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Protein

Spike glycoprotein

Gene

S

Organism
Murine coronavirus (strain JHM) (MHV-JHM) (Murine hepatitis virus)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Spike protein S1: attaches the virion to the cell membrane by interacting with host receptor, initiating the infection.UniRule annotation
Spike protein S2: mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.UniRule annotation
Spike protein S2': Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.UniRule annotation

GO - Biological processi

Keywordsi

Biological processFusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virulence, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Spike glycoproteinUniRule annotation
Short name:
S glycoproteinUniRule annotation
Alternative name(s):
E2UniRule annotation
Peplomer proteinUniRule annotation
Cleaved into the following 3 chains:
Spike protein S1UniRule annotation
Spike protein S2UniRule annotation
Spike protein S2'UniRule annotation
Gene namesi
Name:SUniRule annotation
ORF Names:3
OrganismiMurine coronavirus (strain JHM) (MHV-JHM) (Murine hepatitis virus)
Taxonomic identifieri11144 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
Proteomesi
  • UP000007193 Componenti: Genome

Subcellular locationi

  • Virion membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Host endoplasmic reticulum-Golgi intermediate compartment membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Host cell membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Note: Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers are transported to the host plasma membrane, where they may mediate cell-cell fusion.UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini14 – 1176ExtracellularUniRule annotationAdd BLAST1163
Transmembranei1177 – 1197HelicalUniRule annotationAdd BLAST21
Topological domaini1198 – 1235CytoplasmicUniRule annotationAdd BLAST38

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 13UniRule annotationAdd BLAST13
ChainiPRO_000003722014 – 1235Spike glycoproteinAdd BLAST1222
ChainiPRO_000003722114 – 628Spike protein S1By similarityAdd BLAST615
ChainiPRO_0000037222629 – 1235Spike protein S2By similarityAdd BLAST607
ChainiPRO_0000444086781 – 1235Spike protein S2'UniRule annotationAdd BLAST455

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi31N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi60N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi134N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi192N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi329 ↔ 354UniRule annotation
Glycosylationi357N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi372 ↔ 425UniRule annotation
Glycosylationi435N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi536N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi568N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi576N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi599N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi648N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi665N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi804N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi1091N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi1101N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi1120N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi1136N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi1157N-linked (GlcNAc...) asparagine; by hostUniRule annotation1

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host cell furin or another cellular protease to yield the mature S1 and S2 proteins. Additionally, a second cleavage leads to the release of a fusion peptide after viral attachment to host cell receptor.UniRule annotation
The cytoplasmic Cys-rich domain is palmitoylated. Spike glycoprotein is digested within host endosomes.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei628 – 629Cleavage; by hostBy similarity2
Sitei780 – 781CleavageUniRule annotation2

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PRIDEiP11225

Interactioni

Subunit structurei

Homotrimer; each monomer consists of a S1 and a S2 subunit. The resulting peplomers protrude from the virus surface as spikes.UniRule annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZSVX-ray1.80E/F457-464[»]
2ZSWX-ray2.80M/N/O/P457-464[»]
ProteinModelPortaliP11225
SMRiP11225
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11225

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 330Receptor binding siteAdd BLAST330
Regioni312 – 494Receptor-binding domainUniRule annotationAdd BLAST183
Regioni738 – 760Fusion peptideUniRule annotationAdd BLAST23
Regioni881 – 931Heptad repeat 1UniRule annotationAdd BLAST51
Regioni1125 – 1165Heptad repeat 2UniRule annotationAdd BLAST41

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili910 – 954UniRule annotationAdd BLAST45
Coiled coili1138 – 1166UniRule annotationAdd BLAST29

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1231 – 1235KxHxxUniRule annotation5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1198 – 1215Cys-richAdd BLAST18

