ID A0A5A4M655_9ALPC Unreviewed; 1383 AA. AC A0A5A4M655; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 26-FEB-2020, entry version 3. 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}; OS Porcine epidemic diarrhea virus. OC Viruses; Riboviria; Nidovirales; Cornidovirineae; Coronaviridae; OC Orthocoronavirinae; Alphacoronavirus; Pedacovirus. OX NCBI_TaxID=28295 {ECO:0000313|EMBL:AXS76457.1}; RN [1] {ECO:0000313|EMBL:AXS76457.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AHCZ1601 {ECO:0000313|EMBL:AXS76457.1}; RA Jiao D., Sun J., Fan C.B., Zhu L., Yu Y.Z., He W.K., Li B.; RT "Porcine epidemic diarrhea virus isolate S genes."; RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MG198633; AXS76457.1; -; Genomic_RNA. 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:0009405; P:pathogenesis; IEA:UniProtKB-KW. 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; IPR002551; Corona_S1. DR InterPro; IPR002552; Corona_S2. DR Pfam; PF01600; Corona_S1; 1. DR Pfam; PF01601; Corona_S2; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_04200}; KW Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04200}; KW Host membrane {ECO:0000256|HAMAP-Rule:MF_04200}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04200}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_04200, ECO:0000256|SAM:Phobius}; KW Signal {ECO:0000256|HAMAP-Rule:MF_04200}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_04200, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04200, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|HAMAP-Rule:MF_04200}; KW Viral envelope protein {ECO:0000256|HAMAP-Rule:MF_04200}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04200}; KW Virulence {ECO:0000256|HAMAP-Rule:MF_04200}; KW Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04200}. FT TRANSMEM 1325..1344 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 231..733 FT /note="Corona_S1" FT /evidence="ECO:0000259|Pfam:PF01600" FT DOMAIN 741..1382 FT /note="Corona_S2" FT /evidence="ECO:0000259|Pfam:PF01601" 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; 151704 MW; 32A6F1BA5DAFABA0 CRC64; MKSLNYFWLF LPVLSTLSLP QDVTRCQSTI NFRRFFSKFN VQAPAVVVLG GYLPSMNSSS WYCGTGLETA SGVHGIFLSY IDAGQGFEIG ISQEPFDPSG YQLYLHKATN GNHNAIARLR ICQFPDNKTL GPTVNDVTTG RNCLFNKAIP AYMQDGKNIV VGITWDNDRV TVFADKIYHF YLKNDWSRVA TRCYNKRSCA MQYVYTPTYY MLNVTSAGED GIYYEPCTAN CSGYAANVFA TDSNGHIPEG FSFNNWFLLS NDSTLLHGKV VSNQPLLVNC LLAIPKIYGL GQFFSFNQTM DGVCNGAAAQ RAPEALRFNI NDTSVILAEG SIVLHTALGT NLSFVCSNSS DPHLATFAIP LGATQVPYYC FLKVDTYNST VYKFLAVLPP TVREIVITKY GDVYVNGFGY LHLGLLDAVT INFTGHGTDD DVSGFWTIAS TNFVDALIEV QGTAIQRILY 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 ESAEVNSMLT ISEEALQLAT ISSFNGDGYN FTNVLGVSVY DPASGRVVQK RSFIEDLLFN KVVTNGLGTV DEDYKRCSNG RSVADLVCAQ YYSGVMVLPG VVDAEKLHMY SASLIGGMVL GGFTSAAALP FSYAVQARLN YLALQTDVLQ RNQQMLAESF NSAIGNITSA FESVKEAISQ TSKGLNTVAH ALTKVQEVVN SQGAALTQLT VQLQHNFQAI SSSIDDIYSR LDILSADVQV DRLITGRLSA LNAFVSQTLT KYTEVQASRK LAQQKVNECV KSQSQRYGFC GGDGEHIFSL VQAAPQGLLF LHTVLVPGDF VDVIAIAGLC VNDEIALTLR EPGLVLFTHE LQNHTATEYF VSSRRMFEPR KPTVSDFVQI ESCVVTYVNL TRDQLPDVIP DYIDVNKTLD EILASLPNRT GPSLPLDVFN ATYLNLTGEI ADLEQRSESL RNTTEELQSF IYNINNTLVD LEWLNRVETY IKWPWWVWLI IFIVLIFVVS LLVFCCISTG CCGCCGCCCA CFSGCCRGPR LQPYEVFEKV HVQ //