MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Spike glycoprotein; Short=S glycoprotein; AltName: Full=E2; AltName: Full=Peplomer protein; Contains: RecName: Full=Spike protein S1; Contains: RecName: Full=Spike protein S2; Flags: Precursor; |
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| MyHits synonyms | SPIKE_IBV6 , P05135 , 8FE344CF2995478C |
 Legends: 1, N-linked (GlcNAc...); by host. {ECO:0000255}; 2, SIGNAL {ECO:0000255}; 3, TRANSMEM Helical. {ECO:0000255}; 4, TOPO_DOM Cytoplasmic. {ECO:0000255}; 5, COILED {ECO:0000255}; 6, MOTIF Di-lysine motif. {ECO:0000250}; 7, COMPBIAS Cys-rich; 8, SITE Cleavage; by host. {ECO:0000255}.
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ID SPIKE_IBV6 Reviewed; 1163 AA.
AC P05135;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 07-SEP-2016, entry version 93.
DE RecName: Full=Spike glycoprotein;
DE Short=S glycoprotein;
DE AltName: Full=E2;
DE AltName: Full=Peplomer protein;
DE Contains:
DE RecName: Full=Spike protein S1;
DE Contains:
DE RecName: Full=Spike protein S2;
DE Flags: Precursor;
GN Name=S; ORFNames=2;
OS Avian infectious bronchitis virus (strain 6/82) (IBV).
OC Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
OC Nidovirales; Coronaviridae; Coronavirinae; Gammacoronavirus.
OX NCBI_TaxID=11121;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3025348; DOI=10.1099/0022-1317-67-12-2825;
RA Binns M.M., Boursnell M.E.G., Tomley F.M., Brown T.D.K.;
RT "Comparison of the spike precursor sequences of coronavirus IBV
RT strains M41 and 6/82 with that of IBV Beaudette.";
RL J. Gen. Virol. 67:2825-2831(1986).
CC -!- FUNCTION: S1 attaches the virion to the cell membrane by
CC interacting with cell receptors, initiating the infection.
CC -!- FUNCTION: S2 is a class I viral fusion protein. Under the current
CC model, the protein has at least 3 conformational states: pre-
CC fusion native state, pre-hairpin intermediate state, and post-
CC fusion hairpin state. During viral and target cell membrane
CC fusion, the coiled coil regions (heptad repeats) assume a trimer-
CC of-hairpins structure, positioning the fusion peptide in close
CC proximity to the C-terminal region of the ectodomain. The
CC formation of this structure appears to drive apposition and
CC subsequent fusion of viral and target cell membranes (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer; each monomer consists of a S1 and a S2
CC subunit. The resulting peplomers protrude from the virus surface
CC as spikes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Spike protein S2: Virion membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC Host endoplasmic reticulum-Golgi intermediate compartment membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC Note=Accumulates in the endoplasmic reticulum-Golgi intermediate
CC compartment, where it participates in virus particle assembly.
CC Some S oligomers may be transported to the plasma membrane, where
CC they may mediate cell-cell fusion (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Spike protein S1: Virion membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host
CC endoplasmic reticulum-Golgi intermediate compartment membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=Accumulates in the endoplasmic reticulum-Golgi intermediate
CC compartment, where it participates in virus particle assembly.
CC Some S oligomers may be transported to the plasma membrane, where
CC they may mediate cell-cell fusion. S1 is not anchored to the viral
CC envelope, but associates with the extravirion surface through its
CC binding to S2 (By similarity). {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC The precursor is processed into S1 and S2 by host cell furin or
CC furin-like protease to yield the mature S1 and S2 proteins. The
CC cleavage site between S1 and S2 requires the optimal sequence
CC [KR]-X-[KR]-R. Cleavage is not necessary for virus-cell fusion (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the coronaviruses spike protein family.
CC {ECO:0000305}.
DR EMBL; X04723; CAA28432.1; -; Genomic_RNA.
DR ProteinModelPortal; P05135; -.
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-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
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-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:InterPro.
DR Gene3D; 1.20.5.790; -; 1.
DR InterPro; IPR002551; Corona_S1.
DR InterPro; IPR002552; Corona_S2.
DR InterPro; IPR027400; S_HR2.
DR Pfam; PF01600; Corona_S1; 1.
DR Pfam; PF01601; Corona_S2; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues; Coiled coil;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host membrane; Host-virus interaction; Membrane; Signal;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW Virulence; Virus endocytosis by host; Virus entry into host cell.
FT SIGNAL 1 18 {ECO:0000255}.
FT CHAIN 19 1163 Spike glycoprotein.
