ID   SPIKE_CVCAI             Reviewed;        1451 AA.
AC   P36300;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   29-SEP-2021, entry version 97.
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 Insavc-1) (CCoV) (Canine enteric coronavirus).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Alphacoronavirus; Tegacovirus.
OX   NCBI_TaxID=36391;
OH   NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1431811; DOI=10.1099/0022-1317-73-11-2849;
RA   Horsburgh B.C., Brierley I., Brown T.D.K.;
RT   "Analysis of a 9.6 kb sequence from the 3' end of canine coronavirus
RT   genomic RNA.";
RL   J. Gen. Virol. 73:2849-2862(1992).
RN   [2]
RP   INTERACTION WITH FELINE ANPEP.
RX   PubMed=8970993; DOI=10.1128/jvi.70.12.8669-8674.1996;
RA   Tresnan D.B., Levis R., Holmes K.V.;
RT   "Feline aminopeptidase N serves as a receptor for feline, canine, porcine,
RT   and human coronaviruses in serogroup I.";
RL   J. Virol. 70:8669-8674(1996).
RN   [3]
RP   INTERACTION WITH CANINE ANPEP.
RX   PubMed=8985407; DOI=10.1128/jvi.71.1.734-737.1997;
RA   Benbacer L., Kut E., Besnardeau L., Laude H., Delmas B.;
RT   "Interspecies aminopeptidase-N chimeras reveal species-specific receptor
RT   recognition by canine coronavirus, feline infectious peritonitis virus, and
RT   transmissible gastroenteritis virus.";
RL   J. Virol. 71:734-737(1997).
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, ECO:0000269|PubMed:8970993, ECO:0000269|PubMed:8985407}.
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; D13096; BAA02408.1; -; Genomic_RNA.
DR   PIR; JQ1719; JQ1719.
DR   SMR; P36300; -.
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   1: Evidence at protein level;
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..1451
FT                   /note="Spike glycoprotein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT                   /id="PRO_0000037202"
FT   TOPO_DOM        32..1392
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   TRANSMEM        1393..1412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   TOPO_DOM        1413..1451
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   REGION          32..779
FT                   /note="S1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   REGION          660..803
FT                   /note="Interaction with host ANPEP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   REGION          780..1451
FT                   /note="S2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   REGION          1024..1045
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   REGION          1039..1158
FT                   /note="Heptad repeat 1 (HR1)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01271"
FT   REGION          1307..1404
FT                   /note="Heptad repeat 2 (HR2)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01272"
FT   COILED          1106..1150
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   COILED          1340..1382
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   MOTIF           1447..1451
FT                   /note="KxHxx"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
SQ   SEQUENCE   1451 AA;  160468 MW;  F3E6ECA8B914CE6C CRC64;
     MIVLTLCLFL FLYSSVSCTS NNDCVQVNVT QLPGNENIIK DFLFQNFKEE GSLVVGGYYP
     TEVWYNCSTT QQTTAYKYFS NIHAFYFDME AMENSTGNAR GKPLLVHVHG NPVSIIVYIS
     AYRDDVQFRP LLKHGLLCIT KNDTVDYNSF TINQWRDICL GDDRKIPFSV VPTDNGTKLF
     GLEWNDDYVT AYISDESHRL NINNNWFNNV TLLYSRTSTA TWQHSAAYVY QGVSNFTYYK
     LNKTAGLKSY ELCEDYEYCT GYATNVFAPT SGGYIPDGFS FNNWFMLTNS STFVSGRFVT
     NQPLLVNCLW PVPSFGVAAQ EFCFEGAQFS QCNGVSLNNT VDVIRFNLNF TTDVQSGMGA
     TVFSLNTTGG VILEISCYND TVSESSFYSY GEIPFGVTDG PRYCYVLYNG TALKYLGTLP
     PSVKEIAISK WGHFYINGYN FFSTFPIDCI AFNLTTGASG AFWTIAYTSY TEALVQVENT
     AIKKVTYCNS HINNIKCSQL TANLQNGFYP VASSEVGLVN KSVVLLPSFY SHTSVNITID
     LGMKRSVTVT IASPLSNITL PMQDNNIDVY CIRSNQFSVY VHSTCKSSLW DNNFNSACTD
     VLDATAVIKT GTCPFSFDKL NNYLTFNKFC LSLNPVGANC KLDVAARTRT NEQVFGSLYV
     IYEEGDNIVG VPSDNSGLHD LSVLHLDSCT DYNIYGRTGV GIIRKTNSTL LSGLYYTSLS
     GDLLGFKNVS DGVVYSVTPC DVSAQAAVID GAIVGAMTSI NSELLGLTHW TTTPNFYYYS
     IYNYTNVMNR GTAIDNDIDC EPIITYSNIG VCKNGALVFI NVTHSDGDVQ PISTGNVTIP
     TNFTISVQVE YIQVYTTPVS IDCARYVCNG NPRCNKLLTQ YVSACQTIEQ ALAMGARLEN
     MEIDSMLFVS ENALKLASVE AFNSTENLDP IYKEWPNIGG SWLGGLKDIL PSHNSKRKYR
     SAIEDLLFDK VVTSGLGTVD EDYKRSAGGY DIADLVCARY YNGIMVLPGV ANDDKMTMYT
     ASLTGGITLG ALSGGAVAIP FAVAVQARLN YVALQTDVLN KNQQILANAF NQAIGNITQA
     FGKVNDAIHQ TSKGLATVAK ALAKVQDVVN TQGQALSHLT VQLQNNFQAI SSSISDIYNR
     LDELSADAQV DRLITGRLTA LNAFVSQTLT RQAEVRASRQ LAKDKVNECV RSQSQRFGFC
     GNGTHLFSLA NAAPNGMIFF HTVLLPTAYE TVTAWSGICA SDGSRTFGLV VEDVQLTLFR
     NLDEKFYLTP RTMYQPRVAT SSDFVQIEGC DVLFVNGTVI ELPSIIPDYI DINQTVQDIL
     ENFRPNWTVP ELPLDIFHAT YLNLTGEIND LEFRSEKLHN TTVELAILID NINNTLVNLE
     WLNRIETYVK WPWYVWLLIG LVVIFCIPIL LFCCCSTGCC GCIGCLGSCC HSICSRGQFE
     SYEPIEKVHV H