SPIKE_CVCBG
ID SPIKE_CVCBG Reviewed; 1453 AA.
AC Q7T6T3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 29-SEP-2021, 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};
OS Canine coronavirus (strain BGF10) (CCoV) (Canine enteric coronavirus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Tegacovirus.
OX NCBI_TaxID=441619;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15177889; DOI=10.1016/j.virusres.2004.02.038;
RA Sanchez-Morgado J.M., Poynter S., Morris T.H.;
RT "Molecular characterization of a virulent canine coronavirus BGF strain.";
RL Virus Res. 104:27-31(2004).
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; AY342160; AAQ17220.1; -; Genomic_RNA.
DR SMR; Q7T6T3; -.
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..31
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT CHAIN 32..1453
FT /note="Spike glycoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT /id="PRO_0000289930"
FT TOPO_DOM 32..1394
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TRANSMEM 1395..1414
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TOPO_DOM 1415..1453
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 32..780
FT /note="S1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 661..805
FT /note="Interaction with host ANPEP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 781..1453
FT /note="S2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 1026..1047
FT /note="Fusion peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 1041..1160
FT /note="Heptad repeat 1 (HR1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01271"
FT REGION 1309..1406
FT /note="Heptad repeat 2 (HR2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01272"
FT COILED 1108..1152
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT COILED 1342..1384
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT MOTIF 1449..1453
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
SQ SEQUENCE 1453 AA; 160864 MW; A9FEB7D200CD3B28 CRC64;
MIVLTLCLFL VLYNSVICTS NNECVQVNVT QLPGNENIIR DFLFQNFKEE GTVVVGGYYP
TEVWYNCSRT ARTQAFKTFS NIHAFYFDME AMENSTGDAR GKPLLVHVHG NPVSIIVYIS
AYRHDVQGRP KLKHGLLCIT KNSTTDYDRF TANQWRDICL GEDRKIPFSV VPTDNGTKLF
GLEWNDDYVT AYISDDSHYL NINNNWFNNV TLLYSRSSTA TWQHSAAYVY QGVSNFTYYK
LNNTNGLKSY ELCEDYEYCT GYATNVFAPT PGGYIPEGFS FNNWFMLTNS STFVSGRFVT
NQPLLVNCLW PVPSFGVAAQ EFCFEGAQFS QCNGVSLNNT VDVIRFNLNF TTDVQSGMGA
TVFSLNTTGG VILDISCYND TVSESSFYSY GEIPFGVIDG PRYCYVLYNG TALKYLGTLP
PSVKEIAISK WGHFYINGYN FFSTFPIDCI SFNLTTGASG AFWTIAYTSY TEALVQVENT
AIKKVTYCNS HVNSIKCSQL TANLQNGFYP VASSEVGLVN KSVVLLPSFY SHTSVNITID
LGMRRSGYGQ PVASSLSNIS LPMQDNNTDV YCIRSNQFSF YVHSNCKSAS WDNIFNSACT
DVLEATAVIK TGTCPFSFDK LNNYLTFNKF CLSLNPTGAN CKFDVVARTR TNEQGVGSLY
VIYEEGDNIV GVPSDNSGLH DLSVLHLDSC TDYNIYGRNG VGIIRKTNST LLSGLYYTSL
SGDLLGFKNV SDGVVYSVTP CEVSAQAAVI DGAIVGAMTS INSELLGLTH WTTTPNFYYY
SIYNYTNERV RGTVTDSNDV DCEPIITYSN IGVCKNGALV FINVTHSDGD VQPISTGNVT
IPTNFTISVQ VEYIQVYTTP VSIDCSRYVC NGNSRCNKLL TQYVSACHTI EQALAMGARL
ENMEIDSMLF VSENALKLAS VEAFNSTDNL DPIYREWPNI GGSWLGGLKD ILPSHNSKRK
YRSAIEDLLF DKVVTSGLGT VDEDYKRCTG GYDIADLVCA QYYNGIMVLP GVANDDKMAM
YTASLAGGIT LGALGGGAVS IPFAVAVQAR LNYVALQTDV LNKNQQILAN AFNQAIGNIT
QAFGNVNDAI HQTSKGLATV AKALAKVQDV VNTQGQALSH LTVQLQNNFQ AISSSISDIY
NRLDELSADA QVDRLITGRL TALNAFVSQT LTRQAEVRAS RQLAKDKVNE CVRSQSQRFG
FCGNGTHLFS LANAAPNGMI FFHTVLLPTA YETVTAWSGI CASDGNRTFG LVVKDVQLTL
FRNLDYKFYL TPRTMYQPRV ATSSDFVQIE GCDVLFVNAT VIELPSIIPD YIDINQTVQD
ILENFRPNWT VPELPLDIFN ATYLNLTGEI NDLEFRSEKL HNTTLELATL IDNINNTLVN
LEWLNRIETY VKWPWYVWLL IGLVVIFCIP LLLFCCCSTG CCGCFGCIGS CCHSMCSRRQ
FESYEPIEKV HVH
