SPIKE_IBV6
ID SPIKE_IBV6 Reviewed; 1163 AA.
AC P05135;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 23-FEB-2022, entry version 109.
DE RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04098};
DE Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04098};
DE AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04098};
DE AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04098};
DE Contains:
DE RecName: Full=Spike protein S1 {ECO:0000255|HAMAP-Rule:MF_04098};
DE Contains:
DE RecName: Full=Spike protein S2 {ECO:0000255|HAMAP-Rule:MF_04098};
DE Contains:
DE RecName: Full=Spike protein S2' {ECO:0000255|HAMAP-Rule:MF_04098};
DE Flags: Precursor;
GN Name=S {ECO:0000255|HAMAP-Rule:MF_04098}; ORFNames=2;
OS Avian infectious bronchitis virus (strain 6/82) (IBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Gammacoronavirus; Igacovirus.
OX NCBI_TaxID=11121;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3025348; DOI=10.1099/0022-1317-67-12-2825;
RA Binns M.M., Boursnell M.E.G., Tomley F.M., Brown T.D.K.;
RT "Comparison of the spike precursor sequences of coronavirus IBV strains M41
RT and 6/82 with that of IBV Beaudette.";
RL J. Gen. Virol. 67:2825-2831(1986).
CC -!- FUNCTION: [Spike protein S1]: Attaches the virion to the host cell
CC membrane by interacting with sialic acids, initiating the infection.
CC {ECO:0000255|HAMAP-Rule:MF_04098}.
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 3 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. {ECO:0000255|HAMAP-Rule:MF_04098}.
CC -!- FUNCTION: [Spike protein S2']: Acts as a viral fusion peptide after S2
CC cleavage occurring upon virus endocytosis. {ECO:0000255|HAMAP-
CC Rule:MF_04098}.
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 {ECO:0000255|HAMAP-Rule:MF_04098}.
CC -!- SUBCELLULAR LOCATION: [Spike protein S2]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04098}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04098}. Host endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04098};
CC Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04098}.
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. {ECO:0000255|HAMAP-Rule:MF_04098}.
CC -!- SUBCELLULAR LOCATION: [Spike protein S1]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04098}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04098}. Host endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04098};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04098}.
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.
CC {ECO:0000255|HAMAP-Rule:MF_04098}.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000255|HAMAP-Rule:MF_04098}.
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.
CC Additionally, a second cleavage leads to the release of a fusion
CC peptide after viral attachment to host cell receptor.
CC {ECO:0000255|HAMAP-Rule:MF_04098}.
CC -!- SIMILARITY: Belongs to the gammacoronaviruses spike protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04098}.
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DR EMBL; X04723; CAA28432.1; -; Genomic_RNA.
DR SMR; P05135; -.
DR GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment 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: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:0046813; P:receptor-mediated virion attachment to host cell; IEA:InterPro.
DR HAMAP; MF_04098; GAMMA_CORONA_SPIKE; 1.
DR InterPro; IPR043607; CoV_S1_C.
DR InterPro; IPR043473; S2_sf_CoV.
DR InterPro; IPR002552; Spike_S2_CoV.
DR InterPro; IPR043614; Spike_S2_CoV_C.
DR InterPro; IPR044873; Spike_S2_CoV_HR1.
DR InterPro; IPR044874; Spike_S2_CoV_HR2.
DR Pfam; PF19209; CoV_S1_C; 1.
DR Pfam; PF01601; CoV_S2; 1.
DR Pfam; PF19214; CoV_S2_C; 1.
DR SUPFAM; SSF111474; SSF111474; 2.
DR PROSITE; PS51923; COV_S2_HR1; 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; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virulence;
KW Virus endocytosis by host; Virus entry into host cell.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CHAIN 19..1163
FT /note="Spike glycoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT /id="PRO_0000037159"
FT CHAIN 19..538
FT /note="Spike protein S1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT /id="PRO_0000037160"
FT CHAIN 539..1163
FT /note="Spike protein S2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT /id="PRO_0000037161"
FT CHAIN 692..1163
FT /note="Spike protein S2'"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT /id="PRO_0000444091"
FT TOPO_DOM 19..1096
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT TRANSMEM 1097..1117
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT TOPO_DOM 1118..1163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT REGION 770..875
FT /note="Heptad repeat 1 (HR1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01271"
FT REGION 1025..1106
FT /note="Heptad repeat 2 (HR2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01272"
FT COILED 823..867
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT COILED 1056..1084
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT MOTIF 1160..1163
FT /note="Di-lysine motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT SITE 538..539
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT SITE 691..692
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 961
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 980
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 1015
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 1039
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 1052
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 1075
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
SQ SEQUENCE 1163 AA; 128685 MW; 8FE344CF2995478C CRC64;
MLERSLLLAT LLSALCSANL FGNNSYVYYY QSAFRPSDGW HLHGGAYEVV NVSTESSNAG
TTGCTAGAIY WSKNFSAASV AMTAPQNGMS WSTEQFCTAH CNFTDFVVFV THCYKSGHGS
CPLTGLIPQN HIRISAMKNS SLFYNLTVAV TKYPRFKSLQ CVNNMTSVYL NGDLVFTSNE
TKDVSAAGVH FKAGGPITYK VMREVKALAY FVNGTAQDVI LCDGSPTGLL ACQYNTGNFS
DGFYPFTNSS LVKEKFIVYR ESSVNTTLEL TNFTFSNVSN ATPNTGGVQT IQLYQTITAQ
SGYYNLNFSF LSSFIYKASD YMYGSYHPSC KFRLETINNG LWFNSLSVSL GYGPIQGGCK
QSVFANRATC CYAYSYNGPS LCKGVYRGEL TKSFECGLLV FVTKTDGSRI QTRNEPFTLT
QHNYNNITLD RCVEYNIYGR VGQGFITNVT NYAINYNYLA DGGMAILDTS GAIDIFVVQG
EYGLNYYKVN PCEDVNQQFV VSGGKLVGIL TSRNETGSQP LENQFYIKII NGTRRSRRSI
TGNVTNCPYV TYGKFCIKPD GSISTIVPKE LEHFVAPLLN VTENVLIPDS FNLTVTDEYI
QTRMDKVQIN CLQYVCGNSL ECRKLFQQYG PVCDNILSVV NSVGQKEDME LLYFYSSTKP
SGFNTPVLSN VSTGEFNISL LLTPPSSASG RSFIEDLLFT SVESVGLPTD DAYKKCTAGP
LGFLKDLACA REYNGLLVLP PIITAEMQTL YTSSLVASMA FGGITSAGAI PFATQLQARI
NHLGITQSLL FKNQEKIAAS FNKAIGHMQE GFRSTSLALQ QIQDVVNKQS SILTETMASL
NKNFGAISSV LQDIYQQLDS IQADAQVDRI ITGRLSSLSV LASAKQAEYY RVSQQRELAT
QKINECVKSQ SIRYSFCGNG RHVLTIPQNA PNGIVFIHFT YTPESFVNVT AIVGFCVNPA
NASQYAIVPA NGRGIFIQVN GSYYITARDM YMPRDITAGD IVTLTSCQAN YVSVNKTVIT
TFVDNDDFDF DDELSKWWND TKHELPDFDE FNYTVPILDI GSEIDRIQGV IQGLNDSLID
LETLSILKTY IKWPWYVWLA IAFLTIIFIL VLCWIFFMTG CCGCCCGCFG IIPLMSKCGK
KSSYYTTFDN DVVYEQYRPK KSV
