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

 SPIKE_FIPV              Reviewed;        1452 AA.
P10033; Q4U5G0; Q52PA3;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
10-MAY-2017, entry version 100.
RecName: Full=Spike glycoprotein;
Short=S glycoprotein;
AltName: Full=E2;
AltName: Full=Peplomer protein;
Flags: Precursor;
Name=S; ORFNames=2;
Feline coronavirus (strain FIPV WSU-79/1146) (FCoV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Alphacoronavirus.
NCBI_TaxID=33734;
NCBI_TaxID=9681; Felidae (cat family).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3312491;
de Groot R.J., Maduro J., Lenstra J.A., Horzinek M.C.,
van der Zeijst B.A.M., Spaan W.J.M.;
"cDNA cloning and sequence analysis of the gene encoding the peplomer
protein of feline infectious peritonitis virus.";
J. Gen. Virol. 68:2639-2646(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16033972; DOI=10.1099/vir.0.80985-0;
Dye C., Siddell S.G.;
"Genomic RNA sequence of Feline coronavirus strain FIPV WSU-79/1146.";
J. Gen. Virol. 86:2249-2253(2005).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Haijema B.J., de Groot-Mijnes J.D.F., Vennema H., Raamsman M.J.,
Rottier P.J.M., de Groot R.J.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
INTERACTION WITH M PROTEIN.
PubMed=10627571; DOI=10.1128/JVI.74.3.1566-1571.2000;
Godeke G.J., de Haan C.A., Rossen J.W., Vennema H., Rottier P.J.;
"Assembly of spikes into coronavirus particles is mediated by the
carboxy-terminal domain of the spike protein.";
J. Virol. 74:1566-1571(2000).
[5]
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).
-!- FUNCTION: S1 region attaches the virion to the cell membrane by
interacting with feline 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.
Interacts with feline ANPEP. {ECO:0000269|PubMed:10627571,
ECO:0000269|PubMed:8970993}.
-!- 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; X06170; CAA29535.1; -; Genomic_RNA.
EMBL; DQ010921; AAY32596.1; -; Genomic_RNA.
EMBL; AY994055; AAY16375.1; -; Genomic_RNA.
PIR; A27171; VGIH79.
RefSeq; YP_004070194.1; NC_002306.3.
ProteinModelPortal; P10033; -.
SMR; P10033; -.
GeneID; 920849; -.
KEGG; vg:920849; -.
KO; K19254; -.
OrthoDB; VOG0900000Z; -.
Proteomes; UP000000835; Genome.
Proteomes; UP000140386; Genome.
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.
Gene3D; 1.20.5.790; -; 1.
InterPro; IPR002551; Corona_S1.
InterPro; IPR002552; Corona_S2.
InterPro; IPR027400; S_HR2.
Pfam; PF01600; Corona_S1; 1.
Pfam; PF01601; Corona_S2; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Glycoprotein; Host membrane;
Host-virus interaction; Membrane; Reference proteome; Signal;
Transmembrane; Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Virion; Virulence; Virus entry into host cell.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 1452 Spike glycoprotein. {ECO:0000255}.
/FTId=PRO_0000037183.
TOPO_DOM 20 1395 Virion surface. {ECO:0000255}.
TRANSMEM 1396 1416 Helical. {ECO:0000255}.
TOPO_DOM 1417 1452 Intravirion. {ECO:0000255}.
COILED 1107 1151 {ECO:0000255}.
COILED 1341 1383 {ECO:0000255}.
MOTIF 1448 1452 KxHxx. {ECO:0000250}.
COMPBIAS 1414 1435 Cys-rich.
CARBOHYD 29 29 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 174 174 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 208 208 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 337 337 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 348 348 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 365 365 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 452 452 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 483 483 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 519 519 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 535 535 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 557 557 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 565 565 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 822 822 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 837 837 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 843 843 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 924 924 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1077 1077 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1203 1203 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1297 1297 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1314 1314 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1327 1327 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1339 1339 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1344 1344 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1361 1361 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1374 1374 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
VARIANT 744 744 A -> V.
