SPIKE_BCHK4
ID SPIKE_BCHK4 Reviewed; 1352 AA.
AC A3EX94;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 HKU4 (BtCoV) (BtCoV/HKU4/2004).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Merbecovirus.
OX NCBI_TaxID=694007;
OH NCBI_TaxID=258959; Tylonycteris pachypus (Lesser bamboo bat) (Vespertilio pachypus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HKU4-1;
RX PubMed=17121802; DOI=10.1128/jvi.02182-06;
RA Woo P.C.Y., Wang M., Lau S.K.P., Xu H.F., Poon R.W.S., Guo R., Wong B.H.L.,
RA Gao K., Tsoi H.-W., Huang Y., Li K.S.M., Lam C.S.F., Chan K.-H.,
RA Zheng B.-J., Yuen K.-Y.;
RT "Comparative analysis of twelve genomes of three novel group 2c and group
RT 2d coronaviruses reveals unique group and subgroup features.";
RL J. Virol. 81:1574-1585(2007).
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 -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
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DR EMBL; EF065505; ABN10839.1; -; Genomic_RNA.
DR RefSeq; YP_001039953.1; NC_009019.1.
DR PDB; 4QZV; X-ray; 2.59 A; B/D=372-611.
DR PDB; 7M52; X-ray; 1.50 A; A=1231-1245.
DR PDBsum; 4QZV; -.
DR PDBsum; 7M52; -.
DR SMR; A3EX94; -.
DR GeneID; 4835991; -.
DR KEGG; vg:4835991; -.
DR Proteomes; UP000006574; 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; cd21487; bat_HKU4-like_Spike_S1_RBD; 1.
DR CDD; cd21626; MERS-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; IPR043607; CoV_S1_C.
DR InterPro; IPR043473; S2_sf_CoV.
DR InterPro; IPR043002; Spike_N_sf.
DR InterPro; IPR044337; Spike_S1_N_MERS-CoV-like.
DR InterPro; IPR018548; Spike_S1_RBD_bCoV.
DR InterPro; IPR044378; Spike_S1_RBD_HKU4-like.
DR InterPro; IPR036326; Spike_S1_RBD_sf_bCoV.
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; PF16451; bCoV_S1_N; 1.
DR Pfam; PF09408; bCoV_S1_RBD; 1.
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 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 1: Evidence at protein level;
KW 3D-structure; 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; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; 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..12
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CHAIN 13..1352
FT /note="Spike glycoprotein"
FT /id="PRO_0000290321"
FT CHAIN 13..746
FT /note="Spike protein S1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000444061"
FT CHAIN 750..1235
FT /note="Spike protein S2"
FT /id="PRO_0000290323"
FT CHAIN 887..1352
FT /note="Spike protein S2'"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000444062"
FT TOPO_DOM 13..1297
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TRANSMEM 1298..1318
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TOPO_DOM 1319..1352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DOMAIN 21..356
FT /note="BetaCoV S1-NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DOMAIN 386..592
FT /note="BetaCoV S1-CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT REGION 887..908
FT /note="Fusion peptide 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 906..928
FT /note="Fusion peptide 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 993..1043
FT /note="Heptad repeat 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 1247..1286
FT /note="Heptad repeat 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 1022..1066
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 1259..1287
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT MOTIF 1350..1352
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT SITE 749..750
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 886..887
FT /note="Cleavage"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 132
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 172
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 723