Sequence similaritiesi

Belongs to the betacoronaviruses spike protein family.UniRule annotation

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

OrthoDBiVOG0900000Z

Family and domain databases

Gene3Di1.20.5.790, 1 hit
HAMAPiMF_04099 BETA_CORONA_SPIKE, 1 hit
InterProiView protein in InterPro
IPR002552 Corona_S2
IPR027400 S_HR2
IPR032500 Spike_N
IPR018548 Spike_rcpt-bd
IPR036326 Spike_rcpt-bd_sf
PfamiView protein in Pfam
PF01601 Corona_S2, 1 hit
PF16451 Spike_NTD, 1 hit
PF09408 Spike_rec_bind, 1 hit
SUPFAMiSSF143587 SSF143587, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11225-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFVFILLLP SCLGYIGDFR CIQTVNYNGN NASAPSISTE AVDVSKGRGT
60 70 80 90 100
YYVLDRVYLN ATLLLTGYYP VDGSNYRNLA LTGTNTLSLT WFKPPFLSEF
110 120 130 140 150
NDGIFAKVQN LKTNTPTGAT SYFPTIVIGS LFGNTSYTVV LEPYNNIIMA
160 170 180 190 200
SVCTYTICQL PYTPCKPNTN GNRVIGFWHT DVKPPICLLK RNFTFNVNAP
210 220 230 240 250
WLYFHFYQQG GTFYAYYADK PSATTFLFSV YIGDILTQYF VLPFICTPTA
260 270 280 290 300
GSTLAPLYWV TPLLKRQYLF NFNEKGVITS AVDCASSYIS EIKCKTQSLL
310 320 330 340 350
PSTGVYDLSG YTVQPVGVVY RRVPNLPDCK IEEWLTAKSV PSPLNWERRT
360 370 380 390 400
FQNCNFNLSS LLRYVQAESL SCNNIDASKV YGMCFGSVSV DKFAIPRSRQ
410 420 430 440 450
IDLQIGNSGF LQTANYKIDT AATSCQLYYS LPKNNVTINN YNPSSWNRRY
460 470 480 490 500
GFKVNDRCQI FANILLNGIN SGTTCSTDLQ LPNTEVATGV CVRYDLYGIT
510 520 530 540 550
GQGVFKEVKA DYYNSWQALL YDVNGNLNGF RDLTTNKTYT IRSCYSGRVS
560 570 580 590 600
AAYHKEAPEP ALLYRNINCS YVFTNNISRE ENPLNYFDSY LGCVVNADNR
610 620 630 640 650
TDEALPNCNL RMGAGLCVDY SKSRRARRSV STGYRLTTFE PYMPMLVNDS
660 670 680 690 700
VQSVGGLYEM QIPTNFTIGH HEEFIQIRAP KVTIDCAAFV CGDNAACRQQ
710 720 730 740 750
LVEYGSFCDN VNAILNEVNN LLDNMQLQVA SALMQGVTIS SRLPDGISGP
760 770 780 790 800
IDDINFSPLL GCIGSTCAED GNGPSAIRGR SAIEDLLFDK VKLSDVGFVE
810 820 830 840 850
AYNNCTGGQE VRDLLCVQSF NGIKVLPPVL SESQISGYTA GATAAAMFPP
860 870 880 890 900
WTAAAGVPFS LNVQYRINGL GVTMNVLSEN QKMIASAFNN ALGAIQEGFD
910 920 930 940 950
ATNSALGKIQ SVVNANAEAL NNLLNQLSNR FGAISASLQE ILTRLDAVEA
960 970 980 990 1000
KAQIDRLING RLTALNAYIS KQLSDSTLIK FSAAQAIEKV NECVKSQTTR
1010 1020 1030 1040 1050
INFCGNGNHI LSLVQNAPYG LCFIHFSYVP TSFKTANVSP GLCISGDRGL
1060 1070 1080 1090 1100
APKAGYFVQD NGEWKFTGSN YYYPEPITDK NSVAMISCAV NYTKAPEVFL
1110 1120 1130 1140 1150
NNSIPNLPDF KEELDKWFKN QTSIAPDLSL DFEKLNVTFL DLTYEMNRIQ
1160 1170 1180 1190 1200
DAIKKLNESY INLKEVGTYE MYVKWPWYVW LLIGLAGVAV CVLLFFICCC
1210 1220 1230
TGCGSCCFRK CGSCCDEYGG HQDSIVIHNI SAHED
Length:1,235
Mass (Da):136,654
Last modified:July 1, 1989 - v1
Checksum:i25962AD6C1F92DD2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04797 mRNA Translation: CAA28484.1
PIRiA33095 VGIHMJ

Similar proteinsi

Entry informationi

Entry nameiSPIKE_CVMJH
AccessioniPrimary (citable) accession number: P11225
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 23, 2018
This is version 113 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

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