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SPIKE_CVM4
ID   SPIKE_CVM4              Reviewed;        1376 AA.
AC   P22432;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=3;
OS   Murine coronavirus (strain 4) (MHV-4) (Murine hepatitis virus).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Embecovirus.
OX   NCBI_TaxID=12760;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2556846; DOI=10.1016/0042-6822(89)90579-5;
RA   Parker S.E., Gallagher T.M., Buchmeier M.J.;
RT   "Sequence analysis reveals extensive polymorphism and evidence of deletions
RT   within the E2 glycoprotein gene of several strains of murine hepatitis
RT   virus.";
RL   Virology 173:664-673(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1966429; DOI=10.1007/978-1-4684-5823-7_54;
RA   Parker S.E., Buchmeier M.J.;
RT   "RNA sequence analysis of the E2 genes of wildtype and neuroattenuated
RT   mutants of MHV-4 reveals a hypervariable domain.";
RL   Adv. Exp. Med. Biol. 276:395-402(1990).
RN   [3]
RP   FUNCTION.
RX   PubMed=9201212; DOI=10.1006/viro.1997.8609;
RA   Nash T.C., Buchmeier M.J.;
RT   "Entry of mouse hepatitis virus into cells by endosomal and nonendosomal
RT   pathways.";
RL   Virology 233:1-8(1997).
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       ECO:0000269|PubMed:9201212}.
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   -!- MISCELLANEOUS: The viral fusion process requires lipid rafts of the
CC       host plasma membrane (By similarity). This strain is apparently capable
CC       of entering cells either through direct fusion at the cell surface or
CC       through endocytosis. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04099}.
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DR   EMBL; M32789; AAA46456.1; -; Genomic_RNA.
DR   EMBL; S51114; AAB19590.1; -; Genomic_RNA.
DR   PIR; A33748; VGIHJ2.
DR   SMR; P22432; -.
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; cd21625; MHV-like_Spike_S1_NTD; 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; IPR044339; Spike_S1_NTD_MHV-like.
DR   InterPro; IPR018548; Spike_S1_RBD_bCoV.
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   3: Inferred from homology;
KW   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; Signal; Transmembrane; Transmembrane helix;
KW   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..13
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CHAIN           14..1376
FT                   /note="Spike glycoprotein"
FT                   /id="PRO_0000037211"
FT   CHAIN           14..769
FT                   /note="Spike protein S1"
FT                   /id="PRO_0000037212"
FT   CHAIN           770..1376
FT                   /note="Spike protein S2"
FT                   /id="PRO_0000037213"
FT   CHAIN           922..1376
FT                   /note="Spike protein S2'"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT                   /id="PRO_0000444083"
FT   TOPO_DOM        14..1317
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   TRANSMEM        1318..1338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   TOPO_DOM        1339..1376
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   DOMAIN          15..296
FT                   /note="BetaCoV S1-NTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DOMAIN          327..618
FT                   /note="BetaCoV S1-CTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT   REGION          15..330
FT                   /note="Receptor binding site"
FT   REGION          429..599
FT                   /note="Important for the neurovirulence"
FT   REGION          922..943
FT                   /note="Fusion peptide 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   REGION          941..961
FT                   /note="Fusion peptide 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   REGION          1022..1072
FT                   /note="Heptad repeat 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   REGION          1266..1306
FT                   /note="Heptad repeat 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   COILED          1051..1095
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   COILED          1279..1307
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   MOTIF           1372..1376
FT                   /note="KxHxx"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   SITE            769..770
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000250"
FT   SITE            921..922
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        582
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        677
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        709
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        717
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        740
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        789
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        806
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        945
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1232
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        1261
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1277
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1298
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   DISULFID        21..158
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DISULFID        153..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DISULFID        165..246
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DISULFID        284..294
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DISULFID        329..354
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT   DISULFID        372..425
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT   DISULFID        384..616
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT   DISULFID        946..957
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
SQ   SEQUENCE   1376 AA;  151882 MW;  88C01B97B252094E CRC64;
     MLFVFILLLP SCLGYIGDFR CIQTVNYNGN NASAPSISTE AVDVSKGLGT YYVLDRVYLN
     ATLLLTGYYP VDGSNYRNLA LTGTNTLSLT WFKPPFLSEF NDGIFAKVQN LKTNTPTGAT
     SYFPTIVIGS LFGNTSYTVV LEPYNNIIMA SVCTYTICQL PYTPCKPNTN GNRVIGFWHT
     DVKPPICLLK RNFTFNVNAP WLYFHFYQQG GTFYAYYADK PSATTFLFSV YIGDILTQYF
     VLPFICTPTA GSTLLPLYWV TPLLKRQYLF NFNEKGVITS AVDCASSYIS EIKCKTQSLL
     PSTGVYDLSG YTVQPVGVVY RRVPNLPDCK IEEWLTAKSV PSPLNWERRT FQNCNFNLSS
     LLRYVQAESL SCNNIDASKV YGMCFGSVSV DKFAIPRSRQ IDLQIGNSGF LQTANYKIDT
     AATSCQLYYS LPKNNVTINN YNPSSWNRRY GFNDAGVFGK SKHDVAYAQQ CFTVRPSYCP
     CAQPDIVSAC TSQTKPMSAY CPTGTIHREC SLWNGPHLRS ARVGSGTYTC ECTCKPNPFD
     TYDLRCGQIK TIVNVGDHCE GLGVLEDKCG NSDPHKGCSC ANDSFIGWSH DTCLVNDRCQ
     IFANILLNGI NSGTTCSTDL QLPNTEVATG VCVRYDLYGI TGQGVFKEVK ADYYNSWQAL
     LYDVNGNLNG FRDLTTNKTY TIRSCYSGRV SAAYHKEAPE PALLYRNINC SYVFTNNISR
     EENPLNYFDS YLGCVVNADN RTDEALPNCD LRMGAGLCVD YSKSRRARRS VSTGYRLTTF
     EPYMPMLVND SVQSVGGLYE MQIPTNFTIG HHEEFIQIRA PKVTIDCAAF VCGDNAACRQ
     QLVEYGSFCD NVNAILNEVN NLLDNMQLQV ASALMQGVTI SSRLPDGISG PIDDINFSPL
     LGCIGSTCAE DGNGPSAIRG RSAIEDLLFD KVKLSDVGFV EAYNNCTGGQ EVRDLLCVQS
     FNGIKVLPPV LSESQISGYT AGATAAAMFP PWTAAAGVPF SLNVQYRING LGVTMNVLSE
     NQKMIASAFN NALGAIQEGF DATNSALGKI QSVVNANAEA LNNLLNQLSN RFGAISASLQ
     EILTRLDAVE AKAQIDRLIN GRLTALNAYI SKQLSDSTLI KFSAAQAIEK VNECVKSQTT
     RINFCGNGNH ILSLVQNAPY GLCFIHFSYV PTSFKTANVS PGLCISGDRG LAPKAGYFVQ
     DNGEWKFTGS NYYYPEPITD KNSVVMISCA VNYTKAPEVF LNNSIPNLPD FKEELDKWFK
     NQTSIAPDLS LDFEKLNVTF LDLTYEMNRI QDAIKKLNES YINLKEVGTY EMYVKWPWYV
     WLLIGLAGVA VCVLLFFICC CTGCGSCCFR KCGSCCDEYG GHQDSIVIHN ISAHED
 
 
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