SPIKE_BCHK3
ID SPIKE_BCHK3 Reviewed; 1242 AA.
AC Q3LZX1;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
DE Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
DE AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04099};
DE AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04099};
DE Contains:
DE RecName: Full=Spike protein S1 {ECO:0000255|HAMAP-Rule:MF_04099};
DE Contains:
DE RecName: Full=Spike protein S2 {ECO:0000255|HAMAP-Rule:MF_04099};
DE Contains:
DE RecName: Full=Spike protein S2' {ECO:0000255|HAMAP-Rule:MF_04099};
DE Flags: Precursor;
GN Name=S {ECO:0000255|HAMAP-Rule:MF_04099}; ORFNames=2;
OS Bat coronavirus HKU3 (BtCoV) (SARS-like coronavirus HKU3).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Sarbecovirus.
OX NCBI_TaxID=442736;
OH NCBI_TaxID=89399; Rhinolophus sinicus (Chinese rufous horseshoe bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HKU3-1;
RX PubMed=16169905; DOI=10.1073/pnas.0506735102;
RA Lau S.K.P., Woo P.C.Y., Li K.S.M., Huang Y., Tsoi H.-W., Wong B.H.L.,
RA Wong S.S.Y., Leung S.-Y., Chan K.-H., Yuen K.-Y.;
RT "Severe acute respiratory syndrome coronavirus-like virus in Chinese
RT horseshoe bats.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:14040-14045(2005).
CC -!- FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane
CC by interacting with host receptor, initiating the infection.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
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 three conformational
CC states: pre-fusion native state, pre-hairpin intermediate state, and
CC post-fusion hairpin state. During viral and target cell membrane
CC fusion, the coiled coil regions (heptad repeats) assume a trimer-of-
CC hairpins structure, positioning the fusion peptide in close proximity
CC to the C-terminal region of the ectodomain. The formation of this
CC structure appears to drive apposition and subsequent fusion of viral
CC and target cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- FUNCTION: [Spike protein S2']: Acts as a viral fusion peptide which is
CC unmasked following S2 cleavage occurring upon virus endocytosis.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
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_04099}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass
CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host cell
CC membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_04099}. 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. {ECO:0000255|HAMAP-Rule:MF_04099}.
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 {ECO:0000255|HAMAP-Rule:MF_04099}.
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. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike
CC glycoprotein is digested within host endosomes. {ECO:0000255|HAMAP-
CC Rule:MF_04099}.
CC -!- MISCELLANEOUS: Bat coronavirus HKU3 is highly similar to SARS-CoV
CC (SARS-like).
CC -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ022305; AAY88866.1; -; Genomic_RNA.
DR BMRB; Q3LZX1; -.
DR SMR; Q3LZX1; -.
DR Proteomes; UP000007450; Genome.
DR GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
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-UniRule.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:UniProtKB-UniRule.
DR CDD; cd21624; SARS-CoV-like_Spike_S1_NTD; 1.
DR Gene3D; 2.60.120.960; -; 1.
DR HAMAP; MF_04099; BETA_CORONA_SPIKE; 1.
DR InterPro; IPR032500; bCoV_S1_N.
DR InterPro; IPR042578; BETA_CORONA_SPIKE.
DR InterPro; IPR043473; S2_sf_CoV.
DR InterPro; IPR043002; Spike_N_sf.
DR InterPro; IPR044341; Spike_S1_N_SARS-CoV-like.
DR InterPro; IPR018548; Spike_S1_RBD_bCoV.
DR InterPro; IPR036326; Spike_S1_RBD_sf_bCoV.
DR InterPro; IPR002552; Spike_S2_CoV.
DR InterPro; IPR044873; Spike_S2_CoV_HR1.
DR InterPro; IPR044874; Spike_S2_CoV_HR2.
DR Pfam; PF16451; bCoV_S1_N; 1.
DR Pfam; PF09408; bCoV_S1_RBD; 1.
DR Pfam; PF01601; CoV_S2; 1.
DR SUPFAM; SSF111474; SSF111474; 2.
DR SUPFAM; SSF143587; SSF143587; 1.
DR PROSITE; PS51921; BCOV_S1_CTD; 1.
DR PROSITE; PS51922; BCOV_S1_NTD; 1.
DR PROSITE; PS51923; COV_S2_HR1; 1.
PE 3: Inferred from homology;
KW Coiled coil; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW Membrane; Palmitate; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virulence;
KW Virus entry into host cell.
