ID SPIKE_SARS2 Reviewed; 1273 AA.
AC P0DTC2;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 1.
DT 10-FEB-2021, entry version 6.
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 2 (2019-nCoV) (SARS-CoV-2).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Sarbecovirus.
OX NCBI_TaxID=2697049;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=32015508; DOI=10.1038/s41586-020-2008-3;
RA Wu F., Zhao S., Yu B., Chen Y.-M., Wang W., Song Z.-G., Hu Y., Tao Z.-W.,
RA Tian J.-H., Pei Y.-Y., Yuan M.-L., Zhang Y.-L., Dai F.-H., Liu Y.,
RA Wang Q.-M., Zheng J.-J., Xu L., Holmes E.C., Zhang Y.-Z.;
RT "A new coronavirus associated with human respiratory disease in China.";
RL Nature 579:265-269(2020).
RN [2]
RP FUNCTION (SPIKE PROTEIN S1), AND CLEAVAGE BETWEEN S1 AND S2 BY HOST
RP TMPRSS2.
RX PubMed=32142651; DOI=10.1016/j.cell.2020.02.052;
RA Hoffmann M., Kleine-Weber H., Schroeder S., Krueger N., Herrler T.,
RA Erichsen S., Schiergens T.S., Herrler G., Wu N.H., Nitsche A.,
RA Mueller M.A., Drosten C., Poehlmann S.;
RT "SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a
RT clinically proven protease inhibitor.";
RL Cell 181:1-10(2020).
RN [3]
RP CLEAVAGE BETWEEN S1 AND S2 BY HOST FURIN, FUNCTION, AND MUTAGENESIS OF
RP 681-PRO--ALA-684.
RX PubMed=32362314; DOI=10.1016/j.molcel.2020.04.022;
RA Hoffmann M., Kleine-Weber H., Poehlmann S.;
RT "A multibasic cleavage site in the Spike protein of SARS-CoV-2 is essential
RT for infection of human lung cells.";
RL Mol. Cell 0:0-0(2020).
RN [4]
RP GLYCOSYLATION AT ASN-17; ASN-61; ASN-74; ASN-122; ASN-149; ASN-165;
RP ASN-234; ASN-282; ASN-331; ASN-343; ASN-603; ASN-616; ASN-657; ASN-709;
RP ASN-717; ASN-801; ASN-1074; ASN-1098; ASN-1134; ASN-1158; ASN-1173 AND
RP ASN-1194, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=32366695; DOI=10.1126/science.abb9983;
RA Watanabe Y., Allen J.D., Wrapp D., McLellan J.S., Crispin M.;
RT "Site-specific glycan analysis of the SARS-CoV-2 spike.";
RL Science 0:0-0(2020).
RN [5]
RP GLYCOSYLATION AT ASN-61; ASN-74; ASN-122; ASN-149; ASN-165; ASN-234;
RP ASN-282; THR-323; SER-325; ASN-331; ASN-343; ASN-616; ASN-657; ASN-709;
RP ASN-717; ASN-801; ASN-1074; ASN-1098 AND ASN-1194, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=32363391; DOI=10.1093/glycob/cwaa042;
RA Shajahan A., Supekar N.T., Gleinich A.S., Azadi P.;
RT "Deducing the N- and O- glycosylation profile of the spike protein of novel
RT coronavirus SARS-CoV-2.";
RL Glycobiology 0:0-0(2020).
RN [6]
RP VARIANT GLY-614.
RX PubMed=32820179; DOI=10.1038/s41598-020-70827-z;
RA Isabel S., Grana-Miraglia L., Gutierrez J.M., Bundalovic-Torma C.,
RA Groves H.E., Isabel M.R., Eshaghi A., Patel S.N., Gubbay J.B., Poutanen T.,
RA Guttman D.S., Poutanen S.M.;
RT "Evolutionary and structural analyses of SARS-CoV-2 D614G spike protein
RT mutation now documented worldwide.";
RL Sci. Rep. 10:14031-14031(2020).
RN [7]
RP VARIANT GLY-614, AND MUTAGENESIS OF ASP-614.
RX PubMed=32697968; DOI=10.1016/j.cell.2020.06.043;
RG Sheffield COVID-19 Genomics Group;
RA Korber B., Fischer W.M., Gnanakaran S., Yoon H., Theiler J., Abfalterer W.,
RA Hengartner N., Giorgi E.E., Bhattacharya T., Foley B., Hastie K.M.,
RA Parker M.D., Partridge D.G., Evans C.M., Freeman T.M., de Silva T.I.,
RA McDanal C., Perez L.G., Tang H., Moon-Walker A., Whelan S.P.,
RA LaBranche C.C., Saphire E.O., Montefiori D.C.;
RT "Tracking Changes in SARS-CoV-2 Spike: Evidence that D614G Increases
RT Infectivity of the COVID-19 Virus.";
RL Cell 182:812-827(2020).
RN [8]
RP FUNCTION.
RX PubMed=32817270; DOI=10.1126/science.abd5223;
RA Turonova B., Sikora M., Schuermann C., Hagen W.J.H., Welsch S.,
RA Blanc F.E.C., von Buelow S., Gecht M., Bagola K., Hoerner C.,
RA van Zandbergen G., Landry J., de Azevedo N.T.D., Mosalaganti S.,
RA Schwarz A., Covino R., Muehlebach M.D., Hummer G., Krijnse Locker J.,
RA Beck M.;
RT "In situ structural analysis of SARS-CoV-2 spike reveals flexibility
RT mediated by three hinges.";
RL Science 0:0-0(2020).
RN [9]
RP GLYCOSYLATION.
RX PubMed=32929138; DOI=10.1038/s41598-020-71748-7;
RA Grant O.C., Montgomery D., Ito K., Woods R.J.;
RT "Analysis of the SARS-CoV-2 spike protein glycan shield reveals
RT implications for immune recognition.";
RL Sci. Rep. 10:14991-14991(2020).
RN [10]
RP GLYCOSYLATION AT ASN-17; ASN-61; ASN-74; ASN-122; ASN-149; ASN-165;
RP ASN-234; ASN-282; ASN-331; ASN-343; ASN-603; ASN-616; ASN-657; ASN-709;
RP ASN-717; ASN-801; ASN-1074; ASN-1098; ASN-1134; ASN-1158; ASN-1173 AND
RP ASN-1194, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=32979942; DOI=10.1016/j.cell.2020.09.018;
RA Yao H., Song Y., Chen Y., Wu N., Xu J., Sun C., Zhang J., Weng T.,
RA Zhang Z., Wu Z., Cheng L., Shi D., Lu X., Lei J., Crispin M., Shi Y.,
RA Li L., Li S.;
RT "Molecular Architecture of the SARS-CoV-2 Virus.";
RL Cell 0:0-0(2020).
RN [11]
RP VARIANT GLY-614, AND MUTAGENESIS OF ASP-614.
RX PubMed=33106671; DOI=10.1038/s41586-020-2895-3;
RA Plante J.A., Liu Y., Liu J., Xia H., Johnson B.A., Lokugamage K.G.,
RA Zhang X., Muruato A.E., Zou J., Fontes-Garfias C.R., Mirchandani D.,
RA Scharton D., Bilello J.P., Ku Z., An Z., Kalveram B., Freiberg A.N.,
RA Menachery V.D., Xie X., Plante K.S., Weaver S.C., Shi P.Y.;
RT "Spike mutation D614G alters SARS-CoV-2 fitness.";
RL Nature 0:0-0(2020).
