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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.
28-FEB-2018, entry version 85.
RecName: Full=Spike glycoprotein;
Short=S glycoprotein;
AltName: Full=E2;
AltName: Full=Peplomer protein;
Flags: Precursor;
Name=S;
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 canine 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 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homotrimer. Cytoplasmic tail interacts with M protein (By
similarity). Interacts with canine and feline ANPEP. {ECO:0000250,
ECO:0000269|PubMed:8970993, ECO:0000269|PubMed:8985407}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Host endoplasmic reticulum-
Golgi intermediate compartment membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Note=Accumulates in the
endoplasmic reticulum-Golgi intermediate compartment, where it
participates in virus particle assembly. Some S oligomers may be
transported to the plasma membrane, where they may mediate cell-
cell fusion (By similarity). {ECO:0000250}.
-!- DOMAIN: The KxHxx motif seems to function as an ER retrieval
signal. {ECO:0000250}.
-!- SIMILARITY: Belongs to the coronaviruses spike protein family.
{ECO:0000305}.
-!- CAUTION: In contrast to serogroups 2 and 3, S glycoprotein from
serogroup 1 is not cleaved into S1 and S2. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D13096; BAA02408.1; -; Genomic_RNA.
PIR; JQ1719; JQ1719.
ProteinModelPortal; P36300; -.
SMR; 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.
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 18 {ECO:0000255}.
CHAIN 19 1451 Spike glycoprotein.
/FTId=PRO_0000037202.
TOPO_DOM 19 1393 Virion surface. {ECO:0000255}.
TRANSMEM 1394 1412 Helical. {ECO:0000255}.
TOPO_DOM 1413 1451 Intravirion. {ECO:0000255}.
COILED 1106 1150 {ECO:0000255}.
COILED 1340 1382 {ECO:0000255}.
MOTIF 1447 1451 KxHxx. {ECO:0000250}.
COMPBIAS 1413 1434 Cys-rich.
CARBOHYD 28 28 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 66 66 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 175 175 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 242 242 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 289 289 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 338 338 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 349 349 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 366 366 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 379 379 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 409 409 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 453 453 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 520 520 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 536 536 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 557 557 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 707 707 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 728 728 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 783 783 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 821 821 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 836 836 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 842 842 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 923 923 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1076 1076 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1202 1202 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1296 1296 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1313 1313 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1326 1326 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1343 1343 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1360 1360 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1373 1373 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
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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