SPIKE_IBVK
ID SPIKE_IBVK Reviewed; 1162 AA.
AC P12650;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 23-FEB-2022, entry version 107.
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 KB8523) (IBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Gammacoronavirus; Igacovirus.
OX NCBI_TaxID=11126;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2841803; DOI=10.1016/0042-6822(88)90603-4;
RA Sutou S., Sato S., Okabe T., Nakai M., Sasaki N.;
RT "Cloning and sequencing of genes encoding structural proteins of avian
RT infectious bronchitis virus.";
RL Virology 165:589-595(1988).
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; M21515; AAA66578.1; -; Genomic_RNA.
DR PIR; B29249; VGIHAK.
DR SMR; P12650; -.
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..1162
FT /note="Spike glycoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT /id="PRO_0000037174"
FT CHAIN 19..537
FT /note="Spike protein S1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT /id="PRO_0000037175"
FT CHAIN 538..1162
FT /note="Spike protein S2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT /id="PRO_0000037176"
FT CHAIN 691..1162
FT /note="Spike protein S2'"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT /id="PRO_0000444094"
FT TOPO_DOM 19..1095
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT TRANSMEM 1096..1116
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT TOPO_DOM 1117..1162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT REGION 769..874
FT /note="Heptad repeat 1 (HR1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01271"
FT REGION 1024..1105
FT /note="Heptad repeat 2 (HR2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01272"
FT COILED 822..866
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT COILED 1055..1083
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT MOTIF 1159..1162
FT /note="Di-lysine motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT SITE 537..538
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT SITE 690..691
FT /note="Cleavage; by host furin"
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 77
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 714
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 947
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 960
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 979
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 1014
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 1051
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 1058
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
FT CARBOHYD 1074
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04098"
SQ SEQUENCE 1162 AA; 128538 MW; 2299036B3597EA8F CRC64;
MLVTPLLLVT LLCALCSAAL YDSSSYVYYY QSAFRPPDGW HLHGGAYAVV NISSESNNAG
SSSGCTVGTI HGGRVVNASS IAMTAPSSGM AWSSSQFCTA YCNFSDTTVF VTHCYKHGGC
PITGMLQQHS IRVSAMKNGQ LFYNLTVSVA KYPTFKSFQC VNNLTSVYLN GDLVYTSNET
TDVTSAGVYF KAVGPITYKV MREVRALAYF VNGTAQDVIL CDGSPRGLLA CQYNTGNFSD
GFYPFTNSSL VKQKFIVYRE NSVNTTFTLH NFTFHNETGA NPNPSGVQNI QTYQTQTAQS
GYYNFNFSFL SSFVYKESNF MYGSYHPSCS FRLETINNGL WFNSLSVSIA YGPLQGGCKQ
SVFSGRATCC YAYSYGGPLL CKGVYSGELD HNFECGLLVY VTKSGGSRIQ TATEPPVITQ
HNYNNITLNT CVDYNIYGRI GQGFITNVTD SAVSYNYLAD AGLAILDTSG SIDIFVVQSE
YGLNYYKVNP CEDVNQQFVV SGGKLVGILT SRNETGSQLL ENQFYIKITN GTRRFRRSIT
ESVENCPYVS YGKFCIKPDG SISTIVPKYL EQFVAPLLNV TENVLIPNSF NLTVTDEYIQ
TRMDKVQINC LQYICGNSLE CRNLFQQYGP VCDNMLSVVN SVGQKEDMEL LNFYSSTKPA
GFNTPVLSNV STGEFNISLF LTTPSSPRRR SFIEDLLFTS VESVGLPTDD AYKNCTAGPL
GFLKDLVCAR EYNGLLVLPP IITAEMQTLY TSSLVASMAF GGITAAGAIP FATQLQARIN
HLGITQSLLL KNQEKIAASF NKAIGHMQEG FRSTSLALQQ IQDVVNKQSA ILTETMASLN
KNFGAISSVI QEIYLQLDAI QANAQVDRLI TGRLSSLSVL ASAKQAEYIR VSQQRELATQ
KINECVKSQS TRYSFCGNGR HVLTIPQNAP NGIVFIHFTY TPESFVNVTA IVGFCVKPNN
ASQYAIVPVN GRGIFIQVND SYYITARDMY MPRHITAGDI VTLTSCQANY VSVNKTVITT
FVENDDFDFD DELSKWWIET KYELPDFDQF NYTIPVLNIT YDIDKIEEVI KGLNDSLIDL
ETLSILKTYI KWPWYVWLAI AFATIIFILI LGWVFFMTGC CGCCCGCFGI IPLMSKCGKK
SSYYTTFDND VVTEQYRPKK SV
