000255|HAMAP- CC Rule:MF_04099, ECO:0000269|PubMed:15831954}; Single-pass type I CC membrane protein {ECO:0000255|HAMAP-Rule:MF_04099, CC ECO:0000269|PubMed:15831954}. Note=Accumulates in the endoplasmic CC reticulum-Golgi intermediate compartment, where it participates in CC virus particle assembly. Colocalizes with S in the host endoplasmic CC reticulum-Golgi intermediate compartment (PubMed:20861307). Some S CC oligomers are transported to the host plasma membrane, where they may CC mediate cell-cell fusion. {ECO:0000255|HAMAP-Rule:MF_04099, CC ECO:0000269|PubMed:20861307}. CC -!- DOMAIN: The KxHxx motif seems to function as an ER retrieval and binds CC COPI in vitro. CC -!- DOMAIN: Fusion peptide 1 (FP1) and fusion peptide 2 (FP2) function CC cooperatively and have a membrane-ordering effect on lipid headgroups CC and shallow hydrophobic regions of target bilayers. They are considered CC as two domains of an extended, bipartite FP. The membrane-ordering CC activity is calcium-dependent and also dependent on correct folding, CC which is maintained by an internal disulfide bond in FP2. CC {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:29056462}. CC -!- PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike CC glycoprotein is digested by cathepsin CTSL within endosomes. CC {ECO:0000269|PubMed:17134730}. 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:0000255|HAMAP-Rule:MF_04099}. CC -!- PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike CC glycoprotein is digested within host endosomes. {ECO:0000255|HAMAP- CC Rule:MF_04099}. CC -!- MISCELLANEOUS: Tor2 is the prototype of the virus isolated during the CC severe SARS outbreak in 2002-2003. GD03 has been isolated from the CC second mild SARS outbreak in winter 2003-2004. SZ3 has been isolated CC from palm civet, the presumed animal reservoir. The spike proteins from CC those three isolates display a strong affinity for palm civet ACE2 CC receptor, whereas only the Tor2 spike protein efficiently binds human CC ACE2. This may explain the high pathogenicity of Tor2 virus, whose CC spike is highly adapted to the human host. Therefore, the lack of CC severity of disease during the 2003-2004 outbreak could be due to the CC incomplete adaptation of GD03 virus to bind human ACE2. Mutation Asn- CC 479 and Thr-487 in palm civet coronavirus seems necessary and CC sufficient for the virus to acquire the ability to efficiently infect CC humans. CC -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family. CC {ECO:0000255|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; AY278741; AAP13441.1; -; Genomic_RNA. DR EMBL; AY274119; AAP41037.1; -; Genomic_RNA. DR EMBL; AY282752; AAP30713.1; -; Genomic_RNA. DR EMBL; AY278554; AAP13567.1; -; Genomic_RNA. DR EMBL; AY278491; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR EMBL; AY304495; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR EMBL; AY304492; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR EMBL; AY278487; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR EMBL; AY278488; AAP30030.1; -; Genomic_RNA. DR EMBL; AY278490; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR EMBL; AY279354; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR EMBL; AY278489; AAP51227.1; -; Genomic_RNA. DR EMBL; AY283794; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR EMBL; AY283795; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR EMBL; AY283796; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR EMBL; AY283797; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR EMBL; AY283798; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR EMBL; AY291451; AAP37017.1; -; Genomic_RNA. DR EMBL; AY310120; AAP50485.1; -; Genomic_RNA. DR EMBL; AY291315; AAP33697.1; -; Genomic_RNA. DR EMBL; AY304486; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR EMBL; AY321118; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR EMBL; AY323976; AAP73417.1; -; mRNA. DR EMBL; AH012999; AAP82968.1; -; Genomic_RNA. DR