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 762
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 773
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 784
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 869
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1144
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1147
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1174
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1226
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1242
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1257
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1278
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1289
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DISULFID 191..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 344..354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 388..412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 430..483
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 442..590
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 911..924
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:4QZV"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:4QZV"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:4QZV"
FT HELIX 416..420
FT /evidence="ECO:0007829|PDB:4QZV"
FT STRAND 423..433
FT /evidence="ECO:0007829|PDB:4QZV"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:4QZV"
FT STRAND 443..452
FT /evidence="ECO:0007829|PDB:4QZV"
FT HELIX 455..461
FT /evidence="ECO:0007829|PDB:4QZV"
FT HELIX 468..472
FT /evidence="ECO:0007829|PDB:4QZV"
FT STRAND 482..489
FT /evidence="ECO:0007829|PDB:4QZV"
FT STRAND 499..511
FT /evidence="ECO:0007829|PDB:4QZV"
FT TURN 512..515
FT /evidence="ECO:0007829|PDB:4QZV"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:4QZV"
FT HELIX 532..534
FT /evidence="ECO:0007829|PDB:4QZV"
FT STRAND 544..549
FT /evidence="ECO:0007829|PDB:4QZV"
FT TURN 552..555
FT /evidence="ECO:0007829|PDB:4QZV"
FT STRAND 556..567
FT /evidence="ECO:0007829|PDB:4QZV"
FT STRAND 573..581
FT /evidence="ECO:0007829|PDB:4QZV"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:4QZV"
FT HELIX 1232..1239
FT /evidence="ECO:0007829|PDB:7M52"
SQ SEQUENCE 1352 AA; 149029 MW; 2E75232D7E4E693A CRC64;
MTLLMCLLMS LLIFVRGCDS QFVDMSPASN TSECLESQVD AAAFSKLMWP YPIDPSKVDG
IIYPLGRTYS NITLAYTGLF PLQGDLGSQY LYSVSHAVGH DGDPTKAYIS NYSLLVNDFD
NGFVVRIGAA ANSTGTIVIS PSVNTKIKKA YPAFILGSSL TNTSAGQPLY ANYSLTIIPD
GCGTVLHAFY CILKPRTVNR CPSGTGYVSY FIYETVHNDC QSTINRNASL NSFKSFFDLV
NCTFFNSWDI TADETKEWFG ITQDTQGVHL YSSRKGDLYG GNMFRFATLP VYEGIKYYTV
IPRSFRSKAN KREAWAAFYV YKLHQLTYLL DFSVDGYIRR AIDCGHDDLS QLHCSYTSFE
VDTGVYSVSS YEASATGTFI EQPNATECDF SPMLTGVAPQ VYNFKRLVFS NCNYNLTKLL
SLFAVDEFSC NGISPDSIAR GCYSTLTVDY FAYPLSMKSY IRPGSAGNIP LYNYKQSFAN
PTCRVMASVL ANVTITKPHA YGYISKCSRL TGANQDVETP LYINPGEYSI CRDFSPGGFS
EDGQVFKRTL TQFEGGGLLI GVGTRVPMTD NLQMSFIISV QYGTGTDSVC PMLDLGDSLT
ITNRLGKCVD YSLYGVTGRG VFQNCTAVGV KQQRFVYDSF DNLVGYYSDD GNYYCVRPCV
SVPVSVIYDK STNLHATLFG SVACEHVTTM MSQFSRLTQS NLRRRDSNIP LQTAVGCVIG
LSNNSLVVSD CKLPLGQSLC AVPPVSTFRS YSASQFQLAV LNYTSPIVVT PINSSGFTAA
IPTNFSFSVT QEYIETSIQK VTVDCKQYVC NGFTRCEKLL VEYGQFCSKI NQALHGANLR
QDESVYSLYS NIKTTSTQTL EYGLNGDFNL TLLQVPQIGG SSSSYRSAIE DLLFDKVTIA
DPGYMQGYDD CMKQGPQSAR DLICAQYVSG YKVLPPLYDP NMEAAYTSSL LGSIAGAGWT
AGLSSFAAIP FAQSMFYRLN GVGITQQVLS ENQKLIANKF NQALGAMQTG FTTSNLAFSK
VQDAVNANAQ ALSKLASELS NTFGAISSSI SDILARLDTV EQDAQIDRLI NGRLISLNAF
VSQQLVRSET AARSAQLASD KVNECVKSQS KRNGFCGSGT HIVSFVVNAP NGFYFFHVGY
VPTNYTNVTA AYGLCNNNNP PLCIAPIDGY FITNQTTTYS VDTEWYYTGS SFYKPEPITQ
ANSRYVSSDV KFDKLENNLP PPLLENSTDV DFKDELEEFF KNVTSHGPNF AEISKINTTL
LDLSDEMAML QEVVKQLNDS YIDLKELGNY TYYNKWPWYV WLGFIAGLVA LLLCVFFLLC
CTGCGTSCLG KMKCKNCCDS YEEYDVEKIH VH
