SPIKE_CVMJH
ID SPIKE_CVMJH Reviewed; 1235 AA.
AC P11225;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 135.
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 Murine coronavirus (strain JHM) (MHV-JHM) (Murine hepatitis virus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=11144;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3027248; DOI=10.1099/0022-1317-68-1-47;
RA Schmidt I., Skinner M.A., Siddell S.G.;
RT "Nucleotide sequence of the gene encoding the surface projection
RT glycoprotein of coronavirus MHV-JHM.";
RL J. Gen. Virol. 68:47-56(1987).
RN [2]
RP INTERACTION WITH MURINE CEACAM2.
RX PubMed=8207827; DOI=10.1128/jvi.68.7.4525-4537.1994;
RA Nedellec P., Dveksler G.S., Daniels E., Turbide C., Chow B., Basile A.A.,
RA Holmes K.V., Beauchemin N.;
RT "Bgp2, a new member of the carcinoembryonic antigen-related gene family,
RT encodes an alternative receptor for mouse hepatitis viruses.";
RL J. Virol. 68:4525-4537(1994).
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; X04797; CAA28484.1; -; mRNA.
DR PIR; A33095; VGIHMJ.
DR PDB; 2ZSV; X-ray; 1.80 A; E/F=457-464.
DR PDB; 2ZSW; X-ray; 2.80 A; M/N/O/P=457-464.
DR PDBsum; 2ZSV; -.
DR PDBsum; 2ZSW; -.
DR SMR; P11225; -.
DR EvolutionaryTrace; P11225; -.
DR Proteomes; UP000007193; 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..13
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CHAIN 14..1235
FT /note="Spike glycoprotein"
FT /id="PRO_0000037220"
FT CHAIN 14..628
FT /note="Spike protein S1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037221"
FT CHAIN 629..1235
FT /note="Spike protein S2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037222"
FT CHAIN 781..1235
FT /note="Spike protein S2'"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000444086"
FT TOPO_DOM 14..1176
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TRANSMEM 1177..1197
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TOPO_DOM 1198..1235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DOMAIN 15..296
FT /note="BetaCoV S1-NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DOMAIN 327..477
FT /note="BetaCoV S1-CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT REGION 1..330
FT /note="Receptor binding site"
FT REGION 781..802
FT /note="Fusion peptide 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 800..820
FT /note="Fusion peptide 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 881..931
FT /note="Heptad repeat 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 1125..1165
FT /note="Heptad repeat 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 910..954
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 1138..1166
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT MOTIF 1231..1235
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT SITE 628..629
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 780..781
FT /note="Cleavage"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 134
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 357
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 648
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 804
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1091
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1101
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1120
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1136
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 DISULFID 21..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 153..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 165..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 284..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 329..354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 372..425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 384..475
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 805..816
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
SQ SEQUENCE 1235 AA; 136654 MW; 25962AD6C1F92DD2 CRC64;
MLFVFILLLP SCLGYIGDFR CIQTVNYNGN NASAPSISTE AVDVSKGRGT YYVLDRVYLN
ATLLLTGYYP VDGSNYRNLA LTGTNTLSLT WFKPPFLSEF NDGIFAKVQN LKTNTPTGAT
SYFPTIVIGS LFGNTSYTVV LEPYNNIIMA SVCTYTICQL PYTPCKPNTN GNRVIGFWHT
DVKPPICLLK RNFTFNVNAP WLYFHFYQQG GTFYAYYADK PSATTFLFSV YIGDILTQYF
VLPFICTPTA GSTLAPLYWV TPLLKRQYLF NFNEKGVITS AVDCASSYIS EIKCKTQSLL
PSTGVYDLSG YTVQPVGVVY RRVPNLPDCK IEEWLTAKSV PSPLNWERRT FQNCNFNLSS
LLRYVQAESL SCNNIDASKV YGMCFGSVSV DKFAIPRSRQ IDLQIGNSGF LQTANYKIDT
AATSCQLYYS LPKNNVTINN YNPSSWNRRY GFKVNDRCQI FANILLNGIN SGTTCSTDLQ
LPNTEVATGV CVRYDLYGIT GQGVFKEVKA DYYNSWQALL YDVNGNLNGF RDLTTNKTYT
IRSCYSGRVS AAYHKEAPEP ALLYRNINCS YVFTNNISRE ENPLNYFDSY LGCVVNADNR
TDEALPNCNL RMGAGLCVDY SKSRRARRSV STGYRLTTFE PYMPMLVNDS VQSVGGLYEM
QIPTNFTIGH HEEFIQIRAP KVTIDCAAFV CGDNAACRQQ LVEYGSFCDN VNAILNEVNN
LLDNMQLQVA SALMQGVTIS SRLPDGISGP IDDINFSPLL GCIGSTCAED GNGPSAIRGR
SAIEDLLFDK VKLSDVGFVE AYNNCTGGQE VRDLLCVQSF NGIKVLPPVL SESQISGYTA
GATAAAMFPP WTAAAGVPFS LNVQYRINGL GVTMNVLSEN QKMIASAFNN ALGAIQEGFD
ATNSALGKIQ SVVNANAEAL NNLLNQLSNR FGAISASLQE ILTRLDAVEA KAQIDRLING
RLTALNAYIS KQLSDSTLIK FSAAQAIEKV NECVKSQTTR INFCGNGNHI LSLVQNAPYG
LCFIHFSYVP TSFKTANVSP GLCISGDRGL APKAGYFVQD NGEWKFTGSN YYYPEPITDK
NSVAMISCAV NYTKAPEVFL NNSIPNLPDF KEELDKWFKN QTSIAPDLSL DFEKLNVTFL
DLTYEMNRIQ DAIKKLNESY INLKEVGTYE MYVKWPWYVW LLIGLAGVAV CVLLFFICCC
TGCGSCCFRK CGSCCDEYGG HQDSIVIHNI SAHED
