Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2]

 SPIKE_CVHSA             Reviewed;        1255 AA.
P59594; Q6QU82; Q7T696; Q7TA19; Q7TFA2; Q7TFB1; Q80BV6;
23-APR-2003, integrated into UniProtKB/Swiss-Prot.
23-APR-2003, sequence version 1.
22-NOV-2017, entry version 122.
RecName: Full=Spike glycoprotein;
Short=S glycoprotein;
AltName: Full=E2;
AltName: Full=Peplomer protein;
Contains:
RecName: Full=Spike protein S1;
Contains:
RecName: Full=Spike protein S2;
Flags: Precursor;
Name=S; ORFNames=2;
Human SARS coronavirus (SARS-CoV) (Severe acute respiratory syndrome
coronavirus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=227859;
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9675; Paguma larvata (Masked palm civet).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Urbani;
PubMed=12730500; DOI=10.1126/science.1085952;
Rota P.A., Oberste M.S., Monroe S.S., Nix W.A., Campagnoli R.,
Icenogle J.P., Penaranda S., Bankamp B., Maher K., Chen M.-H.,
Tong S., Tamin A., Lowe L., Frace M., DeRisi J.L., Chen Q., Wang D.,
Erdman D.D., Peret T.C.T., Burns C., Ksiazek T.G., Rollin P.E.,
Sanchez A., Liffick S., Holloway B., Limor J., McCaustland K.,
Olsen-Rasmussen M., Fouchier R., Guenther S., Osterhaus A.D.M.E.,
Drosten C., Pallansch M.A., Anderson L.J., Bellini W.J.;
"Characterization of a novel coronavirus associated with severe acute
respiratory syndrome.";
Science 300:1394-1399(2003).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Tor2;
PubMed=12730501; DOI=10.1126/science.1085953;
Marra M.A., Jones S.J.M., Astell C.R., Holt R.A., Brooks-Wilson A.,
Butterfield Y.S.N., Khattra J., Asano J.K., Barber S.A., Chan S.Y.,
Cloutier A., Coughlin S.M., Freeman D., Girn N., Griffith O.L.,
Leach S.R., Mayo M., McDonald H., Montgomery S.B., Pandoh P.K.,
Petrescu A.S., Robertson A.G., Schein J.E., Siddiqui A., Smailus D.E.,
Stott J.M., Yang G.S., Plummer F., Andonov A., Artsob H., Bastien N.,
Bernard K., Booth T.F., Bowness D., Czub M., Drebot M., Fernando L.,
Flick R., Garbutt M., Gray M., Grolla A., Jones S., Feldmann H.,
Meyers A., Kabani A., Li Y., Normand S., Stroher U., Tipples G.A.,
Tyler S., Vogrig R., Ward D., Watson B., Brunham R.C., Krajden M.,
Petric M., Skowronski D.M., Upton C., Roper R.L.;
"The genome sequence of the SARS-associated coronavirus.";
Science 300:1399-1404(2003).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate CUHK-Su10, and Isolate CUHK-W1;
PubMed=12853594; DOI=10.1056/NEJM200307103490216;
Tsui S.K.W., Chim S.S.C., Lo Y.M.D.;
"Coronavirus genomic-sequence variations and the epidemiology of the
severe acute respiratory syndrome.";
N. Engl. J. Med. 349:187-188(2003).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate HKU-39849;
PubMed=12876307; DOI=10.1177/15353702-0322807-13;
Zeng F.Y., Chan C.W., Chan M.N., Chen J.D., Chow K.Y.C., Hon C.C.C.,
Hui R.K.H., Li J., Li V.Y.Y., Wang C.Y., Wang P.Y., Guan Y., Zheng B.,
Poon L.L.M., Chan K.H., Yuen K.Y., Peiris J.S.M., Leung F.C.;
"The complete genome sequence of severe acute respiratory syndrome
coronavirus strain HKU-39849 (HK-39).";
Exp. Biol. Med. 228:866-873(2003).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate GZ50, and Isolate HKU-36871;
PubMed=12958366; DOI=10.1126/science.1087139;
Guan Y., Zheng B.J., He Y.Q., Liu X.L., Zhuang Z.X., Cheung C.L.,
Luo S.W., Li P.H., Zhang L.J., Guan Y.J., Butt K.M., Wong K.L.,
Chan K.W., Lim W., Shortridge K.F., Yuen K.Y., Peiris J.S.M.,
Poon L.L.M.;
"Isolation and characterization of viruses related to the SARS
coronavirus from animals in southern China.";
Science 302:276-278(2003).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04, and
Isolate GD01;
Qin E., Zhu Q., Yu M., Fan B., Chang G., Si B., Yang B., Peng W.,
Jiang T., Liu B., Deng Y., Liu H., Zhang Y., Wang C., Li Y., Gan Y.,
Li X., Lu F., Tan G., Yang R., Cao W.S., Wang J., Chen W., Cong L.,
Deng Y., Dong W., Han Y., Hu W., Lei M., Li C., Li G., Li G., Li H.,
Li S., Li S., Li W., Li W., Lin W., Liu J., Liu Z., Lu H., Ni P.,
Qi Q., Sun Y., Tang L., Tong Z., Wang J., Wang X., Wu Q., Xi Y.,
Xu Z., Yang L., Ye C., Ye J., Zhang B., Zhang F., Zhang J., Zhang X.,
Zhou J., Yang H.;
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Sin2500, Isolate Sin2677, Isolate Sin2679,
Isolate Sin2748, and Isolate sin2774;
PubMed=12781537; DOI=10.1016/S0140-6736(03)13414-9;
Ruan Y., Wei C.L., Ling A.E., Vega V.B., Thoreau H., Se Thoe S.Y.,
Chia J.-M., Ng P., Chiu K.P., Lim L., Zhang T., Chan K.P., Oon L.E.L.,
Ng M.L., Leo S.Y., Ng L.F.P., Ren E.C., Stanton L.W., Long P.M.,
Liu E.T.;
"Comparative full-length genome sequence analysis of 14 SARS
coronavirus isolates and common mutations associated with putative
origins of infection.";
Lancet 361:1779-1785(2003).
[8]
ERRATUM.
