UniProtKB - Q02385 (SPIKE_CVMJC)
Protein
Spike glycoprotein
Gene
S
Organism
Murine coronavirus (strain JHMV / variant CL-2) (MHV) (Murine hepatitis virus)
Status
Functioni
attaches the virion to the cell membrane by interacting with host receptor, initiating the infection.UniRule annotation
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
Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.UniRule annotation
GO - Biological processi
- endocytosis involved in viral entry into host cell Source: UniProtKB-UniRule
- fusion of virus membrane with host endosome membrane Source: UniProtKB-UniRule
- fusion of virus membrane with host plasma membrane Source: UniProtKB-UniRule
- pathogenesis Source: UniProtKB-KW
- receptor-mediated virion attachment to host cell Source: UniProtKB-UniRule
Keywordsi
Names & Taxonomyi
Protein namesi | Recommended name: Spike glycoproteinUniRule annotationShort 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 |
Organismi | Murine coronavirus (strain JHMV / variant CL-2) (MHV) (Murine hepatitis virus) |
Taxonomic identifieri | 33735 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Nidovirales › Cornidovirineae › Coronaviridae › Orthocoronavirinae › Betacoronavirus › Embecovirus › |
Virus hosti | Mus musculus (Mouse) [TaxID: 10090] |
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 14 – 1317 | ExtracellularUniRule annotationAdd BLAST | 1304 | |
Transmembranei | 1318 – 1338 | HelicalUniRule annotationAdd BLAST | 21 | |
Topological domaini | 1339 – 1376 | CytoplasmicUniRule annotationAdd BLAST | 38 |
GO - Cellular componenti
- host cell endoplasmic reticulum-Golgi intermediate compartment membrane Source: UniProtKB-SubCell
- host cell plasma membrane Source: UniProtKB-SubCell
- integral component of membrane Source: UniProtKB-UniRule
- viral envelope Source: UniProtKB-UniRule
- virion membrane Source: UniProtKB-SubCell
Keywords - Cellular componenti
Host cell membrane, Host membrane, Membrane, Viral envelope protein, VirionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 13 | UniRule annotationAdd BLAST | 13 | |
ChainiPRO_0000037217 | 14 – 1376 | Spike glycoproteinAdd BLAST | 1363 | |
ChainiPRO_0000037218 | 14 – 769 | Spike protein S1Add BLAST | 756 | |
ChainiPRO_0000037219 | 770 – 1376 | Spike protein S2Add BLAST | 607 | |
ChainiPRO_0000444085 | 922 – 1376 | Spike protein S2'UniRule annotationAdd BLAST | 455 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 21 ↔ 158 | PROSITE-ProRule annotation | ||
Glycosylationi | 31 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 60 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 134 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Disulfide bondi | 153 ↔ 187 | PROSITE-ProRule annotation | ||
Disulfide bondi | 165 ↔ 246 | PROSITE-ProRule annotation | ||
Glycosylationi | 192 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Disulfide bondi | 284 ↔ 294 | PROSITE-ProRule annotation | ||
Disulfide bondi | 329 ↔ 354 | PROSITE-ProRule annotation | ||
Glycosylationi | 357 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Disulfide bondi | 372 ↔ 425 | PROSITE-ProRule annotation | ||
Disulfide bondi | 384 ↔ 616 | PROSITE-ProRule annotation | ||
Glycosylationi | 435 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 677 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 709 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 717 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 789 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 806 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 945 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Disulfide bondi | 946 ↔ 957 | UniRule annotation | ||
Glycosylationi | 1232 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 1242 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 1261 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 1277 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 1298 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 |
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 769 – 770 | Cleavage; by hostBy similarity | 2 | |
Sitei | 921 – 922 | CleavageUniRule annotation | 2 |
Keywords - PTMi
Disulfide bond, Glycoprotein, Lipoprotein, PalmitateInteractioni
Subunit structurei
Homotrimer; each monomer consists of a S1 and a S2 subunit. The resulting peplomers protrude from the virus surface as spikes.
