SPIKE_CVPPU
ID SPIKE_CVPPU Reviewed; 1447 AA.
AC P07946; Q02167; Q9IW04;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 2.
DT 29-SEP-2021, entry version 124.
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 Porcine transmissible gastroenteritis coronavirus (strain Purdue) (TGEV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Tegacovirus.
OX NCBI_TaxID=11151;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3037011; DOI=10.1099/0022-1317-68-7-1883;
RA Rasschaert D., Laude H.;
RT "The predicted primary structure of the peplomer protein E2 of the porcine
RT coronavirus transmissible gastroenteritis virus.";
RL J. Gen. Virol. 68:1883-1890(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2829461; DOI=10.1016/0168-1702(87)90008-6;
RA Jacobs L., de Groot R.J., van der Zeijst B.A.M., Horzinek M.C.,
RA Spaan W.J.M.;
RT "The nucleotide sequence of the peplomer gene of porcine transmissible
RT gastroenteritis virus (TGEV): comparison with the sequence of the peplomer
RT protein of feline infectious peritonitis virus (FIPV).";
RL Virus Res. 8:363-371(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate PUR46-MAD;
RX PubMed=1326823; DOI=10.1016/0042-6822(92)91195-z;
RA Sanchez C.M., Gebauer F., Sune C., Mendez A., Dopazo J., Enjuanes L.;
RT "Genetic evolution and tropism of transmissible gastroenteritis
RT coronaviruses.";
RL Virology 190:92-105(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate PUR46-MAD;
RX PubMed=10805807; DOI=10.1073/pnas.97.10.5516;
RA Almazan F., Gonzalez J.M., Penzes Z., Izeta A., Calvo E., Plana-Duran J.,
RA Enjuanes L.;
RT "Engineering the largest RNA virus genome as an infectious bacterial
RT artificial chromosome.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5516-5521(2000).
RN [5]
RP HOMOTRIMERIZATION.
RX PubMed=2170676; DOI=10.1128/jvi.64.11.5367-5375.1990;
RA Delmas B., Laude H.;
RT "Assembly of coronavirus spike protein into trimers and its role in epitope
RT expression.";
RL J. Virol. 64:5367-5375(1990).
RN [6]
RP INTERACTION WITH PORCINE ANPEP.
RX PubMed=1350661; DOI=10.1038/357417a0;
RA Delmas B., Gelfi J., L'Haridon R., Vogel L.K., Sjostrom H., Noren O.,
RA Laude H.;
RT "Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus
RT TGEV.";
RL Nature 357:417-420(1992).
RN [7]
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:1350661, 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}.
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DR EMBL; X05695; CAA29175.1; -; Genomic_RNA.
DR EMBL; M21950; AAA47911.1; -; Genomic_RNA.
DR EMBL; M94101; AAA47109.1; -; Genomic_RNA.
DR EMBL; AJ271965; CAB91145.1; -; Genomic_RNA.
DR PIR; A27106; VGIHE2.
DR SMR; P07946; -.
