SPIKE_BEV
ID SPIKE_BEV Reviewed; 1581 AA.
AC P23052;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Spike glycoprotein;
DE Short=S glycoprotein;
DE AltName: Full=E2;
DE AltName: Full=Peplomer protein;
DE Flags: Precursor;
GN Name=S; Synonyms=P;
OS Berne virus (BEV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Tornidovirineae; Tobaniviridae; Torovirinae; Torovirus;
OC Renitovirus; Equine torovirus.
OX NCBI_TaxID=11156;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Isolate P138/72;
RX PubMed=2219698; DOI=10.1016/0042-6822(90)90332-l;
RA Snijder E.J., den Boon J.A., Spaan W.J.M., Weiss M., Horzinek M.C.;
RT "Primary structure and post-translational processing of the Berne virus
RT peplomer protein.";
RL Virology 178:355-363(1990).
CC -!- FUNCTION: Mediates the binding of virions to the host cell receptor and
CC is involved in membrane fusion. {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the toroviruses spike protein family.
CC {ECO:0000305}.
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DR EMBL; X52506; CAA36748.1; -; mRNA.
DR PIR; A36759; VGWJBV.
DR Proteomes; UP000006571; Genome.
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:0039663; P:membrane fusion involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR031412; S_torovirinae.
DR Pfam; PF17072; Spike_torovirin; 1.
PE 2: Evidence at transcript level;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host-virus interaction; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1581
FT /note="Spike glycoprotein"
FT /id="PRO_0000037434"
FT TOPO_DOM 21..1551
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 1552..1572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1573..1581
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 935
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 969
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1267
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1297
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1385
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1389
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1428
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1431
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1438
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1483
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1487
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1495
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1515
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1581 AA; 178332 MW; 00D91B41837AC769 CRC64;
MFLCFCAATV LCFWINSGGA DVVPNGTLIF SEPVPYPFSL DVLRSFSQHV VLRNKRAVTT
ISWSYSYQIT TSSLSVNSWY VTFTAPLGWN YYTGQSFGTV LNQNAMMRAS QSTFTYDVIS
YVGQRPNLDC QVNSLVNGGL DGWYSTVRVD NCFNAPCHVG GRPGCSIGLP YMSNGVCTRV
LSTTQSPGLQ YEIYSGQQFA VYQITPYTQY TITMPSGILG YCQQTPLYVD CGTWTPFRVH
SYGCDKVTQN CKYTLTSNWV VAFQNKATAV ILPSELIVPV AQKVTRRLGV NTPDYFWLVK
QAYHYLSQAN LSPNYALFSA LCNSLYQQSA TLSTLCFGSP FFVAQECYNN ALYLPDAVFT
TLFSTLFSWD YQINYPLNQV LTQNETFLQL PATNYQGQTL SQGRMLNLFK DAIVFLDFFD
TKFYRTNDAP SSDIFVVVAR QAQLIRYGNF RIEQINGYFQ VKCSSNIIST LEPHPAGVIM
IARHHSMWSV AARNSTSFYC VTHSLTTFGK LDISTSWFFH TLALPSGPVS QVSMPLLSTA
AVGVYMHPMI EHWIPLLTLA QSQYQPSFFN IGINKTITLT TQLQAYAQVY TAWFLSVIYV
RLPEARRLTL GVQLVPFIQA LLSIKQADLD ATDVDSVARY NVLSLMWGRK YAVVNYNQLP
EWTYPLFKGE IGESMWFRKK IMPTTEGCQT SAHFSSITGY LQFSDYVYIP KYNKVSCPIS
TLAPSVLQVY EVQSLFVILI QCVSGSYDWY PGLSGGTAFV YKSYKLGTVC VLLPSDVLST
GPNIGFYSGT ALSIVTVQTT NDVLPNCIGL VQDNIFTPCH PSGCPVRNSY DNYIVCFDSS
TYTFKNYHRT TPPVMNVPIQ EVPLQMEIPT VILQSYELKH TESVLLQDIE GGIIVDHNTG
SIWYPDGQAY DVSFYVSVII RYAPPKLELP STLANFTSCL DYICFGNYQC RTEAQTFCTS
MDYFEQVFNK SLISLKTALQ DLHYVLKLVL PETTLELTEL TRRRRRAVYE FDDTISLLSE
SFERFMSPAS QAYMANMLWW DDAFDGFSLP QRTGSILSRS PSLSSVSSWN SYTSRTPLIS
NVKTPKTTFN VKLSMPKLPK ASTLSKIGSV LSSGLSIASL GLSIFSIVED RRVTELTQQQ
IMALEDQITI LTDYTEKNFK EIQSSLNTLG QQVQDFSQQV TMSLQQLSNG LEQITQQLDK
SIYYVTATQQ YATYMSSLIN HLTELAAAVY KTQDMYVTCI HSLQSGVLSP NCITPSQIFQ
LYQVARNLSG QCQPIFSERE VSRFYSLPLV TDAMVHNDTY WFSWSIPITC SNIQGSVYKV
QPGYIVNPTH PTSLQYDLPS HVVTSNAGAL RFDDHYCDRY NQVYLCTKSA FDLQPSNYLT
MLYSNISENV SLTFHPEPRP DPCVYLSSSA LYCYYSDQCN QCVVAVGNCS NQTVTYRNYT
YPIMDPQCRG FDQITISSPI DIGVDFTALP SRPPLPLHLS YVNVTFNVTI PHGLNWTDLV
LDYSFKDKIY EISKNITDLH QQILQVSSWA SGWFQRIRDF LYNLLPTWIT WLTLGFSLFS
IVISGINIIL FFEMNGKVKK S
