SPIKE_IBVU1
ID SPIKE_IBVU1 Reviewed; 520 AA.
AC P30206;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 29-SEP-2021, entry version 75.
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 Flags: Precursor; Fragment;
GN Name=S; ORFNames=2;
OS Avian infectious bronchitis virus (strain UK/123/82) (IBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Gammacoronavirus; Igacovirus.
OX NCBI_TaxID=31626;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Cavanagh D., Davis P.J., Cook J.K.A., Li D., Kant A., Koch G.;
RL Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases.
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 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. S1 is
CC not anchored to the viral envelope, but associates with the extravirion
CC surface through its binding to S2 (By 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; X58067; CAA41098.1; -; Genomic_RNA.
DR PIR; S14600; S14600.
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:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR043607; CoV_S1_C.
DR Pfam; PF19209; CoV_S1_C; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues;
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; 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 CHAIN 1..>520
FT /note="Spike glycoprotein"
FT /id="PRO_0000037177"
FT CHAIN 1..520
FT /note="Spike protein S1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037178"
FT TOPO_DOM <1..>520
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 520
SQ SEQUENCE 520 AA; 57613 MW; 19FBDFFC35B6FD2C CRC64;
NLFGNNSYVY YYQSAFRPPN GWHLHGGAYE VVNVSTESSN AGTTECTAGA IYWSKNFSAA
SVAMTAPQNG MLWSTAQFCT AHCNFTDFVV FVTHCYKSAS GSCPLTGLIP QYHIRISAMK
NSSLFYNLTV AVTKYPRFKS LQCVNNMTSV YLNGDLVFTS NETKDVSAAG VHFKAGGPIT
YKVMREVKAL AYFVNGTAQD VILCDGSPTG LLACQYNTGN FSDGFYPFTN SSLVKEKFIV
YRESSVNTTL DVTNFTFSNV SNATPNTGGV HTIQLYQTST AQSGYYNFNF SFLSSFIYKE
SDYMYGSYHP SCKFRLETIN NGLXFNPLSV SLGYGPIQGG CKQSVFENRA TCCYAYSYNG
PPLCKGVYRG ELTKSFECGL LVFVTKTDGS RIQTRNEPFT LTQHNYNNIT LDRCVEYNIY
GRVGQGFITN VTNYAINYNY LADGGMAILD TSGAIDIFVV QGEYGLNYYK VNPCEDVNQQ
FVVSGGKLVG ILTSRNETGS QPLENQFYIK IINGTRRSRR
