SPIKE_BC512
ID SPIKE_BC512 Reviewed; 1371 AA.
AC Q0Q466;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 Bat coronavirus 512/2005 (BtCoV) (BtCoV/512/2005).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Pedacovirus.
OX NCBI_TaxID=693999;
OH NCBI_TaxID=153297; Scotophilus kuhlii (Lesser asiatic yellow bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16840328; DOI=10.1128/jvi.00697-06;
RA Tang X.C., Zhang J.X., Zhang S.Y., Wang P., Fan X.H., Li L.F., Li G.,
RA Dong B.Q., Liu W., Cheung C.L., Xu K.M., Song W.J., Vijaykrishna D.,
RA Poon L.L.M., Peiris J.S.M., Smith G.J., Chen H., Guan Y.;
RT "Prevalence and genetic diversity of coronaviruses in bats from China.";
RL J. Virol. 80:7481-7490(2006).
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 -!- MISCELLANEOUS: Bat coronavirus 512/2005 is highly similar to porcine
CC epidemic diarrhea virus (PEDV).
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; DQ648858; ABG47078.1; -; Genomic_RNA.
DR RefSeq; YP_001351684.1; NC_009657.1.
DR SMR; Q0Q466; -.
DR PRIDE; Q0Q466; -.
DR GeneID; 11266523; -.
DR KEGG; vg:11266523; -.
DR Proteomes; UP000113079; 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 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..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT CHAIN 24..1371
FT /note="Spike glycoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT /id="PRO_0000289929"
FT TOPO_DOM 24..1312
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TRANSMEM 1313..1332
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TOPO_DOM 1333..1371
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 24..737
FT /note="S1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 619..748
FT /note="Interaction with host ANPEP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 738..1371
FT /note="S2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 949..969
FT /note="Fusion peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 963..1082
FT /note="Heptad repeat 1 (HR1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01271"
FT REGION 1228..1324
FT /note="Heptad repeat 2 (HR2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01272"
FT COILED 1030..1074
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT COILED 1260..1302
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT MOTIF 1367..1371
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
SQ SEQUENCE 1371 AA; 150804 MW; 67DD597F41AD9224 CRC64;
MKYTLLFCVV FATVSFGFAD NERCNKTVNL TRLFSKFDIQ PPSQVVLAGL LPNQTAQWKC
TTETNKRDEG VGVKGVFLSY VSSGRGFTIG VSQYNFDPST YQLYLHRDTN GNSNAFAYLR
ICKWPSKKWL QSTSNMDTSG RFCLVNKKIP AAFTDHANMV VGITWDQDRV TFYTDKVYHF
YVPNNRWSRV VSWCSAADSC AMQYINSTIY YNLNVTTPGP GGITYSVCTK HCTGLADNVF
STDQGGHIPP IFPYNNWFLL TNTSTLVQGV TRVFQPFLVN CLVALPKLQG LTTTLSFDSP
LNVPGFSCNG ANGSSSAEAF RFNVNDTKLF VGAGAVTLNT VDGVNVSIVC SNNATQPTRS
NNLQEDLPYY CFTNTSSGTN HTVKFLSVFP PIIREFVITK YGNVYVNGYI YLRTRPLTAV
HLNASSHSQD VAGFWTIAAT NFTDVLVEVN NTGIQRLLYC DTPENSVKCS QLSFELEDGF
YSMTADNVYA VTKPHTFVTL PTFNDHGFVN VTVGGNFDSS YPPKFTANGT LVNNGTVVCV
TSNQFTLRHD FMVGYSADMR KGIFEYSSTC PFNRETINNY LTFGRICFST SPADGACELK
YYVWNTIGAV SHLAGTLYVQ HTKGDIITGT PKPLQGLNDI SELHLDTCTT YTIYGFRGDG
VIRLTNQTFL SGVYYTSESG QLLAFKNVTT GQIYSVTPCQ LVQQVAFVED RIVGVISSAN
NTGFFNSTRT FPGFYYHSND TTNCTSPRLV YSNIGVCTSG AIGLLSPKAA QPQVQPMFQG
NISIPTNFTM SVRTEYIQLF NKPVSVDCAM YVCNGNDRCK QLLSQYTSAC KNIESALQLS
ARLESMEVNS MLTVSDEALK LATISQFPGG GYNFTNILPA NPGARSVIED ILFDKVVTSG
LGTVDEDYKR CSNGLSIADL ACAQHYNGIM VLPGVADWEK VHMYSASLVG GMTLGGITSA
AALPFSYAVQ ARLNYVALQT DVLQRNQQML ANSFNSAISN ITLAFESVNN AIYQTSAGLN
TVAEALSKVQ DVVNGQGNAL SQLTVQLQNN FQAISNSIGD IYSRLDQITA DAQVDRLITG
RLAALNAFVA QSLTKYAEVQ ASRTLAKQKV NECVKSQSPR YGFCGDEGEH IFSLTQAAPQ
GLMFLHTVLV PNGFINVTAV TGLCVDETIA MTLRQSGFVL FVQNGNYLVS PRKMFEPRRP
EVADFVQVKT CTISYVNITN NQLPDIIPDY VDVNKTIDEI LANLPNNTVP DLPLDVFNQT
FLNLTGEIAD LEARSESLKN TSEELRQLIQ NINNTLVDLQ WLNRVETFIK WPWYVWLAIV
IALILVVSLL VFCCISTGCC GCCGCCGSCF SGCCRGTKLQ HYEPIEKVHV Q
