SPIKE_PEDV7
ID SPIKE_PEDV7 Reviewed; 1383 AA.
AC Q91AV1;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 23-FEB-2022, 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}; ORFNames=2;
OS Porcine epidemic diarrhea virus (strain CV777) (PEDV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Pedacovirus.
OX NCBI_TaxID=229032;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8291230; DOI=10.1006/viro.1994.1058;
RA Duarte M., Tobler K., Bridgen A., Rasschaert D., Ackermann M., Laude H.;
RT "Sequence analysis of the porcine epidemic diarrhea virus genome between
RT the nucleocapsid and spike protein genes reveals a polymorphic ORF.";
RL Virology 198:466-476(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9782358; DOI=10.1007/978-1-4615-5331-1_101;
RA Bridgen A., Kocherhans R., Tobler K., Carvajal A., Ackermann M.;
RT "Further analysis of the genome of porcine epidemic diarrhea virus.";
RL Adv. Exp. Med. Biol. 440:781-786(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11724265; DOI=10.1023/a:1011831902219;
RA Kocherhans R., Bridgen A., Ackermann M., Tobler K.;
RT "Completion of the porcine epidemic diarrhoea coronavirus (PEDV) genome
RT sequence.";
RL Virus Genes 23:137-144(2001).
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; AF353511; AAK38656.1; -; Genomic_RNA.
DR RefSeq; NP_598310.1; NC_003436.1.
DR PDB; 4J79; X-ray; 1.56 A; B=1378-1383.
DR PDB; 6U7K; EM; 3.14 A; A/B/C=1-1319.
DR PDBsum; 4J79; -.
DR PDBsum; 6U7K; -.
DR SMR; Q91AV1; -.
DR IntAct; Q91AV1; 3.
DR MINT; Q91AV1; -.
DR GeneID; 935184; -.
DR KEGG; vg:935184; -.
DR Proteomes; UP000008159; Genome.
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 3D-structure; Coiled coil; Glycoprotein; Host membrane;
KW Host-virus interaction; Membrane; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Virion; Virulence; Virus entry into host cell.
FT SIGNAL 1..25
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT CHAIN 26..1383
FT /note="Spike glycoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT /id="PRO_0000283925"
FT TOPO_DOM 26..1324
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TRANSMEM 1325..1344
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TOPO_DOM 1345..1383
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 26..734
FT /note="S1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 617..745
FT /note="Interaction with host ANPEP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 735..1383
FT /note="S2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 955..975
FT /note="Fusion peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 969..1088
FT /note="Heptad repeat 1 (HR1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01271"
FT REGION 1240..1336
FT /note="Heptad repeat 2 (HR2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01272"
FT COILED 1036..1080
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT COILED 1272..1314
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT MOTIF 1379..1383
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 169..181
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 267..285
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 341..351
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 368..376
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 379..388
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 416..422
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 434..451
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 454..460
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 464..469
FT /evidence="ECO:0007829|PDB:6U7K"
FT TURN 470..473
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 479..485
FT /evidence="ECO:0007829|PDB:6U7K"
FT TURN 491..493
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 496..499
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 507..519
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 525..533
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 536..540
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 543..554
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 562..570
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 573..576
FT /evidence="ECO:0007829|PDB:6U7K"
FT TURN 577..579
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 581..590
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 596..608
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 610..627
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 647..651
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 654..664
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 671..674
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 680..684
FT /evidence="ECO:0007829|PDB:6U7K"