Ruan Y., Wei C.L., Ling A.E., Vega V.B., Thoreau H., Se Thoe S.Y.,
Chia J.-M., Ng P., Chiu K.P., Lim L., Zhang T., Chan K.P., Oon L.E.L.,
Ng M.L., Leo S.Y., Ng L.F.P., Ren E.C., Stanton L.W., Long P.M.,
Liu E.T.;
Lancet 361:1832-1832(2003).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate TW1;
Yeh S.-H., Kao C.-L., Tsai C.-Y., Liu C.-J., Chen D.-S., Chen P.-J.;
"The complete genome of SARS coronavirus clone TW1.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate FRA;
Eickmann M., Becker S., Klenk H.-D., Doerr H.W., Stadler K.,
Censini S., Guidotti S., Masignani V., Scarselli M., Mora M.,
Donati C., Han J., Song H.C., Abrignani S., Covacci A., Rappuoli R.;
"SARS virus is a close relative of type II coronaviruses.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Frankfurt 1;
PubMed=12917450; DOI=10.1099/vir.0.19424-0;
Thiel V., Ivanov K.A., Putics A., Hertzig T., Schelle B., Bayer S.,
Weissbrich B., Snijder E.J., Rabenau H., Doerr H.W., Gorbalenya A.E.,
Ziebuhr J.;
"Mechanisms and enzymes involved in SARS coronavirus genome
expression.";
J. Gen. Virol. 84:2305-2315(2003).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate TWC;
Yang J.-Y., Lin J.-H., Chiu S.-C., Wang S.-F., Lee S.C., Lin Y.-C.,
Hsu C.-K., Chen H.-Y., Chang J.G., Chen P.-J., Su I.-J.;
"Genomic sequence of SARS isolate from the first fatal case in
Taiwan.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Isolate ZJ01;
Cong L.-M., Ding G.-Q., Lu Y.-Y., Weng J.-Q., Yan J.-Y., Hu N.-P.,
Wo J.-E., Chen S.-Y., Zhang Y.-J., Mei L.-L., Wang Z.-G., Yao J.,
Zhu H.-P., Lu Q.-Y., Li M.-H., Gong L.-M., Shi W., Li L.-J.;
"SARS coronavirus ZJ01 isolate spike glycoprotein.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Shanghai LY;
Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Taiwan TC1, Isolate Taiwan TC2, and Isolate Taiwan TC3;
Chang J.-G.C., Lin T.-H., Chen C.-M., Lin C.-S., Chan W.-L.,
Shih M.-C.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[16]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate TWH, Isolate TWJ, Isolate TWK, Isolate TWS, and
Isolate TWY;
Shu H.Y., Wu K.M., Tsai S.F.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[17]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate HSR 1;
Canducci F., Clementi M., Poli G., Vicenzi E.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[18]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate TWC2, and Isolate TWC3;
Yang J.-Y., Lin J.-H., Chiu S.-C., Wang S.-F., Lee H.-C., Lin Y.-C.,
Hsu C.-K., Chen H.-Y., Chen P.-J., Su I.-J.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[19]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate AS;
Balotta C., Corvasce S., Violin M., Galli M., Moroni M.,
Vigevani G.M., Ruan Y.J., Salemi M.;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[20]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Shanghai QXC1;
Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.;
"Analysis of SARS coronavirus genome in Shanghai isolates.";
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[21]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate GD03;
PubMed=15695582; DOI=10.1073/pnas.0409608102;
Song H.D., Tu C.C., Zhang G.W., Wang S.Y., Zheng K., Lei L.C.,
Chen Q.X., Gao Y.W., Zhou H.Q., Xiang H., Zheng H.J., Chern S.W.,
Cheng F., Pan C.M., Xuan H., Chen S.J., Luo H.M., Zhou D.H., Liu Y.F.,
He J.F., Qin P.Z., Li L.H., Ren Y.Q., Liang W.J., Yu Y.D.,
Anderson L., Wang M., Xu R.H., Wu X.W., Zheng H.Y., Chen J.D.,
Liang G., Gao Y., Liao M., Fang L., Jiang L.Y., Li H., Chen F., Di B.,
He L.J., Lin J.Y., Tong S., Kong X., Du L., Hao P., Tang H.,
Bernini A., Yu X.J., Spiga O., Guo Z.M., Pan H.Y., He W.Z.,
Manuguerra J.C., Fontanet A., Danchin A., Niccolai N., Li Y.X.,
Wu C.I., Zhao G.P.;
"Cross-host evolution of severe acute respiratory syndrome coronavirus
in palm civet and human.";
Proc. Natl. Acad. Sci. U.S.A. 102:2430-2435(2005).
[22]
INTERACTION WITH HUMAN ACE2, AND CHARACTERIZATION OF CELLULAR
RECEPTOR.
PubMed=14647384; DOI=10.1038/nature02145;
Li W., Moore M.J., Vasilieva N., Sui J., Wong S.-K., Berne M.A.,
Somasundaran M., Sullivan J.L., Luzuriaga K., Greenough T.C., Choe H.,
Farzan M.;
"Angiotensin-converting enzyme 2 is a functional receptor for the SARS
coronavirus.";
Nature 426:450-454(2003).
[23]
INTERACTION WITH HUMAN ACE2.
PubMed=14670965; DOI=10.1074/jbc.C300520200;
Wong S.K., Li W., Moore M.J., Choe H., Farzan M.;
"A 193-amino acid fragment of the SARS coronavirus S protein
efficiently binds angiotensin-converting enzyme 2.";
J. Biol. Chem. 279:3197-3201(2004).
[24]
CHARACTERIZATION OF HEPTAD REPEAT REGIONS.
PubMed=15518555; DOI=10.1021/bi049101q;
Xu Y., Zhu J., Liu Y., Lou Z., Yuan F., Liu Y., Cole D.K., Ni L.,
Su N., Qin L., Li X., Bai Z., Bell J.I., Pang H., Tien P., Gao G.F.,
Rao Z.;
"Characterization of the heptad repeat regions, HR1 and HR2, and
design of a fusion core structure model of the spike protein from
severe acute respiratory syndrome (SARS) coronavirus.";
Biochemistry 43:14064-14071(2004).
[25]
CLEAVAGE.
PubMed=15450134; DOI=10.1038/sj.cr.7290240;
Wu X.D., Shang B., Yang R.F., Yu H., Ma Z.H., Shen X., Ji Y.Y.,
Lin Y., Wu Y.D., Lin G.M., Tian L., Gan X.Q., Yang S., Jiang W.H.,
Dai E.H., Wang X.Y., Jiang H.L., Xie Y.H., Zhu X.L., Pei G., Li L.,
Wu J.R., Sun B.;
"The spike protein of severe acute respiratory syndrome (SARS) is
cleaved in virus infected Vero-E6 cells.";
Cell Res. 14:400-406(2004).
