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Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein)

 SPIKE_CVCAI             Reviewed;        1451 AA.
P36300;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
23-MAY-2018, entry version 86.
RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04200};
Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04200};
AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04200};
AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04200};
Flags: Precursor;
Name=S {ECO:0000255|HAMAP-Rule:MF_04200};
Canine coronavirus (strain Insavc-1) (CCoV) (Canine enteric
coronavirus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Alphacoronavirus.
NCBI_TaxID=36391;
NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=1431811; DOI=10.1099/0022-1317-73-11-2849;
Horsburgh B.C., Brierley I., Brown T.D.K.;
"Analysis of a 9.6 kb sequence from the 3' end of canine coronavirus
genomic RNA.";
J. Gen. Virol. 73:2849-2862(1992).
[2]
INTERACTION WITH FELINE ANPEP.
PubMed=8970993;
Tresnan D.B., Levis R., Holmes K.V.;
"Feline aminopeptidase N serves as a receptor for feline, canine,
porcine, and human coronaviruses in serogroup I.";
J. Virol. 70:8669-8674(1996).
[3]
INTERACTION WITH CANINE ANPEP.
PubMed=8985407;
Benbacer L., Kut E., Besnardeau L., Laude H., Delmas B.;
"Interspecies aminopeptidase-N chimeras reveal species-specific
receptor recognition by canine coronavirus, feline infectious
peritonitis virus, and transmissible gastroenteritis virus.";
J. Virol. 71:734-737(1997).
-!- FUNCTION: S1 region attaches the virion to the cell membrane by
interacting with host ANPEP/aminopeptidase N, 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. {ECO:0000255|HAMAP-
Rule:MF_04200}.
-!- SUBUNIT: Homotrimer. During virus morphogenesis, found in a
complex with M and HE proteins. Interacts with host ANPEP.
{ECO:0000255|HAMAP-Rule:MF_04200, ECO:0000269|PubMed:8970993,
ECO:0000269|PubMed:8985407}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
Rule:MF_04200}; Single-pass type I membrane protein
{ECO:0000255|HAMAP-Rule:MF_04200}. Host endoplasmic reticulum-
Golgi intermediate compartment membrane {ECO:0000255|HAMAP-
Rule:MF_04200}; Single-pass type I membrane protein
{ECO:0000255|HAMAP-Rule:MF_04200}. Note=Accumulates in the
endoplasmic reticulum-Golgi intermediate compartment, where it
participates in virus particle assembly. {ECO:0000255|HAMAP-
Rule:MF_04200}.
-!- DOMAIN: The KxHxx motif seems to function as an ER retrieval
signal. {ECO:0000255|HAMAP-Rule:MF_04200}.
-!- SIMILARITY: Belongs to the alphacoronaviruses spike protein
family. {ECO:0000255|HAMAP-Rule:MF_04200}.
-!- CAUTION: In contrast to beta- and gammacoronaviruses, S
glycoprotein is not cleaved into S1 and S2. {ECO:0000255|HAMAP-
Rule:MF_04200}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; D13096; BAA02408.1; -; Genomic_RNA.
PIR; JQ1719; JQ1719.
ProteinModelPortal; P36300; -.
SMR; P36300; -.
PRIDE; P36300; -.
GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:InterPro.
HAMAP; MF_04200; ALPHA_CORONA_SPIKE; 1.
InterPro; IPR002551; Corona_S1.
InterPro; IPR002552; Corona_S2.
Pfam; PF01600; Corona_S1; 1.
Pfam; PF01601; Corona_S2; 1.
1: Evidence at protein level;
Coiled coil; Glycoprotein; Host membrane; Host-virus interaction;
Membrane; Signal; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral envelope protein; Virion;