VARIANT 1325 1325 R -> E.
SEQUENCE 1452 AA; 160470 MW; 942E46AC9D78CA1C CRC64;
MIVLVTCLLL LCSYHTVLST TNNECIQVNV TQLAGNENLI RDFLFSNFKE EGSVVVGGYY
PTEVWYNCSR TARTTAFQYF NNIHAFYFVM EAMENSTGNA RGKPLLFHVH GEPVSVIISA
YRDDVQQRPL LKHGLVCITK NRHINYEQFT SNQWNSTCTG ADRKIPFSVI PTDNGTKIYG
LEWNDDFVTA YISGRSYHLN INTNWFNNVT LLYSRSSTAT WEYSAAYAYQ GVSNFTYYKL
NNTNGLKTYE LCEDYEHCTG YATNVFAPTS GGYIPDGFSF NNWFLLTNSS TFVSGRFVTN
QPLLINCLWP VPSFGVAAQE FCFEGAQFSQ CNGVSLNNTV DVIRFNLNFT ADVQSGMGAT
VFSLNTTGGV ILEISCYSDT VSESSSYSYG EIPFGITDGP RYCYVLYNGT ALKYLGTLPP
SVKEIAISKW GHFYINGYNF FSTFPIGCIS FNLTTGVSGA FWTIAYTSYT EALVQVENTA
IKNVTYCNSH INNIKCSQLT ANLNNGFYPV ASSEVGFVNK SVVLLPSFFT YTAVNITIDL
GMKLSGYGQP IASTLSNITL PMQDNNTDVY CIRSNQFSVY VHSTCKSSLW DNIFNQDCTD
VLEATAVIKT GTCPFSFDKL NNYLTFNKFC LSLSPVGANC KFDVAARTRT NEQVVRSLYV
IYEEGDNIVG VPSDNSGLHD LSVLHLDSCT DYNIYGRTGV GIIRRTNSTL LSGLYYTSLS
GDLLGFKNVS DGVIYSVTPC DVSAQAAVID GAIVGAMTSI NSELLGLTHW TTTPNFYYYS
IYNYTSERTR GTAIDSNDVD CEPVITYSNI GVCKNGALVF INVTHSDGDV QPISTGNVTI
PTNFTISVQV EYMQVYTTPV SIDCARYVCN GNPRCNKLLT QYVSACQTIE QALAMGARLE
NMEVDSMLFV SENALKLASV EAFNSTENLD PIYKEWPSIG GSWLGGLKDI LPSHNSKRKY
GSAIEDLLFD KVVTSGLGTV DEDYKRCTGG YDIADLVCAQ YYNGIMVLPG VANADKMTMY
TASLAGGITL GALGGGAVAI PFAVAVQARL NYVALQTDVL NKNQQILANA FNQAIGNITQ
AFGKVNDAIH QTSQGLATVA KALAKVQDVV NTQGQALSHL TVQLQNNFQA ISSSISDIYN
RLDELSADAQ VDRLITGRLT ALNAFVSQTL TRQAEVRASR QLAKDKVNEC VRSQSQRFGF
CGNGTHLFSL ANAAPNGMIF FHTVLLPTAY ETVTAWSGIC ASDGDRTFGL VVKDVQLTLF
RNLDDKFYLT PRTMYQPRVA TSSDFVQIEG CDVLFVNATV IDLPSIIPDY IDINQTVQDI
LENYRPNWTV PEFTLDIFNA TYLNLTGEID DLEFRSEKLH NTTVELAILI DNINNTLVNL
EWLNRIETYV KWPWYVWLLI GLVVVFCIPL LLFCCFSTGC CGCIGCLGSC CHSICSRRQF
ENYEPIEKVH VH


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