UniRule annotationStructurei
3D structure databases
SMRi | Q02385 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q02385 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 15 – 296 | BetaCoV S1-NTDPROSITE-ProRule annotationAdd BLAST | 282 | |
Domaini | 327 – 618 | BetaCoV S1-CTDPROSITE-ProRule annotationAdd BLAST | 292 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 15 – 330 | Receptor binding siteAdd BLAST | 316 | |
Regioni | 312 – 635 | Receptor-binding domainUniRule annotationAdd BLAST | 324 | |
Regioni | 922 – 943 | Fusion peptide 1UniRule annotationAdd BLAST | 22 | |
Regioni | 941 – 961 | Fusion peptide 2UniRule annotationAdd BLAST | 21 | |
Regioni | 1022 – 1072 | Heptad repeat 1UniRule annotationAdd BLAST | 51 | |
Regioni | 1266 – 1306 | Heptad repeat 2UniRule annotationAdd BLAST | 41 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 1051 – 1095 | UniRule annotationAdd BLAST | 45 | |
Coiled coili | 1279 – 1307 | UniRule annotationAdd BLAST | 29 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 1372 – 1376 | KxHxxUniRule annotation | 5 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 1339 – 1356 | Cys-richAdd BLAST | 18 |
Domaini
Fusion peptide 1 (FP1) and fusion peptide 2 (FP2) function cooperatively and have a membrane-ordering effect on lipid headgroups and shallow hydrophobic regions of target bilayers. They are considered as two domains of an extended, bipartite FP. The membrane-ordering activity is calcium-dependent and also dependent on correct folding, which is maintained by an internal disulfide bond in FP2.UniRule annotation
Sequence similaritiesi
Belongs to the betacoronaviruses spike protein family.UniRule annotation
Keywords - Domaini
Coiled coil, Signal, Transmembrane, Transmembrane helixFamily and domain databases
Gene3Di | 1.20.5.790, 1 hit 2.60.120.960, 1 hit |
HAMAPi | MF_04099, BETA_CORONA_SPIKE, 1 hit |
InterProi | View protein in InterPro IPR032500, bCoV_S1_N IPR042578, BETA_CORONA_SPIKE IPR043607, CoV_S1_C IPR043473, S2_sf_CoV IPR027400, S_HR2_CoV IPR043002, Spike_N_sf IPR018548, Spike_rcpt-bd_bCoV IPR036326, Spike_rcpt-bd_sf_CoV IPR002552, Spike_S2_CoV IPR043614, Spike_S2_CoV_C |
Pfami | View protein in Pfam PF16451, bCoV_S1_N, 1 hit PF09408, bCoV_S1_RBD, 1 hit PF19209, CoV_S1_C, 1 hit PF01601, CoV_S2, 1 hit PF19214, CoV_S2_C, 1 hit |
SUPFAMi | SSF111474, SSF111474, 2 hits SSF143587, SSF143587, 1 hit |
PROSITEi | View protein in PROSITE PS51921, BCOV_S1_CTD, 1 hit PS51922, BCOV_S1_NTD, 1 hit PS51923, COV_S2_HR1, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q02385-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLFVFILFLP SCLGYIGDFR CIQTVNYNGN NASAPSISTE AVDVSKGLGT
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
GSTLLPLYWV 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
GFNDAGVFGK SKHDVAYAQQ CFIVRPSYCP CAQPDIVSAC TSQTKPMSAY
510 520 530 540 550
CPTGTIHREC SLWNGPHLRS ARVGSGTYTC ECTCKPNPFD TYDLRCGQIK
560 570 580 590 600
TIVNVGDHCE GLGVLEDKCG NSDPHKGCSC AHDSFIGWSH DTCLVNDHSQ
610 620 630 640 650
IFANILLNGI NSGTTCSTDL QLPNTEVATG VCVRYDLYGI TGQGVFKEVK
660 670 680 690 700
ADYYNSWQAL LYDVNGNLNG FRDLTTNKTY TIRSCYSGRV SAAYHKEAPE
710 720 730 740 750
PALLYRNINC SYVFTNNISR EENPLNYFDS YLGCVVNADN RPDEALPNCD
760 770 780 790 800
LRMGAGLCVD YSKSRRARRS VSTGYRLTTF EPYMPMLVND SVQSVGGLYE
810 820 830 840 850
MQIPTNFTIG HHEEFIQIRA PKVTIDCAAF VCGDNAACRQ QLVEYGSFCD
860 870 880 890 900
NVNAILNEVN NLLDNMQLQV ASALMQGVTI SSRLPDGISG PIDDINFSPL
910 920 930 940 950
LGCIGSTCAE DGNGPSAMRG RSAIEDLLFD KVKLSDVGFV EAYNNCTGGQ
960 970 980 990 1000
EVRDLLCVQS FNGIKVLPPV LSESQISGYT AGATAAAMFP PWTAAAGVPF
1010 1020 1030 1040 1050
SLNVQYRING LGVTMNVLSE NQKMIASAFN NALGAIQEGF DATNSALGKI
1060 1070 1080 1090 1100
QSVVNANAEA LNNLLNQLSN RFGAISASLQ EILTRLDRVE AKAQIDRLIN
1110 1120 1130 1140 1150
GRLTALNAYI SKQLSDSTLI KFSAAQAIEK VNECVKSQTT RINFCGNGNH
1160 1170 1180 1190 1200
ILSLVQNAPY GLCFIHFSYV PTSFKTANVS PGLCISGDRG LAPKAGYFVQ
1210 1220 1230 1240 1250
DNGEWKFTGS NYYYPEPITD KNSVVMISCA VNYTKAPEVF LNNSIPNLPD
1260 1270 1280 1290 1300
FKEELDKWFK NQTSIAPDLS LDFEKLNVTF LDLTYEMNRI QDAIKKLNES
1310 1320 1330 1340 1350
YINLKEVGTY EMYVKWPWYV WLLIGLAGVA VCVLLFFICC CTGCGSCCFR
1360 1370
KCGSCCDEYG GHQDSIVIYN ISAHED
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D10235 mRNA Translation: BAA01085.1 |
PIRi | JQ1534 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D10235 mRNA Translation: BAA01085.1 |
PIRi | JQ1534 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2ZOK | X-ray | 2.10 | I/J/K/L | 510-518 | [»] | |
2ZOL | X-ray | 2.70 | E/F | 510-518 | [»] | |
4PG2 | X-ray | 2.80 | D | 510-518 | [»] | |
SMRi | Q02385 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q02385 |
Family and domain databases
Gene3Di | 1.20.5.790, 1 hit 2.60.120.960, 1 hit |
HAMAPi | MF_04099, BETA_CORONA_SPIKE, 1 hit |
InterProi | View protein in InterPro IPR032500, bCoV_S1_N IPR042578, BETA_CORONA_SPIKE IPR043607, CoV_S1_C IPR043473, S2_sf_CoV IPR027400, S_HR2_CoV IPR043002, Spike_N_sf IPR018548, Spike_rcpt-bd_bCoV IPR036326, Spike_rcpt-bd_sf_CoV IPR002552, Spike_S2_CoV IPR043614, Spike_S2_CoV_C |
Pfami | View protein in Pfam PF16451, bCoV_S1_N, 1 hit PF09408, bCoV_S1_RBD, 1 hit PF19209, CoV_S1_C, 1 hit PF01601, CoV_S2, 1 hit PF19214, CoV_S2_C, 1 hit |
SUPFAMi | SSF111474, SSF111474, 2 hits SSF143587, SSF143587, 1 hit |
PROSITEi | View protein in PROSITE PS51921, BCOV_S1_CTD, 1 hit PS51922, BCOV_S1_NTD, 1 hit PS51923, COV_S2_HR1, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | SPIKE_CVMJC | |
Accessioni | Q02385Primary (citable) accession number: Q02385 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1994 |
Last sequence update: | February 1, 1994 | |
Last modified: | December 2, 2020 | |
This is version 111 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families