Virulence; Virus entry into host cell.
SIGNAL 1 31 {ECO:0000255|HAMAP-Rule:MF_04200}.
CHAIN 32 1451 Spike glycoprotein. {ECO:0000255|HAMAP-
Rule:MF_04200}.
/FTId=PRO_0000037202.
TOPO_DOM 32 1392 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04200}.
TRANSMEM 1393 1412 Helical. {ECO:0000255|HAMAP-
Rule:MF_04200}.
TOPO_DOM 1413 1451 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04200}.
REGION 32 779 S1. {ECO:0000255|HAMAP-Rule:MF_04200}.
REGION 660 803 Interaction with host ANPEP.
{ECO:0000255|HAMAP-Rule:MF_04200}.
REGION 780 1451 S2. {ECO:0000255|HAMAP-Rule:MF_04200}.
REGION 1024 1045 Fusion peptide. {ECO:0000255|HAMAP-
Rule:MF_04200}.
COILED 1106 1150 {ECO:0000255|HAMAP-Rule:MF_04200}.
COILED 1340 1382 {ECO:0000255|HAMAP-Rule:MF_04200}.
MOTIF 1447 1451 KxHxx. {ECO:0000255|HAMAP-Rule:MF_04200}.
COMPBIAS 1413 1434 Cys-rich.
SEQUENCE 1451 AA; 160468 MW; F3E6ECA8B914CE6C CRC64;
MIVLTLCLFL FLYSSVSCTS NNDCVQVNVT QLPGNENIIK DFLFQNFKEE GSLVVGGYYP
TEVWYNCSTT QQTTAYKYFS NIHAFYFDME AMENSTGNAR GKPLLVHVHG NPVSIIVYIS
AYRDDVQFRP LLKHGLLCIT KNDTVDYNSF TINQWRDICL GDDRKIPFSV VPTDNGTKLF
GLEWNDDYVT AYISDESHRL NINNNWFNNV TLLYSRTSTA TWQHSAAYVY QGVSNFTYYK
LNKTAGLKSY ELCEDYEYCT GYATNVFAPT SGGYIPDGFS FNNWFMLTNS STFVSGRFVT
NQPLLVNCLW PVPSFGVAAQ EFCFEGAQFS QCNGVSLNNT VDVIRFNLNF TTDVQSGMGA
TVFSLNTTGG VILEISCYND TVSESSFYSY GEIPFGVTDG PRYCYVLYNG TALKYLGTLP
PSVKEIAISK WGHFYINGYN FFSTFPIDCI AFNLTTGASG AFWTIAYTSY TEALVQVENT
AIKKVTYCNS HINNIKCSQL TANLQNGFYP VASSEVGLVN KSVVLLPSFY SHTSVNITID
LGMKRSVTVT IASPLSNITL PMQDNNIDVY CIRSNQFSVY VHSTCKSSLW DNNFNSACTD
VLDATAVIKT GTCPFSFDKL NNYLTFNKFC LSLNPVGANC KLDVAARTRT NEQVFGSLYV
IYEEGDNIVG VPSDNSGLHD LSVLHLDSCT DYNIYGRTGV GIIRKTNSTL LSGLYYTSLS
GDLLGFKNVS DGVVYSVTPC DVSAQAAVID GAIVGAMTSI NSELLGLTHW TTTPNFYYYS
IYNYTNVMNR GTAIDNDIDC EPIITYSNIG VCKNGALVFI NVTHSDGDVQ PISTGNVTIP
TNFTISVQVE YIQVYTTPVS IDCARYVCNG NPRCNKLLTQ YVSACQTIEQ ALAMGARLEN
MEIDSMLFVS ENALKLASVE AFNSTENLDP IYKEWPNIGG SWLGGLKDIL PSHNSKRKYR
SAIEDLLFDK VVTSGLGTVD EDYKRSAGGY DIADLVCARY YNGIMVLPGV ANDDKMTMYT
ASLTGGITLG ALSGGAVAIP FAVAVQARLN YVALQTDVLN KNQQILANAF NQAIGNITQA
FGKVNDAIHQ TSKGLATVAK ALAKVQDVVN TQGQALSHLT VQLQNNFQAI SSSISDIYNR
LDELSADAQV DRLITGRLTA LNAFVSQTLT RQAEVRASRQ LAKDKVNECV RSQSQRFGFC
GNGTHLFSLA NAAPNGMIFF HTVLLPTAYE TVTAWSGICA SDGSRTFGLV VEDVQLTLFR
NLDEKFYLTP RTMYQPRVAT SSDFVQIEGC DVLFVNGTVI ELPSIIPDYI DINQTVQDIL
ENFRPNWTVP ELPLDIFHAT YLNLTGEIND LEFRSEKLHN TTVELAILID NINNTLVNLE
WLNRIETYVK WPWYVWLLIG LVVIFCIPIL LFCCCSTGCC GCIGCLGSCC HSICSRGQFE
SYEPIEKVHV H


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Pathways :
WP1970: Glycoprotein VI platelet signaling
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining

Related Genes :
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[S 3] Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[S 2] Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
[S 3] Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[S 3] Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
[S 2] Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[S 3] Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
[S 2] Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[S 3] Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]

Bibliography :
[2159562] Conformational change of the coronavirus peplomer glycoprotein at pH 8.0 and 37 degrees C correlates with virus aggregation and virus-induced cell fusion.