SPIKE_CVPRT
ID SPIKE_CVPRT Reviewed; 1447 AA.
AC Q01977;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 29-SEP-2021, entry version 93.
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 NEB72-rt) (TGEV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Tegacovirus.
OX NCBI_TaxID=33738;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
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).
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}.
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 serogroups 2 and 3, S glycoprotein from
CC serogroup 1 is not cleaved into S1 and S2. {ECO:0000255|HAMAP-
CC Rule:MF_04200, ECO:0000305}.
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DR EMBL; M94099; AAA47108.1; -; Genomic_RNA.
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 3: Inferred from homology;
KW Coiled coil; Glycoprotein; Host membrane; Host-virus interaction; Membrane;
KW Signal; Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Virion; Virulence; 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_0000037228"
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"
SQ SEQUENCE 1447 AA; 160115 MW; F0C63F62A22DD4AD CRC64;
MKKLFVVLVV MPLIYGDNFP CSKLTNRTIG NQWNLIETFL LNYSSRLPPN SDVVLGDYFP
TVQPWFNCIR NNSNDLYVTL ENLKALYWDY ATENITWNHR QRLNVVVNGY PYSITVTTTR
NFNSAEGAII CICKGSPPTT TTESSLTCNW GSECRLNHKF PICPSNSEAN CGNMLYGLQW
FADEVVAYLH GASYRISFEN QWSGTVTFGD MRATTLEVSG 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 GRTGVGIIRK 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
NDAIHXTSRG LATVAKALAK VQDVVXIQGQ 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