RN [12]
RP FUNCTION, AND INTERACTION WITH HUMAN NRP1 AND NRP2.
RC STRAIN=SARS-CoV-2/human/Liverpool/REMRQ001/2020;
RX PubMed=33082294; DOI=10.1126/science.abd3072;
RA Daly J.L., Simonetti B., Klein K., Chen K.E., Williamson M.K.,
RA Anton-Plagaro C., Shoemark D.K., Simon-Gracia L., Bauer M., Hollandi R.,
RA Greber U.F., Horvath P., Sessions R.B., Helenius A., Hiscox J.A.,
RA Teesalu T., Matthews D.A., Davidson A.D., Collins B.M., Cullen P.J.,
RA Yamauchi Y.;
RT "Neuropilin-1 is a host factor for SARS-CoV-2 infection.";
RL Science 0:0-0(2020).
RN [13]
RP FUNCTION, AND INTERACTION WITH HUMAN NRP1 AND NRP2.
RC STRAIN=SARS-CoV-2/human/Finland/1/2020;
RX PubMed=33082293; DOI=10.1126/science.abd2985;
RA Cantuti-Castelvetri L., Ojha R., Pedro L.D., Djannatian M., Franz J.,
RA Kuivanen S., van der Meer F., Kallio K., Kaya T., Anastasina M., Smura T.,
RA Levanov L., Szirovicza L., Tobi A., Kallio-Kokko H., Oesterlund P.,
RA Joensuu M., Meunier F.A., Butcher S.J., Winkler M.S., Mollenhauer B.,
RA Helenius A., Gokce O., Teesalu T., Hepojoki J., Vapalahti O.,
RA Stadelmann C., Balistreri G., Simons M.;
RT "Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity.";
RL Science 0:0-0(2020).
RN [14]
RP INTERACTION WITH HUMAN ITGA5 AND ITGB1.
RX PubMed=33102950; DOI=10.1016/j.jacbts.2020.10.003;
RA Beddingfield B.J., Iwanaga N., Chapagain P.P., Zheng W., Roy C.J., Hu T.Y.,
RA Kolls J.K., Bix G.J.;
RT "The Integrin Binding Peptide, ATN-161, as a Novel Therapy for SARS-CoV-2
RT Infection.";
RL JACC Basic Transl. Sci. 0:0-0(2020).
RN [15] {ECO:0000244|PDB:6M17}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS), FUNCTION (SPIKE PROTEIN
RP S1), DOMAIN, AND INTERACTION WITH HUMAN ACE2 (SPIKE PROTEIN S1).
RX PubMed=32132184; DOI=10.1126/science.abb2762;
RA Yan R., Zhang Y., Li Y., Xia L., Guo Y., Zhou Q.;
RT "Structural basis for the recognition of the SARS-CoV-2 by full-length
RT human ACE2.";
RL Science 0:0-0(2020).
RN [16] {ECO:0000244|PDB:6VSB}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.46 ANGSTROMS), FUNCTION (SPIKE PROTEIN
RP S1), INTERACTION WITH HUMAN ACE2 (SPIKE PROTEIN S1), SUBUNIT, AND
RP GLYCOSYLATION.
RX PubMed=32075877; DOI=10.1126/science.abb2507;
RA Wrapp D., Wang N., Corbett K.S., Goldsmith J.A., Hsieh C.L., Abiona O.,
RA Graham B.S., McLellan J.S.;
RT "Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation.";
RL Science 367:1260-1263(2020).
RN [17] {ECO:0000244|PDB:6VXX, ECO:0000244|PDB:6VYB}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS), FUNCTION (SPIKE PROTEIN
RP S1), SUBUNIT (SPIKE PROTEIN S1), INTERACTION WITH HUMAN ACE2 (SPIKE PROTEIN
RP S1), MUTAGENESIS OF 679-GLN--ALA-684, GLYCOSYLATION AT ASN-61; ASN-122;
RP ASN-61; ASN-165; ASN-234; ASN-282; ASN-331; ASN-343; ASN-603; ASN-616;
RP ASN-657; ASN-709; ASN-717; ASN-801; ASN-1074; ASN-1098 AND ASN-1134, AND
RP DISULFIDE BOND.
RX PubMed=32155444; DOI=10.1016/j.cell.2020.02.058;
RA Walls A.C., Park Y.J., Tortorici M.A., Wall A., McGuire A.T., Veesler D.;
RT "Structure, function, and antigenicity of the SARS-CoV-2 spike
RT glycoprotein.";
RL Cell 180:1-12(2020).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF SPIKE PROTEIN S1 AND IN COMPLEX
RP WITH HOST ACE2.
RX PubMed=32225176; DOI=10.1038/s41586-020-2180-5;
RA Lan J., Ge J., Yu J., Shan S., Zhou H., Fan S., Zhang Q., Shi X., Wang Q.,
RA Zhang L., Wang X.;
RT "Structure of the SARS-CoV-2 spike receptor-binding domain bound to the
RT ACE2 receptor.";
RL Nature 0:0-0(2020).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF SPIKE PROTEIN S1 AND IN COMPLEX
RP WITH HOST ACE2, INTERACTION WITH HOST ACE2, AND MUTAGENESIS OF GLN-493 AND
RP ASN-501.
RX PubMed=32225175; DOI=10.1038/s41586-020-2179-y;
RA Shang J., Ye G., Shi K., Wan Y., Luo C., Aihara H., Geng Q., Auerbach A.,
RA Li F.;
RT "Structural basis of receptor recognition by SARS-CoV-2.";
RL Nature 0:0-0(2020).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (3.08 ANGSTROMS) OF SPIKE PROTEIN S1 AND IN COMPLEX
RP WITH HUMAN ANTIBODY CR3022, AND DISULFIDE BOND.
RX PubMed=32245784; DOI=10.1126/science.abb7269;
RA Yuan M., Wu N.C., Zhu X., Lee C.D., So R.T.Y., Lv H., Mok C.K.P.,
RA Wilson I.A.;
RT "A highly conserved cryptic epitope in the receptor-binding domains of
RT SARS-CoV-2 and SARS-CoV.";
RL Science 0:0-0(2020).
CC -!- FUNCTION: [Spike protein S1]: attaches the virion to the cell membrane
CC by interacting with host receptor, initiating the infection. Binding to
CC human ACE2 receptor and internalization of the virus into the endosomes
CC of the host cell induces conformational changes in the Spike
CC glycoprotein (PubMed:32142651, PubMed:32075877, PubMed:32155444).
CC Binding to host NRP1 and NRP2 via C-terminal polybasic sequence
CC enhances virion entry into host cell (PubMed:33082294,
CC PubMed:33082293). This interaction may explain virus tropism of human
CC olfactory epithelium cells, which express high level of NRP1 and NRP2
CC but low level of ACE2 (PubMed:33082293). The stalk domain of S contains
CC three hinges, giving the head unexpected orientational freedom
CC (PubMed:32817270). Uses human TMPRSS2 for priming in human lung cells
CC which is an essential step for viral entry (PubMed:32142651). Can be
CC alternatively processed by host furin (PubMed:32362314). Proteolysis by
CC cathepsin CTSL may unmask the fusion peptide of S2 and activate
CC membranes fusion within endosomes. {ECO:0000255|HAMAP-Rule:MF_04099,
CC ECO:0000269|PubMed:32075877, ECO:0000269|PubMed:32142651,
CC ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32362314,
CC ECO:0000269|PubMed:32817270, ECO:0000269|PubMed:33082293,
CC ECO:0000269|PubMed:33082294, ECO:0000303|PubMed:33082293}.
