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SPIKE_CVPRM
ID   SPIKE_CVPRM             Reviewed;        1225 AA.
AC   P24413;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   29-SEP-2021, entry version 101.
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   Porcine respiratory coronavirus (strain RM4) (PRCoV) (PRCV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Alphacoronavirus; Tegacovirus.
OX   NCBI_TaxID=11148;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2174956; DOI=10.1099/0022-1317-71-11-2599;
RA   Rasschaert D., Duarte M., Laude H.;
RT   "Porcine respiratory coronavirus differs from transmissible gastroenteritis
RT   virus by a few genomic deletions.";
RL   J. Gen. Virol. 71:2599-2607(1990).
RN   [2]
RP   INTERACTION WITH PORCINE ANPEP.
RX   PubMed=7911642; DOI=10.1007/978-1-4615-2996-5_45;
RA   Delmas B., Gelfi J., Sjostrom H., Noren O., Laude H.;
RT   "Further characterization of aminopeptidase-N as a receptor for
RT   coronaviruses.";
RL   Adv. Exp. Med. Biol. 342:293-298(1993).
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; Z24675; CAA80837.1; -; Genomic_RNA.
DR   PIR; A36607; A36607.
DR   SMR; P24413; -.
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..12
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   CHAIN           13..1225
FT                   /note="Spike glycoprotein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT                   /id="PRO_0000037226"
FT   TOPO_DOM        13..1166
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   TRANSMEM        1167..1186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   TOPO_DOM        1187..1225
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   REGION          13..552
FT                   /note="S1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   REGION          17..552
FT                   /note="S1"
FT   REGION          433..577
FT                   /note="Interaction with host ANPEP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   REGION          553..1225
FT                   /note="S2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   REGION          798..819
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   REGION          813..932
FT                   /note="Heptad repeat 1 (HR1)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01271"
FT   REGION          1081..1178
FT                   /note="Heptad repeat 2 (HR2)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01272"
FT   COILED          880..924
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   COILED          1114..1156
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT   MOTIF           1221..1225
FT                   /note="KxHxx"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
SQ   SEQUENCE   1225 AA;  134794 MW;  6C20A860901C8376 CRC64;
     MKKLFVVLVV MPLIYGDKFP TSVVSNCTDQ CASYVANVFT ILPGGFIPSD FSFNNWFLLT
     NSSTLVNGKL VTKQPLLVNC LWPVPSFEEV ASTFCFEGAD FDQCNGAVLN NTVDVIRFNL
     NFTTNVQSGK GATVFSLNTT GGVTLEISCY NDTVSDSSFS SYGEIPFGVT NGPRYCYVLY
     NGTALKYLGT LPPSVKEIAI SKWGHFYING YNFFSTFPID CISFNLTTGD SDVFWTIAYT
     SYTEALVQVE NTAITNVTYC NSYVNNIKCS QLTANLNNGF YPVSSSEVGS VNKSVVLLPS
     FLTHTIVNIT IGLGMKRSGY GQPIASTLSN ITLPMQDNNN DVYCVRSDQF SVYVHSTCKS
     VLWDNVFKRN CTDVLDATAV IKTGTCPFSF DKLNNYLTFN KFCLSLSPVG ANCKFDVAAR
     TRTNDQVVRS LYVIYEEGDS IVGVPSDNSG LHDLSVLHLD SCTDYNIYGR TGVGIIRQTN
     RTILSGLYYT SLSGDLLGFT NVSDGVIYSV TPCDVSAQAA IIDGTIVGAI TSINSELLGL
     THWTTTPNFY YYSIYNYTND KTRGTPIGSN DVDCEPVITY SNIGVCKNGA LVFINVTHSD
     GDVQPISTGN VTIPTNFTIS VQVEYIQVYT TPVSIDCSRY VCNGNPRCNK LLTQYVSACQ
     TIEQALAMGA RLENMEVDSM LFVSENALKL ASVEAFNSSE TLDPIYKEWP NIGGFWLEGL
     KYILPSDNSK RKYRSAIEDL LFSKVVTSGL GTVDEDYKRC TGGYDIADLV CAQYYNGIMV
     LPGVANADKM TMYTASLAGG ITLGALGGGA VAIPFAVAVQ ARLNYVALQT DVLNKNQQIL
     ASAFNQAIGN ITQSFGKVND AIHQTSRGLT TVAKALAKVQ DVVNTQGQAL RHLTVQLQNN
     FQAISSSISD IYNRLDELSA DAQVDRLITG RLTALNAFVS QTLTRQAEVR ASRQLAKDKV
     NECVRSQSQR FGFCGNGTHL FSLANAAPNG MIFFHTVLLP TAYETVTAWS GICALDVDRT
     FGLVVKDVQL TLFRNLDDKF YLTPRTMYQP RVATSSDFVQ IEGCDVLFVN TTVSDLPSII
     PDYIDINQTV QDILENFRPN WTVPELTLDV FNATYLNLTG EIDDLEFRSE KLHNTTVELA
     ILIDNINNTV VNLEWLNRIE TYVKWPWYVW LLIGLVVIFC IPLLLFCCCS TGCCGCIGCL
     GSCCHSIFSR RQFENYEPIE KVHVH
 
 
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