Spike glycoprotein
Details
- Name
- Spike glycoprotein
- Synonyms
- E2
- Peplomer protein
- S glycoprotein
- Gene Name
- S
- Organism
- SARS-CoV-2
- Amino acid sequence
>lcl|BSEQ0052516|Spike glycoprotein MFVFLVLLPLVSSQCVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFS NVTWFHAIHVSGTNGTKRFDNPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIV NNATNVVIKVCEFQFCNDPFLGVYYHKNNKSWMESEFRVYSSANNCTFEYVSQPFLMDLE GKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQT LLALHRSYLTPGDSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETK CTLKSFTVEKGIYQTSNFRVQPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISN CVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAPGQTGKIAD YNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPC NGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVN FNFNGLTGTGVLTESNKKFLPFQQFGRDIADTTDAVRDPQTLEILDITPCSFGGVSVITP GTNTSNQVAVLYQDVNCTEVPVAIHADQLTPTWRVYSTGSNVFQTRAGCLIGAEHVNNSY ECDIPIGAGICASYQTQTNSPRRARSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTI SVTTEILPVSMTKTSVDCTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQE VFAQVKQIYKTPPIKDFGGFNFSQILPDPSKPSKRSFIEDLLFNKVTLADAGFIKQYGDC LGDIAARDLICAQKFNGLTVLPPLLTDEMIAQYTSALLAGTITSGWTFGAGAALQIPFAM QMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALN TLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRA SANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPA ICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNTFVSGNCDVVIGIVNNTVYDP LQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDL QELGKYEQYIKWPWYIWLGFIAGLIAIVMVTIMLCCMTSCCSCLKGCCSCGSCCKFDEDD SEPVLKGVKLHYT
- Number of residues
- 1273
- Molecular Weight
- 141177.29
- Theoretical pI
- Not Available
- GO Classification
- Functionshost cell surface receptor binding / identical protein bindingProcessesendocytosis involved in viral entry into host cell / fusion of virus membrane with host endosome membrane / fusion of virus membrane with host plasma membrane / pathogenesis / receptor-mediated virion attachment to host cell / suppression by virus of host tetherin activity / suppression by virus of host type I interferon-mediated signaling pathway / viral entry into host cellComponentshost cell endoplasmic reticulum-Golgi intermediate compartment membrane / host cell plasma membrane / integral component of membrane / viral envelope / virion membrane
- General Function
- Spike protein S1 attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein (PubMed:32142651, PubMed:32075877, PubMed:32155444). Uses also human TMPRSS2 for priming in human lung cells which is an essential step for viral entry (PubMed:32142651). Can be alternatively processed by host furin (PubMed:32362314). Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes.
- Specific Function
- Host cell surface receptor binding
- Pfam Domain Function
- Transmembrane Regions
- 1214-1234
- Cellular Location
- Virion membrane
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0DTC2 UniProtKB Entry Name SPIKE_SARS2 - General References
- Wu F, Zhao S, Yu B, Chen YM, Wang W, Song ZG, Hu Y, Tao ZW, Tian JH, Pei YY, Yuan ML, Zhang YL, Dai FH, Liu Y, Wang QM, Zheng JJ, Xu L, Holmes EC, Zhang YZ: A new coronavirus associated with human respiratory disease in China. Nature. 2020 Mar;579(7798):265-269. doi: 10.1038/s41586-020-2008-3. Epub 2020 Feb 3. [Article]
- Hoffmann M, Kleine-Weber H, Schroeder S, Kruger N, Herrler T, Erichsen S, Schiergens TS, Herrler G, Wu NH, Nitsche A, Muller MA, Drosten C, Pohlmann S: SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. Cell. 2020 Apr 16;181(2):271-280.e8. doi: 10.1016/j.cell.2020.02.052. Epub 2020 Mar 5. [Article]
- Hoffmann M, Kleine-Weber H, Pohlmann S: A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells. Mol Cell. 2020 May 21;78(4):779-784.e5. doi: 10.1016/j.molcel.2020.04.022. Epub 2020 May 1. [Article]
- Watanabe Y, Allen JD, Wrapp D, McLellan JS, Crispin M: Site-specific glycan analysis of the SARS-CoV-2 spike. Science. 2020 Jul 17;369(6501):330-333. doi: 10.1126/science.abb9983. Epub 2020 May 4. [Article]
- Shajahan A, Supekar NT, Gleinich AS, Azadi P: Deducing the N- and O- glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2. Glycobiology. 2020 May 4. pii: 5826952. doi: 10.1093/glycob/cwaa042. [Article]
- Yan R, Zhang Y, Li Y, Xia L, Guo Y, Zhou Q: Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. Science. 2020 Mar 27;367(6485):1444-1448. doi: 10.1126/science.abb2762. Epub 2020 Mar 4. [Article]
- Wrapp D, Wang N, Corbett KS, Goldsmith JA, Hsieh CL, Abiona O, Graham BS, McLellan JS: Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science. 2020 Mar 13;367(6483):1260-1263. doi: 10.1126/science.abb2507. Epub 2020 Feb 19. [Article]
- Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D: Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Cell. 2020 Apr 16;181(2):281-292.e6. doi: 10.1016/j.cell.2020.02.058. Epub 2020 Mar 9. [Article]
- Lan J, Ge J, Yu J, Shan S, Zhou H, Fan S, Zhang Q, Shi X, Wang Q, Zhang L, Wang X: Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. Nature. 2020 May;581(7807):215-220. doi: 10.1038/s41586-020-2180-5. Epub 2020 Mar 30. [Article]
- Shang J, Ye G, Shi K, Wan Y, Luo C, Aihara H, Geng Q, Auerbach A, Li F: Structural basis of receptor recognition by SARS-CoV-2. Nature. 2020 May;581(7807):221-224. doi: 10.1038/s41586-020-2179-y. Epub 2020 Mar 30. [Article]
- Yuan M, Wu NC, Zhu X, Lee CD, So RTY, Lv H, Mok CKP, Wilson IA: A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV. Science. 2020 May 8;368(6491):630-633. doi: 10.1126/science.abb7269. Epub 2020 Apr 3. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB15897 Etesevimab investigational yes binder Details DB15718 Bamlanivimab approved, investigational yes antagonist Details DB15691 Anti-SARS-CoV-2 REGN-COV2 investigational yes binder Details DB15940 Imdevimab approved, experimental yes binder Details DB15941 Casirivimab approved, experimental yes binder Details DB16355 Sotrovimab approved, investigational unknown binder Details DB16405 Regdanvimab approved, investigational yes antibody Details DB16393 Cilgavimab approved, investigational yes binder Details DB16394 Tixagevimab approved, investigational yes binder Details DB16755 Bebtelovimab investigational, withdrawn yes antibody Details DB12411 Bemcentinib investigational yes inhibitor Details