[26]
INTERACTION WITH HUMAN CLEC4M/DC-SIGNR, AND MUTAGENESIS OF CYS-323;
CYS-348; GLU-452; ASP-454; ASP-463; CYS-467; CYS-474 AND ASP-480.
PubMed=15496474; DOI=10.1073/pnas.0403812101;
Jeffers S.A., Tusell S.M., Gillim-Ross L., Hemmila E.M.,
Achenbach J.E., Babcock G.J., Thomas W.D. Jr., Thackray L.B.,
Young M.D., Mason R.J., Ambrosino D.M., Wentworth D.E.,
Demartini J.C., Holmes K.V.;
"CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome
coronavirus.";
Proc. Natl. Acad. Sci. U.S.A. 101:15748-15753(2004).
[27]
HOMOTRIMERIZATION.
PubMed=15313178; DOI=10.1016/j.bbrc.2004.07.084;
Xiao X., Feng Y., Chakraborti S., Dimitrov D.S.;
"Oligomerization of the SARS-CoV S glycoprotein: dimerization of the
N-terminus and trimerization of the ectodomain.";
Biochem. Biophys. Res. Commun. 322:93-99(2004).
[28]
CHARACTERIZATION OF FUSION PEPTIDE.
PubMed=15890958; DOI=10.1128/JVI.79.11.7195-7206.2005;
Sainz B. Jr., Rausch J.M., Gallaher W.R., Garry R.F., Wimley W.C.;
"Identification and characterization of the putative fusion peptide of
the severe acute respiratory syndrome-associated coronavirus spike
protein.";
J. Virol. 79:7195-7206(2005).
[29]
SUBCELLULAR LOCATION.
PubMed=15831954; DOI=10.1099/vir.0.80671-0;
Nal B., Chan C., Kien F., Siu L., Tse J., Chu K., Kam J.,
Staropoli I., Crescenzo-Chaigne B., Escriou N., van der Werf S.,
Yuen K.Y., Altmeyer R.;
"Differential maturation and subcellular localization of severe acute
respiratory syndrome coronavirus surface proteins S, M and E.";
J. Gen. Virol. 86:1423-1434(2005).
[30]
CHARACTERIZATION OF VARIANTS ARG-344; SER-360; LYS-479 AND SER-487.
PubMed=15791205; DOI=10.1038/sj.emboj.7600640;
Li W., Zhang C., Sui J., Kuhn J.H., Moore M.J., Luo S., Wong S.-K.,
Huang I.-C., Xu K., Vasilieva N., Murakami A., He Y., Marasco W.A.,
Guan Y., Choe H., Farzan M.;
"Receptor and viral determinants of SARS-coronavirus adaptation to
human ACE2.";
EMBO J. 24:1634-1643(2005).
[31]
PROTEOLYSIS BY HUMAN CTSL.
PubMed=16081529; DOI=10.1073/pnas.0505577102;
Simmons G., Gosalia D.N., Rennekamp A.J., Reeves J.D., Diamond S.L.,
Bates P.;
"Inhibitors of cathepsin L prevent severe acute respiratory syndrome
coronavirus entry.";
Proc. Natl. Acad. Sci. U.S.A. 102:11876-11881(2005).
[32]
INTERACTION WITH ACCESSORY PROTEIN 3A.
PubMed=15194747; DOI=10.1128/JVI.78.13.6723-6734.2004;
Tan Y.-J., Teng E., Shen S., Tan T.H.P., Goh P.-Y., Fielding B.C.,
Ooi E.-E., Tan H.-C., Lim S.G., Hong W.;
"A novel severe acute respiratory syndrome coronavirus protein, U274,
is transported to the cell surface and undergoes endocytosis.";
J. Virol. 78:6723-6734(2004).
[33]
INTERACTION WITH ACCESSORY PROTEIN 7A.
PubMed=16840309; DOI=10.1128/JVI.00414-06;
Huang C., Ito N., Tseng C.-T.K., Makino S.;
"Severe acute respiratory syndrome coronavirus 7a accessory protein is
a viral structural protein.";
J. Virol. 80:7287-7294(2006).
[34]
MUTAGENESIS OF ARG-667 AND LYS-672.
PubMed=16519916; DOI=10.1016/j.virol.2006.02.003;
Follis K.E., York J., Nunberg J.H.;
"Furin cleavage of the SARS coronavirus spike glycoprotein enhances
cell-cell fusion but does not affect virion entry.";
Virology 350:358-369(2006).
[35]
PALMITOYLATION.
PubMed=17134730; DOI=10.1016/j.virol.2006.10.034;
Petit C.M., Chouljenko V.N., Iyer A., Colgrove R., Farzan M.,
Knipe D.M., Kousoulas K.G.;
"Palmitoylation of the cysteine-rich endodomain of the SARS-
coronavirus spike glycoprotein is important for spike-mediated cell
fusion.";
Virology 360:264-274(2007).
[36]
ENDOPLASMIC RETICULUM RETENTION MOTIF, AND MUTAGENESIS OF LYS-1251 AND
HIS-1253.
PubMed=17166901; DOI=10.1128/JVI.02146-06;
McBride C.E., Li J., Machamer C.E.;
"The cytoplasmic tail of the severe acute respiratory syndrome
coronavirus spike protein contains a novel endoplasmic reticulum
retrieval signal that binds COPI and promotes interaction with
membrane protein.";
J. Virol. 81:2418-2428(2007).
[37]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 900-948.
PubMed=15345712; DOI=10.1074/jbc.M408782200;
Xu Y., Lou Z., Liu Y., Pang H., Tien P., Gao G.F., Rao Z.;
"Crystal structure of severe acute respiratory syndrome coronavirus
spike protein fusion core.";
J. Biol. Chem. 279:49414-49419(2004).
[38]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 895-972 AND 1142-1180.
PubMed=15604146; DOI=10.1073/pnas.0406128102;
Supekar V.M., Bruckmann C., Ingallinella P., Bianchi E., Pessi A.,
Carfi A.;
"Structure of a proteolytically resistant core from the severe acute
respiratory syndrome coronavirus S2 fusion protein.";
Proc. Natl. Acad. Sci. U.S.A. 101:17958-17963(2004).