EMBL; AY338174; AAQ01597.1; -; Genomic_RNA. DR EMBL; AY338175; AAQ01609.1; -; Genomic_RNA. DR EMBL; AY348314; AAP97882.1; -; Genomic_RNA. DR EMBL; AP006557; BAC81348.1; -; Genomic_RNA. DR EMBL; AP006558; BAC81362.1; -; Genomic_RNA. DR EMBL; AP006559; BAC81376.1; -; Genomic_RNA. DR EMBL; AP006560; BAC81390.1; -; Genomic_RNA. DR EMBL; AP006561; BAC81404.1; -; Genomic_RNA. DR EMBL; AY323977; AAP72986.1; -; Genomic_RNA. DR EMBL; AY362698; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR EMBL; AY362699; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR EMBL; AY427439; AAQ94060.1; -; Genomic_RNA. DR EMBL; AY463059; AAR86788.1; -; Genomic_RNA. DR EMBL; AY525636; AAS10463.1; -; Genomic_RNA. DR PDB; 1WNC; X-ray; 2.80 A; A/B/C/D/E/F=900-948, A/B/C/D/E/F=1144-1185. DR PDB; 1WYY; X-ray; 2.20 A; A/B=885-981, A/B=1145-1189. DR PDB; 1ZV7; X-ray; 1.70 A; A/B=1150-1193. DR PDB; 1ZV8; X-ray; 1.94 A; A/C/E/G/I/K=901-950, B/D/F/H/J/L=1150-1185. DR PDB; 1ZVA; X-ray; 1.50 A; A=926-962. DR PDB; 1ZVB; X-ray; 1.70 A; A/B/C=940-973. DR PDB; 2AJF; X-ray; 2.90 A; E/F=323-502. DR PDB; 2BEQ; X-ray; 1.60 A; A/B/C=914-949, D/E/F=1148-1193. DR PDB; 2BEZ; X-ray; 1.60 A; C=896-972, F=1142-1183. DR PDB; 2DD8; X-ray; 2.30 A; S=317-518. DR PDB; 2FXP; NMR; -; A/B/C=1141-1193. DR PDB; 2GHV; X-ray; 2.20 A; C/E=317-510. DR PDB; 2GHW; X-ray; 2.30 A; A/C=317-510. DR PDB; 2RUM; NMR; -; A=770-788. DR PDB; 2RUN; NMR; -; A=1185-1202. DR PDB; 2RUO; NMR; -; A=873-888. DR PDB; 3BGF; X-ray; 3.00 A; A/S=318-510. DR PDB; 3D0G; X-ray; 2.80 A; E/F=324-502. DR PDB; 3D0H; X-ray; 3.10 A; E/F=324-502. DR PDB; 3D0I; X-ray; 2.90 A; E/F=324-502. DR PDB; 3SCI; X-ray; 2.90 A; E/F=306-527. DR PDB; 3SCJ; X-ray; 3.00 A; E/F=323-502. DR PDB; 3SCK; X-ray; 3.00 A; E/F=324-502. DR PDB; 3SCL; X-ray; 3.00 A; E/F=324-502. DR PDB; 5WRG; EM; 4.30 A; A/B/C=1-1196. DR PDB; 5X4S; X-ray; 2.20 A; A=14-292. DR PDB; 5X58; EM; 3.20 A; A/B/C=14-1193. DR PDB; 5X5B; EM; 3.70 A; A/B/C=14-1193. DR PDB; 5XJK; NMR; -; A=758-821. DR PDB; 5XLR; EM; 3.80 A; A/B/C=1-1196. DR PDB; 5ZVM; X-ray; 3.30 A; A/B/C=892-970. DR PDB; 6ACC; EM; 3.60 A; A/B/C=1-1196. DR PDB; 6ACD; EM; 3.90 A; A/B/C=1-1196. DR PDB; 6ACG; EM; 5.40 A; A/B/C=1-1196. DR PDB; 6ACJ; EM; 4.20 A; A/B/C=1-1196. DR PDB; 6ACK; EM; 4.50 A; A/B/C=1-1196. DR PDB; 6CRV; EM; 3.20 A; A/B/C=14-1190. DR PDB; 6CRW; EM; 3.90 A; A/B/C=14-1190. DR PDB; 6CRX; EM; 3.90 A; A/B/C=14-1190. DR PDB; 6CRZ; EM; 3.30 A; A/B/C=14-1190. DR PDB; 6CS0; EM; 3.80 A; A/B/C=14-1190. DR PDB; 6CS1; EM; 4.60 A; A/B/C=14-1190. DR PDB; 6CS2; EM; 4.40 A; A/B/C=14-1190. DR PDB; 6M3W; EM; 3.90 A; A/B/C=688-1178. DR PDB; 6NB6; EM; 4.20 A; A/B/C=14-1193. DR PDB; 6NB7; EM; 4.50 A; A/B/C=14-1193. DR PDB; 6VW1; X-ray; 2.68 A; E/F=306-441, E/F=505-521. DR PDB; 6WAQ; X-ray; 2.20 A; B/D=320-502. DR PDB; 7AKJ; EM; 3.80 A; A/B/C=18-1160. DR PDB; 7FC6; X-ray; 2.65 A; S=321-512. DR PDB; 7JN5; X-ray; 2.71 A; F=306-527. DR PDB; 7RKS; X-ray; 2.70 A; R/S=321-510. DR PDB; 7SG4; EM; 3.43 A; A/B/C=1-1190. DR PDB; 7WR9; EM; 3.24 A; F=323-502. DR PDB; 7WSF; EM; 2.87 A; B=321-502. DR PDB; 7WSG; EM; 3.03 A; B=321-502. DR PDB; 7X2J; X-ray; 2.40 A; S=306-516. DR PDB; 7X7V; EM; 3.83 A; E=320-508. DR PDB; 7Y3N; X-ray; 2.97 A; A/B/E=306-527. DR PDB; 7ZH1; EM; 2.48 A; A/B/C=14-1193. DR PDB; 7ZH2; EM; 2.71 A; A/B/C=14-1193. DR PDB; 7ZH5; EM; 3.30 A; A/B/C=14-1193. DR PDB; 8H0X; EM; 2.57 A; A/B/C=15-1193. DR PDB; 8H0Y; EM; 2.85 A; A/B/C=15-1193. DR PDB; 8H0Z; EM; 2.99 A; A/B/C=15-1193. DR PDB; 8H10; EM; 2.99 A; A/B/C=15-1193. DR PDB; 8H11; EM; 2.72 A; A/B/C=15-1193. DR PDB; 8H12; EM; 3.45 A; A/B/C=15-1193. DR PDB; 8H13; EM; 4.05 A; A/B/C=15-1193. DR PDB; 8H14; EM; 3.39 A; A/B/C=15-1193. DR PDB; 8H15; EM; 3.14 A; A/B/C=15-1193. DR PDB; 8H16; EM; 3.36 A; A/B/C=15-1193. DR PDB; 8KDM; EM; 2.87 A; A/B/C=1-1190. DR PDB; 8KDS; EM; 3.05 A; A/B/C=1-1190. DR PDB; 8KDT; EM; 3.04 A; A=1-1190. DR PDB; 8KEK; EM; 3.54 A; A=1-1190. DR PDB; 8SPH; X-ray; 2.71 A; E/F=306-521. DR PDB; 8SPI; X-ray; 3.06 A; E/F=306-521. DR PDB; 8TC5; EM; 2.11 