AC   MF_04099;
DC   Protein; auto
TR   HAMAP; MF_04099; -; 1; level=0
XX
Names: BETA_CORONA_SPIKE
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ID   SPIKE
DE   RecName: Full=Spike glycoprotein;
DE            Short=S glycoprotein;
DE   AltName: Full=E2;
DE   AltName: Full=Peplomer protein;
DE   Contains:
DE     RecName: Full=Spike protein S1;
DE   Contains:
DE     RecName: Full=Spike protein S2;
DE   Contains:
DE     RecName: Full=Spike protein S2';
DE   Flags: Precursor;
GN   Name=S;
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CC   -!- FUNCTION: Spike protein S1: attaches the virion to the cell membrane by
CC       interacting with host receptor, initiating the infection.
CC   -!- FUNCTION: Spike protein S2: mediates fusion of the virion and cellular
CC       membranes by acting as a class I viral fusion protein. Under the
CC       current model, the protein has at least three conformational states:
CC       pre-fusion native state, pre-hairpin intermediate state, and post-
CC       fusion hairpin state. During viral and target cell membrane fusion, the
CC       coiled coil regions (heptad repeats) assume a trimer-of-hairpins
CC       structure, positioning the fusion peptide in close proximity to the C-
CC       terminal region of the ectodomain. The formation of this structure
CC       appears to drive apposition and subsequent fusion of viral and target
CC       cell membranes.
CC   -!- FUNCTION: Spike protein S2': Acts as a viral fusion peptide which is
CC       unmasked following S2 cleavage occurring upon virus endocytosis.
CC   -!- SUBUNIT: Homotrimer; each monomer consists of a S1 and a S2 subunit.
CC       The resulting peplomers protrude from the virus surface as spikes.
CC   -!- SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane
CC       protein. Host endoplasmic reticulum-Golgi intermediate compartment
CC       membrane; Single-pass type I membrane protein. Host cell membrane;
CC       Single-pass type I membrane protein. Note=Accumulates in the
CC       endoplasmic reticulum-Golgi intermediate compartment, where it
CC       participates in virus particle assembly. Some S oligomers are
CC       transported to the host plasma membrane, where they may mediate cell-
CC       cell fusion.
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   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC       precursor is processed into S1 and S2 by host cell furin or another
CC       cellular protease to yield the mature S1 and S2 proteins. Additionally,
CC       a second cleavage leads to the release of a fusion peptide after viral
CC       attachment to host cell receptor.
CC   -!- PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike
CC       glycoprotein is digested within host endosomes.
CC   -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family.
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DR   PROSITE; PS00001; ASN_GLYCOSYLATION; 0-unlimited; trigger=yes
DR   Pfam; PF01601; Corona_S2; 1; trigger=no
DR   Pfam; PF16451; Spike_NTD; 1; trigger=no
DR   Pfam; PF09408; Spike_rec_bind; 1; trigger=no
DR   General; Coiled_coil; -; 0-unlimited; trigger=no
DR   General; Signal; -; 1; trigger=no
DR   General; Transmembrane; -; 1; trigger=no
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KW   Coiled coil
KW   Disulfide bond
KW   Fusion of virus membrane with host endosomal membrane
KW   Fusion of virus membrane with host membrane
KW   Glycoprotein
KW   Host cell membrane
KW   Host membrane
KW   Host-virus interaction
KW   Lipoprotein
KW   Membrane
KW   Palmitate
KW   Signal
KW   Transmembrane
KW   Transmembrane helix
KW   Viral attachment to host cell
KW   Viral envelope protein
KW   Viral penetration into host cytoplasm
KW   Virion
KW   Virulence
KW   Virus entry into host cell
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GO   GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane
GO   GO:0016020; C:membrane
GO   GO:0019031; C:viral envelope
GO   GO:0055036; C:virion membrane
GO   GO:0075509; P:endocytosis involved in viral entry into host cell
GO   GO:0039654; P:fusion of virus membrane with host endosome membrane
GO   GO:0019064; P:fusion of virus membrane with host plasma membrane
GO   GO:0046813; P:receptor-mediated virion attachment to host cell
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FT   From: SPIKE_SARS (P59594)
FT   SIGNAL          Nter..13
FT   CHAIN           14..667
FT                   /note="Spike protein S1"
FT   CHAIN           668..Cter
FT                   /note="Spike protein S2"
FT   CHAIN           798..Cter
FT                   /note="Spike protein S2'"
FT   TOPO_DOM        14..1195
FT                   /note="Extracellular"
FT   TRANSMEM        1196..1216
FT                   /note="Helical"
FT   TOPO_DOM        1217..Cter
FT                   /note="Cytoplasmic"
FT   REGION          798..819
FT                   /note="Fusion peptide 1"
FT   REGION          817..837
FT                   /note="Fusion peptide 2"
FT   REGION          902..952
FT                   /note="Heptad repeat 1"
FT   REGION          1145..1184
FT                   /note="Heptad repeat 2"
FT   COILED          931..975
FT   COILED          1157..1185
FT   MOTIF           1251..Cter
FT                   /note="KxHxx"
FT   SITE            667..668
FT                   /note="Cleavage"
FT   Condition: R-S
FT   SITE            797..798
FT                   /note="Cleavage"
FT   Condition: R-S
FT   DISULFID        323..348
FT   Condition: C-x*-C
FT   DISULFID        366..419
FT   Condition: C-x*-C
FT   DISULFID        822..833
FT   Condition: C-x*-C
FT   SITE            760..761
FT                   /note="Cleavage"
FT   Condition: R-S
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Size: 1235-1376;
Related: None;
Template: P59594;
Scope:
 Viruses; Betacoronavirus
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
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# Revision 1.10 2022/09/29
//