[39]
3D-STRUCTURE MODELING OF 17-680.
PubMed=14511651; DOI=10.1016/j.bbrc.2003.08.122;
Spiga O., Bernini A., Ciutti A., Chiellini S., Menciassi N.,
Finetti F., Causarono V., Anselmi F., Prischi F., Niccolai N.;
"Molecular modelling of S1 and S2 subunits of SARS coronavirus spike
glycoprotein.";
Biochem. Biophys. Res. Commun. 310:78-83(2003).
[40]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 323-502 IN COMPLEX WITH HUMAN
ACE2.
PubMed=16166518; DOI=10.1126/science.1116480;
Li F., Li W., Farzan M., Harrison S.C.;
"Structure of SARS coronavirus spike receptor-binding domain complexed
with receptor.";
Science 309:1864-1868(2005).
[41]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1150-1193.
PubMed=16698550; DOI=10.1016/j.str.2006.03.007;
Deng Y., Liu J., Zheng Q., Yong W., Lu M.;
"Structures and polymorphic interactions of two heptad-repeat regions
of the SARS virus S2 protein.";
Structure 14:889-899(2006).
-!- FUNCTION: S1 attaches the virion to the cell membrane by
interacting with human ACE2 and CLEC4M/DC-SIGNR, initiating the
infection. Binding to the receptor and internalization of the
virus into the endosomes of the host cell probably induces
conformational changes in the S glycoprotein. Proteolysis by
cathepsin CTSL may unmask the fusion peptide of S2 and activate
membranes fusion within endosomes.
-!- FUNCTION: S2 is a class I viral fusion protein. Under the current
model, the protein has at least three conformational states: pre-
fusion native state, pre-hairpin intermediate state, and post-
fusion hairpin state. During viral and target cell membrane
fusion, the coiled coil regions (heptad repeats) assume a trimer-
of-hairpins structure, positioning the fusion peptide in close
proximity to the C-terminal region of the ectodomain. The
formation of this structure appears to drive apposition and
subsequent fusion of viral and target cell membranes.
-!- SUBUNIT: Homotrimer. Binds to human and palm civet ACE2 and human
CLEC4M/DC-SIGNR. Interacts with the accessory proteins 3a and 7a.
{ECO:0000269|PubMed:14647384, ECO:0000269|PubMed:14670965,
ECO:0000269|PubMed:15194747, ECO:0000269|PubMed:15496474,
ECO:0000269|PubMed:16166518, ECO:0000269|PubMed:16840309}.
-!- INTERACTION:
Self; NbExp=9; IntAct=EBI-15582614, EBI-15582614;
-!- SUBCELLULAR LOCATION: Virion membrane
{ECO:0000269|PubMed:15831954}; Single-pass type I membrane protein
{ECO:0000269|PubMed:15831954}. Host endoplasmic reticulum-Golgi
intermediate compartment membrane {ECO:0000250}; Single-pass type
I membrane protein {ECO:0000250}. Host cell membrane
{ECO:0000269|PubMed:15831954}; Single-pass type I membrane protein
{ECO:0000269|PubMed:15831954}. Note=Accumulates in the endoplasmic
reticulum-Golgi intermediate compartment, where it participates in
virus particle assembly (By similarity). Some S oligomers are
transported to the plasma membrane, where they may mediate cell-
cell fusion. {ECO:0000250}.
-!- DOMAIN: The KxHxx motif seems to function as an ER retrieval and
binds COPI in vitro.
-!- PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike
glycoprotein is digested by cathepsin CTSL within endosomes.
{ECO:0000269|PubMed:17134730}.
-!- MISCELLANEOUS: Tor2 is the prototype of the virus isolated during
the severe SARS outbreak in 2002-2003. GD03 has been isolated from
the second mild SARS outbreak in winter 2003-2004. SZ3 has been
isolated from palm civet, the presumed animal reservoir. The spike
proteins from those three isolates display a strong affinity for
palm civet ACE2 receptor, whereas only the Tor2 spike protein
efficiently binds human ACE2. This may explain the high
pathogenicity of Tor2 virus, whose spike is highly adapted to the
human host. Therefore, the lack of severity of disease during the
2003-2004 outbreak could be due to the incomplete adaptation of
GD03 virus to bind human ACE2. Mutation Asn-479 and Thr-487 in
palm civet coronavirus seems necessary and sufficient for the
virus to acquire the ability to efficiently infect humans.
-!- SIMILARITY: Belongs to the coronaviruses spike protein family.
{ECO:0000305}.
-!- CAUTION: Cleavage into S1 and S2 remains controversial, since
biochemical evidence for this proteolytic cleavage is largely
negative. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY278741; AAP13441.1; -; Genomic_RNA.
EMBL; AY274119; AAP41037.1; -; Genomic_RNA.
EMBL; AY282752; AAP30713.1; -; Genomic_RNA.
EMBL; AY278554; AAP13567.1; -; Genomic_RNA.
EMBL; AY278491; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY304495; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY304492; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY278487; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY278488; AAP30030.1; -; Genomic_RNA.
EMBL; AY278490; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY279354; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY278489; AAP51227.1; -; Genomic_RNA.
EMBL; AY283794; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY283795; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY283796; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY283797; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY283798; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY291451; AAP37017.1; -; Genomic_RNA.
EMBL; AY310120; AAP50485.1; -; Genomic_RNA.
EMBL; AY291315; AAP33697.1; -; Genomic_RNA.
EMBL; AY304486; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY321118; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY323976; AAP73417.1; -; mRNA.
EMBL; AY322207; AAP82968.1; -; Genomic_RNA.
EMBL; AY338174; AAQ01597.1; -; Genomic_RNA.
EMBL; AY338175; AAQ01609.1; -; Genomic_RNA.
EMBL; AY348314; AAP97882.1; -; Genomic_RNA.
EMBL; AP006557; BAC81348.1; -; Genomic_RNA.
EMBL; AP006558; BAC81362.1; -; Genomic_RNA.
EMBL; AP006559; BAC81376.1; -; Genomic_RNA.
EMBL; AP006560; BAC81390.1; -; Genomic_RNA.
EMBL; AP006561; BAC81404.1; -; Genomic_RNA.
