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SPIKE_BCHK5
ID   SPIKE_BCHK5             Reviewed;        1352 AA.
AC   A3EXD0;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
DE            Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
DE   AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04099};
DE   AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04099};
DE   Contains:
DE     RecName: Full=Spike protein S1 {ECO:0000255|HAMAP-Rule:MF_04099};
DE   Contains:
DE     RecName: Full=Spike protein S2 {ECO:0000255|HAMAP-Rule:MF_04099};
DE   Contains:
DE     RecName: Full=Spike protein S2' {ECO:0000255|HAMAP-Rule:MF_04099};
DE   Flags: Precursor;
GN   Name=S {ECO:0000255|HAMAP-Rule:MF_04099}; ORFNames=2;
OS   Bat coronavirus HKU5 (BtCoV) (BtCoV/HKU5/2004).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Merbecovirus.
OX   NCBI_TaxID=694008;
OH   NCBI_TaxID=105295; Pipistrellus abramus (Japanese pipistrelle) (Pipistrellus javanicus abramus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate HKU5-1;
RX   PubMed=17121802; DOI=10.1128/jvi.02182-06;
RA   Woo P.C.Y., Wang M., Lau S.K.P., Xu H.F., Poon R.W.S., Guo R., Wong B.H.L.,
RA   Gao K., Tsoi H.-W., Huang Y., Li K.S.M., Lam C.S.F., Chan K.-H.,
RA   Zheng B.-J., Yuen K.-Y.;
RT   "Comparative analysis of twelve genomes of three novel group 2c and group
RT   2d coronaviruses reveals unique group and subgroup features.";
RL   J. Virol. 81:1574-1585(2007).
CC   -!- FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane
CC       by interacting with host receptor, initiating the infection.
CC       {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- FUNCTION: [Spike protein S2]: Mediates fusion of the virion and
CC       cellular membranes by acting as a class I viral fusion protein. Under
CC       the current model, the protein has at least three conformational
CC       states: pre-fusion native state, pre-hairpin intermediate state, and
CC       post-fusion hairpin state. During viral and target cell membrane
CC       fusion, the coiled coil regions (heptad repeats) assume a trimer-of-
CC       hairpins structure, positioning the fusion peptide in close proximity
CC       to the C-terminal region of the ectodomain. The formation of this
CC       structure appears to drive apposition and subsequent fusion of viral
CC       and target cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- FUNCTION: [Spike protein S2']: Acts as a viral fusion peptide which is
CC       unmasked following S2 cleavage occurring upon virus endocytosis.
CC       {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- SUBUNIT: Homotrimer; each monomer consists of a S1 and a S2 subunit.
CC       The resulting peplomers protrude from the virus surface as spikes.
CC       {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate
CC       compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass
CC       type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host cell
CC       membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_04099}. Note=Accumulates in the
CC       endoplasmic reticulum-Golgi intermediate compartment, where it
CC       participates in virus particle assembly. Some S oligomers are
CC       transported to the host plasma membrane, where they may mediate cell-
CC       cell fusion. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- DOMAIN: Fusion peptide 1 (FP1) and fusion peptide 2 (FP2) function
CC       cooperatively and have a membrane-ordering effect on lipid headgroups
CC       and shallow hydrophobic regions of target bilayers. They are considered
CC       as two domains of an extended, bipartite FP. The membrane-ordering
CC       activity is calcium-dependent and also dependent on correct folding,
CC       which is maintained by an internal disulfide bond in FP2.
CC       {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC       precursor is processed into S1 and S2 by host cell furin or another
CC       cellular protease to yield the mature S1 and S2 proteins. Additionally,
CC       a second cleavage leads to the release of a fusion peptide after viral
CC       attachment to host cell receptor. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike
CC       glycoprotein is digested within host endosomes. {ECO:0000255|HAMAP-
CC       Rule:MF_04099}.
CC   -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04099}.