FT TURN 686..688
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 691..695
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 700..706
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 709..716
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 721..727
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 732..736
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 742..748
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 751..754
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 759..761
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 775..782
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 784..795
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 801..803
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 805..810
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 814..820
FT /evidence="ECO:0007829|PDB:6U7K"
FT TURN 824..827
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 828..848
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 853..859
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 872..875
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 893..902
FT /evidence="ECO:0007829|PDB:6U7K"
FT TURN 914..918
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 926..932
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 935..937
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 944..956
FT /evidence="ECO:0007829|PDB:6U7K"
FT TURN 957..959
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 971..980
FT /evidence="ECO:0007829|PDB:6U7K"
FT TURN 989..993
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 994..1010
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 1015..1017
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 1020..1023
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 1028..1039
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 1041..1043
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 1044..1051
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 1052..1054
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 1064..1067
FT /evidence="ECO:0007829|PDB:6U7K"
FT TURN 1068..1070
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 1073..1119
FT /evidence="ECO:0007829|PDB:6U7K"
FT TURN 1127..1131
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 1132..1144
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 1147..1158
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 1160..1165
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 1169..1171
FT /evidence="ECO:0007829|PDB:6U7K"
FT TURN 1172..1174
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 1175..1180
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 1184..1189
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 1193..1195
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 1200..1206
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 1216..1222
FT /evidence="ECO:0007829|PDB:6U7K"
FT STRAND 1227..1230
FT /evidence="ECO:0007829|PDB:6U7K"
FT TURN 1232..1234
FT /evidence="ECO:0007829|PDB:6U7K"
FT HELIX 1235..1238
FT /evidence="ECO:0007829|PDB:6U7K"
SQ SEQUENCE 1383 AA; 151353 MW; 022E5E5E5435876D CRC64;
MRSLIYFWLL LPVLPTLSLP QDVTRCQSTT NFRRFFSKFN VQAPAVVVLG GYLPSMNSSS
WYCGTGIETA SGVHGIFLSY IDSGQGFEIG ISQEPFDPSG YQLYLHKATN GNTNAIARLR
ICQFPDNKTL GPTVNDVTTG RNCLFNKAIP AYMRDGKDIV VGITWDNDRV TVFADKIYHF
YLKNDWSRVA TRCYNRRSCA MQYVYTPTYY MLNVTSAGED GIYYEPCTAN CTGYAANVFA
TDSNGHIPEG FSFNNWFLLS NDSTLLHGKV VSNQPLLVNC LLAIPKIYGL GQFFSFNHTM
DGVCNGAAVD RAPEALRFNI NDTSVILAEG SIVLHTALGT NLSFVCSNSS DPHLAIFAIP
LGATEVPYYC FLKVDTYNST VYKFLAVLPP TVREIVITKY GDVYVNGFGY LHLGLLDAVT
INFTGHGTDD DVSGFWTIAS TNFVDALIEV QGTSIQRILY CDDPVSQLKC SQVAFDLDDG
FYPISSRNLL SHEQPISFVT LPSFNDHSFV NITVSAAFGG LSSANLVASD TTINGFSSFC
VDTRQFTITL FYNVTNSYGY VSKSQDSNCP FTLQSVNDYL SFSKFCVSTS LLAGACTIDL
FGYPAFGSGV KLTSLYFQFT KGELITGTPK PLEGITDVSF MTLDVCTKYT IYGFKGEGII
TLTNSSILAG VYYTSDSGQL LAFKNVTSGA VYSVTPCSFS EQAAYVNDDI VGVISSLSNS
TFNNTRELPG FFYHSNDGSN CTEPVLVYSN IGVCKSGSIG YVPSQYGQVK IAPTVTGNIS
IPTNFSMSIR TEYLQLYNTP VSVDCATYVC NGNSRCKQLL TQYTAACKTI ESALQLSARL
ESVEVNSMLT ISEEALQLAT ISSFNGDGYN FTNVLGASVY DPASGRVVQK RSVIEDLLFN
KVVTNGLGTV DEDYKRCSNG RSVADLVCAQ YYSGVMVLPG VVDAEKLHMY SASLIGGMAL
GGITAAAALP FSYAVQARLN YLALQTDVLQ RNQQLLAESF NSAIGNITSA FESVKEAISQ
TSKGLNTVAH ALTKVQEVVN SQGSALNQLT VQLQHNFQAI SSSIDDIYSR LDILSADVQV
DRLITGRLSA LNAFVAQTLT KYTEVQASRK LAQQKVNECV KSQSQRYGFC GGDGEHIFSL
VQAAPQGLLF LHTVLVPGDF VNVLAIAGLC VNGEIALTLR EPGLVLFTHE LQTYTATEYF
VSSRRMFEPR KPTVSDFVQI ESCVVTYVNL TSDQLPDVIP DYIDVNKTLD EILASLPNRT
GPSLPLDVFN ATYLNLTGEI ADLEQRSESL RNTTEELRSL INNINNTLVD LEWLNRVETY
IKWPWWVWLI IVIVLIFVVS LLVFCCISTG CCGCCGCCGA CFSGCCRGPR LQPYEAFEKV
HVQ