EMBL; AY323977; AAP72986.1; -; Genomic_RNA.
EMBL; AY362698; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY362699; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY427439; AAQ94060.1; -; Genomic_RNA.
EMBL; AY463059; AAR86788.1; -; Genomic_RNA.
EMBL; AY525636; AAS10463.1; -; Genomic_RNA.
PDB; 1Q4Z; Model; -; A=17-680.
PDB; 1T7G; Model; -; A/C/E=17-680, B/D/F=737-1026.
PDB; 1U4K; Model; -; D=764-1089.
PDB; 1WNC; X-ray; 2.80 A; A/B/C/D/E/F=900-948, A/B/C/D/E/F=1144-1185.
PDB; 1WYY; X-ray; 2.20 A; A/B=885-981, A/B=1145-1189.
PDB; 1XJP; Model; -; A=17-680.
PDB; 1ZV7; X-ray; 1.70 A; A/B=1150-1193.
PDB; 1ZV8; X-ray; 1.94 A; A/C/E/G/I/K=901-950, B/D/F/H/J/L=1150-1185.
PDB; 1ZVB; X-ray; 1.70 A; A/B/C=940-973.
PDB; 2AJF; X-ray; 2.90 A; E/F=323-502.
PDB; 2BEQ; X-ray; 1.60 A; A/B/C=914-949, D/E/F=1148-1193.
PDB; 2BEZ; X-ray; 1.60 A; C=896-972, F=1142-1183.
PDB; 2DD8; X-ray; 2.30 A; S=317-518.
PDB; 2FXP; NMR; -; A/B/C=1141-1193.
PDB; 2GHV; X-ray; 2.20 A; C/E=317-510.
PDB; 2GHW; X-ray; 2.30 A; A/C=317-510.
PDB; 2RUM; NMR; -; A=770-788.
PDB; 2RUN; NMR; -; A=1185-1202.
PDB; 2RUO; NMR; -; A=873-888.
PDB; 3BGF; X-ray; 3.00 A; A/S=318-510.
PDB; 3D0G; X-ray; 2.80 A; E/F=324-502.
PDB; 3D0H; X-ray; 3.10 A; E/F=324-502.
PDB; 3D0I; X-ray; 2.90 A; E/F=324-502.
PDB; 3SCI; X-ray; 2.90 A; E/F=306-527.
PDB; 3SCJ; X-ray; 3.00 A; E/F=323-502.
PDB; 3SCK; X-ray; 3.00 A; E/F=324-502.
PDB; 3SCL; X-ray; 3.00 A; E/F=324-502.
PDB; 5WRG; EM; 4.30 A; A/B/C=1-1196.
PDB; 5X4S; X-ray; 2.20 A; A=14-292.
PDB; 5X58; EM; 3.20 A; A/B/C=14-1193.
PDB; 5X5B; EM; 3.70 A; A/B/C=14-1193.
PDB; 5XJK; NMR; -; A=758-821.
PDB; 5XLR; EM; 3.80 A; A/B/C=1-1196.
PDBsum; 1Q4Z; -.
PDBsum; 1T7G; -.
PDBsum; 1U4K; -.
PDBsum; 1WNC; -.
PDBsum; 1WYY; -.
PDBsum; 1XJP; -.
PDBsum; 1ZV7; -.
PDBsum; 1ZV8; -.
PDBsum; 1ZVB; -.
PDBsum; 2AJF; -.
PDBsum; 2BEQ; -.
PDBsum; 2BEZ; -.
PDBsum; 2DD8; -.
PDBsum; 2FXP; -.
PDBsum; 2GHV; -.
PDBsum; 2GHW; -.
PDBsum; 2RUM; -.
PDBsum; 2RUN; -.
PDBsum; 2RUO; -.
PDBsum; 3BGF; -.
PDBsum; 3D0G; -.
PDBsum; 3D0H; -.
PDBsum; 3D0I; -.
PDBsum; 3SCI; -.
PDBsum; 3SCJ; -.
PDBsum; 3SCK; -.
PDBsum; 3SCL; -.
PDBsum; 5WRG; -.
PDBsum; 5X4S; -.
PDBsum; 5X58; -.
PDBsum; 5X5B; -.
PDBsum; 5XJK; -.
PDBsum; 5XLR; -.
ProteinModelPortal; P59594; -.
SMR; P59594; -.
DIP; DIP-29105N; -.
IntAct; P59594; 1.
PRIDE; P59594; -.
OrthoDB; VOG0900000Z; -.
EvolutionaryTrace; P59594; -.
Proteomes; UP000000354; Genome.
Proteomes; UP000103670; Genome.
Proteomes; UP000109640; Genome.
Proteomes; UP000116947; Genome.
Proteomes; UP000121636; Genome.
Proteomes; UP000131569; Genome.
Proteomes; UP000131955; Genome.
Proteomes; UP000137377; Genome.
Proteomes; UP000138690; Genome.
Proteomes; UP000143093; Genome.
Proteomes; UP000145651; Genome.
Proteomes; UP000146108; Genome.
Proteomes; UP000146181; Genome.
Proteomes; UP000146296; Genome.
Proteomes; UP000148194; Genome.
Proteomes; UP000153467; Genome.
Proteomes; UP000160648; Genome.
Proteomes; UP000164441; Genome.
Proteomes; UP000172416; Genome.
GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0046789; F:host cell surface receptor binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:BHF-UCL.
Gene3D; 1.20.5.790; -; 1.
InterPro; IPR002552; Corona_S2.
InterPro; IPR027400; S_HR2.
InterPro; IPR032500; Spike_N.
InterPro; IPR018548; Spike_rcpt-bd.
InterPro; IPR036326; Spike_rcpt-bd_sf.
Pfam; PF01601; Corona_S2; 1.
Pfam; PF16451; Spike_NTD; 1.
Pfam; PF09408; Spike_rec_bind; 1.
SUPFAM; SSF143587; SSF143587; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host membrane; Host-virus interaction;
Lipoprotein; Membrane; Palmitate; Reference proteome; Signal;
Transmembrane; Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Viral penetration into host cytoplasm; Virion;
Virulence; Virus entry into host cell.
SIGNAL 1 13 {ECO:0000255}.
CHAIN 14 1255 Spike glycoprotein.
/FTId=PRO_0000037208.
CHAIN 14 667 Spike protein S1. {ECO:0000255}.
