位置:首页 > 蛋白库 > GP_HANTL
GP_HANTL
ID   GP_HANTL                Reviewed;        1135 AA.
AC   P16853;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Envelopment polyprotein;
DE   AltName: Full=M polyprotein;
DE   Contains:
DE     RecName: Full=Glycoprotein N {ECO:0000250|UniProtKB:P08668};
DE              Short=Gn;
DE     AltName: Full=Glycoprotein G1;
DE   Contains:
DE     RecName: Full=Glycoprotein C {ECO:0000250|UniProtKB:P08668};
DE              Short=Gc;
DE     AltName: Full=Glycoprotein G2;
DE   Flags: Precursor;
GN   Name=GP;
OS   Hantaan virus (strain Lee) (Lee virus) (Korean hemorrhagic fever virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC   Orthohantavirus.
OX   NCBI_TaxID=11601;
OH   NCBI_TaxID=39030; Apodemus agrarius (Eurasian field mouse).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2900289; DOI=10.1099/0022-1317-69-8-1949;
RA   Schmaljohn C.S., Arikawa J., Hasty S.E., Rasmussen L., Lee H.W., Lee P.W.,
RA   Dalrymple J.M.;
RT   "Conservation of antigenic properties and sequences encoding the envelope
RT   proteins of prototype Hantaan virus and two virus isolates from Korean
RT   haemorrhagic fever patients.";
RL   J. Gen. Virol. 69:1949-1955(1988).
RN   [2]
RP   REVIEW.
RX   PubMed=24755564; DOI=10.3390/v6041801;
RA   Cifuentes-Munoz N., Salazar-Quiroz N., Tischler N.D.;
RT   "Hantavirus Gn and Gc envelope glycoproteins: key structural units for
RT   virus cell entry and virus assembly.";
RL   Viruses 6:1801-1822(2014).
CC   -!- FUNCTION: [Glycoprotein N]: Forms homotetramers with glycoprotein C at
CC       the surface of the virion (By similarity). Attaches the virion to host
CC       cell receptors including integrin ITGAV/ITGB3 (By similarity). This
CC       attachment induces virion internalization predominantly through
CC       clathrin-dependent endocytosis (By similarity). May also bind to host
CC       C1QBP for virus entry into the host cell (By similarity). Mediates the
CC       assembly and budding of infectious virus particles through its
CC       interaction with the nucleocapsid protein and the viral genome (By
CC       similarity). May dysregulate normal immune and endothelial cell
CC       responses through an ITAM motif (By similarity). Translocates to
CC       mitochondria, binds to host TUFM and recruits MAP1LC3B (By similarity).
CC       These interactions induce mitochondrial autophagy and therefore
CC       destruction of host MAVS leading to inhibition of type I interferon
CC       (IFN) responses (By similarity). Concomitant breakdown of glycoprotein
CC       N is apparently prevented by the nucleoprotein that may inhibit Gn-
CC       stimulated autophagosome-lysosome fusion (By similarity). Interacts
CC       with the viral genomic RNA (By similarity).
CC       {ECO:0000250|UniProtKB:P08668, ECO:0000250|UniProtKB:P27312}.
CC   -!- FUNCTION: [Glycoprotein C]: Forms homotetramers with glycoprotein N at
CC       the surface of the virion (By similarity). Attaches the virion to host
CC       cell receptors including integrin ITGAV/ITGB3 (By similarity). This
CC       attachment induces virion internalization predominantly through
CC       clathrin-dependent endocytosis (By similarity). May also bind to host
CC       C1QBP for virus entry into the host cell (By similarity). Class II
CC       fusion protein that promotes fusion of viral membrane with host
CC       endosomal membrane after endocytosis of the virion (By similarity).
CC       {ECO:0000250|UniProtKB:P08668}.
CC   -!- SUBUNIT: [Glycoprotein N]: Homodimer (By similarity). Homotetramer;
CC       forms heterotetrameric Gn-Gc spikes in the pre-fusion conformation (By
CC       similarity). Interacts (via C-terminus) with the nucleoprotein (By
CC       similarity). Interacts with host TUFM; this interaction contributes to
CC       the virus-induced degradation of mitochondria by autophagy, which leads
CC       to degradation of host MAVS and inhibition of type I interferon (IFN)
CC       responses (By similarity). Interacts with host MAP1LC3B; this
CC       interaction contributes to the virus-induced degradation of
CC       mitochondria by autophagy, which leads to degradation of host MAVS and
CC       inhibition of type I interferon (IFN) responses (By similarity).