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}.
CC -!- FUNCTION: [Spike glycoprotein]: May down-regulate host tetherin (BST2)
CC by lysosomal degradation, thereby counteracting its antiviral activity.
CC {ECO:0000250|UniProtKB:P59594}.
CC -!- SUBUNIT: [Spike glycoprotein]: Homotrimer; each monomer consists of a
CC S1 and a S2 subunit (PubMed:32075877, PubMed:32155444,
CC PubMed:32245784). The resulting peplomers protrude from the virus
CC surface as spikes (PubMed:32979942). Interacts with ORF3a protein and
CC ORF7a protein (By similarity) (PubMed:32075877, PubMed:32155444,
CC PubMed:32245784, PubMed:32979942). There are an average of 26 +/-15
CC spike trimers at the surface of virion particles (PubMed:32979942).
CC {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32075877,
CC ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32245784,
CC ECO:0000269|PubMed:32979942}.
CC -!- SUBUNIT: [Spike protein S1]: Binds to host ACE2 (PubMed:32075877,
CC PubMed:32132184, PubMed:32155444, PubMed:32225175, PubMed:32225176).
CC Cleavage of S generates a polybasic C-terminal sequence on S1 that
CC binds to host Neuropilin-1 (NRP1) and Neuropilin-2 (NRP2) receptors
CC (PubMed:33082294, PubMed:33082293). Interacts with host integrin alpha-
CC 5/beta-1 (ITGA5:ITGB1) and with ACE2 in complex with integrin alpha-
CC 5/beta-1 (ITGA5:ITGB1) (PubMed:33102950). {ECO:0000269|PubMed:32075877,
CC ECO:0000269|PubMed:32132184, ECO:0000269|PubMed:32155444,
CC ECO:0000269|PubMed:32225175, ECO:0000269|PubMed:32225176,
CC ECO:0000269|PubMed:33082293, ECO:0000269|PubMed:33082294,
CC ECO:0000269|PubMed:33102950}.
CC -!- INTERACTION:
CC P0DTC2; P0DTC2: S; NbExp=13; IntAct=EBI-25474821, EBI-25474821;
CC P0DTC2; Q9BYF1: ACE2; Xeno; NbExp=84; IntAct=EBI-25474821, EBI-7730807;
CC P0DTC2; P35613: BSG; Xeno; NbExp=5; IntAct=EBI-25474821, EBI-750709;
CC P0DTC2; Q9NNX6: CD209; Xeno; NbExp=4; IntAct=EBI-25474821, EBI-9257341;
CC P0DTC2; Q8IUN9-2: CLEC10A; Xeno; NbExp=3; IntAct=EBI-25474821, EBI-25776912;
CC P0DTC2; Q9H2X3: CLEC4M; Xeno; NbExp=5; IntAct=EBI-25474821, EBI-1391211;
CC P0DTC2; P09958: FURIN; Xeno; NbExp=4; IntAct=EBI-25474821, EBI-1056807;
CC P0DTC2; Q96D42: HAVCR1; Xeno; NbExp=5; IntAct=EBI-25474821, EBI-953786;
CC P0DTC2; Q61830: Mrc1; Xeno; NbExp=2; IntAct=EBI-25474821, EBI-642509;
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04099,
CC ECO:0000269|PubMed:32979942}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04099}. Host endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099};
CC Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}.
CC Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type
CC I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Note=Accumulates
CC in the endoplasmic reticulum-Golgi intermediate compartment, where it
CC participates in virus particle assembly. Colocalizes with S in the host
CC endoplasmic reticulum-Golgi intermediate compartment. Some S oligomers
CC are transported to the host plasma membrane, where they may mediate
CC cell-cell fusion (By similarity). An average of 26 +/-15 S trimers are
CC found randomly distributed at the surface of the virion
CC (PubMed:32979942). {ECO:0000255|HAMAP-Rule:MF_04099,
CC ECO:0000269|PubMed:32979942}.
CC -!- DOMAIN: The KxHxx motif seems to function as an ER retrieval and binds
CC COPI in vitro. {ECO:0000250|UniProtKB:P59594}.
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}.
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 -!- 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
CC (PubMed:32155444). Additionally, a second cleavage leads to the release
CC of a fusion peptide after viral attachment to host cell receptor (By
CC similarity). The presence of a furin polybasic cleavage site sets SARS-
CC CoV-2 S apart from SARS-CoV S that possesses a monobasic S1/S2 cleavage
CC site processed upon entry of target cells (PubMed:32155444,
CC PubMed:32362314). {ECO:0000255|HAMAP-Rule:MF_04099,
CC ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32362314}.
CC -!- PTM: Highly decorated by heterogeneous N-linked glycans protruding from
CC the trimer surface (PubMed:32075877, PubMed:32155444, PubMed:32929138).
CC Highly glycosylated by host both on S1 and S2 subunits, occluding many
CC regions across the surface of the protein (PubMed:32366695,
CC PubMed:32363391, PubMed:32929138). Approximately 40% of the protein
CC surface is shielded from antibody recognition by glycans, with the
CC notable exception of the ACE2 receptor binding domain
CC (PubMed:32929138). {ECO:0000269|PubMed:32075877,
CC ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
CC ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32929138}.
CC -!- MISCELLANEOUS: Variant D614G has become the most prevalent circulating
CC sequence in the global pandemic since april 2020 (PubMed:32697968). The
CC mutation is associated with higher viral loads produced in cell culture
CC and animal models (PubMed:32697968, PubMed:33106671). It may be
CC prevalent because the mutation increases virus transmission in human
CC population (PubMed:33106671). {ECO:0000269|PubMed:32697968,
CC ECO:0000269|PubMed:33106671}.
CC -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- CAUTION: Asn-17, Asn-603, Asn-1134, Asn-1158, and Asn-1173 are non
CC glycosylated when S1 or S2 are expressed individually in HEK293 cells.
CC {ECO:0000269|PubMed:32363391}.
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DR EMBL; MN908947; QHD43416.1; -; Genomic_RNA.
DR RefSeq; YP_009724390.1; NC_045512.2.
DR PDB; 6LVN; X-ray; 2.47 A; A/B/C/D=1168-1203.
DR PDB; 6LXT; X-ray; 2.90 A; A/B/C/D/E/F=910-988, A/B/C/D/E/F=1162-1206.
DR PDB; 6LZG; X-ray; 2.50 A; B=319-527.
DR PDB; 6M0J; X-ray; 2.45 A; E=319-541.
DR PDB; 6M17; EM; 2.90 A; E/F=319-541.
DR PDB; 6M1V; X-ray; 1.50 A; A=917-966.
DR PDB; 6VSB; EM; 3.46 A; A/B/C=1-1208.
DR PDB; 6VW1; X-ray; 2.68 A; E/F=455-518.
DR PDB; 6VXX; EM; 2.80 A; A/B/C=14-1211.
DR PDB; 6VYB; EM; 3.20 A; A/B/C=14-1211.
DR PDB; 6W41; X-ray; 3.08 A; C=319-541.