/FTId=PRO_0000037209.
CHAIN 668 1255 Spike protein S2. {ECO:0000255}.
/FTId=PRO_0000037210.
TOPO_DOM 14 1195 Extracellular. {ECO:0000255}.
TRANSMEM 1196 1216 Helical. {ECO:0000255}.
TOPO_DOM 1217 1255 Cytoplasmic. {ECO:0000255}.
REGION 306 527 Receptor-binding domain.
REGION 424 494 Receptor-binding motif; binding to human
ACE2.
REGION 770 788 Fusion peptide. {ECO:0000255}.
REGION 902 952 Heptad repeat 1.
REGION 1145 1184 Heptad repeat 2.
COILED 931 975 {ECO:0000255}.
COILED 1157 1185 {ECO:0000255}.
MOTIF 1251 1255 KxHxx.
COMPBIAS 1217 1236 Cys-rich.
SITE 667 668 Cleavage. {ECO:0000255}.
CARBOHYD 29 29 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 118 118 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 119 119 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 158 158 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 227 227 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 269 269 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 318 318 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 357 357 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 589 589 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 602 602 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 691 691 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 699 699 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 783 783 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1056 1056 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1080 1080 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1116 1116 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1140 1140 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1155 1155 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1176 1176 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 323 348
DISULFID 366 419
DISULFID 467 474
VARIANT 49 49 S -> L (in strain: Isolate GZ50).
VARIANT 77 77 G -> D (in strain: Isolate BJ01, Isolate
BJ02, Isolate BJ03, Isolate GZ50, Isolate
CUHK-W1, Isolate HKU-36871, Isolate GD01,
Isolate GD03 and Isolate SZ3).
VARIANT 78 78 N -> D (in strain: Isolate GD03).
VARIANT 118 118 N -> S (in strain: Isolate Shanghai LY).
VARIANT 139 139 A -> V (in strain: Isolate GD03).
VARIANT 144 144 M -> L (in strain: Isolate BJ03).
VARIANT 147 147 Q -> R (in strain: Isolate GD03).
VARIANT 193 193 F -> S (in strain: Isolate Shanghai LY).
VARIANT 227 227 N -> K (in strain: Isolate SZ3).
VARIANT 239 239 S -> L (in strain: Isolate GD01 and
Isolate SZ3).
VARIANT 244 244 I -> T (in strain: Isolate BJ01, Isolate
BJ02, Isolate BJ03, Isolate BJ04, Isolate
GZ50, Isolate CUHK-W1, Isolate HKU-36871,
Isolate GD01, Isolate GD03 and Isolate
SZ3).
VARIANT 261 261 T -> K (in strain: Isolate SZ3).
VARIANT 311 311 G -> R (in strain: Isolate GD01 and
Isolate BJ02).
VARIANT 344 344 K -> R (in strain: Isolate GD01, Isolate
GD03 and Isolate SZ3; no effect on
affinity with either human or palm civet
ACE2). {ECO:0000269|PubMed:15791205}.
VARIANT 360 360 F -> S (in strain: Isolate GD03 and
Isolate SZ3; no effect on affinity with
either human or palm civet ACE2).
{ECO:0000269|PubMed:15791205}.
VARIANT 426 426 R -> G (in strain: Isolate Shanghai LY).
VARIANT 437 437 N -> D (in strain: Isolate Shanghai LY).
VARIANT 472 472 L -> P (in strain: Isolate GD03).
VARIANT 479 479 N -> K (in strain: Isolate SZ3; 20fold
decrease of affinity with human ACE2; no
effect on affinity with palm civet ACE2).
{ECO:0000269|PubMed:15791205}.
VARIANT 480 480 D -> G (in strain: Isolate GD03).
VARIANT 487 487 T -> S (in strain: Isolate GD03 and
Isolate SZ3; 20fold decrease of affinity
with human ACE2; decrease of affinity
with palm civet ACE2).
{ECO:0000269|PubMed:15791205}.
VARIANT 501 501 F -> Y (in strain: Isolate GD01).
VARIANT 577 577 S -> A (in strain: Isolate Tor2 and
Isolate Shanghai QXC1).
VARIANT 605 605 D -> N (in strain: Isolate Shanghai
QXC1).
VARIANT 607 607 S -> P (in strain: Isolate SZ3).
VARIANT 608 608 T -> A (in strain: Isolate Shanghai
QXC1).
VARIANT 609 609 A -> L (in strain: Isolate GD03).
VARIANT 613 613 D -> E (in strain: Isolate GD03).
VARIANT 665 665 L -> S (in strain: Isolate GD03 and
Isolate SZ3).
VARIANT 701 701 S -> L (in strain: Isolate SZ3).
VARIANT 743 743 T -> A (in strain: Isolate SZ3).
VARIANT 743 743 T -> R (in strain: Isolate GD03).
VARIANT 754 754 A -> V (in strain: Isolate SZ3).
VARIANT 765 765 A -> V (in strain: Isolate GD03).
VARIANT 778 778 Y -> D (in strain: Isolate GD01, Isolate
GZ50, Isolate GD03 and Isolate SZ3).
VARIANT 794 794 P -> S (in strain: Isolate GD01).
VARIANT 804 804 L -> P (in strain: Isolate Shanghai LY).
VARIANT 860 861 VS -> LR (in strain: Isolate BJ03).
VARIANT 894 894 T -> A (in strain: Isolate SZ3).
VARIANT 999 999 E -> G (in strain: Isolate Shanghai LY).
VARIANT 1001 1001 R -> M (in strain: Isolate BJ04).
VARIANT 1132 1132 E -> G (in strain: Isolate Shanghai
QXC1).
VARIANT 1148 1148 L -> F (in strain: Isolate Frankfurt 1
and Isolate FRA).
VARIANT 1163 1163 K -> E (in strain: Isolate GD03 and
Isolate SZ3).
MUTAGEN 323 323 C->A: No effect on human ACE2 binding in
vitro. {ECO:0000269|PubMed:15496474}.
MUTAGEN 348 348 C->A: Complete loss of human ACE2 binding
in vitro. {ECO:0000269|PubMed:15496474}.
MUTAGEN 452 452 E->A: 90% loss of human ACE2 binding in
vitro. {ECO:0000269|PubMed:15496474}.
MUTAGEN 454 454 D->A: Complete loss of human ACE2 binding
in vitro. {ECO:0000269|PubMed:15496474}.
