SPIKE_CVHN5
ID SPIKE_CVHN5 Reviewed; 1351 AA.
AC Q0ZME7;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=3;
OS Human coronavirus HKU1 (isolate N5) (HCoV-HKU1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=443241;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16809319; DOI=10.1128/jvi.00509-06;
RA Woo P.C.Y., Lau S.K.P., Yip C.C.Y., Huang Y., Tsoi H.-W., Chan K.-H.,
RA Yuen K.-Y.;
RT "Comparative analysis of 22 coronavirus HKU1 genomes reveals a novel
RT genotype and evidence of natural recombination in coronavirus HKU1.";
RL J. Virol. 80:7136-7145(2006).
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 -!- INTERACTION:
CC Q0ZME7; Q0ZME7: S; NbExp=2; IntAct=EBI-16201169, EBI-16201169;
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: Isolate N5 belongs to genotype C. Genotype C probably
CC arose from recombination between genotypes A and B.
CC -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
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DR EMBL; DQ339101; ABC70719.1; -; Genomic_RNA.
DR PDB; 5I08; EM; 4.04 A; A/B/C=14-1276.
DR PDBsum; 5I08; -.
DR SMR; Q0ZME7; -.
DR DIP; DIP-61948N; -.
DR PRIDE; Q0ZME7; -.
DR Proteomes; UP000001985; 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:0042802; F:identical protein binding; IPI:IntAct.
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; cd21482; HKU1_N5-like_CoV_Spike_S1_RBD; 1.
DR CDD; cd21625; MHV-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; IPR044339; Spike_S1_NTD_MHV-like.
DR InterPro; IPR018548; Spike_S1_RBD_bCoV.
DR InterPro; IPR044375; Spike_S1_RBD_CoV_HKU1-like.
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; PF19209; CoV_S1_C; 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 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; 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..12
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CHAIN 13..1351
FT /note="Spike glycoprotein"
FT /id="PRO_0000297809"
FT CHAIN 13..756
FT /note="Spike protein S1"
FT /id="PRO_0000297810"
FT CHAIN 757..1351
FT /note="Spike protein S2"
FT /id="PRO_0000297811"
FT CHAIN 901..1351
FT /note="Spike protein S2'"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000444080"
FT TOPO_DOM 13..1295
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TRANSMEM 1296..1316
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TOPO_DOM 1317..1351
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..605
FT /note="BetaCoV S1-CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT REGION 901..922
FT /note="Fusion peptide 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 920..940
FT /note="Fusion peptide 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 1001..1051
FT /note="Heptad repeat 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 1245..1284
FT /note="Heptad repeat 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 1030..1074
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 1257..1285
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT MOTIF 1347..1351
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT SITE 756..757
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 900..901
FT /note="Cleavage"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine; by host"
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 58
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 114
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 171
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 664
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 725
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 776
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 793
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 924
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1181
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1211
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1221
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 1240
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1247
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1255
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1276
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DISULFID 20..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 151..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 163..242
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..603
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 925..936
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
SQ SEQUENCE 1351 AA; 150795 MW; 3FD3F7A5B3BEDE5C CRC64;
MFLIIFILPT TLAVIGDFNC TNSFINDYNK TIPRISEDVV DVSLGLGTYY VLNRVYLNTT
LLFTGYFPKS GANFRDLALK GSIYLSTLWY KPPFLSDFNN GIFSKVKNTK LYVNNTLYSE
FSTIVIGSVF VNTSYTIVVQ PHNGILEITA CQYTMCEYPH TVCKSKGSIR NESWHIDSSE
PLCLFKKNFT YNVSADWLYF HFYQERGVFY AYYADVGMPT TFLFSLYLGT ILSHYYVMPL
TCNAISSNTD NETLEYWVTP LSRRQYLLNF DEHGVITNAV DCSSSFLSEI QCKTQSFAPN
TGVYDLSGFT VKPVATVYRR IPNLPDCDID NWLNNVSVPS PLNWERRIFS NCNFNLSTLL
RLVHVDSFSC NNLDKSKIFG SCFNSITVDK FAIPNRRRDD LQLGSSGFLQ SSNYKIDISS
SSCQLYYSLP LVNVTINNFN PSSWNRRYGF GSFNLSSYDV VYSDHCFSVN SDFCPCADPS
VVNSCAKSKP PSAICPAGTK YRHCDLDTTL YVKNWCRCSC LPDPISTYSP NTCPQKKVVV
GIGEHCPGLG INEEKCGTQL NHSSCFCSPD AFLGWSFDSC ISNNRCNIFS NFIFNGINSG
TTCSNDLLYS NTEISTGVCV NYDLYGITGQ GIFKEVSAAY YNNWQNLLYD SNGNIIGFKD
FLTNKTYTIL PCYSGRVSAA FYQNSSSPAL LYRNLKCSYV LNNISFISQP FYFDSYLGCV
LNAVNLTSYS VSSCDLRMGS GFCIDYALPS SRRKRRGISS PYRFVTFEPF NVSFVNDSVE
TVGGLFEIQI PTNFTIAGHE EFIQTSSPKV TIDCSAFVCS NYAACHDLLS EYGTFCDNIN
SILNEVNDLL DITQLQVANA LMQGVTLSSN LNTNLHSDVD NIDFKSLLGC LGSQCGSSSR
SLLEDLLFNK VKLSDVGFVE AYNNCTGGSE IRDLLCVQSF NGIKVLPPIL SETQISGYTT
AATVAAMFPP WSAAAGVPFS LNVQYRINGL GVTMDVLNKN QKLIANAFNK ALLSIQNGFT
ATNSALAKIQ SVVNANAQAL NSLLQQLFNK FGAISSSLQE ILSRLDNLEA QVQIDRLING
RLTALNAYVS QQLSDITLIK AGASRAIEKV NECVKSQSPR INFCGNGNHI LSLVQNAPYG
LLFIHFSYKP TSFKTVLVSP GLCLSGDRGI APKQGYFIKQ NDSWMFTGSS YYYPEPISDK
NVVFMNSCSV NFTKAPFIYL NNSIPNLSDF EAELSLWFKN HTSIAPNLTF NSHINATFLD
LYYEMNVIQE SIKSLNSSFI NLKEIGTYEM YVKWPWYIWL LIVILFIIFL MILFFICCCT
GCGSACFSKC HNCCDEYGGH NDFVIKASHD D