DR PDB; 6WPS; EM; 3.10 A; A/B/E=11-1211.
DR PDB; 6WPT; EM; 3.70 A; A/B/C=11-1211.
DR PDB; 6X29; EM; 2.70 A; A/B/C=16-1208.
DR PDB; 6X2A; EM; 3.30 A; A/B/C=16-1208.
DR PDB; 6X2B; EM; 3.60 A; A/B/C=16-1208.
DR PDB; 6X2C; EM; 3.20 A; A/B/C=16-1208.
DR PDB; 6X6P; EM; 3.22 A; A/B/C=15-1208.
DR PDB; 6X79; EM; 2.90 A; A/B/C=14-1211.
DR PDB; 6XC2; X-ray; 3.11 A; A/Z=319-541.
DR PDB; 6XC3; X-ray; 2.70 A; C=319-541.
DR PDB; 6XC4; X-ray; 2.34 A; A/Z=319-541.
DR PDB; 6XC7; X-ray; 2.88 A; A=319-541.
DR PDB; 6XCM; EM; 3.42 A; A/B/C=1-1213.
DR PDB; 6XCN; EM; 3.66 A; A/C/E=1-1213.
DR PDB; 6XDG; EM; 3.90 A; E=319-541.
DR PDB; 6XE1; X-ray; 2.75 A; E=319-591.
DR PDB; 6XEY; EM; 3.25 A; A/B/C=1-1208.
DR PDB; 6XF5; EM; 3.45 A; A/B/C=14-1208.
DR PDB; 6XF6; EM; 4.00 A; A/B/C=14-1208.
DR PDB; 6XKL; EM; 3.21 A; A/B/C=1-1208.
DR PDB; 6XKP; X-ray; 2.72 A; A/B=319-541.
DR PDB; 6XKQ; X-ray; 2.55 A; A=319-541.
DR PDB; 6XLU; EM; 2.40 A; A/B/C=14-1208.
DR PDB; 6XM0; EM; 2.70 A; A/B/C=14-1208.
DR PDB; 6XM3; EM; 2.90 A; A/B/C=14-1208.
DR PDB; 6XM4; EM; 2.90 A; A/B/C=14-1208.
DR PDB; 6XM5; EM; 3.10 A; A/B/C=14-1208.
DR PDB; 6XR8; EM; 2.90 A; A/B/C=1-1273.
DR PDB; 6XRA; EM; 3.00 A; A/B/C=1-1273.
DR PDB; 6XS6; EM; 3.70 A; A/B/C=1-1213.
DR PDB; 6YLA; X-ray; 2.42 A; A/E=330-532.
DR PDB; 6YM0; X-ray; 4.36 A; E=330-532.
DR PDB; 6YOR; EM; 3.30 A; A/E=330-532.
DR PDB; 6YZ5; X-ray; 1.80 A; E=330-532.
DR PDB; 6YZ7; X-ray; 3.30 A; AAA/EEE=330-532.
DR PDB; 6Z2M; X-ray; 2.71 A; A/E=332-528.
DR PDB; 6Z43; EM; 3.30 A; A/B/C=1-1208.
DR PDB; 6Z97; EM; 3.40 A; A/B/C=1-1208.
DR PDB; 6ZB4; EM; 3.03 A; A/B/C=1-1213.
DR PDB; 6ZB5; EM; 2.85 A; A/B/C=1-1213.
DR PDB; 6ZBP; X-ray; 1.85 A; EEE=330-532.
DR PDB; 6ZCZ; X-ray; 2.65 A; E=333-528.
DR PDB; 6ZDG; EM; 4.70 A; A/D/E=333-526.
DR PDB; 6ZDH; EM; 3.70 A; A/B/C=1-1208.
DR PDB; 6ZER; X-ray; 3.80 A; A/D/E=330-532.
DR PDB; 6ZFO; EM; 4.40 A; A/E=333-526.
DR PDB; 6ZGE; EM; 2.60 A; A/B/C=1-1208.
DR PDB; 6ZGG; EM; 3.80 A; A/B/C=1-1208.
DR PDB; 6ZGI; EM; 2.90 A; A/B/C=1-1208.
DR PDB; 6ZH9; X-ray; 3.31 A; EEE=332-528.
DR PDB; 6ZHD; EM; 3.70 A; A/B/C=1-1208.
DR PDB; 6ZOW; EM; 3.00 A; A/B/C/a=1-1273.
DR PDB; 6ZOX; EM; 3.00 A; A/B/C=14-1211.
DR PDB; 6ZOY; EM; 3.10 A; A/B/C=14-1211.
DR PDB; 6ZOZ; EM; 3.50 A; A/B/C=14-1211.
DR PDB; 6ZP0; EM; 3.00 A; A/B/C=14-1211.
DR PDB; 6ZP1; EM; 3.30 A; A/B/C=14-1211.
DR PDB; 6ZP2; EM; 3.10 A; A/B/C=14-1211.
DR PDB; 6ZP5; EM; 3.10 A; A/B/C=1-1273.
DR PDB; 6ZP7; EM; 3.30 A; A/B/C=1-1273.
DR PDB; 6ZWV; EM; 3.50 A; A/B/C=1-1273.
DR PDB; 6ZXN; EM; 2.93 A; A/B/C=1-1208.
DR PDB; 7A29; EM; 2.94 A; A/B/C=1-1208.
DR PDB; 7A4N; EM; 2.75 A; A/B/C=1-1208.
DR PDB; 7A5R; EM; 3.70 A; A/B=1-1208.
DR PDB; 7A5S; EM; 3.90 A; A/B=1-1208.
DR PDB; 7A91; EM; 3.60 A; A=1-685.
DR PDB; 7A92; EM; 4.20 A; A=1-676.
DR PDB; 7A93; EM; 5.90 A; A/B/C=1-1208.
DR PDB; 7A94; EM; 3.90 A; A/B/C=1-1208.
DR PDB; 7A95; EM; 4.30 A; A/B/C=1-1208.
DR PDB; 7A96; EM; 4.80 A; A/B/C=1-1208.
DR PDB; 7A97; EM; 4.40 A; A/B/C=1-1208.
DR PDB; 7A98; EM; 5.40 A; A/B/C=1-1208.
DR PDB; 7AD1; EM; 2.92 A; A/B/C=1-1208.
DR PDB; 7BWJ; X-ray; 2.85 A; E=319-529.
DR PDB; 7BYR; EM; 3.84 A; A/B/C=1-1208.
DR PDB; 7BZ5; X-ray; 1.84 A; A=319-541.
DR PDB; 7C01; X-ray; 2.88 A; A/B=319-541.
DR PDB; 7C2L; EM; 3.10 A; A/B/C=1-1273.
DR PDB; 7C8D; EM; 3.00 A; B=333-527.
DR PDB; 7C8V; X-ray; 2.15 A; B=330-531.
DR PDB; 7C8W; X-ray; 2.77 A; B=330-531.
DR PDB; 7CAH; EM; 3.90 A; A=334-527.
DR PDB; 7CAI; EM; 3.49 A; A/B/C=1-1208.
DR PDB; 7CAK; EM; 3.58 A; A/B/C=1-1208.
DR PDB; 7CAN; X-ray; 2.94 A; B=330-531.
DR PDB; 7CH4; X-ray; 3.15 A; R=319-541.
DR PDB; 7CH5; X-ray; 2.70 A; R=319-541.