A; A/B/C=16-1121. DR PDB; 8WOZ; EM; 3.25 A; B=306-527. DR PDB; 8XZB; EM; 3.12 A; C=306-527. DR PDBsum; 1WNC; -. DR PDBsum; 1WYY; -. DR PDBsum; 1ZV7; -. DR PDBsum; 1ZV8; -. DR PDBsum; 1ZVA; -. DR PDBsum; 1ZVB; -. DR PDBsum; 2AJF; -. DR PDBsum; 2BEQ; -. DR PDBsum; 2BEZ; -. DR PDBsum; 2DD8; -. DR PDBsum; 2FXP; -. DR PDBsum; 2GHV; -. DR PDBsum; 2GHW; -. DR PDBsum; 2RUM; -. DR PDBsum; 2RUN; -. DR PDBsum; 2RUO; -. DR PDBsum; 3BGF; -. DR PDBsum; 3D0G; -. DR PDBsum; 3D0H; -. DR PDBsum; 3D0I; -. DR PDBsum; 3SCI; -. DR PDBsum; 3SCJ; -. DR PDBsum; 3SCK; -. DR PDBsum; 3SCL; -. DR PDBsum; 5WRG; -. DR PDBsum; 5X4S; -. DR PDBsum; 5X58; -. DR PDBsum; 5X5B; -. DR PDBsum; 5XJK; -. DR PDBsum; 5XLR; -. DR PDBsum; 5ZVM; -. DR PDBsum; 6ACC; -. DR PDBsum; 6ACD; -. DR PDBsum; 6ACG; -. DR PDBsum; 6ACJ; -. DR PDBsum; 6ACK; -. DR PDBsum; 6CRV; -. DR PDBsum; 6CRW; -. DR PDBsum; 6CRX; -. DR PDBsum; 6CRZ; -. DR PDBsum; 6CS0; -. DR PDBsum; 6CS1; -. DR PDBsum; 6CS2; -. DR PDBsum; 6M3W; -. DR PDBsum; 6NB6; -. DR PDBsum; 6NB7; -. DR PDBsum; 6VW1; -. DR PDBsum; 6WAQ; -. DR PDBsum; 7AKJ; -. DR PDBsum; 7FC6; -. DR PDBsum; 7JN5; -. DR PDBsum; 7RKS; -. DR PDBsum; 7SG4; -. DR PDBsum; 7WR9; -. DR PDBsum; 7WSF; -. DR PDBsum; 7WSG; -. DR PDBsum; 7X2J; -. DR PDBsum; 7X7V; -. DR PDBsum; 7Y3N; -. DR PDBsum; 7ZH1; -. DR PDBsum; 7ZH2; -. DR PDBsum; 7ZH5; -. DR PDBsum; 8H0X; -. DR PDBsum; 8H0Y; -. DR PDBsum; 8H0Z; -. DR PDBsum; 8H10; -. DR PDBsum; 8H11; -. DR PDBsum; 8H12; -. DR PDBsum; 8H13; -. DR PDBsum; 8H14; -. DR PDBsum; 8H15; -. DR PDBsum; 8H16; -. DR PDBsum; 8KDM; -. DR PDBsum; 8KDS; -. DR PDBsum; 8KDT; -. DR PDBsum; 8KEK; -. DR PDBsum; 8SPH; -. DR PDBsum; 8SPI; -. DR PDBsum; 8TC5; -. DR PDBsum; 8WOZ; -. DR PDBsum; 8XZB; -. DR BMRB; P59594; -. DR EMDB; EMD-0403; -. DR EMDB; EMD-0404; -. DR EMDB; EMD-11813; -. DR EMDB; EMD-11953; -. DR EMDB; EMD-11954; -. DR EMDB; EMD-13917; -. DR EMDB; EMD-13918; -. DR EMDB; EMD-13920; -. DR EMDB; EMD-14810; -. DR EMDB; EMD-14811; -. DR EMDB; EMD-22861; -. DR EMDB; EMD-22862; -. DR EMDB; EMD-22863; -. DR EMDB; EMD-22864; -. DR EMDB; EMD-25105; -. DR EMDB; EMD-30072; -. DR EMDB; EMD-32719; -. DR EMDB; EMD-32756; -. DR EMDB; EMD-32757; -. DR EMDB; EMD-33049; -. DR EMDB; EMD-34417; -. DR EMDB; EMD-34418; -. DR EMDB; EMD-34419; -. DR EMDB; EMD-34420; -. DR EMDB; EMD-34421; -. DR EMDB; EMD-34422; -. DR EMDB; EMD-34423; -. DR EMDB; EMD-34424; -. DR EMDB; EMD-34425; -. DR EMDB; EMD-34426; -. DR EMDB; EMD-36892; -. DR EMDB; EMD-37139; -. DR EMDB; EMD-37144; -. DR EMDB; EMD-37145; -. DR EMDB; EMD-37161; -. DR EMDB; EMD-37703; -. DR EMDB; EMD-38792; -. DR EMDB; EMD-6703; -. DR EMDB; EMD-6705; -. DR EMDB; EMD-6732; -. DR EMDB; EMD-9588; -. DR EMDB; EMD-9589; -. DR EMDB; EMD-9591; -. DR EMDB; EMD-9593; -. DR EMDB; EMD-9594; -. DR SMR; P59594; -. DR BioGRID; 4383915; 241. DR ComplexPortal; CPX-5694; SARS-CoV cleaved Spike protein complex. DR ComplexPortal; CPX-7088; SARS-CoV uncleaved Spike protein complex. DR DIP; DIP-29105N; -. DR IntAct; P59594; 27. DR BindingDB; P59594; -. DR ChEMBL; CHEMBL4802007; -. DR DrugCentral; P59594; -. DR GlyConnect; 3006; 8 N-Linked glycans. DR GlyCosmos; P59594; 23 sites, No reported glycans. DR GlyGen; P59594; 24 sites, 8 N-linked glycans (13 sites). DR iPTMnet; P59594; -. DR SwissPalm; P59594; -. DR ABCD; P59594; 120 sequenced antibodies. DR DNASU; 1489668; -. DR Reactome; R-HSA-9678110; Attachment and Entry. DR Reactome; R-HSA-9679509; Virion Assembly and Release. DR Reactome; R-HSA-9683686; Maturation of spike protein. DR Reactome; R-HSA-9683701; Translation of Structural Proteins. DR Reactome; R-HSA-9692916; SARS-CoV-1 activates/modulates innate immune responses. DR SABIO-RK; P59594; -. DR SIGNOR; P59594; -. DR EvolutionaryTrace; P59594; -. DR Proteomes; UP000000354; Segment. DR Proteomes; UP000103670; Segment. DR Proteomes; UP000109640; Segment. DR Proteomes; UP000116947; Segment. DR Proteomes; UP000121636; Segment. DR Proteomes; UP000131569; Segment. DR Proteomes; UP000131955; Segment. DR Proteomes; UP000137377; Genome. DR Proteomes; UP000138690; Segment. DR Proteomes; UP000143093; Segment. DR Proteomes; UP000145651; Segment. DR Proteomes; UP000146108; Segment. DR Proteomes; UP000146181; Segment. DR Proteomes; UP000146296; Segment. DR Proteomes; UP000148194; Segment. DR Proteomes; UP000153467; Segment. DR Proteomes; UP000160648; Segment. DR Proteomes; UP000164441; Segment. DR Proteomes; UP000172416; Segment. DR Proteomes; UP000180358; Segment. 