SPIKE_BCHK5
ID SPIKE_BCHK5 Reviewed; 1352 AA.
AC A3EXD0;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 HKU5 (BtCoV) (BtCoV/HKU5/2004).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Merbecovirus.
OX NCBI_TaxID=694008;
OH NCBI_TaxID=105295; Pipistrellus abramus (Japanese pipistrelle) (Pipistrellus javanicus abramus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HKU5-1;
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; EF065509; ABN10875.1; -; Genomic_RNA.
DR RefSeq; YP_001039962.1; NC_009020.1.
DR PDB; 5XGR; X-ray; 2.10 A; A/B/C/D/E/F/G/H=389-586.
DR PDBsum; 5XGR; -.
DR SMR; A3EXD0; -.
DR GeneID; 4836002; -.
DR KEGG; vg:4836002; -.
DR Proteomes; UP000007451; 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; cd21626; MERS-CoV-like_Spike_S1_NTD; 1.
DR CDD; cd21479; MERS-like_CoV_Spike_S1_RBD; 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; IPR044364; Spike_S1_RBD_MERS-CoV-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_0000290324"
FT CHAIN 13..745
FT /note="Spike protein S1"
FT /id="PRO_0000444063"
FT CHAIN 746..1352
FT /note="Spike protein S2"
FT /id="PRO_0000290326"
FT CHAIN 885..1352
FT /note="Spike protein S2'"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000444064"
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 22..359
FT /note="BetaCoV S1-NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DOMAIN 389..585
FT /note="BetaCoV S1-CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT REGION 885..906
FT /note="Fusion peptide 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 904..926
FT /note="Fusion peptide 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 991..1041
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 1020..1064
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 745..746
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 884..885
FT /note="Cleavage"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 73
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 167
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 716
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 760
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 867
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1145
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 1214
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 193..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 347..357
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 391..415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 433..486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 445..583
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 909..922
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:5XGR"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:5XGR"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:5XGR"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:5XGR"
FT HELIX 419..423
FT /evidence="ECO:0007829|PDB:5XGR"
FT STRAND 426..435
FT /evidence="ECO:0007829|PDB:5XGR"
FT HELIX 438..443
FT /evidence="ECO:0007829|PDB:5XGR"
FT STRAND 446..455
FT /evidence="ECO:0007829|PDB:5XGR"
FT HELIX 458..464
FT /evidence="ECO:0007829|PDB:5XGR"
FT HELIX 471..475
FT /evidence="ECO:0007829|PDB:5XGR"
FT STRAND 485..491
FT /evidence="ECO:0007829|PDB:5XGR"
FT STRAND 503..514
FT /evidence="ECO:0007829|PDB:5XGR"
FT STRAND 516..521
FT /evidence="ECO:0007829|PDB:5XGR"
FT HELIX 533..536
FT /evidence="ECO:0007829|PDB:5XGR"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:5XGR"
FT STRAND 550..560
FT /evidence="ECO:0007829|PDB:5XGR"
FT STRAND 566..574
FT /evidence="ECO:0007829|PDB:5XGR"
FT TURN 577..580
FT /evidence="ECO:0007829|PDB:5XGR"
FT STRAND 581..584
FT /evidence="ECO:0007829|PDB:5XGR"
SQ SEQUENCE 1352 AA; 149697 MW; E636107C2D80BA9A CRC64;
MIRSVLVLMC SLTFIGNLTR GQSVDMGHNG TGSCLDSQVQ PDYFESVHTT WPMPIDTSKA
EGVIYPNGKS YSNITLTYTG LYPKANDLGK QYLFSDGHSA PGRLNNLFVS NYSSQVESFD
DGFVVRIGAA ANKTGTTVIS QSTFKPIKKI YPAFLLGHSV GNYTPSNRTG RYLNHTLVIL
PDGCGTILHA FYCVLHPRTQ QNCAGETNFK SLSLWDTPAS DCVSGSYNQE ATLGAFKVYF
DLINCTFRYN YTITEDENAE WFGITQDTQG VHLYSSRKEN VFRNNMFHFA TLPVYQKILY
YTVIPRSIRS PFNDRKAWAA FYIYKLHPLT YLLNFDVEGY ITKAVDCGYD DLAQLQCSYE
SFEVETGVYS VSSFEASPRG EFIEQATTQE CDFTPMLTGT PPPIYNFKRL VFTNCNYNLT
KLLSLFQVSE FSCHQVSPSS LATGCYSSLT VDYFAYSTDM SSYLQPGSAG AIVQFNYKQD
FSNPTCRVLA TVPQNLTTIT KPSNYAYLTE CYKTSAYGKN YLYNAPGAYT PCLSLASRGF
STKYQSHSDG ELTTTGYIYP VTGNLQMAFI ISVQYGTDTN SVCPMQALRN DTSIEDKLDV
CVEYSLHGIT GRGVFHNCTS VGLRNQRFVY DTFDNLVGYH SDNGNYYCVR PCVSVPVSVI
YDKASNSHAT LFGSVACSHV TTMMSQFSRM TKTNLLARTT PGPLQTTVGC AMGFINSSMV
VDECQLPLGQ SLCAIPPTTS SRVRRATSGA SDVFQIATLN FTSPLTLAPI NSTGFVVAVP
TNFTFGVTQE FIETTIQKIT VDCKQYVCNG FKKCEDLLKE YGQFCSKINQ ALHGANLRQD
ESIANLFSSI KTQNTQPLQA GLNGDFNLTM LQIPQVTTGE RKYRSTIEDL LFNKVTIADP
GYMQGYDECM QQGPQSARDL ICAQYVAGYK VLPPLYDPYM EAAYTSSLLG SIAGASWTAG
LSSFAAIPFA QSIFYRLNGV GITQQVLSEN QKIIANKFNQ ALGAMQTGFT TTNLAFNKVQ
DAVNANAMAL SKLAAELSNT FGAISSSISD ILARLDTVEQ EAQIDRLING RLTSLNAFVA
QQLVRTEAAA RSAQLAQDKV NECVKSQSKR NGFCGTGTHI VSFAINAPNG LYFFHVGYQP
TSHVNATAAY GLCNTENPQK CIAPIDGYFV LNQTTSTVAD SDQQWYYTGS SFFHPEPITE
ANSKYVSMDV KFENLTNRLP PPLLSNSTDL DFKEELEEFF KNVSSQGPNF QEISKINTTL
LNLNTELMVL SEVVKQLNES YIDLKELGNY TFYQKWPWYI WLGFIAGLVA LALCVFFILC
CTGCGTSCLG KLKCNRCCDS YDEYEVEKIH VH