DR PDB; 7CHB; X-ray; 2.40 A; R=319-541.
DR PDB; 7CHC; X-ray; 2.71 A; R=319-541.
DR PDB; 7CHE; X-ray; 3.42 A; R=319-541.
DR PDB; 7CHF; X-ray; 2.67 A; R=319-541.
DR PDB; 7CHH; EM; 3.49 A; A/B/C=1-1208.
DR PDB; 7CN9; EM; 4.70 A; A/B/C=14-1140.
DR PDB; 7JJC; X-ray; 2.36 A; E/F/G/H=679-685.
DR PDB; 7JJI; EM; 3.60 A; A/B/C=1-1273.
DR PDB; 7JJJ; EM; 4.50 A; A/B/C/D/E/F=1-1273.
DR PDB; 7JMO; X-ray; 2.36 A; A=319-541.
DR PDB; 7JMP; X-ray; 1.71 A; A=319-541.
DR PDB; 7JMW; X-ray; 2.89 A; A=319-541.
DR PDB; 7JV2; EM; 3.50 A; A=14-1211.
DR PDB; 7JV4; EM; 3.40 A; A/B/C=14-1211.
DR PDB; 7JV6; EM; 3.00 A; A/B/E=14-1211.
DR PDB; 7JVA; EM; 3.60 A; A=14-1211.
DR PDB; 7JVC; EM; 3.30 A; A/B/E=14-1211.
DR PDB; 7JW0; EM; 4.30 A; A/B/E=14-1211.
DR PDB; 7JWB; EM; 6.00 A; A/B/C=1-1208.
DR PDB; 7JX3; X-ray; 2.65 A; R=328-531.
DR PDB; 7JZL; EM; 2.70 A; A/B/C=1-1208.
DR PDB; 7JZM; EM; 3.50 A; B=1-1208.
DR PDB; 7JZN; EM; 3.10 A; A/B/C=1-1208.
DR PDB; 7JZU; EM; 3.10 A; B=1-1208.
DR PDB; 7K43; EM; 2.60 A; A/B/E=14-1211.
DR PDB; 7K45; EM; 3.70 A; B=1-1208.
DR PDB; 7K4N; EM; 3.30 A; A/B/E=1-1208.
DR PDB; 7K8S; EM; 3.40 A; A/B/C=1-1213.
DR PDB; 7K8T; EM; 3.40 A; A/B/C=1-1213.
DR PDB; 7K8U; EM; 3.80 A; A/B/C=1-1213.
DR PDB; 7K8V; EM; 3.80 A; A/B/C=1-1213.
DR PDB; 7K8W; EM; 3.60 A; A/B/G=1-1213.
DR PDB; 7K8X; EM; 3.90 A; A/B/C=1-1213.
DR PDB; 7K8Y; EM; 4.40 A; B/D/E=1-1213.
DR PDB; 7K8Z; EM; 3.50 A; A/B/C=1-1213.
DR PDB; 7K90; EM; 3.24 A; A/B/C=1-1208.
DR PDB; 7K9Z; X-ray; 2.95 A; E=319-541.
DR PDB; 7KDG; EM; 3.01 A; A/B/C=1-1208.
DR PDB; 7KDH; EM; 3.33 A; A/B/C=1-1208.
DR PDB; 7KDI; EM; 3.26 A; A/B/C=1-1208.
DR PDB; 7KDJ; EM; 3.49 A; A/B/C=1-1208.
DR PDB; 7KDK; EM; 2.80 A; A/B/C=1-1208.
DR PDB; 7KDL; EM; 2.96 A; A/B/C=1-1208.
DR PDB; 7KE4; EM; 3.21 A; A/B/C=1-1208.
DR PDB; 7KE6; EM; 3.10 A; A/B/C=1-1208.
DR PDB; 7KE7; EM; 3.32 A; A/B/C=1-1208.
DR PDB; 7KE8; EM; 3.26 A; A/B/C=1-1208.
DR PDB; 7KE9; EM; 3.08 A; A/B/C=1-1208.
DR PDB; 7KEA; EM; 3.33 A; A/B/C=1-1208.
DR PDB; 7KEB; EM; 3.48 A; A/B/C=1-1208.
DR PDB; 7KEC; EM; 3.84 A; A/B/C=1-1208.
DR PDBsum; 6LVN; -.
DR PDBsum; 6LXT; -.
DR PDBsum; 6LZG; -.
DR PDBsum; 6M0J; -.
DR PDBsum; 6M17; -.
DR PDBsum; 6M1V; -.
DR PDBsum; 6VSB; -.
DR PDBsum; 6VW1; -.
DR PDBsum; 6VXX; -.
DR PDBsum; 6VYB; -.
DR PDBsum; 6W41; -.
DR PDBsum; 6WPS; -.
DR PDBsum; 6WPT; -.
DR PDBsum; 6X29; -.
DR PDBsum; 6X2A; -.
DR PDBsum; 6X2B; -.
DR PDBsum; 6X2C; -.
DR PDBsum; 6X6P; -.
DR PDBsum; 6X79; -.
DR PDBsum; 6XC2; -.
DR PDBsum; 6XC3; -.
DR PDBsum; 6XC4; -.
DR PDBsum; 6XC7; -.
DR PDBsum; 6XCM; -.
DR PDBsum; 6XCN; -.
DR PDBsum; 6XDG; -.
DR PDBsum; 6XE1; -.
DR PDBsum; 6XEY; -.
DR PDBsum; 6XF5; -.
DR PDBsum; 6XF6; -.
DR PDBsum; 6XKL; -.
DR PDBsum; 6XKP; -.
DR PDBsum; 6XKQ; -.
DR PDBsum; 6XLU; -.
DR PDBsum; 6XM0; -.
DR PDBsum; 6XM3; -.
DR PDBsum; 6XM4; -.
DR PDBsum; 6XM5; -.
DR PDBsum; 6XR8; -.
DR PDBsum; 6XRA; -.
DR PDBsum; 6XS6; -.
DR PDBsum; 6YLA; -.
DR PDBsum; 6YM0; -.
DR PDBsum; 6YOR; -.
DR PDBsum; 6YZ5; -.
DR PDBsum; 6YZ7; -.
DR PDBsum; 6Z2M; -.
DR PDBsum; 6Z43; -.
DR PDBsum; 6Z97; -.
DR PDBsum; 6ZB4; -.
DR PDBsum; 6ZB5; -.
DR PDBsum; 6ZBP; -.
DR PDBsum; 6ZCZ; -.
DR PDBsum; 6ZDG; -.
DR PDBsum; 6ZDH; -.
DR PDBsum; 6ZER; -.
DR PDBsum; 6ZFO; -.
DR PDBsum; 6ZGE; -.
DR PDBsum; 6ZGG; -.
DR PDBsum; 6ZGI; -.
DR PDBsum; 6ZH9; -.
DR PDBsum; 6ZHD; -.
DR PDBsum; 6ZOW; -.
DR PDBsum; 6ZOX; -.
DR PDBsum; 6ZOY; -.
DR PDBsum; 6ZOZ; -.
DR PDBsum; 6ZP0; -.
DR PDBsum; 6ZP1; -.
DR PDBsum; 6ZP2; -.
DR PDBsum; 6ZP5; -.
DR PDBsum; 6ZP7; -.
DR PDBsum; 6ZWV; -.
DR PDBsum; 6ZXN; -.