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:0016020; C:membrane; IEA:UniProtKB-UniRule. DR GO; GO:0019031; C:viral envelope; NAS:ComplexPortal. DR GO; GO:0055036; C:virion membrane; TAS:Reactome. DR GO; GO:0046789; F:host cell surface receptor binding; IPI:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. 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:0061025; P:membrane fusion; NAS:ComplexPortal. DR GO; GO:0046598; P:positive regulation of viral entry into host cell; EXP:ComplexPortal. DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:BHF-UCL. DR GO; GO:0039587; P:suppression by virus of host tetherin activity; IEA:UniProtKB-KW. DR GO; GO:0052170; P:symbiont-mediated suppression of host innate immune response; IEA:UniProtKB-KW. DR CDD; cd21624; SARS-CoV-like_Spike_S1_NTD; 1. DR CDD; cd22378; SARS-CoV-like_Spike_SD1-2_S1-S2_S2; 1. DR CDD; cd21481; SARS-CoV_Spike_S1_RBD; 1. DR DisProt; DP02879; -. DR FunFam; 1.20.5.300:FF:000003; Spike glycoprotein; 1. DR FunFam; 2.60.120.960:FF:000001; Spike glycoprotein; 1. DR Gene3D; 1.20.5.300; -; 1. DR Gene3D; 3.30.70.1840; -; 2. DR Gene3D; 1.20.5.790; Single helix bin; 1. DR Gene3D; 2.60.120.960; Spike glycoprotein, N-terminal domain; 1. DR HAMAP; MF_04099; BETA_CORONA_SPIKE; 1. DR InterPro; IPR032500; bCoV_S1_N. DR InterPro; IPR042578; BETA_CORONA_SPIKE. DR InterPro; IPR043473; S2_sf_CoV. DR InterPro; IPR043002; Spike_N_sf. DR InterPro; IPR044341; Spike_S1_N_SARS-CoV-like. DR InterPro; IPR018548; Spike_S1_RBD_bCoV. DR InterPro; IPR044370; Spike_S1_RBD_SARS-CoV. DR InterPro; IPR036326; Spike_S1_RBD_sf_bCoV. DR InterPro; IPR002552; Spike_S2_CoV. DR InterPro; IPR044873; Spike_S2_CoV_HR1. DR InterPro; IPR044874; Spike_S2_CoV_HR2. DR Pfam; PF16451; bCoV_S1_N; 1. DR Pfam; PF09408; bCoV_S1_RBD; 1. DR Pfam; PF01601; CoV_S2; 1. DR SUPFAM; SSF111474; Coronavirus S2 glycoprotein; 2. DR SUPFAM; SSF143587; SARS receptor-binding domain-like; 1. DR PROSITE; PS51921; BCOV_S1_CTD; 1. DR PROSITE; PS51922; BCOV_S1_NTD; 1. DR PROSITE; PS51923; COV_S2_HR1; 1. DR PROSITE; PS51924; COV_S2_HR2; 1. PE 1: Evidence at protein level; KW 3D-structure; Coiled coil; Disulfide bond; KW Fusion of virus membrane with host endosomal membrane; KW Fusion of virus membrane with host membrane; Glycoprotein; KW Host cell membrane; Host membrane; Host-virus interaction; KW Inhibition of host innate immune response by virus; KW Inhibition of host tetherin by virus; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Viral attachment to host cell; Viral envelope protein; Viral immunoevasion; KW Viral penetration into host cytoplasm; Virion; Virulence; KW Virus entry into host cell. FT SIGNAL 1..13 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CHAIN 14..1255 FT /note="Spike glycoprotein" FT /id="PRO_0000037208" FT CHAIN 14..667 FT /note="Spike protein S1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT /id="PRO_0000037209" FT CHAIN 668..1255 FT /note="Spike protein S2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT /id="PRO_0000037210" FT CHAIN 798..1255 FT /note="Spike protein S2'" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT /id="PRO_0000444082" FT TOPO_DOM 14..1195 FT /note="Extracellular" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT TRANSMEM 1196..1216 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT TOPO_DOM 1217..1255 FT /note="Cytoplasmic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT DOMAIN 14..290 FT /note="BetaCoV S1-NTD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270" FT DOMAIN 321..513 FT /note="BetaCoV