MUTAGEN 463 463 D->A: Partial loss of human ACE2 binding
in vitro. {ECO:0000269|PubMed:15496474}.
MUTAGEN 467 467 C->A: Complete loss of human ACE2 binding
in vitro. {ECO:0000269|PubMed:15496474}.
MUTAGEN 474 474 C->A: Complete loss of human ACE2 binding
in vitro. {ECO:0000269|PubMed:15496474}.
MUTAGEN 480 480 D->A: No effect on human ACE2 binding in
vitro. {ECO:0000269|PubMed:15496474}.
MUTAGEN 667 667 R->S: 40% loss of cell-cell fusion.
{ECO:0000269|PubMed:16519916}.
MUTAGEN 672 672 K->S: No effect on cell-cell fusion.
{ECO:0000269|PubMed:16519916}.
MUTAGEN 1251 1251 K->A: Decrease in Golgi localization, and
complete loss of COPI binding; when
associated with A-1253.
{ECO:0000269|PubMed:17166901}.
MUTAGEN 1253 1253 H->A: Decrease in Golgi localization, and
complete loss of COPI binding; when
associated with A-1251.
{ECO:0000269|PubMed:17166901}.
STRAND 31 34 {ECO:0000244|PDB:5X4S}.
STRAND 37 41 {ECO:0000244|PDB:5X58}.
STRAND 44 48 {ECO:0000244|PDB:5X58}.
STRAND 50 59 {ECO:0000244|PDB:5X4S}.
STRAND 65 72 {ECO:0000244|PDB:5X4S}.
STRAND 73 75 {ECO:0000244|PDB:5X58}.
STRAND 87 95 {ECO:0000244|PDB:5X4S}.
STRAND 100 111 {ECO:0000244|PDB:5X4S}.
STRAND 113 118 {ECO:0000244|PDB:5X4S}.
STRAND 123 141 {ECO:0000244|PDB:5X4S}.
TURN 142 144 {ECO:0000244|PDB:5X4S}.
STRAND 146 164 {ECO:0000244|PDB:5X4S}.
STRAND 177 190 {ECO:0000244|PDB:5X4S}.
STRAND 193 208 {ECO:0000244|PDB:5X4S}.
STRAND 216 222 {ECO:0000244|PDB:5X4S}.
STRAND 229 239 {ECO:0000244|PDB:5X4S}.
STRAND 250 256 {ECO:0000244|PDB:5X4S}.
STRAND 258 266 {ECO:0000244|PDB:5X4S}.
STRAND 268 270 {ECO:0000244|PDB:5X58}.
STRAND 272 277 {ECO:0000244|PDB:5X4S}.
TURN 282 288 {ECO:0000244|PDB:5X4S}.
STRAND 297 299 {ECO:0000244|PDB:5X58}.
STRAND 310 312 {ECO:0000244|PDB:5X58}.
HELIX 326 329 {ECO:0000244|PDB:2GHV}.
HELIX 337 339 {ECO:0000244|PDB:2GHV}.
STRAND 341 345 {ECO:0000244|PDB:2GHV}.
STRAND 347 349 {ECO:0000244|PDB:2GHV}.
HELIX 352 354 {ECO:0000244|PDB:2GHV}.
STRAND 362 368 {ECO:0000244|PDB:2GHV}.
HELIX 371 378 {ECO:0000244|PDB:2GHV}.
STRAND 380 390 {ECO:0000244|PDB:2GHV}.
HELIX 391 396 {ECO:0000244|PDB:2GHV}.
STRAND 397 400 {ECO:0000244|PDB:3D0G}.
HELIX 404 408 {ECO:0000244|PDB:2GHV}.
STRAND 414 416 {ECO:0000244|PDB:5X58}.
STRAND 418 424 {ECO:0000244|PDB:2GHV}.
HELIX 426 429 {ECO:0000244|PDB:2GHV}.
STRAND 431 433 {ECO:0000244|PDB:2DD8}.
STRAND 439 441 {ECO:0000244|PDB:2GHV}.
STRAND 462 464 {ECO:0000244|PDB:3D0I}.
STRAND 469 471 {ECO:0000244|PDB:2GHW}.
STRAND 478 480 {ECO:0000244|PDB:2GHV}.
STRAND 483 487 {ECO:0000244|PDB:2GHV}.
HELIX 489 491 {ECO:0000244|PDB:2GHV}.
STRAND 492 501 {ECO:0000244|PDB:2GHV}.
STRAND 509 511 {ECO:0000244|PDB:2DD8}.
STRAND 523 527 {ECO:0000244|PDB:5X58}.
STRAND 536 540 {ECO:0000244|PDB:5X58}.
STRAND 551 563 {ECO:0000244|PDB:5X58}.
TURN 565 567 {ECO:0000244|PDB:5X58}.
STRAND 570 574 {ECO:0000244|PDB:5X58}.
STRAND 583 585 {ECO:0000244|PDB:5X58}.
TURN 588 590 {ECO:0000244|PDB:5X58}.
STRAND 596 599 {ECO:0000244|PDB:5X58}.
HELIX 604 610 {ECO:0000244|PDB:5X58}.
TURN 611 613 {ECO:0000244|PDB:5X58}.
STRAND 635 638 {ECO:0000244|PDB:5X58}.
STRAND 649 653 {ECO:0000244|PDB:5X58}.
STRAND 656 659 {ECO:0000244|PDB:5X58}.
STRAND 675 678 {ECO:0000244|PDB:5X58}.
STRAND 682 685 {ECO:0000244|PDB:5X58}.
STRAND 691 698 {ECO:0000244|PDB:5X58}.
STRAND 704 710 {ECO:0000244|PDB:5X58}.
HELIX 720 725 {ECO:0000244|PDB:5X58}.
HELIX 730 735 {ECO:0000244|PDB:5X58}.
HELIX 736 738 {ECO:0000244|PDB:5X58}.
STRAND 740 744 {ECO:0000244|PDB:5X58}.
HELIX 745 764 {ECO:0000244|PDB:5X58}.
STRAND 768 771 {ECO:0000244|PDB:5X58}.
HELIX 773 777 {ECO:0000244|PDB:2RUM}.
HELIX 780 783 {ECO:0000244|PDB:2RUM}.
TURN 784 786 {ECO:0000244|PDB:2RUM}.
STRAND 790 792 {ECO:0000244|PDB:5X58}.