DR PDBsum; 7A29; -.
DR PDBsum; 7A4N; -.
DR PDBsum; 7A5R; -.
DR PDBsum; 7A5S; -.
DR PDBsum; 7A91; -.
DR PDBsum; 7A92; -.
DR PDBsum; 7A93; -.
DR PDBsum; 7A94; -.
DR PDBsum; 7A95; -.
DR PDBsum; 7A96; -.
DR PDBsum; 7A97; -.
DR PDBsum; 7A98; -.
DR PDBsum; 7AD1; -.
DR PDBsum; 7BWJ; -.
DR PDBsum; 7BYR; -.
DR PDBsum; 7BZ5; -.
DR PDBsum; 7C01; -.
DR PDBsum; 7C2L; -.
DR PDBsum; 7C8D; -.
DR PDBsum; 7C8V; -.
DR PDBsum; 7C8W; -.
DR PDBsum; 7CAH; -.
DR PDBsum; 7CAI; -.
DR PDBsum; 7CAK; -.
DR PDBsum; 7CAN; -.
DR PDBsum; 7CH4; -.
DR PDBsum; 7CH5; -.
DR PDBsum; 7CHB; -.
DR PDBsum; 7CHC; -.
DR PDBsum; 7CHE; -.
DR PDBsum; 7CHF; -.
DR PDBsum; 7CHH; -.
DR PDBsum; 7CN9; -.
DR PDBsum; 7JJC; -.
DR PDBsum; 7JJI; -.
DR PDBsum; 7JJJ; -.
DR PDBsum; 7JMO; -.
DR PDBsum; 7JMP; -.
DR PDBsum; 7JMW; -.
DR PDBsum; 7JV2; -.
DR PDBsum; 7JV4; -.
DR PDBsum; 7JV6; -.
DR PDBsum; 7JVA; -.
DR PDBsum; 7JVC; -.
DR PDBsum; 7JW0; -.
DR PDBsum; 7JWB; -.
DR PDBsum; 7JX3; -.
DR PDBsum; 7JZL; -.
DR PDBsum; 7JZM; -.
DR PDBsum; 7JZN; -.
DR PDBsum; 7JZU; -.
DR PDBsum; 7K43; -.
DR PDBsum; 7K45; -.
DR PDBsum; 7K4N; -.
DR PDBsum; 7K8S; -.
DR PDBsum; 7K8T; -.
DR PDBsum; 7K8U; -.
DR PDBsum; 7K8V; -.
DR PDBsum; 7K8W; -.
DR PDBsum; 7K8X; -.
DR PDBsum; 7K8Y; -.
DR PDBsum; 7K8Z; -.
DR PDBsum; 7K90; -.
DR PDBsum; 7K9Z; -.
DR PDBsum; 7KDG; -.
DR PDBsum; 7KDH; -.
DR PDBsum; 7KDI; -.
DR PDBsum; 7KDJ; -.
DR PDBsum; 7KDK; -.
DR PDBsum; 7KDL; -.
DR PDBsum; 7KE4; -.
DR PDBsum; 7KE6; -.
DR PDBsum; 7KE7; -.
DR PDBsum; 7KE8; -.
DR PDBsum; 7KE9; -.
DR PDBsum; 7KEA; -.
DR PDBsum; 7KEB; -.
DR PDBsum; 7KEC; -.
DR SASBDB; P0DTC2; -.
DR SMR; P0DTC2; -.
DR BioGRID; 4383848; 620.
DR ComplexPortal; CPX-5682; SARS-CoV-2 Spike protein complex.
DR IntAct; P0DTC2; 36.
DR GlyConnect; 2838; 153 N-Linked glycans (18 sites), 4 O-Linked glycans (2 sites).
DR GlyConnect; 2839; 66 N-Linked glycans (20 sites).
DR GlyConnect; 2840; 109 N-Linked glycans (22 sites).
DR GlyGen; P0DTC2; 24 sites, 172 N-linked glycans (22 sites), 4 O-linked glycans (2 sites).
DR ABCD; P0DTC2; 662 sequenced antibodies.
DR GeneID; 43740568; -.
DR KEGG; vg:43740568; -.
DR Reactome; R-HSA-9694322; Virion Assembly and Release.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR Reactome; R-HSA-9694614; Attachment and Entry.
DR Reactome; R-HSA-9694635; Translation of structural proteins.
DR SABIO-RK; P0DTC2; -.
DR SIGNOR; P0DTC2; -.
DR PRO; PR:P0DTC2; -.
DR Proteomes; UP000464024; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046789; F:host cell surface receptor binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:InterPro.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:InterPro.
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 GO; GO:0046718; P:viral entry into host cell; IDA:UniProtKB.
DR DisProt; DP02772; -.
DR Gene3D; 1.20.5.790; -; 1.
DR HAMAP; MF_04099; BETA_CORONA_SPIKE; 1.
DR InterPro; IPR032500; bCoV_S1_N.
DR InterPro; IPR043607; CoV_S1_C.
DR InterPro; IPR043473; S2_sf_CoV.
DR InterPro; IPR027400; S_HR2_CoV.
DR InterPro; IPR018548; Spike_rcpt-bd_bCoV.
DR InterPro; IPR036326; Spike_rcpt-bd_sf_CoV.
DR InterPro; IPR002552; Spike_S2_CoV.
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; SSF111474; 2.
DR SUPFAM; SSF143587; SSF143587; 1.
DR PROSITE; PS51921; BCOV_S1_CTD; 1.
DR PROSITE; PS51922; BCOV_S1_NTD; 1.
