SPIKE_CVHN1
ID SPIKE_CVHN1 Reviewed; 1356 AA.
AC Q5MQD0;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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 N1) (HCoV-HKU1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=443239;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15613317; DOI=10.1128/jvi.79.2.884-895.2005;
RA Woo P.C.Y., Lau S.K.P., Chu C.-M., Chan K.-H., Tsoi H.-W., Huang Y.,
RA Wong B.H.L., Poon R.W.S., Cai J.J., Luk W.-K., Poon L.L.M., Wong S.S.Y.,
RA Guan Y., Peiris J.S.M., Yuen K.-Y.;
RT "Characterization and complete genome sequence of a novel coronavirus,
RT coronavirus HKU1, from patients with pneumonia.";
RL J. Virol. 79:884-895(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: Isolate N1 belongs to genotype A.
CC -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
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DR EMBL; AY597011; AAT98580.1; -; Genomic_RNA.
DR RefSeq; YP_173238.1; NC_006577.2.
DR PDB; 5GNB; X-ray; 2.30 A; A=307-677.
DR PDB; 5KWB; X-ray; 1.91 A; A=307-677.
DR PDBsum; 5GNB; -.
DR PDBsum; 5KWB; -.
DR SMR; Q5MQD0; -.
DR GeneID; 3200426; -.
DR KEGG; vg:3200426; -.
DR Proteomes; UP000008170; 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; 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; 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; 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..1356
FT /note="Spike glycoprotein"
FT /id="PRO_0000297803"
FT CHAIN 13..760
FT /note="Spike protein S1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000297804"
FT CHAIN 761..1356
FT /note="Spike protein S2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000297805"
FT CHAIN 905..1356
FT /note="Spike protein S2'"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000444078"
FT TOPO_DOM 13..1300
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TRANSMEM 1301..1321
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TOPO_DOM 1322..1356
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..607
FT /note="BetaCoV S1-CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT REGION 905..926
FT /note="Fusion peptide 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 924..944
FT /note="Fusion peptide 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 1005..1055
FT /note="Heptad repeat 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 1249..1289
FT /note="Heptad repeat 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 1034..1078
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 1262..1290
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT MOTIF 1352..1356
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT SITE 760..761
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 904..905
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 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 470
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 666
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 705
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 726
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 775
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 928
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1215
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1225
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1244
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1251
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1260
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1281
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..605
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 929..940
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:5KWB"
FT HELIX 329..333
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:5KWB"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:5KWB"
FT HELIX 356..362
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 364..373
FT /evidence="ECO:0007829|PDB:5KWB"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 382..392
FT /evidence="ECO:0007829|PDB:5KWB"
FT HELIX 395..401
FT /evidence="ECO:0007829|PDB:5KWB"
FT HELIX 408..412
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 422..430
FT /evidence="ECO:0007829|PDB:5KWB"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:5KWB"
FT HELIX 443..447
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 459..464
FT /evidence="ECO:0007829|PDB:5KWB"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 504..509
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 512..520
FT /evidence="ECO:0007829|PDB:5KWB"
FT TURN 524..526
FT /evidence="ECO:0007829|PDB:5KWB"
FT HELIX 530..532
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:5KWB"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 556..558
FT /evidence="ECO:0007829|PDB:5KWB"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 576..581
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 587..598
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 602..606
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 619..626
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 629..638
FT /evidence="ECO:0007829|PDB:5KWB"
FT HELIX 640..642
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 646..651
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 657..661
FT /evidence="ECO:0007829|PDB:5KWB"
FT TURN 663..665
FT /evidence="ECO:0007829|PDB:5KWB"
FT STRAND 668..672
FT /evidence="ECO:0007829|PDB:5KWB"
SQ SEQUENCE 1356 AA; 151711 MW; EE319676930C844E CRC64;
MLLIIFILPT TLAVIGDFNC TNFAINDLNT TVPRISEYVV DVSYGLGTYY ILDRVYLNTT
ILFTGYFPKS GANFRDLSLK GTTYLSTLWY QKPFLSDFNN GIFSRVKNTK LYVNKTLYSE
FSTIVIGSVF INNSYTIVVQ PHNGVLEITA CQYTMCEYPH TICKSKGSSR NESWHFDKSE
PLCLFKKNFT YNVSTDWLYF HFYQERGTFY AYYADSGMPT TFLFSLYLGT LLSHYYVLPL
TCNAISSNTD NETLQYWVTP LSKRQYLLKF DNRGVITNAV DCSSSFFSEI QCKTKSLLPN
TGVYDLSGFT VKPVATVHRR IPDLPDCDID KWLNNFNVPS PLNWERKIFS NCNFNLSTLL
RLVHTDSFSC NNFDESKIYG SCFKSIVLDK FAIPNSRRSD LQLGSSGFLQ SSNYKIDTTS
SSCQLYYSLP AINVTINNYN PSSWNRRYGF NNFNLSSHSV VYSRYCFSVN NTFCPCAKPS
FASSCKSHKP PSASCPIGTN YRSCESTTVL DHTDWCRCSC LPDPITAYDP RSCSQKKSLV
GVGEHCAGFG VDEEKCGVLD GSYNVSCLCS TDAFLGWSYD TCVSNNRCNI FSNFILNGIN
SGTTCSNDLL QPNTEVFTDV CVDYDLYGIT GQGIFKEVSA VYYNSWQNLL YDSNGNIIGF
KDFVTNKTYN IFPCYAGRVS AAFHQNASSL ALLYRNLKCS YVLNNISLTT QPYFDSYLGC
VFNADNLTDY SVSSCALRMG SGFCVDYNSP SSSSSRRKRR SISASYRFVT FEPFNVSFVN
DSIESVGGLY EIKIPTNFTI VGQEEFIQTN SPKVTIDCSL FVCSNYAACH DLLSEYGTFC
DNINSILDEV NGLLDTTQLH VADTLMQGVT LSSNLNTNLH FDVDNINFKS LVGCLGPHCG
SSSRSFFEDL LFDKVKLSDV GFVEAYNNCT GGSEIRDLLC VQSFNGIKVL PPILSESQIS
GYTTAATVAA MFPPWSAAAG IPFSLNVQYR INGLGVTMDV LNKNQKLIAT AFNNALLSIQ
NGFSATNSAL AKIQSVVNSN AQALNSLLQQ LFNKFGAISS SLQEILSRLD ALEAQVQIDR
LINGRLTALN AYVSQQLSDI SLVKFGAALA MEKVNECVKS QSPRINFCGN GNHILSLVQN
APYGLLFMHF SYKPISFKTV LVSPGLCISG DVGIAPKQGY FIKHNDHWMF TGSSYYYPEP
ISDKNVVFMN TCSVNFTKAP LVYLNHSVPK LSDFESELSH WFKNQTSIAP NLTLNLHTIN
ATFLDLYYEM NLIQESIKSL NNSYINLKDI GTYEMYVKWP WYVWLLISFS FIIFLVLLFF
ICCCTGCGSA CFSKCHNCCD EYGGHHDFVI KTSHDD