CC       {ECO:0000250|UniProtKB:P08668, ECO:0000250|UniProtKB:P0DTJ1}.
CC   -!- SUBUNIT: [Glycoprotein C]: Homodimer. Homotetramer; forms
CC       heterotetrameric Gn-Gc spikes in the pre-fusion conformation.
CC       Homotrimer; forms homotrimer in the post-fusion conformation at acidic
CC       pH (By similarity). Interacts (via C-terminus) with the nucleoprotein
CC       (By similarity). {ECO:0000250|UniProtKB:P08668,
CC       ECO:0000250|UniProtKB:P27312}.
CC   -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane
CC       {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein. Host cell
CC       surface {ECO:0000250|UniProtKB:P08668}. Host Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P08668}. Host endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P08668}. Host mitochondrion
CC       {ECO:0000250|UniProtKB:P08668}. Note=Interaction between glycoprotein N
CC       and glycoprotein C is essential for proper targeting of glycoprotein N
CC       to the host Golgi complex, where virion budding occurs.
CC       {ECO:0000250|UniProtKB:P27312}.
CC   -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane
CC       {ECO:0000250|UniProtKB:P08668}; Single-pass type I membrane protein.
CC       Host cell surface {ECO:0000250|UniProtKB:P08668}. Host Golgi apparatus
CC       membrane {ECO:0000250|UniProtKB:P08668}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:P08668}. Host endoplasmic reticulum
CC       membrane {ECO:0000250|UniProtKB:P08668}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:P08668}. Note=Budding probably takes
CC       place at the host Golgi (Probable). Glycoprotein C cytoplasmic tail is
CC       important for efficient Golgi localization (By similarity).
CC       {ECO:0000250|UniProtKB:P08668, ECO:0000305}.
CC   -!- DOMAIN: [Glycoprotein N]: The YxxL motif at the C-terminus is
CC       indispensable for the interaction with MAP1LC3B and for the Gn-mediated
CC       induction of mitochondrial autophagy (By similarity). The cytoplasmic
CC       tail is involved in the inhibition of the host innate immune response
CC       (By similarity). The C-terminus of the cytoplasmic tail is involved in
CC       binding to the viral genome and the nucleocapsid (By similarity).
CC       Contains 2 contiguous zinc-fingers (By similarity).
CC       {ECO:0000250|UniProtKB:P08668, ECO:0000250|UniProtKB:P0DTJ1,
CC       ECO:0000250|UniProtKB:P27312, ECO:0000250|UniProtKB:Q9E006}.
CC   -!- DOMAIN: [Glycoprotein C]: The C-terminus is necessary for proper
CC       localization in the Golgi (By similarity). The cytoplasmic tail is
CC       involved in binding to the nucleocapsid (By similarity).
CC       {ECO:0000250|UniProtKB:P27312}.
CC   -!- PTM: [Envelopment polyprotein]: Envelope polyprotein precursor is
CC       quickly cleaved in vivo just after synthesis, presumably by host signal
CC       peptidase. {ECO:0000250|UniProtKB:P08668}.
CC   -!- SIMILARITY: Belongs to the hantavirus envelope glycoprotein family.
CC       {ECO:0000305}.
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; D00377; BAA00280.1; -; Genomic_RNA.
DR   PIR; JS0605; JS0605.
DR   SMR; P16853; -.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0039547; P:suppression by virus of host TRAF activity; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR016402; Envelope_glycoprot_Hantavirus.
DR   InterPro; IPR002532; Hanta_Gc.
DR   InterPro; IPR002534; Hanta_Gn.
DR   InterPro; IPR012316; ITAM_motif_hantavir-typ.
DR   Pfam; PF01567; Hanta_G1; 1.
DR   Pfam; PF01561; Hanta_G2; 1.
DR   Pfam; PF10538; ITAM_Cys-rich; 1.
DR   PIRSF; PIRSF003945; M_poly_HantaV; 1.
