SPIKE_FIPV
ID SPIKE_FIPV Reviewed; 1452 AA.
AC P10033; Q4U5G0; Q52PA3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 29-SEP-2021, entry version 114.
DE RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04200};
DE Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04200};
DE AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04200};
DE AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04200};
DE Flags: Precursor;
GN Name=S {ECO:0000255|HAMAP-Rule:MF_04200}; ORFNames=2;
OS Feline coronavirus (strain FIPV WSU-79/1146) (FCoV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Tegacovirus.
OX NCBI_TaxID=33734;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3312491; DOI=10.1099/0022-1317-68-10-2639;
RA de Groot R.J., Maduro J., Lenstra J.A., Horzinek M.C.,
RA van der Zeijst B.A.M., Spaan W.J.M.;
RT "cDNA cloning and sequence analysis of the gene encoding the peplomer
RT protein of feline infectious peritonitis virus.";
RL J. Gen. Virol. 68:2639-2646(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16033972; DOI=10.1099/vir.0.80985-0;
RA Dye C., Siddell S.G.;
RT "Genomic RNA sequence of Feline coronavirus strain FIPV WSU-79/1146.";
RL J. Gen. Virol. 86:2249-2253(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Haijema B.J., de Groot-Mijnes J.D.F., Vennema H., Raamsman M.J.,
RA Rottier P.J.M., de Groot R.J.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH M PROTEIN.
RX PubMed=10627571; DOI=10.1128/jvi.74.3.1566-1571.2000;
RA Godeke G.J., de Haan C.A., Rossen J.W., Vennema H., Rottier P.J.;
RT "Assembly of spikes into coronavirus particles is mediated by the carboxy-
RT terminal domain of the spike protein.";
RL J. Virol. 74:1566-1571(2000).
RN [5]
RP INTERACTION WITH FELINE ANPEP.
RX PubMed=8970993; DOI=10.1128/jvi.70.12.8669-8674.1996;
RA Tresnan D.B., Levis R., Holmes K.V.;
RT "Feline aminopeptidase N serves as a receptor for feline, canine, porcine,
RT and human coronaviruses in serogroup I.";
RL J. Virol. 70:8669-8674(1996).
CC -!- FUNCTION: S1 region attaches the virion to the cell membrane by
CC interacting with host ANPEP/aminopeptidase N, initiating the infection.
CC Binding to the receptor probably induces conformational changes in the
CC S glycoprotein unmasking the fusion peptide of S2 region and activating
CC membranes fusion. S2 region belongs to the class I viral fusion
CC protein. Under the current model, the protein has at least 3
CC conformational states: pre-fusion native state, pre-hairpin
CC intermediate state, and post-fusion hairpin state. During viral and
CC target cell membrane fusion, the coiled coil regions (heptad repeats)
CC regions assume a trimer-of-hairpins structure, positioning the fusion
CC peptide in close proximity to the C-terminal region of the ectodomain.
CC The formation of this structure appears to drive apposition and
CC subsequent fusion of viral and target cell membranes.
CC {ECO:0000255|HAMAP-Rule:MF_04200}.
CC -!- SUBUNIT: Homotrimer. During virus morphogenesis, found in a complex
CC with M and HE proteins. Interacts with host ANPEP. {ECO:0000255|HAMAP-
CC Rule:MF_04200, ECO:0000269|PubMed:10627571,
CC ECO:0000269|PubMed:8970993}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04200}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04200}. Host endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000255|HAMAP-Rule:MF_04200}; Single-pass
CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04200}.
CC Note=Accumulates in the endoplasmic reticulum-Golgi intermediate
CC compartment, where it participates in virus particle assembly.
CC {ECO:0000255|HAMAP-Rule:MF_04200}.
CC -!- DOMAIN: The KxHxx motif seems to function as an ER retrieval signal.
CC {ECO:0000255|HAMAP-Rule:MF_04200}.
CC -!- SIMILARITY: Belongs to the alphacoronaviruses spike protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04200}.
CC -!- CAUTION: In contrast to beta- and gammacoronaviruses, S glycoprotein is
CC not cleaved into S1 and S2. {ECO:0000255|HAMAP-Rule:MF_04200}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X06170; CAA29535.1; -; Genomic_RNA.
DR EMBL; DQ010921; AAY32596.1; -; Genomic_RNA.
DR EMBL; AY994055; AAY16375.1; -; Genomic_RNA.
DR PIR; A27171; VGIH79.
DR RefSeq; YP_004070194.1; NC_002306.3.
DR SMR; P10033; -.
DR GeneID; 920849; -.
DR KEGG; vg:920849; -.
DR Proteomes; UP000000835; Genome.
DR Proteomes; UP000140386; Genome.
DR GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04200; ALPHA_CORONA_SPIKE; 1.
DR InterPro; IPR042552; ALPHA_CORONA_SPIKE.
DR InterPro; IPR043607; CoV_S1_C.
DR InterPro; IPR043473; S2_sf_CoV.
DR InterPro; IPR002551; Spike_S1_CoV.
DR InterPro; IPR002552; Spike_S2_CoV.
DR InterPro; IPR043614; Spike_S2_CoV_C.
DR InterPro; IPR044873; Spike_S2_CoV_HR1.
DR InterPro; IPR044874; Spike_S2_CoV_HR2.
DR Pfam; PF01600; CoV_S1; 1.
DR Pfam; PF19209; CoV_S1_C; 1.
DR Pfam; PF01601; CoV_S2; 1.
DR Pfam; PF19214; CoV_S2_C; 1.
DR SUPFAM; SSF111474; SSF111474; 2.
DR PROSITE; PS51923; COV_S2_HR1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Glycoprotein; Host membrane; Host-virus interaction; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion; Virulence;
KW Virus entry into host cell.
FT SIGNAL 1..32
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT CHAIN 33..1452
FT /note="Spike glycoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT /id="PRO_0000037183"
FT TOPO_DOM 33..1393
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TRANSMEM 1394..1413
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TOPO_DOM 1414..1452
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 33..779
FT /note="S1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 660..804
FT /note="Interaction with host ANPEP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 780..1452
FT /note="S2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 1025..1046
FT /note="Fusion peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 1040..1159
FT /note="Heptad repeat 1 (HR1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01271"
FT REGION 1308..1405
FT /note="Heptad repeat 2 (HR2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01272"
FT COILED 1107..1151
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT COILED 1341..1383
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT MOTIF 1448..1452
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT VARIANT 744
FT /note="A -> V"
FT VARIANT 1325
FT /note="R -> E"
SQ 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
