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SPIKE_CVBQ
ID   SPIKE_CVBQ              Reviewed;        1363 AA.
AC   P25193; Q77NC4;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
DE            Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
DE   AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04099};
DE   AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04099};
DE   Contains:
DE     RecName: Full=Spike protein S1 {ECO:0000255|HAMAP-Rule:MF_04099};
DE   Contains:
DE     RecName: Full=Spike protein S2 {ECO:0000255|HAMAP-Rule:MF_04099};
DE   Contains:
DE     RecName: Full=Spike protein S2' {ECO:0000255|HAMAP-Rule:MF_04099};
DE   Flags: Precursor;
GN   Name=S {ECO:0000255|HAMAP-Rule:MF_04099}; ORFNames=3;
OS   Bovine coronavirus (strain Quebec) (BCoV) (BCV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Embecovirus.
OX   NCBI_TaxID=11133;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2155283; DOI=10.1099/0022-1317-71-2-263;
RA   Parker M.D., Yoo D., Cox G.J., Babiuk L.A.;
RT   "Primary structure of the S peplomer gene of bovine coronavirus and surface
RT   expression in insect cells.";
RL   J. Gen. Virol. 71:263-270(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11774548;
RA   Yoo D., Pei Y.;
RT   "Full-length genomic sequence of bovine coronavirus (31 kb). Completion of
RT   the open reading frame 1a/1b sequences.";
RL   Adv. Exp. Med. Biol. 494:73-76(2001).
CC   -!- FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane
CC       by interacting with host receptor, initiating the infection.
CC       {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- FUNCTION: [Spike protein S2]: Mediates fusion of the virion and
CC       cellular membranes by acting as a class I viral fusion protein. Under
CC       the current model, the protein has at least three conformational
CC       states: pre-fusion native state, pre-hairpin intermediate state, and
CC       post-fusion hairpin state. During viral and target cell membrane
CC       fusion, the coiled coil regions (heptad repeats) assume a trimer-of-
CC       hairpins structure, positioning the fusion peptide in close proximity
CC       to the C-terminal region of the ectodomain. The formation of this
CC       structure appears to drive apposition and subsequent fusion of viral
CC       and target cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- FUNCTION: [Spike protein S2']: Acts as a viral fusion peptide which is
CC       unmasked following S2 cleavage occurring upon virus endocytosis.
CC       {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- SUBUNIT: Homotrimer; each monomer consists of a S1 and a S2 subunit.
CC       The resulting peplomers protrude from the virus surface as spikes.
CC       {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate
CC       compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass
CC       type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host cell
CC       membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_04099}. Note=Accumulates in the
CC       endoplasmic reticulum-Golgi intermediate compartment, where it
CC       participates in virus particle assembly. Some S oligomers are
CC       transported to the host plasma membrane, where they may mediate cell-
CC       cell fusion. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- DOMAIN: Fusion peptide 1 (FP1) and fusion peptide 2 (FP2) function
CC       cooperatively and have a membrane-ordering effect on lipid headgroups
CC       and shallow hydrophobic regions of target bilayers. They are considered
CC       as two domains of an extended, bipartite FP. The membrane-ordering
CC       activity is calcium-dependent and also dependent on correct folding,
CC       which is maintained by an internal disulfide bond in FP2.
CC       {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC       precursor is processed into S1 and S2 by host cell furin or another
CC       cellular protease to yield the mature S1 and S2 proteins. Additionally,
CC       a second cleavage leads to the release of a fusion peptide after viral
CC       attachment to host cell receptor. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike
CC       glycoprotein is digested within host endosomes. {ECO:0000255|HAMAP-
CC       Rule:MF_04099}.
CC   -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04099}.
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DR   EMBL; D00662; BAA00557.1; -; Genomic_RNA.
DR   EMBL; AF220295; AAL40400.1; -; Genomic_RNA.
DR   PIR; A34147; VGIHQU.
DR   SMR; P25193; -.
DR   Proteomes; UP000008572; Genome.
DR   GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma 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   CDD; cd21485; HCoV-OC43-like_Spike_S1_RBD; 1.
DR   CDD; cd21625; MHV-like_Spike_S1_NTD; 1.
DR   Gene3D; 2.60.120.960; -; 1.
DR   HAMAP; MF_04099; BETA_CORONA_SPIKE; 1.
DR   InterPro; IPR032500; bCoV_S1_N.
DR   InterPro; IPR042578; BETA_CORONA_SPIKE.
DR   InterPro; IPR043607; CoV_S1_C.
DR   InterPro; IPR043473; S2_sf_CoV.
DR   InterPro; IPR043002; Spike_N_sf.
DR   InterPro; IPR044339; Spike_S1_NTD_MHV-like.
DR   InterPro; IPR018548; Spike_S1_RBD_bCoV.
DR   InterPro; IPR044372; Spike_S1_RBD_HCoV-OC43-like.
DR   InterPro; IPR036326; Spike_S1_RBD_sf_bCoV.
DR   InterPro; IPR002552; Spike_S2_CoV.
DR   InterPro; IPR044873; Spike_S2_CoV_HR1.
DR   InterPro; IPR044874; Spike_S2_CoV_HR2.
DR   Pfam; PF16451; bCoV_S1_N; 1.
DR   Pfam; PF09408; bCoV_S1_RBD; 1.
DR   Pfam; PF19209; CoV_S1_C; 1.
DR   Pfam; PF01601; CoV_S2; 1.
DR   SUPFAM; SSF111474; SSF111474; 2.
DR   SUPFAM; SSF143587; SSF143587; 1.