FT SIGNAL 1..13
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CHAIN 14..1242
FT /note="Spike glycoprotein"
FT /id="PRO_0000291365"
FT CHAIN 14..654
FT /note="Spike protein S1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000444059"
FT CHAIN 655..1242
FT /note="Spike protein S2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000291367"
FT CHAIN 785..1242
FT /note="Spike protein S2'"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000444060"
FT TOPO_DOM 14..1182
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TRANSMEM 1183..1203
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TOPO_DOM 1204..1242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DOMAIN 14..294
FT /note="BetaCoV S1-NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DOMAIN 325..500
FT /note="BetaCoV S1-CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT REGION 785..806
FT /note="Fusion peptide 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 804..824
FT /note="Fusion peptide 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 889..939
FT /note="Heptad repeat 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 1132..1171
FT /note="Heptad repeat 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 918..962
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 1144..1172
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT MOTIF 1238..1242
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT SITE 654..655
FT /note="Cleavage"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT SITE 784..785
FT /note="Cleavage"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 678
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 686
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 770
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1043
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1067
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1103
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1127
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1142
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1163
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DISULFID 19..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 134..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 282..292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 327..352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 370..423
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 382..498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 809..820
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
SQ SEQUENCE 1242 AA; 137570 MW; 67E4E434992929AB CRC64;
MKILIFAFLA NLAKAQEGCG IISRKPQPKM AQVSSSRRGV YYNDDIFRSD VLHLTQDYFL
PFDSNLTQYF SLNVDSDRYT YFDNPILDFG DGVYFAATEK SNVIRGWIFG SSFDNTTQSA
VIVNNSTHII IRVCNFNLCK EPMYTVSRGT QQNAWVYQSA FNCTYDRVEK SFQLDTTPKT
GNFKDLREYV FKNRDGFLSV YQTYTAVNLP RGLPTGFSVL KPILKLPFGI NITSYRVVMA
MFSQTTSNFL PESAAYYVGN LKYSTFMLRF NENGTITDAV DCSQNPLAEL KCTIKNFNVD
KGIYQTSNFR VSPTQEVIRF PNITNRCPFD KVFNATRFPN VYAWERTKIS DCVADYTVLY
NSTSFSTFKC YGVSPSKLID LCFTSVYADT FLIRSSEVRQ VAPGETGVIA DYNYKLPDDF
TGCVIAWNTA KHDTGNYYYR SHRKTKLKPF ERDLSSDDGN GVYTLSTYDF NPNVPVAYQA
TRVVVLSFEL LNAPATVCGP KLSTELVKNQ CVNFNFNGLK GTGVLTSSSK RFQSFQQFGR
DTSDFTDSVR DPQTLEILDI SPCSFGGVSV ITPGTNASSE VAVLYQDVNC TDVPTAIRAD
QLTPAWRVYS TGVNVFQTQA GCLIGAEHVN ASYECDIPIG AGICASYHTA SVLRSTGQKS
IVAYTMSLGA ENSIAYANNS IAIPTNFSIS VTTEVMPVSM AKTAVDCTMY ICGDSLECSN
LLLQYGSFCT QLNRALTGIA IEQDKNTQEV FAQVKQMYKT PAIKDFGGFN FSQILPDPSK
PTKRSFIEDL LFNKVTLADA GFMKQYGDCL GDVSARDLIC AQKFNGLTVL PPLLTDEMVA
AYTAALVSGT ATAGWTFGAG AALQIPFAMQ MAYRFNGIGV TQNVLYENQK LIANQFNSAI
GKIQESLSST ASALGKLQDV VNQNAQALNT LVKQLSSNFG AISSVLNDIL SRLDKVEAEV
QIDRLITGRL QSLQTYVTQQ LIRAAEIRAS ANLAATKMSE CVLGQSKRVD FCGKGYHLMS
FPQSAPHGVV FLHVTYVPSQ EKNFTTAPAI CHEGKAYFPR EGVFVSNGTS WFITQRNFYS
PQLITTDNTF VSGNCDVVIG IINNTVYDPL QPELDSFKEE LDKYFKNHTS PDVDLGDISG
INASVVNIQK EIDRLNEVAK NLNESLIDLQ ELGKYEQYIK WPWYVWLGFI AGLIAIVMVT
ILLCCMTSCC SCLKGACSCG SCCKFDEDDS EPVLKGVKLH YT