DR Proteomes; UP000001440; 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..28
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT CHAIN 29..1447
FT /note="Spike glycoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT /id="PRO_0000037225"
FT TOPO_DOM 29..1388
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TRANSMEM 1389..1408
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TOPO_DOM 1409..1447
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 17..774
FT /note="S1"
FT REGION 29..774
FT /note="S1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 655..799
FT /note="Interaction with host ANPEP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 775..1447
FT /note="S2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 1020..1041
FT /note="Fusion peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 1035..1154
FT /note="Heptad repeat 1 (HR1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01271"
FT REGION 1303..1400
FT /note="Heptad repeat 2 (HR2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01272"
FT COILED 1102..1146
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT COILED 1336..1378
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT MOTIF 1443..1447
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT VARIANT 72
FT /note="N -> D (in strain: Isolate PUR46-MAD)"
FT CONFLICT 53
FT /note="V -> D (in Ref. 1; CAA29175)"
FT CONFLICT 86
FT /note="L -> V (in Ref. 2; AAA47911)"
FT CONFLICT 706
FT /note="L -> I (in Ref. 1; CAA29175)"
FT CONFLICT 794
FT /note="V -> F (in Ref. 2; AAA47911)"
SQ SEQUENCE 1447 AA; 160118 MW; BB41B95D05DC9422 CRC64;
MKKLFVVLVV MPLIYGDNFP CSKLTNRTIG NQWNLIETFL LNYSSRLPPN SDVVLGDYFP
TVQPWFNCIR NNSNDLYVTL ENLKALYWDY ATENITWNHR QRLNVVVNGY PYSITVTTTR
NFNSAEGAII CICKGSPPTT TTESSLTCNW GSECRLNHKF PICPSNSEAN CGNMLYGLQW
FADEVVAYLH GASYRISFEN QWSGTVTFGD MRATTLEVAG TLVDLWWFNP VYDVSYYRVN
NKNGTTVVSN CTDQCASYVA NVFTTQPGGF IPSDFSFNNW FLLTNSSTLV SGKLVTKQPL
LVNCLWPVPS FEEAASTFCF EGAGFDQCNG AVLNNTVDVI RFNLNFTTNV QSGKGATVFS
LNTTGGVTLE ISCYTVSDSS FFSYGEIPFG VTDGPRYCYV HYNGTALKYL GTLPPSVKEI
AISKWGHFYI NGYNFFSTFP IDCISFNLTT GDSDVFWTIA YTSYTEALVQ VENTAITKVT
YCNSHVNNIK CSQITANLNN GFYPVSSSEV GLVNKSVVLL PSFYTHTIVN ITIGLGMKRS
GYGQPIASTL SNITLPMQDH NTDVYCIRSD QFSVYVHSTC KSALWDNIFK RNCTDVLDAT
AVIKTGTCPF SFDKLNNYLT FNKFCLSLSP VGANCKFDVA ARTRTNEQVV RSLYVIYEEG
DNIVGVPSDN SGVHDLSVLH LDSCTDYNIY GRTGVGIIRQ TNRTLLSGLY YTSLSGDLLG
FKNVSDGVIY SVTPCDVSAQ AAVIDGTIVG AITSINSELL GLTHWTTTPN FYYYSIYNYT
NDRTRGTAID SNDVDCEPVI TYSNIGVCKN GAFVFINVTH SDGDVQPIST GNVTIPTNFT
ISVQVEYIQV YTTPVSIDCS RYVCNGNPRC NKLLTQYVSA CQTIEQALAM GARLENMEVD
SMLFVSENAL KLASVEAFNS SETLDPIYKE WPNIGGSWLE GLKYILPSHN SKRKYRSAIE
DLLFDKVVTS GLGTVDEDYK RCTGGYDIAD LVCAQYYNGI MVLPGVANAD KMTMYTASLA
GGITLGALGG GAVAIPFAVA VQARLNYVAL QTDVLNKNQQ ILASAFNQAI GNITQSFGKV
NDAIHQTSRG LATVAKALAK VQDVVNIQGQ ALSHLTVQLQ NNFQAISSSI SDIYNRLDEL
SADAQVDRLI TGRLTALNAF VSQTLTRQAE VRASRQLAKD KVNECVRSQS QRFGFCGNGT
HLFSLANAAP NGMIFFHTVL LPTAYETVTA WPGICASDGD RTFGLVVKDV QLTLFRNLDD
KFYLTPRTMY QPRVATSSDF VQIEGCDVLF VNATVSDLPS IIPDYIDINQ TVQDILENFR
PNWTVPELTF DIFNATYLNL TGEIDDLEFR SEKLHNTTVE LAILIDNINN TLVNLEWLNR
IETYVKWPWY VWLLIGLVVI FCIPLLLFCC CSTGCCGCIG CLGSCCHSIC SRRQFENYEP
IEKVHVH
