ID   A0A7D4X0M7_9ALPC        Unreviewed;      1383 AA.
AC   A0A7D4X0M7;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   14-DEC-2022, entry version 6.
DE   RecName: Full=Spike glycoprotein {ECO:0000256|HAMAP-Rule:MF_04200};
DE            Short=S glycoprotein {ECO:0000256|HAMAP-Rule:MF_04200};
DE   AltName: Full=E2 {ECO:0000256|HAMAP-Rule:MF_04200};
DE   AltName: Full=Peplomer protein {ECO:0000256|HAMAP-Rule:MF_04200};
GN   Name=S {ECO:0000256|HAMAP-Rule:MF_04200, ECO:0000313|EMBL:QKV43707.1};
OS   Porcine epidemic diarrhea virus.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Alphacoronavirus; Pedacovirus.
OX   NCBI_TaxID=28295 {ECO:0000313|EMBL:QKV43707.1};
RN   [1] {ECO:0000313|EMBL:QKV43707.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEDV-1576-Zamora-Santibanez_de_Vidriales
RC   {ECO:0000313|EMBL:QKV43707.1};
RA   de Nova P.J., Cortey M., Diaz I., Rubio P., Martin M., Carvajal A.;
RL   Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QKV43707.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEDV-1576-Zamora-Santibanez_de_Vidriales
RC   {ECO:0000313|EMBL:QKV43707.1};
RX   PubMed=32511876;
RA   de Nova P.J.G., Cortey M., Diaz I., Puente H., Rubio P., Martin M.,
RA   Carvajal A.;
RT   "A retrospective study of porcine epidemic diarrhoea virus (PEDV) reveals
RT   the presence of swine enteric coronavirus (SeCoV) since 1993 and the recent
RT   introduction of a recombinant PEDV-SeCoV in Spain.";
RL   Transbound. Emerg. Dis. 0:0-0(2020).
CC   -!- FUNCTION: S1 region attaches the virion to the cell membrane by
CC       interacting with the host receptor, initiating the infection. Binding
CC       to the receptor probably induces conformational changes in the S
CC       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:0000256|HAMAP-Rule:MF_04200}.
CC   -!- SUBUNIT: Homotrimer. During virus morphogenesis, found in a complex
CC       with M and HE proteins. Interacts with host receptor.
CC       {ECO:0000256|HAMAP-Rule:MF_04200}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000256|HAMAP-
CC       Rule:MF_04200}; Single-pass type I membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_04200}. Host endoplasmic reticulum-Golgi intermediate
CC       compartment membrane {ECO:0000256|HAMAP-Rule:MF_04200}; Single-pass
CC       type I membrane protein {ECO:0000256|HAMAP-Rule:MF_04200}.
CC       Note=Accumulates in the endoplasmic reticulum-Golgi intermediate
CC       compartment, where it participates in virus particle assembly.
CC       {ECO:0000256|HAMAP-Rule:MF_04200}.
CC   -!- DOMAIN: The KxHxx motif seems to function as an ER retrieval signal.
CC       {ECO:0000256|HAMAP-Rule:MF_04200}.
CC   -!- SIMILARITY: Belongs to the alphacoronaviruses spike protein family.
CC       {ECO:0000256|HAMAP-Rule:MF_04200}.
CC   -!- CAUTION: In contrast to serogroups 2 and 3, S glycoprotein from
CC       serogroup 1 is not cleaved into S1 and S2. {ECO:0000256|HAMAP-
CC       Rule:MF_04200}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_04200}.
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DR   EMBL; MN692765; QKV43707.1; -; Genomic_RNA.
DR   GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; Coronavirus S2 glycoprotein; 2.
DR   PROSITE; PS51923; COV_S2_HR1; 1.
DR   PROSITE; PS51924; COV_S2_HR2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW   Rule:MF_04200};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|HAMAP-
KW   Rule:MF_04200};
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870, ECO:0000256|HAMAP-
KW   Rule:MF_04200};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP-
KW   Rule:MF_04200};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04200};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_04200};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_04200};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_04200};
KW   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804,
KW   ECO:0000256|HAMAP-Rule:MF_04200};
KW   Viral envelope protein {ECO:0000256|ARBA:ARBA00022879, ECO:0000256|HAMAP-
KW   Rule:MF_04200};
KW   Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04200};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026, ECO:0000256|HAMAP-Rule:MF_04200};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296,
KW   ECO:0000256|HAMAP-Rule:MF_04200}.