FT /FTId=PRO_0000037159.
FT CHAIN 19 538 Spike protein S1. {ECO:0000255}.
FT /FTId=PRO_0000037160.
FT CHAIN 539 1163 Spike protein S2. {ECO:0000255}.
FT /FTId=PRO_0000037161.
FT TOPO_DOM 19 1096 Extracellular. {ECO:0000255}.
FT TRANSMEM 1097 1117 Helical. {ECO:0000255}.
FT TOPO_DOM 1118 1163 Cytoplasmic. {ECO:0000255}.
FT COILED 823 867 {ECO:0000255}.
FT COILED 1056 1084 {ECO:0000255}.
FT MOTIF 1160 1163 Di-lysine motif. {ECO:0000250}.
FT COMPBIAS 1121 1138 Cys-rich.
FT SITE 538 539 Cleavage; by host. {ECO:0000255}.
FT CARBOHYD 23 23 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 51 51 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 74 74 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 102 102 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 139 139 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 145 145 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 164 164 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 179 179 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 213 213 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 238 238 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 248 248 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 265 265 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 272 272 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 277 277 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 307 307 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 426 426 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 448 448 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 514 514 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 531 531 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 543 543 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 580 580 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 592 592 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 670 670 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 677 677 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 948 948 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 961 961 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 980 980 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 1015 1015 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 1039 1039 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 1052 1052 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
FT CARBOHYD 1075 1075 N-linked (GlcNAc...); by host.
FT {ECO:0000255}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 26 526 ipfam:Corona_S1 [T]
FT MYHIT 547 1163 ipfam:Corona_S2 [T]
SQ SEQUENCE 1163 AA; 128685 MW; 8FE344CF2995478C CRC64;
MLERSLLLAT LLSALCSANL FGNNSYVYYY QSAFRPSDGW HLHGGAYEVV NVSTESSNAG
TTGCTAGAIY WSKNFSAASV AMTAPQNGMS WSTEQFCTAH CNFTDFVVFV THCYKSGHGS
CPLTGLIPQN HIRISAMKNS SLFYNLTVAV TKYPRFKSLQ CVNNMTSVYL NGDLVFTSNE
TKDVSAAGVH FKAGGPITYK VMREVKALAY FVNGTAQDVI LCDGSPTGLL ACQYNTGNFS
DGFYPFTNSS LVKEKFIVYR ESSVNTTLEL TNFTFSNVSN ATPNTGGVQT IQLYQTITAQ
SGYYNLNFSF LSSFIYKASD YMYGSYHPSC KFRLETINNG LWFNSLSVSL GYGPIQGGCK
QSVFANRATC CYAYSYNGPS LCKGVYRGEL TKSFECGLLV FVTKTDGSRI QTRNEPFTLT
QHNYNNITLD RCVEYNIYGR VGQGFITNVT NYAINYNYLA DGGMAILDTS GAIDIFVVQG
EYGLNYYKVN PCEDVNQQFV VSGGKLVGIL TSRNETGSQP LENQFYIKII NGTRRSRRSI
TGNVTNCPYV TYGKFCIKPD GSISTIVPKE LEHFVAPLLN VTENVLIPDS FNLTVTDEYI
QTRMDKVQIN CLQYVCGNSL ECRKLFQQYG PVCDNILSVV NSVGQKEDME LLYFYSSTKP
SGFNTPVLSN VSTGEFNISL LLTPPSSASG RSFIEDLLFT SVESVGLPTD DAYKKCTAGP
LGFLKDLACA REYNGLLVLP PIITAEMQTL YTSSLVASMA FGGITSAGAI PFATQLQARI
NHLGITQSLL FKNQEKIAAS FNKAIGHMQE GFRSTSLALQ QIQDVVNKQS SILTETMASL
NKNFGAISSV LQDIYQQLDS IQADAQVDRI ITGRLSSLSV LASAKQAEYY RVSQQRELAT
QKINECVKSQ SIRYSFCGNG RHVLTIPQNA PNGIVFIHFT YTPESFVNVT AIVGFCVNPA
NASQYAIVPA NGRGIFIQVN GSYYITARDM YMPRDITAGD IVTLTSCQAN YVSVNKTVIT
TFVDNDDFDF DDELSKWWND TKHELPDFDE FNYTVPILDI GSEIDRIQGV IQGLNDSLID
LETLSILKTY IKWPWYVWLA IAFLTIIFIL VLCWIFFMTG CCGCCCGCFG IIPLMSKCGK
KSSYYTTFDN DVVYEQYRPK KSV
//
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