SPIKE_BCHK9
ID SPIKE_BCHK9 Reviewed; 1274 AA.
AC A3EXG6;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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 HKU9 (BtCoV) (BtCoV/HKU9).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Nobecovirus.
OX NCBI_TaxID=694006;
OH NCBI_TaxID=9408; Rousettus leschenaultii (Leschenault's rousette).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HKU9-1;
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; EF065513; ABN10911.1; -; Genomic_RNA.
DR RefSeq; YP_001039971.1; NC_009021.1.
DR PDB; 5GYQ; X-ray; 2.10 A; A=355-521.
DR PDBsum; 5GYQ; -.
DR SMR; A3EXG6; -.
DR IntAct; A3EXG6; 1.
DR GeneID; 4836012; -.
DR KEGG; vg:4836012; -.
DR Proteomes; UP000006576; 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; cd21627; batCoV-HKU9-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; IPR044338; Spike_S1_N_batCoV-HKU9-like.
DR InterPro; IPR018548; Spike_S1_RBD_bCoV.
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..11
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CHAIN 12..1274
FT /note="Spike glycoprotein"
FT /id="PRO_0000291368"
FT CHAIN 12..676
FT /note="Spike protein S1"
FT /id="PRO_0000291369"
FT CHAIN 677..1274
FT /note="Spike protein S2"
FT /id="PRO_0000291370"
FT CHAIN 810..1274
FT /note="Spike protein S2'"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000444065"
FT TOPO_DOM 12..1212
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TRANSMEM 1213..1233
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TOPO_DOM 1234..1274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DOMAIN 15..325
FT /note="BetaCoV S1-NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DOMAIN 355..519
FT /note="BetaCoV S1-CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT REGION 810..831
FT /note="Fusion peptide 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 829..852
FT /note="Fusion peptide 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 917..967
FT /note="Heptad repeat 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 1162..1201
FT /note="Heptad repeat 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 946..990
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 1174..1202
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT MOTIF 1273..1274
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT SITE 676..677
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 809..810
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 34
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 688
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 705
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1042
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1081
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1096
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1113
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1128
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1133
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1157
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 CARBOHYD 1172
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1193
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DISULFID 19..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 163..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 313..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 357..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 399..452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 411..517
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 834..848
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:5GYQ"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:5GYQ"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:5GYQ"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:5GYQ"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:5GYQ"
FT STRAND 394..402
FT /evidence="ECO:0007829|PDB:5GYQ"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:5GYQ"
FT STRAND 412..422
FT /evidence="ECO:0007829|PDB:5GYQ"
FT HELIX 424..432
FT /evidence="ECO:0007829|PDB:5GYQ"
FT HELIX 437..441
FT /evidence="ECO:0007829|PDB:5GYQ"
FT STRAND 451..462
FT /evidence="ECO:0007829|PDB:5GYQ"
FT HELIX 481..490
FT /evidence="ECO:0007829|PDB:5GYQ"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:5GYQ"
FT STRAND 497..508
FT /evidence="ECO:0007829|PDB:5GYQ"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:5GYQ"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:5GYQ"
SQ SEQUENCE 1274 AA; 139717 MW; C338AAD47B846966 CRC64;
MLLILVLGVS LAAASRPECF NPRFTLTPLN HTLNYTSIKA KVSNVLLPDP YIAYSGQTLR
QNLFMADMSN TILYPVTPPA NGANGGFIYN TSIIPVSAGL FVNTWMYRQP ASSRAYCQEP
FGVAFGDTFE NDRIAILIMA PDNLGSWSAV APRNQTNIYL LVCSNATLCI NPGFNRWGPA
GSFIAPDALV DHSNSCFVNN TFSVNISTSR ISLAFLFKDG DLLIYHSGWL PTSNFEHGFS
RGSHPMTYFM SLPVGGNLPR AQFFQSIVRS NAIDKGDGMC TNFDVNLHVA HLINRDLLVS
YFNNGSVANA ADCADSAAEE LYCVTGSFDP PTGVYPLSRY RAQVAGFVRV TQRGSYCTPP
YSVLQDPPQP VVWRRYMLYD CVFDFTVVVD SLPTHQLQCY GVSPRRLASM CYGSVTLDVM
RINETHLNNL FNRVPDTFSL YNYALPDNFY GCLHAFYLNS TAPYAVANRF PIKPGGRQSN
SAFIDTVINA AHYSPFSYVY GLAVITLKPA AGSKLVCPVA NDTVVITDRC VQYNLYGYTG
TGVLSKNTSL VIPDGKVFTA SSTGTIIGVS INSTTYSIMP CVTVPVSVGY HPNFERALLF
NGLSCSQRSR AVTEPVSVLW SASATAQDAF DTPSGCVVNV ELRNTTIVNT CAMPIGNSLC
FINGSIATAN ADSLPRLQLV NYDPLYDNST ATPMTPVYWV KVPTNFTLSA TEEYIQTTAP
KITIDCARYL CGDSSRCLNV LLHYGTFCND INKALSRVST ILDSALLSLV KELSINTRDE
VTTFSFDGDY NFTGLMGCLG PNCGATTYRS AFSDLLYDKV RITDPGFMQS YQKCIDSQWG
GSIRDLLCTQ TYNGIAVLPP IVSPAMQALY TSLLVGAVAS SGYTFGITSA GVIPFATQLQ
FRLNGIGVTT QVLVENQKLI ASSFNNALVN IQKGFTETSI ALSKMQDVIN QHAAQLHTLV
VQLGNSFGAI SSSINEIFSR LEGLAANAEV DRLINGRMMV LNTYVTQLLI QASEAKAQNA
LAAQKISECV KAQSLRNDFC GNGTHVLSIP QLAPNGVLFI HYAYTPTEYA FVQTSAGLCH
NGTGYAPRQG MFVLPNNTNM WHFTTMQFYN PVNISASNTQ VLTSCSVNYT SVNYTVLEPS
VPGDYDFQKE FDKFYKNLST IFNNTFNPND FNFSTVDVTA QIKSLHDVVN QLNQSFIDLK
KLNVYEKTIK WPWYVWLAMI AGIVGLVLAV IMLMCMTNCC SCFKGMCDCR RCCGSYDSYD
DVYPAVRVNK KRTV