DR PROSITE; PS51923; COV_S2_HR1; 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 interferon signaling pathway 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..12
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CHAIN 13..1273
FT /note="Spike glycoprotein"
FT /id="PRO_0000449646"
FT CHAIN 13..685
FT /note="Spike protein S1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000449647"
FT CHAIN 686..1273
FT /note="Spike protein S2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000449648"
FT CHAIN 816..1273
FT /note="Spike protein S2'"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000449649"
FT TOPO_DOM 13..1213
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TRANSMEM 1214..1234
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TOPO_DOM 1235..1273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DOMAIN 13..303
FT /note="BetaCoV S1-NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DOMAIN 334..527
FT /note="BetaCoV S1-CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269,
FT ECO:0000269|PubMed:32132184"
FT REGION 319..541
FT /note="Receptor-binding domain (RBD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32132184"
FT REGION 403..405
FT /note="Integrin-binding motif;"
FT /evidence="ECO:0000269|PubMed:33102950"
FT REGION 437..508
FT /note="Receptor-binding motif; binding to human ACE2"
FT /evidence="ECO:0000250|UniProtKB:P59594"
FT REGION 816..837
FT /note="Fusion peptide 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 835..855
FT /note="Fusion peptide 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 920..970
FT /note="Heptad repeat 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 1163..1202
FT /note="Heptad repeat 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 949..993
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 1176..1203
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT MOTIF 1269..1273
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT SITE 685..686
FT /note="Cleavage; by TMPRSS2 or furin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32142651, ECO:0000269|PubMed:32362314"
FT SITE 815..816
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695,
FT ECO:0000269|PubMed:32979942"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695,
FT ECO:0000269|PubMed:32979942"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) (high mannose) asparagine; by
FT host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 323
FT /note="O-linked (GalNAc) threonine; by host"
FT /evidence="ECO:0000269|PubMed:32363391"
FT CARBOHYD 325
FT /note="O-linked (HexNAc...) serine; by host"
FT /evidence="ECO:0000269|PubMed:32363391"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695,
FT ECO:0000269|PubMed:32979942"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 709
FT /note="N-linked (GlcNAc...) (high mannose) asparagine; by
FT host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 717
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 801
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 1074
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 1098
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 1134
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695,
FT ECO:0000269|PubMed:32979942"
FT CARBOHYD 1158
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 1173
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942"
FT CARBOHYD 1194
FT /note="N-linked (GlcNAc...) (complex) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695,
FT ECO:0000269|PubMed:32979942"
FT DISULFID 15..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 131..166
FT /evidence="ECO:0000244|PDB:6VXX, ECO:0000255|PROSITE-
FT ProRule:PRU01270, ECO:0000269|PubMed:32155444"
FT DISULFID 291..301
FT /evidence="ECO:0000244|PDB:6VXX, ECO:0000255|PROSITE-
FT ProRule:PRU01270, ECO:0000269|PubMed:32155444"
FT DISULFID 336..361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32245784"
FT DISULFID 379..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269,
FT ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32245784"
FT DISULFID 391..525
FT /evidence="ECO:0000244|PDB:6VXX, ECO:0000255|PROSITE-
FT ProRule:PRU01269, ECO:0000269|PubMed:32155444,
FT ECO:0000269|PubMed:32225175, ECO:0000269|PubMed:32225176,
FT ECO:0000269|PubMed:32245784"
FT DISULFID 480..488
FT /evidence="ECO:0000269|PubMed:32245784"
FT DISULFID 538..590
FT /evidence="ECO:0000244|PDB:6VXX,
FT ECO:0000269|PubMed:32155444"
FT DISULFID 617..649
FT /evidence="ECO:0000244|PDB:6VXX,
FT ECO:0000269|PubMed:32155444"
FT DISULFID 662..671
FT /evidence="ECO:0000244|PDB:6VXX,
FT ECO:0000269|PubMed:32155444"
FT DISULFID 738..760
FT /evidence="ECO:0000244|PDB:6VXX,
FT ECO:0000269|PubMed:32155444"
FT DISULFID 743..749
FT /evidence="ECO:0000244|PDB:6VXX,
FT ECO:0000269|PubMed:32155444"
FT DISULFID 840..851
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DISULFID 1032..1043
FT /evidence="ECO:0000244|PDB:6VXX,
FT ECO:0000269|PubMed:32155444"
FT DISULFID 1082..1126
FT /evidence="ECO:0000244|PDB:6VXX,
FT ECO:0000269|PubMed:32155444"
FT VARIANT 614
FT /note="D -> G (common variant; produces more infectious
FT particles when pseudotyped on VSV ex vivo; increases viral
FT load in hamster upper respiratory tract)"
FT /evidence="ECO:0000305|PubMed:32697968,
FT ECO:0000305|PubMed:32820179, ECO:0000305|PubMed:33106671"
FT MUTAGEN 493
FT /note="Q->N: Reduced host ACE2-binding affinity in vitro."
FT /evidence="ECO:0000269|PubMed:32225175"
FT MUTAGEN 493
FT /note="Q->Y: Reduced host ACE2-binding affinity in vitro."
FT /evidence="ECO:0000269|PubMed:32225175"
FT MUTAGEN 501
FT /note="N->T: Reduced host ACE2-binding affinity in vitro."
FT /evidence="ECO:0000269|PubMed:32225175"
FT MUTAGEN 614
FT /note="D->G: Increase of pseudotyped VSV particle
FT production ex vivo. Increase of viral load in hamster upper
FT respiratory tract."
FT /evidence="ECO:0000269|PubMed:32697968,
FT ECO:0000269|PubMed:33106671"
FT MUTAGEN 679..684
FT /note="NSPRRA->IL: About 50% stronger entry efficiency in
FT Vero E6 cells while 30% weaker entry efficiency in hACE2-
FT expressing BHK cells."
FT /evidence="ECO:0000269|PubMed:32155444"
FT MUTAGEN 681..684
FT /note="PRRA->RRRK: Optimized cleavage by host furin."
FT /evidence="ECO:0000269|PubMed:32362314"
FT MUTAGEN 682..684
FT /note="Missing: Complete loss of cleavage by host furin."
FT /evidence="ECO:0000269|PubMed:32362314"
FT STRAND 27..30
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 40..43
FT /evidence="ECO:0000244|PDB:6X29"
FT STRAND 46..55
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 61..67
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 83..85
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 90..98
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 103..109
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 111..114
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 116..121
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 123..125
FT /evidence="ECO:0000244|PDB:6XCM"
FT STRAND 126..131
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 133..146
FT /evidence="ECO:0000244|PDB:6ZGE"
FT TURN 147..150
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 151..163
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 168..171
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 184..197
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 200..215
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 223..230
