SPIKE_IBVD3
ID SPIKE_IBVD3 Reviewed; 550 AA.
AC P17662;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 23-FEB-2022, entry version 95.
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 Flags: Precursor; Fragment;
GN Name=S; ORFNames=2;
OS Avian infectious bronchitis virus (strain D3896) (IBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Gammacoronavirus; Igacovirus.
OX NCBI_TaxID=11125;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2161519; DOI=10.1093/nar/18.10.3063;
RA Koch G., Kant A.;
RT "Nucleotide and amino acid sequence of the S1 subunit of the spike
RT glycoprotein of avian infectious bronchitis virus, strain D3896.";
RL Nucleic Acids Res. 18:3063-3064(1990).
CC -!- FUNCTION: S1 attaches the virion to the cell membrane by interacting
CC with cell receptors, initiating the infection.
CC -!- FUNCTION: S2 is a class I viral fusion protein. Under the current
CC model, the protein has at least 3 conformational states: pre-fusion
CC native state, pre-hairpin intermediate state, and post-fusion hairpin
CC state. During viral and target cell membrane fusion, the coiled coil
CC regions (heptad repeats) assume a trimer-of-hairpins structure,
CC positioning the fusion peptide in close proximity to the C-terminal
CC region of the ectodomain. The formation of this structure appears to
CC drive apposition and subsequent fusion of viral and target cell
CC membranes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer; each monomer consists of a S1 and a S2 subunit.
CC The resulting peplomers protrude from the virus surface as spikes (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Spike protein S2]: Virion membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host
CC endoplasmic reticulum-Golgi intermediate compartment membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC Note=Accumulates in the endoplasmic reticulum-Golgi intermediate
CC compartment, where it participates in virus particle assembly. Some S
CC oligomers may be transported to the plasma membrane, where they may
CC mediate cell-cell fusion (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Spike protein S1]: Virion membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host
CC endoplasmic reticulum-Golgi intermediate compartment membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=Accumulates in the endoplasmic reticulum-Golgi intermediate
CC compartment, where it participates in virus particle assembly. Some S
CC oligomers may be transported to the plasma membrane, where they may
CC mediate cell-cell fusion. S1 is not anchored to the viral envelope, but
CC associates with the extravirion surface through its binding to S2 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC precursor is processed into S1 and S2 by host cell furin or furin-like
CC protease to yield the mature S1 and S2 proteins. The cleavage site
CC between S1 and S2 requires the optimal sequence [KR]-X-[KR]-R. Cleavage
CC is not necessary for virus-cell fusion (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the coronaviruses spike protein family.
CC {ECO:0000305}.
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DR EMBL; X52084; CAA36302.1; -; Genomic_RNA.
DR PIR; S10175; VGIHD6.
DR SMR; P17662; -.
DR GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C: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:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
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:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR043607; CoV_S1_C.
DR InterPro; IPR002551; Spike_S1_CoV.
DR Pfam; PF01600; CoV_S1; 1.
DR Pfam; PF19209; CoV_S1_C; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues; Coiled coil;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; Host membrane;
KW Host-virus interaction; Membrane; Signal; Viral attachment to host cell;
KW Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW Virulence; Virus endocytosis by host; Virus entry into host cell.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..>550
FT /note="Spike glycoprotein"
FT /id="PRO_0000037168"
FT CHAIN 19..538
FT /note="Spike protein S1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037169"
FT CHAIN 539..>550
FT /note="Spike protein S2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037170"
FT TOPO_DOM 19..>550
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT SITE 538..539
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT NON_TER 550
SQ SEQUENCE 550 AA; 60877 MW; D6FFEA93C78C4F95 CRC64;
MLEKSLLLVT LLFALCSANL FGNNSYVYYY QSAFRPPNGW HLHGGAYEVV NVSTESSNAG
TTECTAGAIY WSKNFSAASV AMTAPQNGML WSTAQFCTAH CNFTDFVVFV THCYKSASGS
CPLTGLIPQY HIRISAMKNS SLFYNLTVAV TKYPRFKSLQ CVNNMTSVYL NGDLVFTSNE
TKDVSAAGVH FKAGGPITYK VMREVKALAY FVNGTAQDVI LCDGSPTGLL ACQYNTGNFS
DGFYPFTNSS LVKEKFIVYR ESSVNTTLEL TNFTFSNVSN ANPNTGGVHT IQLYQTSTAQ
SGHYNFNFSF LSSFTYKESD YMYGSYHPSC KFRLETINNG LWFNSLSVSL GYGPIQGGCK
QSVFQNRATC CYAYSYNGPP LCKGVYRGEL TKSFECGLLV FVTKTDGSRI QTRNEPFTLT
QHNYNNITLD RCVEYNIYGR VGQGFITNVT NYAINYNYLA DGGMAILDTS GAIDIFVVQG
EYGLNYYKVN PCEDVNQQFV VSGGKLVGIL TSRNETGSQP LENQFYIKII NGTRRSRRSI
TGNVTNCPYV