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DR   EMBL; EF065509; ABN10875.1; -; Genomic_RNA.
DR   RefSeq; YP_001039962.1; NC_009020.1.
DR   PDB; 5XGR; X-ray; 2.10 A; A/B/C/D/E/F/G/H=389-586.
DR   PDBsum; 5XGR; -.
DR   SMR; A3EXD0; -.
DR   GeneID; 4836002; -.
DR   KEGG; vg:4836002; -.
DR   Proteomes; UP000007451; Genome.
DR   GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma 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   CDD; cd21626; MERS-CoV-like_Spike_S1_NTD; 1.
DR   CDD; cd21479; MERS-like_CoV_Spike_S1_RBD; 1.
DR   Gene3D; 2.60.120.960; -; 1.
DR   HAMAP; MF_04099; BETA_CORONA_SPIKE; 1.
DR   InterPro; IPR032500; bCoV_S1_N.
DR   InterPro; IPR042578; BETA_CORONA_SPIKE.
DR   InterPro; IPR043607; CoV_S1_C.
DR   InterPro; IPR043473; S2_sf_CoV.
DR   InterPro; IPR043002; Spike_N_sf.
DR   InterPro; IPR044337; Spike_S1_N_MERS-CoV-like.
DR   InterPro; IPR018548; Spike_S1_RBD_bCoV.
DR   InterPro; IPR044364; Spike_S1_RBD_MERS-CoV-like.
DR   InterPro; IPR036326; Spike_S1_RBD_sf_bCoV.
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; PF16451; bCoV_S1_N; 1.
DR   Pfam; PF09408; bCoV_S1_RBD; 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   SUPFAM; SSF143587; SSF143587; 1.
DR   PROSITE; PS51921; BCOV_S1_CTD; 1.
DR   PROSITE; PS51922; BCOV_S1_NTD; 1.
DR   PROSITE; PS51923; COV_S2_HR1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein;
KW   Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW   Membrane; Palmitate; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virulence;
KW   Virus entry into host cell.
FT   SIGNAL          1..12
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CHAIN           13..1352
FT                   /note="Spike glycoprotein"
FT                   /id="PRO_0000290324"
FT   CHAIN           13..745
FT                   /note="Spike protein S1"
FT                   /id="PRO_0000444063"
FT   CHAIN           746..1352
FT                   /note="Spike protein S2"
FT                   /id="PRO_0000290326"
FT   CHAIN           885..1352
FT                   /note="Spike protein S2'"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT                   /id="PRO_0000444064"
FT   TOPO_DOM        13..1297
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   TRANSMEM        1298..1318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   TOPO_DOM        1319..1352
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   DOMAIN          22..359
FT                   /note="BetaCoV S1-NTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DOMAIN          389..585
FT                   /note="BetaCoV S1-CTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT   REGION          885..906
FT                   /note="Fusion peptide 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   REGION          904..926
FT                   /note="Fusion peptide 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   REGION          991..1041
FT                   /note="Heptad repeat 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   REGION          1247..1286
FT                   /note="Heptad repeat 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   COILED          1020..1064
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   COILED          1259..1287
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   MOTIF           1350..1352
FT                   /note="KxHxx"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   SITE            745..746
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   SITE            884..885
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        244
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        495
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        590
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        617
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        716
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        760
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        771
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        782
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        867
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1145