S1-CTD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269" FT REGION 306..527 FT /note="Receptor-binding domain (RBD)" FT /evidence="ECO:0000250|UniProtKB:P0DTC2" FT REGION 424..494 FT /note="Receptor-binding motif; binding to human ACE2" FT REGION 798..819 FT /note="Fusion peptide 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099, FT ECO:0000305|PubMed:29056462" FT REGION 817..837 FT /note="Fusion peptide 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099, FT ECO:0000305|PubMed:29056462" FT REGION 902..952 FT /note="Heptad repeat 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT REGION 1145..1184 FT /note="Heptad repeat 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT COILED 931..975 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT COILED 1157..1185 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT MOTIF 1251..1255 FT /note="KxHxx" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT SITE 667..668 FT /note="Cleavage" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099, FT ECO:0000269|PubMed:19321428" FT SITE 797..798 FT /note="Cleavage" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099, FT ECO:0000269|PubMed:19321428" FT CARBOHYD 29 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 65 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 73 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 109 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 118 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 119 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 158 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 227 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 269 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 318 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 330 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 357 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 589 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 602 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 691 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 699 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 783 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 1056 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 1080 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 1116 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 1140 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 1155 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT CARBOHYD 1176 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099" FT DISULFID 19..133 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270" FT DISULFID 128..159 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270" FT DISULFID 278..288 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270" FT DISULFID 323..348 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269" FT DISULFID 366..419 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269" FT DISULFID 378..511 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269" FT DISULFID 467..474 FT DISULFID 822..833 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099, FT ECO:0000305|PubMed:29056462" FT VARIANT 49 FT /note="S -> L (in strain: Isolate GZ50)" FT VARIANT 77 FT /note="G -> D (in strain: Isolate BJ01, Isolate BJ02, FT Isolate BJ03, Isolate GZ50, Isolate CUHK-W1, Isolate HKU- FT 36871, Isolate GD01, Isolate GD03 and Isolate SZ3)" FT VARIANT 78 FT /note="N -> D (in strain: Isolate GD03)" FT VARIANT 118 FT /note="N -> S (in strain: Isolate Shanghai LY)" FT VARIANT 139 FT /note="A -> V (in strain: Isolate GD03)" FT VARIANT 144 FT /note="M -> L (in strain: Isolate BJ03)" FT VARIANT 147 FT /note="Q -> R (in strain: Isolate GD03)" FT VARIANT 193 FT /note="F -> S (in strain: Isolate Shanghai LY)" FT VARIANT 227 FT /note="N -> K (in strain: Isolate SZ3)" FT VARIANT 239 FT /note="S -> L (in strain: Isolate GD01 and Isolate SZ3)" FT VARIANT 244 FT /note="I -> T (in strain: Isolate BJ01, Isolate BJ02, FT Isolate BJ03, Isolate BJ04, Isolate