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 237..241
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 243..246
FT /evidence="ECO:0000244|PDB:6ZGE"
FT TURN 254..256
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 263..269
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 271..279
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 281..283
FT /evidence="ECO:0000244|PDB:7C2L"
FT STRAND 285..290
FT /evidence="ECO:0000244|PDB:6ZGE"
FT HELIX 291..293
FT /evidence="ECO:0000244|PDB:6ZOY"
FT HELIX 295..303
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 310..314
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 324..328
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 333..335
FT /evidence="ECO:0000244|PDB:6YLA"
FT HELIX 338..342
FT /evidence="ECO:0000244|PDB:6YZ5"
FT STRAND 343..345
FT /evidence="ECO:0000244|PDB:6WPS"
FT HELIX 350..352
FT /evidence="ECO:0000244|PDB:6YZ5"
FT STRAND 354..358
FT /evidence="ECO:0000244|PDB:6YZ5"
FT STRAND 360..362
FT /evidence="ECO:0000244|PDB:6YZ5"
FT HELIX 366..369
FT /evidence="ECO:0000244|PDB:6YZ5"
FT STRAND 375..381
FT /evidence="ECO:0000244|PDB:6YZ5"
FT HELIX 384..387
FT /evidence="ECO:0000244|PDB:6YZ5"
FT STRAND 388..390
FT /evidence="ECO:0000244|PDB:6M17"
FT STRAND 391..403
FT /evidence="ECO:0000244|PDB:6YZ5"
FT HELIX 404..409
FT /evidence="ECO:0000244|PDB:6YZ5"
FT STRAND 411..413
FT /evidence="ECO:0000244|PDB:6M17"
FT HELIX 417..421
FT /evidence="ECO:0000244|PDB:6YZ5"
FT STRAND 431..437
FT /evidence="ECO:0000244|PDB:6YZ5"
FT HELIX 439..442
FT /evidence="ECO:0000244|PDB:6YZ5"
FT TURN 445..447
FT /evidence="ECO:0000244|PDB:6M17"
FT STRAND 452..454
FT /evidence="ECO:0000244|PDB:6YZ5"
FT STRAND 457..459
FT /evidence="ECO:0000244|PDB:7C2L"
FT STRAND 476..478
FT /evidence="ECO:0000244|PDB:6YZ5"
FT STRAND 481..483
FT /evidence="ECO:0000244|PDB:7C8W"
FT STRAND 485..488
FT /evidence="ECO:0000244|PDB:6XEY"
FT STRAND 491..494
FT /evidence="ECO:0000244|PDB:6YZ5"
FT STRAND 499..501
FT /evidence="ECO:0000244|PDB:6ZGE"
FT HELIX 503..505
FT /evidence="ECO:0000244|PDB:6YZ5"
FT STRAND 506..516
FT /evidence="ECO:0000244|PDB:6YZ5"
FT STRAND 518..520
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 524..526
FT /evidence="ECO:0000244|PDB:6ZCZ"
FT STRAND 536..543
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 546..554
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 565..567
FT /evidence="ECO:0000244|PDB:6ZGE"
FT TURN 569..571
FT /evidence="ECO:0000244|PDB:6XKL"
FT STRAND 573..577
FT /evidence="ECO:0000244|PDB:6ZGE"
FT TURN 579..581
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 584..588
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 595..600
FT /evidence="ECO:0000244|PDB:6ZGE"
FT TURN 602..604
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 609..612
FT /evidence="ECO:0000244|PDB:6ZGE"
FT TURN 617..619
FT /evidence="ECO:0000244|PDB:6VXX"
FT HELIX 620..623
FT /evidence="ECO:0000244|PDB:6ZOZ"
FT TURN 625..627
FT /evidence="ECO:0000244|PDB:6X6P"
FT TURN 630..635
FT /evidence="ECO:0000244|PDB:6ZOZ"
FT STRAND 639..641
FT /evidence="ECO:0000244|PDB:6ZOZ"
FT STRAND 643..645
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 648..652
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 663..667
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 670..675
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 691..696
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 702..704
FT /evidence="ECO:0000244|PDB:6X29"
FT STRAND 712..715
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 717..728
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 733..736
FT /evidence="ECO:0000244|PDB:6ZGE"
FT HELIX 738..742
FT /evidence="ECO:0000244|PDB:6ZGE"
FT TURN 743..745
FT /evidence="ECO:0000244|PDB:6ZGE"
FT HELIX 747..753
FT /evidence="ECO:0000244|PDB:6ZGE"
FT HELIX 754..756
FT /evidence="ECO:0000244|PDB:6ZGE"
FT HELIX 757..782
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 785..790
FT /evidence="ECO:0000244|PDB:6X29"
FT TURN 803..805
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 811..813
FT /evidence="ECO:0000244|PDB:6ZGE"
FT HELIX 817..823
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 829..833
FT /evidence="ECO:0000244|PDB:6ZP2"
FT HELIX 837..839
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 842..845
FT /evidence="ECO:0000244|PDB:6ZGE"
FT HELIX 849..854
FT /evidence="ECO:0000244|PDB:6ZGE"
FT TURN 855..857
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 858..861
FT /evidence="ECO:0000244|PDB:6ZGE"
FT HELIX 867..884
FT /evidence="ECO:0000244|PDB:6ZGE"
FT HELIX 887..889
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 890..892
FT /evidence="ECO:0000244|PDB:6ZOZ"
FT HELIX 898..907
FT /evidence="ECO:0000244|PDB:6ZGE"
FT TURN 908..910
FT /evidence="ECO:0000244|PDB:6ZGE"
FT HELIX 913..918
FT /evidence="ECO:0000244|PDB:6ZGE"
FT HELIX 919..966
FT /evidence="ECO:0000244|PDB:6M1V"
FT HELIX 977..981
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 982..984
FT /evidence="ECO:0000244|PDB:6ZGE"
FT HELIX 986..1032
FT /evidence="ECO:0000244|PDB:6ZGE"
FT TURN 1040..1043
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 1044..1056
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 1059..1069
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 1072..1079
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 1081..1085
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 1087..1100
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 1102..1106
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 1109..1113
FT /evidence="ECO:0000244|PDB:6ZGE"
FT TURN 1117..1119
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 1120..1122
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 1126..1128
FT /evidence="ECO:0000244|PDB:6ZGE"
FT STRAND 1129..1134
FT /evidence="ECO:0000244|PDB:6XRA"
FT HELIX 1142..1145
FT /evidence="ECO:0000244|PDB:6ZGE"
FT HELIX 1148..1153
FT /evidence="ECO:0000244|PDB:6XRA"
FT HELIX 1170..1201
FT /evidence="ECO:0000244|PDB:6LVN"
SQ SEQUENCE 1273 AA; 141178 MW; B17BE6D9F1C4EA34 CRC64;
MFVFLVLLPL VSSQCVNLTT RTQLPPAYTN SFTRGVYYPD KVFRSSVLHS TQDLFLPFFS
NVTWFHAIHV SGTNGTKRFD NPVLPFNDGV YFASTEKSNI IRGWIFGTTL DSKTQSLLIV
NNATNVVIKV CEFQFCNDPF LGVYYHKNNK SWMESEFRVY SSANNCTFEY VSQPFLMDLE
GKQGNFKNLR EFVFKNIDGY FKIYSKHTPI NLVRDLPQGF SALEPLVDLP IGINITRFQT
LLALHRSYLT PGDSSSGWTA GAAAYYVGYL QPRTFLLKYN ENGTITDAVD CALDPLSETK
CTLKSFTVEK GIYQTSNFRV QPTESIVRFP NITNLCPFGE VFNATRFASV YAWNRKRISN
CVADYSVLYN SASFSTFKCY GVSPTKLNDL CFTNVYADSF VIRGDEVRQI APGQTGKIAD
YNYKLPDDFT GCVIAWNSNN LDSKVGGNYN YLYRLFRKSN LKPFERDIST EIYQAGSTPC
NGVEGFNCYF PLQSYGFQPT NGVGYQPYRV VVLSFELLHA PATVCGPKKS TNLVKNKCVN
FNFNGLTGTG VLTESNKKFL PFQQFGRDIA DTTDAVRDPQ TLEILDITPC SFGGVSVITP
GTNTSNQVAV LYQDVNCTEV PVAIHADQLT PTWRVYSTGS NVFQTRAGCL IGAEHVNNSY
ECDIPIGAGI CASYQTQTNS PRRARSVASQ SIIAYTMSLG AENSVAYSNN SIAIPTNFTI
SVTTEILPVS MTKTSVDCTM YICGDSTECS NLLLQYGSFC TQLNRALTGI AVEQDKNTQE
VFAQVKQIYK TPPIKDFGGF NFSQILPDPS KPSKRSFIED LLFNKVTLAD AGFIKQYGDC
LGDIAARDLI CAQKFNGLTV LPPLLTDEMI AQYTSALLAG TITSGWTFGA GAALQIPFAM
QMAYRFNGIG VTQNVLYENQ KLIANQFNSA IGKIQDSLSS TASALGKLQD VVNQNAQALN
TLVKQLSSNF GAISSVLNDI LSRLDKVEAE VQIDRLITGR LQSLQTYVTQ QLIRAAEIRA
SANLAATKMS ECVLGQSKRV DFCGKGYHLM SFPQSAPHGV VFLHVTYVPA QEKNFTTAPA
ICHDGKAHFP REGVFVSNGT HWFVTQRNFY EPQIITTDNT FVSGNCDVVI GIVNNTVYDP
LQPELDSFKE ELDKYFKNHT SPDVDLGDIS GINASVVNIQ KEIDRLNEVA KNLNESLIDL
QELGKYEQYI KWPWYIWLGF IAGLIAIVMV TIMLCCMTSC CSCLKGCCSC GSCCKFDEDD
SEPVLKGVKL HYT
//