GENTAUR Molecular Products.

 SPIKE_CVCAI             Reviewed;        1451 AA.
 P36300;
 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
 01-JUN-1994, sequence version 1.
 28-FEB-2018, entry version 85.
 RecName: Full=Spike glycoprotein;
          Short=S glycoprotein;
 AltName: Full=E2;
 AltName: Full=Peplomer protein;
 Flags: Precursor;
 Name=S;
 Canine coronavirus (strain Insavc-1) (CCoV) (Canine enteric
 coronavirus).
 Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
 Nidovirales; Coronaviridae; Coronavirinae; Alphacoronavirus.
 NCBI_TaxID=36391;
 NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
 [1]
 NUCLEOTIDE SEQUENCE [GENOMIC RNA].
 PubMed=1431811; DOI=10.1099/0022-1317-73-11-2849;
 Horsburgh B.C., Brierley I., Brown T.D.K.;
 "Analysis of a 9.6 kb sequence from the 3' end of canine coronavirus
 genomic RNA.";
 J. Gen. Virol. 73:2849-2862(1992).
 [2]
 INTERACTION WITH FELINE ANPEP.
 PubMed=8970993;
 Tresnan D.B., Levis R., Holmes K.V.;
 "Feline aminopeptidase N serves as a receptor for feline, canine,
 porcine, and human coronaviruses in serogroup I.";
 J. Virol. 70:8669-8674(1996).
 [3]
 INTERACTION WITH CANINE ANPEP.
 PubMed=8985407;
 Benbacer L., Kut E., Besnardeau L., Laude H., Delmas B.;
 "Interspecies aminopeptidase-N chimeras reveal species-specific
 receptor recognition by canine coronavirus, feline infectious
 peritonitis virus, and transmissible gastroenteritis virus.";
 J. Virol. 71:734-737(1997).
 -!- FUNCTION: S1 region attaches the virion to the cell membrane by
     interacting with canine ANPEP/aminopeptidase N, initiating the
     infection. Binding to the receptor probably induces conformational
     changes in the S glycoprotein unmasking the fusion peptide of S2
     region and activating membranes fusion. S2 region belongs to the
     class I viral fusion protein. Under the current model, the protein
     has at least 3 conformational states: pre-fusion native state,
     pre-hairpin intermediate state, and post-fusion hairpin state.
     During viral and target cell membrane fusion, the coiled coil
     regions (heptad repeats) regions assume a trimer-of-hairpins
     structure, positioning the fusion peptide in close proximity to
     the C-terminal region of the ectodomain. The formation of this
     structure appears to drive apposition and subsequent fusion of
     viral and target cell membranes (By similarity). {ECO:0000250}.
 -!- SUBUNIT: Homotrimer. Cytoplasmic tail interacts with M protein (By
     similarity). Interacts with canine and feline ANPEP. {ECO:0000250,
     ECO:0000269|PubMed:8970993, ECO:0000269|PubMed:8985407}.
 -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass
     type I membrane protein {ECO:0000250}. Host endoplasmic reticulum-
     Golgi intermediate compartment membrane {ECO:0000250}; Single-pass
     type I membrane protein {ECO:0000250}. Note=Accumulates in the
     endoplasmic reticulum-Golgi intermediate compartment, where it
     participates in virus particle assembly. Some S oligomers may be
     transported to the plasma membrane, where they may mediate cell-
     cell fusion (By similarity). {ECO:0000250}.
 -!- DOMAIN: The KxHxx motif seems to function as an ER retrieval
     signal. {ECO:0000250}.
 -!- SIMILARITY: Belongs to the coronaviruses spike protein family.
     {ECO:0000305}.
 -!- CAUTION: In contrast to serogroups 2 and 3, S glycoprotein from
     serogroup 1 is not cleaved into S1 and S2. {ECO:0000305}.
 -----------------------------------------------------------------------
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 EMBL; D13096; BAA02408.1; -; Genomic_RNA.
 PIR; JQ1719; JQ1719.
 ProteinModelPortal; P36300; -.
 SMR; P36300; -.
 GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
 GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
 GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
 GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
 GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
 GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:InterPro.
 InterPro; IPR002551; Corona_S1.
 InterPro; IPR002552; Corona_S2.
 Pfam; PF01600; Corona_S1; 1.
 Pfam; PF01601; Corona_S2; 1.
 1: Evidence at protein level;
 Coiled coil; Glycoprotein; Host membrane; Host-virus interaction;
 Membrane; Signal; Transmembrane; Transmembrane helix;
 Viral attachment to host cell; Viral envelope protein; Virion;
 Virulence; Virus entry into host cell.
 SIGNAL        1     18       {ECO:0000255}.
 CHAIN        19   1451       Spike glycoprotein.
                              /FTId=PRO_0000037202.
 TOPO_DOM     19   1393       Virion surface. {ECO:0000255}.
 TRANSMEM   1394   1412       Helical. {ECO:0000255}.
 TOPO_DOM   1413   1451       Intravirion. {ECO:0000255}.
 COILED     1106   1150       {ECO:0000255}.
 COILED     1340   1382       {ECO:0000255}.
 MOTIF      1447   1451       KxHxx. {ECO:0000250}.
 COMPBIAS   1413   1434       Cys-rich.
 CARBOHYD     28     28       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD     66     66       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD     94     94       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    142    142       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    175    175       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    209    209       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    235    235       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    242    242       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    289    289       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    338    338       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    349    349       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    366    366       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    379    379       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    409    409       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    453    453       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    520    520       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    536    536       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    557    557       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    707    707       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    728    728       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    783    783       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    821    821       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    836    836       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    842    842       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD    923    923       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD   1076   1076       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD   1202   1202       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD   1296   1296       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD   1313   1313       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD   1326   1326       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD   1343   1343       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD   1360   1360       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 CARBOHYD   1373   1373       N-linked (GlcNAc...) asparagine; by host.
                              {ECO:0000255}.
 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

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