GZ50, Isolate CUHK-W1, FT Isolate HKU-36871, Isolate GD01, Isolate GD03 and Isolate FT SZ3)" FT VARIANT 261 FT /note="T -> K (in strain: Isolate SZ3)" FT VARIANT 311 FT /note="G -> R (in strain: Isolate GD01 and Isolate BJ02)" FT VARIANT 344 FT /note="K -> R (in strain: Isolate GD01, Isolate GD03 and FT Isolate SZ3; no effect on affinity with either human or FT palm civet ACE2)" FT /evidence="ECO:0000269|PubMed:15791205" FT VARIANT 360 FT /note="F -> S (in strain: Isolate GD03 and Isolate SZ3; no FT effect on affinity with either human or palm civet ACE2)" FT /evidence="ECO:0000269|PubMed:15791205" FT VARIANT 426 FT /note="R -> G (in strain: Isolate Shanghai LY)" FT VARIANT 437 FT /note="N -> D (in strain: Isolate Shanghai LY)" FT VARIANT 472 FT /note="L -> P (in strain: Isolate GD03)" FT VARIANT 479 FT /note="N -> K (in strain: Isolate SZ3; 20fold decrease of FT affinity with human ACE2; no effect on affinity with palm FT civet ACE2)" FT /evidence="ECO:0000269|PubMed:15791205" FT VARIANT 480 FT /note="D -> G (in strain: Isolate GD03)" FT VARIANT 487 FT /note="T -> S (in strain: Isolate GD03 and Isolate SZ3; FT 20fold decrease of affinity with human ACE2; decrease of FT affinity with palm civet ACE2)" FT /evidence="ECO:0000269|PubMed:15791205" FT VARIANT 501 FT /note="F -> Y (in strain: Isolate GD01)" FT VARIANT 577 FT /note="S -> A (in strain: Isolate Tor2 and Isolate Shanghai FT QXC1)" FT VARIANT 605 FT /note="D -> N (in strain: Isolate Shanghai QXC1)" FT VARIANT 607 FT /note="S -> P (in strain: Isolate SZ3)" FT VARIANT 608 FT /note="T -> A (in strain: Isolate Shanghai QXC1)" FT VARIANT 609 FT /note="A -> L (in strain: Isolate GD03)" FT VARIANT 613 FT /note="D -> E (in strain: Isolate GD03)" FT VARIANT 665 FT /note="L -> S (in strain: Isolate GD03 and Isolate SZ3)" FT VARIANT 701 FT /note="S -> L (in strain: Isolate SZ3)" FT VARIANT 743 FT /note="T -> A (in strain: Isolate SZ3)" FT VARIANT 743 FT /note="T -> R (in strain: Isolate GD03)" FT VARIANT 754 FT /note="A -> V (in strain: Isolate SZ3)" FT VARIANT 765 FT /note="A -> V (in strain: Isolate GD03)" FT VARIANT 778 FT /note="Y -> D (in strain: Isolate GD01, Isolate GZ50, FT Isolate GD03 and Isolate SZ3)" FT VARIANT 794 FT /note="P -> S (in strain: Isolate GD01)" FT VARIANT 804 FT /note="L -> P (in strain: Isolate Shanghai LY)" FT VARIANT 860..861 FT /note="VS -> LR (in strain: Isolate BJ03)" FT VARIANT 894 FT /note="T -> A (in strain: Isolate SZ3)" FT VARIANT 999 FT /note="E -> G (in strain: Isolate Shanghai LY)" FT VARIANT 1001 FT /note="R -> M (in strain: Isolate BJ04)" FT VARIANT 1132 FT /note="E -> G (in strain: Isolate Shanghai QXC1)" FT VARIANT 1148 FT /note="L -> F (in strain: Isolate Frankfurt 1 and Isolate FT FRA)" FT VARIANT 1163 FT /note="K -> E (in strain: Isolate GD03 and Isolate SZ3)" FT MUTAGEN 323 FT /note="C->A: No effect on human ACE2 binding in vitro." FT /evidence="ECO:0000269|PubMed:14670965" FT MUTAGEN 348 FT /note="C->A: Complete loss of human ACE2 binding in vitro." FT /evidence="ECO:0000269|PubMed:14670965" FT MUTAGEN 452 FT /note="E->A: 90% loss of human ACE2 binding in vitro." FT /evidence="ECO:0000269|PubMed:14670965" FT MUTAGEN 454 FT /note="D->A: Complete loss of human ACE2 binding in vitro." FT /evidence="ECO:0000269|PubMed:14670965" FT MUTAGEN 463 FT /note="D->A: Partial loss of human ACE2 binding in vitro." FT /evidence="ECO:0000269|PubMed:14670965" FT MUTAGEN 467 FT /note="C->A: Complete loss of human ACE2 binding in vitro." FT /evidence="ECO:0000269|PubMed:14670965" FT MUTAGEN 474 FT /note="C->A: Complete loss of human ACE2 binding in vitro." FT /evidence="ECO:0000269|PubMed:14670965" FT MUTAGEN 480 FT /note="D->A: No effect on human ACE2 binding in vitro." FT /evidence="ECO:0000269|PubMed:14670965" FT MUTAGEN 667 FT /note="R->S: 40% loss of cell-cell fusion." FT /evidence="ECO:0000269|PubMed:16519916" FT MUTAGEN 672 FT /note="K->S: No effect on cell-cell fusion." FT /evidence="ECO:0000269|PubMed:16519916" FT MUTAGEN 797 FT /note="R->N: Complete loss of trypsin-induced membrane FT fusion." FT /evidence="ECO:0000269|PubMed:19321428" FT MUTAGEN 1251 FT /note="K->A: Decrease in Golgi localization, and complete FT loss of COPI binding; when associated with A-1253." FT /evidence="ECO:0000269|PubMed:17166901" FT MUTAGEN 1253 FT /note="H->A: Decrease in Golgi localization, and complete FT loss of COPI binding; when associated with A-1251." FT /evidence="ECO:0000269|PubMed:17166901" FT STRAND 31..34 FT /evidence="ECO:0007829|PDB:5X4S" FT STRAND 37..41 FT /evidence="ECO:0007829|PDB:5X58" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 50..59 FT /evidence="ECO:0007829|PDB:5X4S" FT STRAND 65..72 FT /evidence="ECO:0007829|PDB:5X4S" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:5X58" FT STRAND 87..95 FT /evidence="ECO:0007829|PDB:5X4S" FT STRAND 100..111 FT /evidence="ECO:0007829|PDB:5X4S" FT STRAND 113..118 FT /evidence="ECO:0007829|PDB:5X4S" FT STRAND 123..141 FT /evidence="ECO:0007829|PDB:5X4S" FT TURN 142..144 FT /evidence="ECO:0007829|PDB:5X4S" FT STRAND 146..164 FT /evidence="ECO:0007829|PDB:5X4S" FT HELIX 170..173 FT /evidence="ECO:0007829|PDB:7SG4" FT STRAND 177..190 FT /evidence="ECO:0007829|PDB:5X4S" FT STRAND 193..208 FT /evidence="ECO:0007829|PDB:5X4S" FT STRAND 216..222 FT /evidence="ECO:0007829|PDB:5X4S" FT STRAND 229..239 FT /evidence="ECO:0007829|PDB:5X4S" FT STRAND 250..256 FT /evidence="ECO:0007829|PDB:5X4S" FT STRAND 258..266 FT /evidence="ECO:0007829|PDB:5X4S" FT STRAND 268..270 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 272..277 FT /evidence="ECO:0007829|PDB:5X4S" FT TURN 282..288 FT /evidence="ECO:0007829|PDB:5X4S" FT STRAND 297..301 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 311..315 FT /evidence="ECO:0007829|PDB:8H0X" FT HELIX 326..329 FT /evidence="ECO:0007829|PDB:2GHV" FT HELIX 337..339 FT /evidence="ECO:0007829|PDB:2GHV" FT STRAND 341..345 FT /evidence="ECO:0007829|PDB:2GHV" FT STRAND 347..349 FT /evidence="ECO:0007829|PDB:2GHV" FT HELIX 352..354 FT /evidence="ECO:0007829|PDB:2GHV" FT TURN 356..358 FT /evidence="ECO:0007829|PDB:8H0Z" FT STRAND 362..368 FT /evidence="ECO:0007829|PDB:2GHV" FT HELIX 371..378 FT /evidence="ECO:0007829|PDB:2GHV" FT STRAND 380..390 FT /evidence="ECO:0007829|PDB:2GHV" FT HELIX 391..396 FT /evidence="ECO:0007829|PDB:2GHV" FT STRAND 397..400 FT /evidence="ECO:0007829|PDB:3D0G" FT HELIX 404..408 FT /evidence="ECO:0007829|PDB:2GHV" FT STRAND 414..416 FT /evidence="ECO:0007829|PDB:5X58" FT STRAND 418..424 FT /evidence="ECO:0007829|PDB:2GHV" FT HELIX 426..429 FT /evidence="ECO:0007829|PDB:2GHV" FT STRAND 431..433 FT /evidence="ECO:0007829|PDB:2DD8" FT STRAND 439..441 FT /evidence="ECO:0007829|PDB:2GHV" FT TURN 450..454 FT /evidence="ECO:0007829|PDB:7SG4" FT STRAND 462..465 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 471..473 FT /evidence="ECO:0007829|PDB:6WAQ" FT STRAND 478..480 FT /evidence="ECO:0007829|PDB:2GHV" FT STRAND 483..487 FT /evidence="ECO:0007829|PDB:2GHV" FT HELIX 489..491 FT /evidence="ECO:0007829|PDB:2GHV" FT STRAND 492..501 FT /evidence="ECO:0007829|PDB:2GHV" FT STRAND 503..506 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 509..511 FT /evidence="ECO:0007829|PDB:2DD8" FT STRAND 522..529 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 532..540 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 551..553 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 555..557 FT /evidence="ECO:0007829|PDB:6CRV" FT STRAND 559..563 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 565..567 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 570..574 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 581..585 FT /evidence="ECO:0007829|PDB:8H0X" FT TURN 588..590 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 595..600 FT /evidence="ECO:0007829|PDB:8H0X" FT HELIX 603..611 FT /evidence="ECO:0007829|PDB:8H11" FT HELIX 612..614 FT /evidence="ECO:0007829|PDB:8H0Y" FT STRAND 615..617 FT /evidence="ECO:0007829|PDB:8H11" FT TURN 621..623 FT /evidence="ECO:0007829|PDB:8H0Z" FT STRAND 624..626 FT /evidence="ECO:0007829|PDB:8H10" FT STRAND 628..630 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 635..638 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 640..646 FT /evidence="ECO:0007829|PDB:6CRV" FT STRAND 649..653 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 656..661 FT /evidence="ECO:0007829|PDB:8H0X" FT HELIX 665..671 FT /evidence="ECO:0007829|PDB:7SG4" FT STRAND 673..678 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 683..685 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 691..710 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 715..718 FT /evidence="ECO:0007829|PDB:8H0X" FT HELIX 720..724 FT /evidence="ECO:0007829|PDB:8H0X" FT TURN 725..727 FT /evidence="ECO:0007829|PDB:8H11" FT HELIX 729..735 FT /evidence="ECO:0007829|PDB:8H0X" FT HELIX 736..738 FT /evidence="ECO:0007829|PDB:8H0X" FT HELIX 739..764 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 768..771 FT /evidence="ECO:0007829|PDB:8H0X" FT HELIX 773..777 FT /evidence="ECO:0007829|PDB:2RUM" FT STRAND 778..781 FT /evidence="ECO:0007829|PDB:6CRZ" FT STRAND 785..788 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 791..797 FT /evidence="ECO:0007829|PDB:8H0X" FT HELIX 799..807 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 813..815 FT /evidence="ECO:0007829|PDB:8H0X" FT HELIX 819..824 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 826..828 FT /evidence="ECO:0007829|PDB:8H0X" FT HELIX 831..836 FT /evidence="ECO:0007829|PDB:8H0X" FT TURN 837..839 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 840..843 FT /evidence="ECO:0007829|PDB:8H0X" FT HELIX 849..865 FT /evidence="ECO:0007829|PDB:8H0X" FT TURN 866..872 FT /evidence="ECO:0007829|PDB:8H0X" FT HELIX 880..890 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 898..900 FT /evidence="ECO:0007829|PDB:2BEZ" FT HELIX 902..921 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 924..926 FT /evidence="ECO:0007829|PDB:6CRZ" FT HELIX 927..962 FT /evidence="ECO:0007829|PDB:1ZVA" FT STRAND 963..966 FT /evidence="ECO:0007829|PDB:8H10" FT HELIX 968..1014 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 1024..1038 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 1041..1061 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 1063..1067 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 1069..1079 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 1084..1087 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 1089..1091 FT /evidence="ECO:0007829|PDB:8H0X" FT TURN 1099..1101 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 1102..1104 FT /evidence="ECO:0007829|PDB:8H0X" FT STRAND 1114..1116 FT /evidence="ECO:0007829|PDB:6CRV" FT HELIX 1124..1127 FT /evidence="ECO:0007829|PDB:7SG4" FT HELIX 1148..1151 FT /evidence="ECO:0007829|PDB:2FXP" FT HELIX 1154..1180 FT /evidence="ECO:0007829|PDB:1ZVA" FT HELIX 1182..1192 FT /evidence="ECO:0007829|PDB:2BEQ" SQ SEQUENCE 1255 AA; 139125 MW; 1C49ACA2CFD38FC0 CRC64; MFIFLLFLTL TSGSDLDRCT TFDDVQAPNY TQHTSSMRGV YYPDEIFRSD TLYLTQDLFL PFYSNVTGFH TINHTFGNPV IPFKDGIYFA ATEKSNVVRG WVFGSTMNNK SQSVIIINNS TNVVIRACNF ELCDNPFFAV SKPMGTQTHT MIFDNAFNCT FEYISDAFSL DVSEKSGNFK HLREFVFKNK DGFLYVYKGY QPIDVVRDLP SGFNTLKPIF KLPLGINITN FRAILTAFSP AQDIWGTSAA AYFVGYLKPT TFMLKYDENG TITDAVDCSQ NPLAELKCSV KSFEIDKGIY QTSNFRVVPS GDVVRFPNIT NLCPFGEVFN ATKFPSVYAW ERKKISNCVA DYSVLYNSTF FSTFKCYGVS ATKLNDLCFS NVYADSFVVK GDDVRQIAPG QTGVIADYNY KLPDDFMGCV LAWNTRNIDA TSTGNYNYKY RYLRHGKLRP FERDISNVPF SPDGKPCTPP ALNCYWPLND YGFYTTTGIG YQPYRVVVLS FELLNAPATV CGPKLSTDLI KNQCVNFNFN GLTGTGVLTP SSKRFQPFQQ FGRDVSDFTD SVRDPKTSEI LDISPCSFGG VSVITPGTNA SSEVAVLYQD VNCTDVSTAI HADQLTPAWR IYSTGNNVFQ TQAGCLIGAE HVDTSYECDI PIGAGICASY HTVSLLRSTS QKSIVAYTMS LGADSSIAYS NNTIAIPTNF SISITTEVMP VSMAKTSVDC NMYICGDSTE CANLLLQYGS FCTQLNRALS GIAAEQDRNT REVFAQVKQM YKTPTLKYFG 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 IQKEIDRLNE VAKNLNESLI DLQELGKYEQ YIKWPWYVWL GFIAGLIAIV MVTILLCCMT SCCSCLKGAC SCGSCCKFDE DDSEPVLKGV KLHYT //