FT   TRANSMEM        1325..1344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          969..1088
FT                   /note="COV_S2_HR1"
FT                   /evidence="ECO:0000259|PROSITE:PS51923"
FT   DOMAIN          1240..1336
FT                   /note="COV_S2_HR2"
FT                   /evidence="ECO:0000259|PROSITE:PS51924"
FT   REGION          955..975
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04200"
FT   COILED          1036..1080
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04200"
FT   COILED          1272..1314
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04200"
FT   MOTIF           1379..1383
FT                   /note="KxHxx"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04200"
SQ   SEQUENCE   1383 AA;  151618 MW;  6E1AC5B7964B9547 CRC64;
     MKSLNYFWLF LPVLSTLSLP QDVTRCQSTI NFRRFFSKFN VQAPAVVVLG GYLPSMNSSS
     WYCGTGLETA SGVHGIFLSY IDAGQGFEIG ISQEPFDPSG YQLYLHKATN GNHNAIARLR
     ICQFPDNKTL GPTVNDVTTG RNCLFNKAIP AYMQDGKNIV VGITWDNDRV TLLADKIYHF
     YLKNDWSRVA TRCYNKRSCA MQYVYTPTYY MLNVTSAGED GIYYEPCTAN CSGYAANVFA
     TDSNGHIPEG FSFNNWFLLS NDSTLLHGKV VSNQPLLVNC LLAIPKIYGL GQFFSFNQTM
     AGVCNGAAAQ RAPEALRFNI NDTSVILAEG SIVLHTALGT NLSFVCSNSS DPHLATFAIP
     LGATQVPYYC FLKVDTYNST VYKFLAVLPP TVREIVITKY GDVYVNGFGY LHLGLLDAVT
     INFTGHGTDD DVSGFWTIAS TNFVDALIEV QGTVIQRILY CDDPVSQLKC SQVAFDLDDG
     FYPISSRNLL SHEQPISFVT LPSFNDHSFV NITVSASFGG HSGANLIASD TTINGFSSFC
     VDTRQFTISL FYNVTNSYGY VSKSQDSNCP FTLQSVNDYL SFSKFCVSTS LLASACTIDL
     FGYPEFGSGV KFTSLYFQFT KGELITGTPK PLEGVTDVSF MTLDVCTKYT IYGFKGEGII
     TLTNSSFLAG VYYTSDSGQL LAFKNVTSGA VYSVTPCSFS EQAAYVDDDI VGVISSLSSS
     TFNSTRELPG FFYHSNDGSN CTEPVLVYSN IGVCKSGSIG YVPSQSGQVK IAPTVTGNIS
     IPTNFSMSIR TEYLQLYNTP VSVDCATYVC NGNSRCKQLL TQYTAACKTI ESALQLSARL
     ESVEVNSMLT ISEEALQLAT ISSFNGDGYN FTNVLGVSVY DPASGRVVQK RSFIEDLLFN
     KVVTNGLGTV DEDYKRCSNG RSVADLVCAQ YYSGVMVLPG VVDAEKLHMY SASLIGGMVL
     GGFTSAAALP FSYAVQARLN YLALQTDVLQ RNQQLLAESF NSAIGNITSA FESVKEAISQ
     TSKGLNTVAH ALTKVQEVVN SQGAALTQLT VQLQHNFQAI SSSIDDIYSR LDSLSADVQV
     DRLITGRLSA LNAFVSQTLT KYTEVQASRK LAQQKVNECV KSQSQRYGFC GGDGEHIFSL
     VQAAPQGLLF LHTVLVPGDF VDVIAIAGLC VNDEIALTLR EPGLVLFTHE LQNHTATEYF
     VSSRRMFEPR KPTVSDFVQI ESCVVTYVNL TRDQLPDVIP DYIDVNKTLD EILASLPNRT
     GPSLPLDVFN ATYLNLTGEI ADLEQRSESL RNTTEELQSL IYNINNTLVD LEWLNRVETY
     IKWPWWVWLI IFIVLIFVVS LLVFCCISTG CCGCCGCCCA CFSGCCRGPR LQPYEVFEKV
     HVQ
//