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1172
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1214
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1226
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1242
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1257
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1278
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1289
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   DISULFID        193..245
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DISULFID        347..357
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DISULFID        391..415
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT   DISULFID        433..486
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT   DISULFID        445..583
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT   DISULFID        909..922
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   HELIX           394..397
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   HELIX           404..406
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   STRAND          408..412
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   STRAND          414..417
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   HELIX           419..423
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   STRAND          426..435
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   HELIX           438..443
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   STRAND          446..455
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   HELIX           458..464
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   HELIX           471..475
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   STRAND          485..491
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   STRAND          503..514
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   STRAND          516..521
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   HELIX           533..536
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   STRAND          545..548
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   STRAND          550..560
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   STRAND          566..574
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   TURN            577..580
FT                   /evidence="ECO:0007829|PDB:5XGR"
FT   STRAND          581..584
FT                   /evidence="ECO:0007829|PDB:5XGR"
SQ   SEQUENCE   1352 AA;  149697 MW;  E636107C2D80BA9A CRC64;
     MIRSVLVLMC SLTFIGNLTR GQSVDMGHNG TGSCLDSQVQ PDYFESVHTT WPMPIDTSKA
     EGVIYPNGKS YSNITLTYTG LYPKANDLGK QYLFSDGHSA PGRLNNLFVS NYSSQVESFD
     DGFVVRIGAA ANKTGTTVIS QSTFKPIKKI YPAFLLGHSV GNYTPSNRTG RYLNHTLVIL
     PDGCGTILHA FYCVLHPRTQ QNCAGETNFK SLSLWDTPAS DCVSGSYNQE ATLGAFKVYF
     DLINCTFRYN YTITEDENAE WFGITQDTQG VHLYSSRKEN VFRNNMFHFA TLPVYQKILY
     YTVIPRSIRS PFNDRKAWAA FYIYKLHPLT YLLNFDVEGY ITKAVDCGYD DLAQLQCSYE
     SFEVETGVYS VSSFEASPRG EFIEQATTQE CDFTPMLTGT PPPIYNFKRL VFTNCNYNLT
     KLLSLFQVSE FSCHQVSPSS LATGCYSSLT VDYFAYSTDM SSYLQPGSAG AIVQFNYKQD
     FSNPTCRVLA TVPQNLTTIT KPSNYAYLTE CYKTSAYGKN YLYNAPGAYT PCLSLASRGF
     STKYQSHSDG ELTTTGYIYP VTGNLQMAFI ISVQYGTDTN SVCPMQALRN DTSIEDKLDV
     CVEYSLHGIT GRGVFHNCTS VGLRNQRFVY DTFDNLVGYH SDNGNYYCVR PCVSVPVSVI
     YDKASNSHAT LFGSVACSHV TTMMSQFSRM TKTNLLARTT PGPLQTTVGC AMGFINSSMV
     VDECQLPLGQ SLCAIPPTTS SRVRRATSGA SDVFQIATLN FTSPLTLAPI NSTGFVVAVP
     TNFTFGVTQE FIETTIQKIT VDCKQYVCNG FKKCEDLLKE YGQFCSKINQ ALHGANLRQD
     ESIANLFSSI KTQNTQPLQA GLNGDFNLTM LQIPQVTTGE RKYRSTIEDL LFNKVTIADP
     GYMQGYDECM QQGPQSARDL ICAQYVAGYK VLPPLYDPYM EAAYTSSLLG SIAGASWTAG
     LSSFAAIPFA QSIFYRLNGV GITQQVLSEN QKIIANKFNQ ALGAMQTGFT TTNLAFNKVQ
     DAVNANAMAL SKLAAELSNT FGAISSSISD ILARLDTVEQ EAQIDRLING RLTSLNAFVA
     QQLVRTEAAA RSAQLAQDKV NECVKSQSKR NGFCGTGTHI VSFAINAPNG LYFFHVGYQP
     TSHVNATAAY GLCNTENPQK CIAPIDGYFV LNQTTSTVAD SDQQWYYTGS SFFHPEPITE
     ANSKYVSMDV KFENLTNRLP PPLLSNSTDL DFKEELEEFF KNVSSQGPNF QEISKINTTL
     LNLNTELMVL SEVVKQLNES YIDLKELGNY TFYQKWPWYI WLGFIAGLVA LALCVFFILC
     CTGCGTSCLG KLKCNRCCDS YDEYEVEKIH VH
 
 
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