SPIKE_CVPFS
ID SPIKE_CVPFS Reviewed; 1449 AA.
AC P18450; Q85087; Q85088;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 29-SEP-2021, entry version 105.
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 FS772/70) (TGEV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Tegacovirus.
OX NCBI_TaxID=11150;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1964522; DOI=10.1016/0168-1702(90)90090-x;
RA Britton P., Page K.W.;
RT "Sequence of the S gene from a virulent British field isolate of
RT transmissible gastroenteritis virus.";
RL Virus Res. 18:71-80(1990).
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 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; X53128; CAA37285.1; -; Genomic_RNA.
DR PIR; B43489; VGIHFS.
DR SMR; P18450; -.
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..1449
FT /note="Spike glycoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT /id="PRO_0000037223"
FT TOPO_DOM 29..1390
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TRANSMEM 1391..1410
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TOPO_DOM 1411..1449
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 17..776
FT /note="S1"
FT REGION 29..776
FT /note="S1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 657..801
FT /note="Interaction with host ANPEP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 777..1449
FT /note="S2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 1022..1043
FT /note="Fusion peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 1037..1156
FT /note="Heptad repeat 1 (HR1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01271"
FT REGION 1305..1402
FT /note="Heptad repeat 2 (HR2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01272"
FT COILED 1104..1148
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT COILED 1338..1380
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT MOTIF 1445..1449
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
SQ SEQUENCE 1449 AA; 159958 MW; 971BBAE191FDD1AF CRC64;
MKKLFVVLVV MPLIYGDNFP CSKLTNRTIG NHWNLIETFL LNYSSRLSPN SDVVLGDYFP
TVQPWFNCIH NNSNDLYVTL ENLKALYWDY ATENSTWNHK QRLNVVVNGY PYSITVTTTR
NFNSAEGAII CICKGSPPTT TTESSLTCNW GSECRLNHKF PICPSNSEAN CGNMLYGLQW
FADAVVAYLH GASYRISFEN QWSGTVTLGD MRATTLETAG TLVDLWWFNP VYDVSYYRVN
NKNGTTVVSN CTDQCASYVA NVFTTQPGGF IPSDFSFNNW FLLTNSSTLV SGKLVTKQPL
LVNCLWPVPS FEEAASTFCF EGAGFDQCNG AVLNNTVDVI RFNLNFTTNV QSGKGATVFS
LNTTGGVTLE ISCYNDTVSD SSFSSYGEIP FGVTDGPRYC YVLYNGTALK YLGTLPPSVK
EIAISKWGHF YINGYNFFST FPIDCISFNL TTGDSDVFWT IAYTSYTEAL VQVENTAITK
VTYCNSYVNN IKCSQLTANL NNGFYPVSSS EVGFVNKSVV LLPTFYTHTI VNITIGLGMK
RSGYGQPIAS TLSNITLPMQ DNNIDVYCIR SDQFSVYVHS TCKSALWDNV FKRNCTDVLD
ATAVIKTGTC PFSFDKLNNY LTFNKFCLSL SPVGANCKFD VAARTRANDQ VVRSLYVIYE
EGDNIVGVPS DNSGLHDLSV LHLDSCTDYN IYGRSGVGII RQTNRTLLSG LYYTSLSGDL
LGFKNVSDGV IYSVTPCDVS AQAAVIDGTI VGAITSINSE LLGLTHWTTT PNFYYYSIYN
YTNDMTRGTA IDSNDVDCEP VITYSNIGVC KNGALVFINV THSDGDVQPI STGNVTIPTN
FTISVQVEYI QVYTTPVSID CSRYVCNGNP RCNKLLTQYV SACQTIEQAL AVGARLENME
VDSMLFVSEN ALKLASVEAF NSSETLDPIY KEWPNIGGSW LEGLKYILPS DNSKRKYRSA
IEDLLFSKVV TSGLGTVDED YKRCTGGYDI ADLVCAQYYN GIMVLPGVAN ADKMTMYTAS
LAGGITLGAL GGGAVAIPFA VAVQARLNYV ALQTDVLNKN QQILASAFNQ AIGNITQSFG
KVNDAIHQTS RGLATVAKAL AKVQDVVNTQ GQALSHLTVQ LQNNFQAISS SISDIYNRLD
ELSADAHVDR LITGRLTALN AFVSQTLTRQ AEVRASRQLA KDKVNECVRS QSQRFGFCGN
GTHLFSLANA APNGMIFFHA VLLPTAYETV TAWAGICALD GDRTFGLVVK DVQLTLFRNL
DDKFYLTPRT MYQPRVATSS DFVQIEGCDV LFVNATLSDL PSIIPDYIDI NQTVQDILEN
FRPNWTVPEL TFDIFNATYL NLTGEIDDLE FRSEKLHNTT VELAILIDNI NNTLVNLEWL
NRIETYVKWP WYVWLLIGLV VIFCIPLLLF CCCSTGCCGC IGCLGSCCHS ICSRRQFENY
EPIEKVHIH