DR   PROSITE; PS51921; BCOV_S1_CTD; 1.
DR   PROSITE; PS51922; BCOV_S1_NTD; 1.
DR   PROSITE; PS51923; COV_S2_HR1; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein;
KW   Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW   Membrane; Palmitate; Signal; Transmembrane; Transmembrane helix;
KW   Viral attachment to host cell; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virulence;
KW   Virus entry into host cell.
FT   SIGNAL          1..13
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CHAIN           14..1363
FT                   /note="Spike glycoprotein"
FT                   /id="PRO_0000037196"
FT   CHAIN           14..768
FT                   /note="Spike protein S1"
FT                   /id="PRO_0000037197"
FT   CHAIN           769..1363
FT                   /note="Spike protein S2"
FT                   /id="PRO_0000037198"
FT   CHAIN           914..1363
FT                   /note="Spike protein S2'"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT                   /id="PRO_0000444076"
FT   TOPO_DOM        14..1307
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   TRANSMEM        1308..1328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   TOPO_DOM        1329..1363
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   DOMAIN          15..298
FT                   /note="BetaCoV S1-NTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DOMAIN          329..617
FT                   /note="BetaCoV S1-CTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT   REGION          914..935
FT                   /note="Fusion peptide 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   REGION          933..953
FT                   /note="Fusion peptide 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   REGION          1014..1064
FT                   /note="Heptad repeat 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   REGION          1258..1296
FT                   /note="Heptad repeat 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   COILED          1043..1087
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   COILED          1269..1297
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   MOTIF           1359..1363
FT                   /note="KxHxx"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   SITE            768..769
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000250"
FT   SITE            913..914
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        359
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        649
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        676
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        696
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        714
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        739
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        788
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        937
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1194
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1224
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1234
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1253
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1267
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1288
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   DISULFID        21..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DISULFID        160..193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DISULFID        172..252
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DISULFID        286..296
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DISULFID        331..356
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT   DISULFID        374..427
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT   DISULFID        386..615
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT   DISULFID        938..949
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
SQ   SEQUENCE   1363 AA;  150870 MW;  6A6587B07A102B71 CRC64;
     MFLILLISLP MAFAVIGDLK CTTVSINDVD TGAPSISTDI VDVTNGLGTY YVLDRVYLNT
     TLLLNGYYPT SGSTYRNMAL KGTLLLSRLW FKPPFLSDFI NGIFAKVKNT KVIKKGVMYS
     EFPAITIGST FVNTSYSVVV QPHTTNLDNK LQGLLEISVC QYTMCEYPHT ICHPKLGNKR
     VELWHWDTGV VSCLYKRNFT YDVNADYLYF HFYQEGGTFY AYFTDTGVVT KFLFNVYLGT
     VLSHYYVLPL TCSSAMTLEY WVTPLTSKQY LLAFNQDGVI FNAVDCKSDF MSEIKCKTLS
     IAPSTGVYEL NGYTVQPIAD VYRRIPNLPD CNIEAWLNDK SVPSPLNWER KTFSNCNFNM
     SSLMSFIQAD SFTCNNIDAA KIYGMCFSSI TIDKFAIPNG RKVDLQLGNL GYLQSFNYRI
     DTTATSCQLY YNLPAANVSV SRFNPSTWNR RFGFTEQFVF KPQPVGVFTH HDVVYAQHCF
     KAPKNFCPCK LDGSLCVGNG PGIDAGYKNS GIGTCPAGTN YLTCHNAAQC DCLCTPDPIT
     SKSTGPYKCP QTKYLVGIGE HCSGLAIKSD YCGGNPCTCQ PQAFLGWSVD SCLQGDRCNI
     FANFIFHDVN SGTTCSTDLQ KSNTDIILGV CVNYDLYGIT GQGIFVEVNA TYYNSWQNLL
     YDSNGNLYGF RDYLTNRTFM IRSCYSGRVS AAFHANSSEP ALLFRNIKCN YVFNNTLSRQ
     LQPINYFDSY LGCVVNADNS TSSVVQTCDL TVGSGYCVDY STKRRSRRAI TTGYRFTNFE
     PFTVNSVNDS LEPVGGLYEI QIPSEFTIGN MEEFIQTSSP KVTIDCSAFV CGDYAACKSQ
     LVEYGSFCDN INAILTEVNE LLDTTQLQVA NSLMNGVTLS TKLKDGVNFN VDDINFSPVL
     GCLGSACNKV SSRSAIEDLL FSKVKLSDVG FVEAYNNCTG GAEIRDLICV QSYNGIKVLP
     PLLSVNQISG YTLAATSASL FPPLSAAVGV PFYLNVQYRI NGIGVTMDVL SQNQKLIANA
     FNNALDAIQE GFDATNSALV KIQAVVNANA EALNNLLQQL SNRFGAISSS LQEILSRLDA
     LEAQAQIDRL INGRLTALNV YVSQQLSDST LVKFSAAQAM EKVNECVKSQ SSRINFCGNG
     NHIISLVQNA PYGLYFIHFS YVPTKYVTAK VSPGLCIAGD RGIAPKSGYF VNVNNTWMFT
     GSGYYYPEPI TGNNVVVMST CAVNYTKAPD VMLNISTPNL HDFKEELDQW FKNQTSVAPD
     LSLDYINVTF LDLQDEMNRL QEAIKVLNQS YINLKDIGTY EYYVKWPWYV WLLIGFAGVA
     MLVLLFFICC CTGCGTSCFK ICGGCCDDYT GHQELVIKTS HDD
 
 
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