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-MAR-2024, entry version 155.
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 ---------------------------------------------------------------------------
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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; 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; 8SPH; X-ray; 2.71 A; E/F=306-521.
DR PDB; 8SPI; X-ray; 3.06 A; E/F=306-521.
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; 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; 8SPH; -.
DR PDBsum; 8SPI; -.
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-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-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; 235.
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 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; Genome.
DR Proteomes; UP000109640; Genome.
DR Proteomes; UP000116947; Genome.
DR Proteomes; UP000121636; Genome.
DR Proteomes; UP000131569; Genome.
DR Proteomes; UP000131955; Genome.
DR Proteomes; UP000137377; Genome.
DR Proteomes; UP000138690; Genome.
DR Proteomes; UP000143093; Genome.
DR Proteomes; UP000145651; Genome.
DR Proteomes; UP000146108; Genome.
DR Proteomes; UP000146181; Genome.
DR Proteomes; UP000146296; Genome.
DR Proteomes; UP000148194; Genome.
DR Proteomes; UP000153467; Genome.
DR Proteomes; UP000160648; Genome.
DR Proteomes; UP000164441; Genome.
DR Proteomes; UP000172416; Genome.
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:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; 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 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; IPR043607; CoV_S1_C.
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; PF19209; CoV_S1_C; 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 1162..1172
FT /evidence="ECO:0007829|PDB:2BEQ"
FT HELIX 1173..1178
FT /evidence="ECO:0007829|PDB:2BEQ"
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
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