STRAND 794 797 {ECO:0000244|PDB:5X58}.
HELIX 799 806 {ECO:0000244|PDB:5X58}.
HELIX 813 817 {ECO:0000244|PDB:5XJK}.
HELIX 818 820 {ECO:0000244|PDB:5XJK}.
HELIX 849 865 {ECO:0000244|PDB:5X58}.
HELIX 869 872 {ECO:0000244|PDB:5X58}.
HELIX 880 891 {ECO:0000244|PDB:5X58}.
STRAND 898 900 {ECO:0000244|PDB:2BEZ}.
HELIX 915 948 {ECO:0000244|PDB:2BEQ}.
HELIX 959 963 {ECO:0000244|PDB:5X58}.
TURN 964 969 {ECO:0000244|PDB:5X58}.
HELIX 971 1013 {ECO:0000244|PDB:5X58}.
TURN 1014 1016 {ECO:0000244|PDB:5X58}.
STRAND 1027 1032 {ECO:0000244|PDB:5X58}.
STRAND 1035 1038 {ECO:0000244|PDB:5X58}.
STRAND 1041 1048 {ECO:0000244|PDB:5X58}.
STRAND 1054 1059 {ECO:0000244|PDB:5X58}.
STRAND 1061 1063 {ECO:0000244|PDB:5X58}.
STRAND 1066 1068 {ECO:0000244|PDB:5X58}.
STRAND 1070 1074 {ECO:0000244|PDB:5X58}.
STRAND 1078 1080 {ECO:0000244|PDB:5X58}.
STRAND 1083 1086 {ECO:0000244|PDB:5X58}.
HELIX 1148 1151 {ECO:0000244|PDB:2FXP}.
HELIX 1162 1172 {ECO:0000244|PDB:2BEQ}.
HELIX 1173 1178 {ECO:0000244|PDB:2BEQ}.
HELIX 1182 1192 {ECO:0000244|PDB:2BEQ}.
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


Related products :

Catalog number Product name Quantity
20-663-48070 SARS Spike protein - Mouse Anti SARS Spike protein; S glycoprotein; Peplomer protein; E2 Monoclonal 0.1 mg
20-663-48070 SARS Spike protein - Mouse Anti SARS Spike protein; S glycoprotein; Peplomer protein; E2 Monoclonal 0.2 mg
10-271-82347 SARS-Associated Coronavirus Spike mosaic S(M) - S glycoprotein; Peplomer protein; E2 1 mg
10-271-82346 SARS-Associated Coronavirus Spike mosaic S(C) - S glycoprotein; Peplomer protein; E2 1 mg
orb81530 SARS Associated Spike Mosaic S(M) protein The E.coli derived 38 kDa recombinant mosaic protein contains the middle section of the Spike protein 408-470, 540-573 amino acids immunodominant regions. For 100
orb81529 SARS Associated Spike Mosaic S(N) protein The E.coli derived 38 kDa mosaic protein contains the N-terminal section of the Spike protein 12-53, 90-115, 171-203 amino acids immunodominant regions. For r 100
SCH-OBT1901 RECOMBINANT SARS SPIKE PROTEIN, Product Type Recombinant Protein, Specificity SARS SPIKE PROTEIN, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, Clone 0.1 mg
OBT1901X RECOMBINANT SARS SPIKE PROTEIN, Product Type Recombinant Protein, Specificity SARS SPIKE PROTEIN, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, WB, Clone 1 mg
SCH-OBT1901X RECOMBINANT SARS SPIKE PROTEIN, Product Type Recombinant Protein, Specificity SARS SPIKE PROTEIN, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, WB, Clone 1 mg
OBT1901 RECOMBINANT SARS SPIKE PROTEIN, Product Type Recombinant Protein, Specificity SARS SPIKE PROTEIN, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, Clone 0.1 mg
18-663-49005 SARS Spike Protein - Rabbit Anti SARS Spike Protein Polyclonal 0.1 mg
18-663-49005 SARS Spike Protein - Rabbit Anti SARS Spike Protein Polyclonal 0.2 mg
RANT-157C SARS Spike Polyclonal Rabbit Anti SARS Spike Protein 300µg
RANT-157B SARS Spike Polyclonal Rabbit Anti SARS Spike Protein 200µg
RANT-157A SARS Spike Polyclonal Rabbit Anti SARS Spike Protein 100µg
orb82497 SARS-CoV, Spike (N-term) recombinant protein SARS-Associated Coronavirus (SARS-CoV) Spike protein (N-terminal) Recombinant is an infectious disease antigen_toxin. For research use only. 1 mg
orb82489 SARS-CoV, Spike (C-term) recombinant protein SARS-Associated Coronavirus (SARS-CoV) Spike protein (C-terminal) Recombinant is an infectious disease antigen_toxin. For research use only. 1 mg
OBT1902X RECOMBINANT SARS SPIKE MOSAIC S(M) (aa408_470 540_573), Product Type Recombinant Protein, Specificity SARS SPIKE MOSAIC, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applicati 1 mg
SCH-OBT1902X RECOMBINANT SARS SPIKE MOSAIC S(M) (aa408_470 540_573), Product Type Recombinant Protein, Specificity SARS SPIKE MOSAIC, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applicati 1 mg
SCH-OBT1903X RECOMBINANT SARS SPIKE MOSAIC S(C) (aa1051_1076 1121_1154 1162_1190), Product Type Recombinant Protein, Specificity SARS SPIKE MOSAIC, Target Species Viral, Host N_A, Format Rec. Protein, Isotype 1 mg
OBT1903X RECOMBINANT SARS SPIKE MOSAIC S(C) (aa1051_1076 1121_1154 1162_1190), Product Type Recombinant Protein, Specificity SARS SPIKE MOSAIC, Target Species Viral, Host N_A, Format Rec. Protein, Isotype 1 mg
ant-157 Polyclonal Rabbit Anti SARS Spike Protein SARS Spike 100
ant-157 Polyclonal Rabbit Anti SARS Spike Protein SARS Spike 200
ant-157 Polyclonal Rabbit Anti SARS Spike Protein SARS Spike 300
SCH-AHP889 RABBIT ANTI SARS SPIKE PROTEIN (N_TERMINAL), Product Type Polyclonal Antibody, Specificity SARS SPIKE PROTEIN , Target Species Viral, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Appli 0.1 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur