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Protein

Spike glycoprotein

Gene

S

Organism
Porcine epidemic diarrhea virus (strain CV777) (PEDV)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

S1 region attaches the virion to the cell membrane by interacting with cell receptors, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide of S2 region and activating membranes fusion. S2 region belongs to the class I viral fusion protein. Under the current model, the protein has at least 3 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) regions 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 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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 glycoprotein
Short name:
S glycoprotein
Alternative name(s):
E2
Peplomer protein
Gene namesi
Name:S
ORF Names:2
OrganismiPorcine epidemic diarrhea virus (strain CV777) (PEDV)
Taxonomic identifieri229032 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeAlphacoronavirus
Virus hostiSus scrofa (Pig) [TaxID: 9823]
Proteomesi
  • UP000008159 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 1324Virion surfaceSequence analysisAdd BLAST1306
Transmembranei1325 – 1344HelicalSequence analysisAdd BLAST20
Topological domaini1345 – 1383IntravirionSequence analysisAdd BLAST39

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000028392519 – 1383Spike glycoproteinAdd BLAST1365

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi57N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi127N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi213N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi230N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi261N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi297N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi321N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi341N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi348N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi378N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi422N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi511N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi553N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi664N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi685N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi719N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi723N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi740N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi778N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi784N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi870N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1006N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1229N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1246N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1258N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1270N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1275N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1292N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1305N-linked (GlcNAc...); by hostSequence analysis1

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homotrimer.By similarity

Protein-protein interaction databases

IntActiQ91AV1. 3 interactors.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4J79X-ray1.56B1378-1383[»]
ProteinModelPortaliQ91AV1.
SMRiQ91AV1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni17 – 734S1By similarityAdd BLAST718
Regioni735 – 1383S2By similarityAdd BLAST649

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1036 – 1080Sequence analysisAdd BLAST45
Coiled coili1272 – 1314Sequence analysisAdd BLAST43

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1379 – 1383KxHxxBy similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1345 – 1366Cys-richAdd BLAST22

Domaini

The KxHxx motif seems to function as an ER retrieval signal.By similarity

Sequence similaritiesi

Belongs to the coronaviruses spike protein family.Curated

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK19254.

Family and domain databases

Gene3Di1.20.5.790. 1 hit.
InterProiIPR002551. Corona_S1.
IPR002552. Corona_S2.
IPR027400. S_HR2.
[Graphical view]
PfamiPF01600. Corona_S1. 1 hit.
PF01601. Corona_S2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q91AV1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSLIYFWLL LPVLPTLSLP QDVTRCQSTT NFRRFFSKFN VQAPAVVVLG
60 70 80 90 100
GYLPSMNSSS WYCGTGIETA SGVHGIFLSY IDSGQGFEIG ISQEPFDPSG
110 120 130 140 150
YQLYLHKATN GNTNAIARLR ICQFPDNKTL GPTVNDVTTG RNCLFNKAIP
160 170 180 190 200
AYMRDGKDIV VGITWDNDRV TVFADKIYHF YLKNDWSRVA TRCYNRRSCA
210 220 230 240 250
MQYVYTPTYY MLNVTSAGED GIYYEPCTAN CTGYAANVFA TDSNGHIPEG
260 270 280 290 300
FSFNNWFLLS NDSTLLHGKV VSNQPLLVNC LLAIPKIYGL GQFFSFNHTM
310 320 330 340 350
DGVCNGAAVD RAPEALRFNI NDTSVILAEG SIVLHTALGT NLSFVCSNSS
360 370 380 390 400
DPHLAIFAIP LGATEVPYYC FLKVDTYNST VYKFLAVLPP TVREIVITKY
410 420 430 440 450
GDVYVNGFGY LHLGLLDAVT INFTGHGTDD DVSGFWTIAS TNFVDALIEV
460 470 480 490 500
QGTSIQRILY CDDPVSQLKC SQVAFDLDDG FYPISSRNLL SHEQPISFVT
510 520 530 540 550
LPSFNDHSFV NITVSAAFGG LSSANLVASD TTINGFSSFC VDTRQFTITL
560 570 580 590 600
FYNVTNSYGY VSKSQDSNCP FTLQSVNDYL SFSKFCVSTS LLAGACTIDL
610 620 630 640 650
FGYPAFGSGV KLTSLYFQFT KGELITGTPK PLEGITDVSF MTLDVCTKYT
660 670 680 690 700
IYGFKGEGII TLTNSSILAG VYYTSDSGQL LAFKNVTSGA VYSVTPCSFS
710 720 730 740 750
EQAAYVNDDI VGVISSLSNS TFNNTRELPG FFYHSNDGSN CTEPVLVYSN
760 770 780 790 800
IGVCKSGSIG YVPSQYGQVK IAPTVTGNIS IPTNFSMSIR TEYLQLYNTP
810 820 830 840 850
VSVDCATYVC NGNSRCKQLL TQYTAACKTI ESALQLSARL ESVEVNSMLT
860 870 880 890 900
ISEEALQLAT ISSFNGDGYN FTNVLGASVY DPASGRVVQK RSVIEDLLFN
910 920 930 940 950
KVVTNGLGTV DEDYKRCSNG RSVADLVCAQ YYSGVMVLPG VVDAEKLHMY
960 970 980 990 1000
SASLIGGMAL GGITAAAALP FSYAVQARLN YLALQTDVLQ RNQQLLAESF
1010 1020 1030 1040 1050
NSAIGNITSA FESVKEAISQ TSKGLNTVAH ALTKVQEVVN SQGSALNQLT
1060 1070 1080 1090 1100
VQLQHNFQAI SSSIDDIYSR LDILSADVQV DRLITGRLSA LNAFVAQTLT
1110 1120 1130 1140 1150
KYTEVQASRK LAQQKVNECV KSQSQRYGFC GGDGEHIFSL VQAAPQGLLF
1160 1170 1180 1190 1200
LHTVLVPGDF VNVLAIAGLC VNGEIALTLR EPGLVLFTHE LQTYTATEYF
1210 1220 1230 1240 1250
VSSRRMFEPR KPTVSDFVQI ESCVVTYVNL TSDQLPDVIP DYIDVNKTLD
1260 1270 1280 1290 1300
EILASLPNRT GPSLPLDVFN ATYLNLTGEI ADLEQRSESL RNTTEELRSL
1310 1320 1330 1340 1350
INNINNTLVD LEWLNRVETY IKWPWWVWLI IVIVLIFVVS LLVFCCISTG
1360 1370 1380
CCGCCGCCGA CFSGCCRGPR LQPYEAFEKV HVQ
Length:1,383
Mass (Da):151,353
Last modified:December 1, 2001 - v1
Checksum:i022E5E5E5435876D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF353511 Genomic RNA. Translation: AAK38656.1.
RefSeqiNP_598310.1. NC_003436.1.

Genome annotation databases

GeneIDi935184.
KEGGivg:935184.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF353511 Genomic RNA. Translation: AAK38656.1.
RefSeqiNP_598310.1. NC_003436.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4J79X-ray1.56B1378-1383[»]
ProteinModelPortaliQ91AV1.
SMRiQ91AV1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ91AV1. 3 interactors.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi935184.
KEGGivg:935184.

Phylogenomic databases

KOiK19254.

Family and domain databases

Gene3Di1.20.5.790. 1 hit.
InterProiIPR002551. Corona_S1.
IPR002552. Corona_S2.
IPR027400. S_HR2.
[Graphical view]
PfamiPF01600. Corona_S1. 1 hit.
PF01601. Corona_S2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSPIKE_PEDV7
AccessioniPrimary (citable) accession number: Q91AV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Caution

In contrast to serogroups 2 and 3, S glycoprotein from serogroup 1 is not cleaved into S1 and S2.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.