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

 SPIKE_CVCAK             Reviewed;        1453 AA.
Q65984;
08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 87.
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 K378) (CCoV) (Canine enteric coronavirus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Alphacoronavirus.
NCBI_TaxID=33732;
NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8021609; DOI=10.1099/0022-1317-75-7-1789;
Wesseling J.G., Vennema H., Godeke G.J., Spaan W.J.M., Horzinek M.C.,
Rottier P.J.M.;
"Nucleotide sequence and expression of the spike (S) gene of canine
coronavirus and comparison with the S proteins of feline and swine
coronaviruses.";
J. Gen. Virol. 75:1789-1794(1994).
-!- 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}.
-!- 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}.
-----------------------------------------------------------------------
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EMBL; X77047; CAA54335.1; -; mRNA.
PIR; S41453; S41453.
ProteinModelPortal; Q65984; -.
SMR; Q65984; -.
PRIDE; Q65984; -.
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.
2: Evidence at transcript 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 1453 Spike glycoprotein. {ECO:0000255|HAMAP-
Rule:MF_04200}.
/FTId=PRO_0000042720.
TOPO_DOM 32 1394 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04200}.
TRANSMEM 1395 1414 Helical. {ECO:0000255|HAMAP-
Rule:MF_04200}.
TOPO_DOM 1415 1453 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04200}.
REGION 19 791 S1.
REGION 32 780 S1. {ECO:0000255|HAMAP-Rule:MF_04200}.
REGION 661 805 Interaction with host ANPEP.
{ECO:0000255|HAMAP-Rule:MF_04200}.
REGION 781 1453 S2. {ECO:0000255|HAMAP-Rule:MF_04200}.
REGION 794 1453 S2.
REGION 1026 1047 Fusion peptide. {ECO:0000255|HAMAP-
Rule:MF_04200}.
COILED 1108 1152 {ECO:0000255|HAMAP-Rule:MF_04200}.
COILED 1342 1384 {ECO:0000255|HAMAP-Rule:MF_04200}.
MOTIF 1449 1453 KxHxx. {ECO:0000255|HAMAP-Rule:MF_04200}.
COMPBIAS 1408 1436 Cys-rich.
SEQUENCE 1453 AA; 160741 MW; 8955E6B61AB8983A CRC64;
MIVLILCLLL FSYNSVICTS NNDCVQGNVT QLPGNENIIK DFLFHTFKEE PSVVVGGYYP
TEVWYNCSRS ATTTAYKDFS NIHAFYFDME AMENSTGNAR GKPLLVHVHG DPVSIIIYIS
AYRDDVQPRP LLKHGLLCIT KNKIIDYNTF TSAQWSAICL GDDRKIPFSV IPTDNGTKIF
GLEWNDDYVT AYISDRSHHL NINNNWFNNV TILYSRSSSA TWQKSAAYVY QGVSNFTYYK
LNNTNGLKSY ELCEDYEYCT GYATNVFAPT VGGYIPHGFS FNNWFMRTNS STFVSGRFVT
NQPLLVNCLW PVPSFGVAAQ QFCFEGAQFS QCNGVSLNNT VDVIRFNLNF TALVQSGMGA
TVFSLNTTGG VILEISCYND TVSESSFYSY GEISFGVTDG PRYCFALYNG TALKYLGTLP
PSVKEIAISK WGHFYINGYN FFSTFPIDCI SFNLTTGDSG AFWTIAYTSY TDALVQVENT
AIKKVTYCNS HINNIKCSQL TANLQNGFYP VASSEVGLVN KSVVLLPSFY SHTSVNITID
LGMKRSGYGQ PIASTLSNIT LPMQDNNTDV YCIRSNRFSV YFHSTCKSSL WDDVFNSDCT
DVLYATAVIK TGTCPFSFDK LNNYLTFNKF CLSLNPVGAN CKFDVAARTR TNEQVVRSLY
VIYEEGDNIV GVPSDNSGLH DLSVLHLDSC TDYNIYGITG VGIIRQTNST LLSGLYYTSL
SGDLLGFKNV SDGVIYSVTP CDVSAHAAVI DGAIVGAMTS INSELLGLTH WTTTPNFYYY
SIYNYTNERT RGTAIDSNDV DCEPIITYSN IGVCKNGALV FINVTHSDGD VQPISTGNVT
IPTNFTISVQ VEYIQVYTTP VSIDCSRYVC NGNPRCNKLL TQYVSACQTI EQALAMGARL
ENMEIDSMLF VSENALKLAS VEAFNSTETL DPIYKEWPNI GGSWLGGLKD ILPSHNSKRK
YRSAIEDLLF DKVVTSGLGT VDEDYKRCTG GYDIADLVCA QYYNGIMVLP GVANDDKMAM
YTASLAGGIT LGSLGGGAVS IPFAIAVQAR LNYVALQTDV LNKNQQILAN AFNQAIGNIT
QAFGKVNDAI HQTSQGLATV AKVLAKVQDV VNTQGQALSH LTLQLQNNFQ AISSSISDIY
NRLDELSADA QVDRLITGRL TALNAFVSQT LTRQAEVRAS RQLAKDKVNE CVRSQSQRFG
FCGNGTHLFS LANAAPNGMI FFHTVLLPTA YETVTAWSGI CASDGDRTFG LVVKDVQLTL
FRNLDDKFYL TPRTMYQPIV ATSSDFVQIE GCDVLFVNAT VIDLPSIIPD YIDINQTVQD
ILENFRPNWT VPELPLDIFN ATYLNLTGEI NDLEFRSEKL HNTTVELAIL IDNINNTLVN
LEWLNRIETY VKWPWYVWLL IGLVVIFCIP ILLFCCCSTG CCGCIGCLGS CCHSICSRRQ
FESYEPIEKV HVH


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