SPIKE_CVPR8
ID SPIKE_CVPR8 Reviewed; 1225 AA.
AC P27655;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 29-SEP-2021, entry version 102.
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};
OS Porcine respiratory coronavirus (strain 86/137004 / isolate British)
OS (PRCoV) (PRCV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Tegacovirus.
OX NCBI_TaxID=33736;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1662846; DOI=10.1016/0168-1702(91)90032-q;
RA Britton P., Mawditt K.L., Page K.W.;
RT "The cloning and sequencing of the virion protein genes from a British
RT isolate of porcine respiratory coronavirus: comparison with transmissible
RT gastroenteritis virus genes.";
RL Virus Res. 21:181-198(1991).
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; X60089; CAA42686.1; -; Genomic_RNA.
DR PIR; S24284; S24284.
DR SMR; P27655; -.
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..12
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT CHAIN 13..1225
FT /note="Spike glycoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT /id="PRO_0000037227"
FT TOPO_DOM 13..1166
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TRANSMEM 1167..1186
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TOPO_DOM 1187..1225
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 13..552
FT /note="S1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 17..552
FT /note="S1"
FT REGION 433..577
FT /note="Interaction with host ANPEP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 553..1225
FT /note="S2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 798..819
FT /note="Fusion peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 813..932
FT /note="Heptad repeat 1 (HR1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01271"
FT REGION 1081..1178
FT /note="Heptad repeat 2 (HR2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01272"
FT COILED 880..924
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT COILED 1114..1156
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT MOTIF 1221..1225
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
SQ SEQUENCE 1225 AA; 134729 MW; 1D7650D89AB48C9D CRC64;
MKKLFVVLVV MPLIYGDKFP TSVVSNCTDQ CASYVANVFT TQPGGFIPSD FSFNNWFILT
NSSTLVSGKL VTKQPLLVNC LWPVPSFEEA ASTFCFEGAD FDQCNGAVLN NTVDVIRFNL
NFTTNVQSGK GATVFSLNTT GGVTLEISCY NDTVSDSSFS SYGEIPFGVT NGPRYCYVLY
NGTALKYLGT LPPSVKEIAI SKWGHFYING YNFFSTFPID CISFNLTTGD SDVFWTIAYT
SYTEALVQVE NTAITNVTYC NSYVNNIKCS QLTANLNNGF YPVSSSEVGS VNKSVVLLPS
FLTHTIVNIT IGLGMKRSGY GQPIASTLSN ITLPMQDNNT DVYCVRSDQF SVYVHSTCKS
ALWDNVFKRN CTDVLDATAV IKTGTCPFSF DKLNNYLTFN KFCLSLSPVG ANCKFDVAAR
TRTNDQFVRS LYVIYEEGDS IVGVPSDNSG LHDLSVLHLD SCTDYNIYGR TGVGIIRQTN
RTLLSGLYYT SLSGDLLGFK NVSDGVIYSV TPCDVSAQAA IIDGAIVGAI TSINSELLAL
THWTITPNFY YYSIYNYTND KTRGTPIGSN DVDCEPVITY SNIGVCKNGA LVFINVTHSD
GDVQPISTGN VTIPTNFTIS VQVEYIQVYT TPVSIDCSRY VCNGNPRCNK LLTQYVSACQ
TIEQALAMGA RLENMEVDSM LFVSENALKL ASVEAFNSSE TLDPIYKEWP NIGGFWLEGL
KYILPSDNSK RKYRSAIEDL LFSKVVTSGL GTVDEDYKRC TGGYDIADLV CAQYYNGIMV
LPGVANADKM TMYTASLAGG ITLGALGGGA VAIPFAVAVQ ARLNYVALQT DVLNKNQQIL
ASAFNQAIGN ITQSFGKVND AIHQTSRGLT TVAKALAKVQ DVVNTQGQAL RHLTVQLQNN
FQAISSSISD IYNRLDELSA DAQVDRLITG RLTALNAFVS QTLTRQAEVR ASRQLAKDKV
NECVKSQSHR FGFCGNGTHL FSLANAAPNG MIFFHTVLLP TAYETVTAWS GICALDGDRT
FGLVVKDVQL TLFRNLDDNF YLTPRTMYQP RVATSSDFVQ IEGCDVLFVN TTVSDLPSII
PDYIDINQTV QDILENFRPN WTVPELTMDV FNATYLNLTG EIDDLEFRSE KLHNTTVELA
ILIDNINNTL VNLEWLNRIE TYVKWPWYVW LLIGLVVIFC IPLLLFCCCS TGCCGCIGCL
GSCCHSIFSR RQFENYEPIE KVHVH
