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 02-DEC-2020, entry version 5. 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] {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 [10] {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 [11] {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 [12] 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 [13] 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 [14] 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). The CC stalk domain of S contains three hinges, giving the head unexpected CC orientational freedom (PubMed:32817270). Uses human TMPRSS2 for priming CC in human lung cells which is an essential step for viral entry CC (PubMed:32142651). Can be alternatively processed by host furin CC (PubMed:32362314). Proteolysis by cathepsin CTSL may unmask the fusion CC peptide of S2 and activate membranes fusion within endosomes. CC {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32075877, CC ECO:0000269|PubMed:32142651, ECO:0000269|PubMed:32155444, CC ECO:0000269|PubMed:32362314, ECO:0000269|PubMed:32817270}. 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 (By similarity). Interacts with ORF3a protein and CC ORF7a protein. {ECO:0000255|HAMAP-Rule:MF_04099, CC ECO:0000269|PubMed:32075877, ECO:0000269|PubMed:32155444, CC ECO:0000269|PubMed:32245784}. CC -!- SUBUNIT: [Spike protein S1]: Binds to host ACE2. CC {ECO:0000269|PubMed:32075877, ECO:0000269|PubMed:32132184, CC ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32225175, CC ECO:0000269|PubMed:32225176}. CC -!- INTERACTION: CC P0DTC2; P0DTC2: S; NbExp=4; IntAct=EBI-25474821, EBI-25474821; CC P0DTC2; Q9BYF1: ACE2; Xeno; NbExp=35; IntAct=EBI-25474821, EBI-7730807; CC P0DTC2; P35613: BSG; Xeno; NbExp=5; IntAct=EBI-25474821, EBI-750709; CC P0DTC2; Q9H2X3: CLEC4M; Xeno; NbExp=2; IntAct=EBI-25474821, EBI-1391211; CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP- CC Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP- CC Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate CC compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host cell CC membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane CC protein {ECO:0000255|HAMAP-Rule:MF_04099}. Note=Accumulates in the CC 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. {ECO:0000255|HAMAP-Rule:MF_04099}. 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). Highly CC glycosylated by host both on S1 and S2 subunits, occluding many regions CC across the surface of the protein. This may shield viral epitopes from CC acquired immune response (PubMed:32366695, PubMed:32363391). CC {ECO:0000269|PubMed:32075877, ECO:0000269|PubMed:32155444, CC ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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; 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; 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; 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; 7CAN; X-ray; 2.94 A; B=330-531. DR PDB; 7CN9; EM; 4.70 A; A/B/C=14-1140. 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 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; 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; 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; 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; 7CAN; -. DR PDBsum; 7CN9; -. DR PDBsum; 7JJI; -. DR PDBsum; 7JJJ; -. DR PDBsum; 7JMO; -. DR PDBsum; 7JMP; -. DR SASBDB; P0DTC2; -. DR SMR; P0DTC2; -. DR BioGRID; 4383848; 31. DR ComplexPortal; CPX-5682; SARS-CoV-2 Spike protein complex. DR IntAct; P0DTC2; 26. 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 SABIO-RK; P0DTC2; -. DR SIGNOR; 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 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" 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" 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 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" 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 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" 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" 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" 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" 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" 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 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" 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" 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" 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" 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" 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" 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" 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 CARBOHYD 1158 FT /note="N-linked (GlcNAc...) (complex) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099, FT ECO:0000269|PubMed:32366695" 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" 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 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 polymorphism; Produces more FT infectious particles when pseudotyped on VSV ex vivo;)" FT /evidence="ECO:0000305|PubMed:32697968, FT ECO:0000305|PubMed:32820179" 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." FT /evidence="ECO:0000269|PubMed:32697968" 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 //