DR   PROSITE; PS51056; ITAM_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein;
KW   Host endoplasmic reticulum; Host Golgi apparatus; Host membrane;
KW   Host mitochondrion; Host-virus interaction;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host RLR pathway by virus; Inhibition of host TRAFs by virus;
KW   Membrane; Metal-binding; Phosphoprotein; Repeat; Signal; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW   Viral immunoevasion; Viral penetration into host cytoplasm; Virion;
KW   Virus endocytosis by host; Virus entry into host cell; Zinc; Zinc-finger.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..1135
FT                   /note="Envelopment polyprotein"
FT                   /id="PRO_0000036812"
FT   CHAIN           19..648
FT                   /note="Glycoprotein N"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036813"
FT   CHAIN           649..1135
FT                   /note="Glycoprotein C"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036814"
FT   TOPO_DOM        19..485
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        486..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        507..627
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        628..648
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        649..1105
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1106..1126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1127..1135
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          611..634
FT                   /note="ITAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT   ZN_FING         545..565
FT                   /note="CCHC-type 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   ZN_FING         570..591
FT                   /note="CCHC-type 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   REGION          516..533
FT                   /note="Binding to the ribonucleoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   REGION          588..605
FT                   /note="Binding to the ribonucleoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:P27312"
FT   REGION          592..603
FT                   /note="Binding to the ribonucleoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   REGION          611..625
FT                   /note="Binding to the ribonucleoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:P27312"
FT   REGION          757..777
FT                   /note="Fusion loop"
FT                   /evidence="ECO:0000250|UniProtKB:P41266"
FT   REGION          1122..1135
FT                   /note="Binding to the ribonucleoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:P27312"
FT   MOTIF           615..618
FT                   /note="YxxL"
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   SITE            648..649
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        399
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        928
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        29..151
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        63..157
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        109..128
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        133..138
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        175..185
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        210..247
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        234..351
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        376..435
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        380..389
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        405..424
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        452..475
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        735..770
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        739..777
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        751..885
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        765..896
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        780..904
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        806..815
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        823..832
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        863..867
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        970..1000
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        993..1045
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        1010..1015
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        1046..1051
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        1085..1089
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
SQ   SEQUENCE   1135 AA;  126470 MW;  B9C759ED6592265A CRC64;
     MGIWKWLVMA SLVWPVLTLR NVYDMKIECP HTVSFGENSV IGYVELPPMP LADTAQLVPE
     SSCSMDNHQS LNTITKYTQV SWRGKADQSQ SSQTSFETVS TEVDLKGTCV LKHKMVEESY
     RSRKSITCYD LSCNSTYCKP TLYMIVPIHA CNMMKSCLIA LGPYRVQVVY ERTYCMTGVL
     IEGKCFVPDQ SVVSIIKHGI FDIASVHIVC FFVAVKGNTY KIFEQVKKSF ESTCNDTENK
     VQGYYICIVG GNSAPIYVPT LDDFRSMEAF TGIFRSPHGE DHDLAGEETA TYSIVGPANA
     KVPHSASSDT LSLIAFSGIP SDSSLSILTS STEAKHVFSP GLFPKLNHTN CDKGAIPLMW
     TGMIDLPGYY EAIHPCTVFC VLSGPGASCE AFSEGGIFNI TYPMCLVSKQ NRFRLTEQQV
     NFVCQRVDVD IVVYCNGQRK VILTKTLVIG QCIYTITSLF SLLPGVAHSI AVELCVPGFH
     GWATAALLVT FCFGWVLIPA ITFIILTILK FIANIFHTSN QENRLKSVLR KIKEEFEKTK
     GSMVCDVCKY ECETYKELKA HGVSCPQSQC PYCFTHCEPT EAAFQAHYKV CQVTHRFRDD
     LKKTVTPQNF TPGCYRTLNL FRYKSRCYIF TMWIFLLVLE SILWAASASE TPLTPVWNDN
     AHGVGSVPMH TDLELDFSLT SSSKYTYRRK LTNPLEEAQS IDLHIEIEEQ TIGVDVHALG
     HWFDGRLNLK TSFHCYGACT KYEYPWHTAK CHYERDYQYE TSWGCNPSDC PGVGTGCTAC
     GLYLDRLKPV GSAYKIITIR YSRRVCVQFG EENLCKIIDM NDCFVSRHVK VCIIGTVSKF
     SQGDTLLFFG PLEGGGLIFK HWCTSTCQFG DPGDIMSPRD KGFLCPEFPG SFRKKCNFAT
     TPICEYDGNM VSGYKKVMAT IDSFQSFNTS TMHFTDERIE WKDPDGMLRD HINILVTKDI
     DFDNLGENPC KIGLQTSSIE GAWGSGVGFT LTCLVSLTEC PTFLTSIKAC DKAICYGAES
     VTLTRGQNTV KVSGKGGHSG STFKCCHGED CSQIGLHAAA PHLDKVNGIS EMENSKEYDD
     GAPQCGIKCW FVKSGEWISG IFSGNWIVLI VLCVFLLFSL VLLSILCPVR KHKKS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024