GP_PTPV
ID GP_PTPV Reviewed; 1313 AA.
AC P03517;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Envelopment polyprotein;
DE AltName: Full=M polyprotein;
DE Contains:
DE RecName: Full=NSm-Gn protein {ECO:0000250|UniProtKB:P21401};
DE Contains:
DE RecName: Full=Glycoprotein N {ECO:0000250|UniProtKB:P21401};
DE Short=Gn;
DE AltName: Full=Glycoprotein G1;
DE Contains:
DE RecName: Full=Glycoprotein C {ECO:0000250|UniProtKB:P21401};
DE Short=Gc;
DE AltName: Full=Glycoprotein G2;
DE Flags: Precursor;
GN Name=GP;
OS Punta toro phlebovirus.
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Phenuiviridae; Phlebovirus.
OX NCBI_TaxID=11587;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=29031; Phlebotomus papatasi (Sandfly).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2998043; DOI=10.1016/0042-6822(85)90321-6;
RA Ihara T., Smith J., Dalrymple J.M., Bishop D.H.L.;
RT "Complete sequences of the glycoproteins and M RNA of Punta Toro
RT phlebovirus compared to those of Rift Valley fever virus.";
RL Virology 144:246-259(1985).
RN [2]
RP FUNCTION (GLYCOPROTEIN N), AND FUNCTION (GLYCOPROTEIN C).
RX PubMed=21767814; DOI=10.1016/j.chom.2011.06.007;
RA Lozach P.Y., Kuehbacher A., Meier R., Mancini R., Bitto D., Bouloy M.,
RA Helenius A.;
RT "DC-SIGN as a receptor for phleboviruses.";
RL Cell Host Microbe 10:75-88(2011).
CC -!- FUNCTION: [Glycoprotein N]: Structural component of the virion that
CC interacts with glycoprotein C (By similarity). It shields the
CC hydrophobic fusion loops of the glycoprotein C, preventing premature
CC fusion (By similarity). The glycoprotein protrusions are arranged on an
CC icosahedral lattice, with T=12 triangulation (By similarity). They are
CC able to attach the virion to the host cell receptor CD209/DC-SIGN and
CC to promote fusion of membranes with the late endosome after endocytosis
CC of the virion (PubMed:21767814). Plays a role in the packaging of
CC ribonucleoproteins and polymerase during virus assembly (By
CC similarity). {ECO:0000250|UniProtKB:P03518,
CC ECO:0000250|UniProtKB:P09613, ECO:0000250|UniProtKB:P21401,
CC ECO:0000269|PubMed:21767814}.
CC -!- FUNCTION: [Glycoprotein C]: Structural component of the virion that
CC interacts with glycoprotein N (By similarity). Acts as a class II
CC fusion protein that is activated upon acidification and subsequent
CC repositioning of the glycoprotein N. The glycoprotein protrusions are
CC arranged on an icosahedral lattice, with T=12 triangulation (By
CC similarity). They are able to attach the virion to the host cell
CC receptor CD209/DC-SIGN and to promote fusion of membranes with the late
CC endosome after endocytosis of the virion (PubMed:21767814).
CC {ECO:0000250|UniProtKB:P03518, ECO:0000250|UniProtKB:P09613,
CC ECO:0000269|PubMed:21767814}.
CC -!- FUNCTION: [NSm-Gn protein]: Plays a role for virus dissemination in
CC mosquitoes. {ECO:0000250|UniProtKB:P21401}.
CC -!- SUBUNIT: [Glycoprotein N]: Heterodimer with glycoprotein C (By
CC similarity). Interacts with nucleocapsid protein N and with the
CC polymerase L in order to package them into virus particles (By
CC similarity). {ECO:0000250|UniProtKB:P03518,
CC ECO:0000250|UniProtKB:P21401}.
CC -!- SUBUNIT: [Glycoprotein C]: Heterodimer with glycoprotein C. Homotrimer
CC (postfusion) (By similarity). Interacts with nucleocapsid protein N and
CC with the polymerase L in order to package them into virus particles.
CC Interacts with host E3 ubiquitin-protein ligase UBR4; this interaction
CC is important for viral RNA production (By similarity).
CC {ECO:0000250|UniProtKB:P03518, ECO:0000250|UniProtKB:P09613}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane
CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Note=Interaction between Glycoprotein N
CC and Glycoprotein C is essential for proper targeting of Glycoprotein C
CC to the Golgi complex, where virion budding occurs.
CC {ECO:0000250|UniProtKB:P09613}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane
CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Note=Interaction between Glycoprotein N
CC and Glycoprotein C is essential for proper targeting of Glycoprotein C
CC to the Golgi complex, where virion budding occurs.
CC {ECO:0000250|UniProtKB:P09613}.
CC -!- DOMAIN: [Glycoprotein N]: Contains a Golgi retention signal on its C-
CC terminus. The cytoplasmic tail specifically interacts with the
CC ribonucleoproteins and is critical for genome packaging.
CC {ECO:0000250|UniProtKB:P09613}.
CC -!- PTM: [Envelopment polyprotein]: Specific enzymatic cleavages in vivo
CC yield mature proteins including NSm protein, Glycoprotein C, and
CC Glycoprotein N. {ECO:0000250|UniProtKB:P21401}.
CC -!- PTM: [Glycoprotein N]: Glycosylated. The glycans can attach to host
CC CD209/DC-SIGN, and may play a role in virus entry into dendritic cells.
CC {ECO:0000250|UniProtKB:P21401}.
CC -!- PTM: [Glycoprotein C]: Glycosylated. The glycans can attach to host
CC CD209/DC-SIGN, and may play a role in virus entry into dendritic cells.
CC {ECO:0000250|UniProtKB:P21401}.
CC -!- PTM: [Glycoprotein C]: Palmitoylated. {ECO:0000250|UniProtKB:P09613}.
CC -!- SIMILARITY: Belongs to the phlebovirus envelope glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; M11156; AAA47110.1; -; Genomic_RNA.
DR PIR; A04109; VGVUPT.
DR SMR; P03517; -.
DR PRIDE; P03517; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR InterPro; IPR016404; M_polyprot_prcur_phlebovir.
DR InterPro; IPR043603; Phlebo_G2_C.
DR InterPro; IPR010826; Phlebovirus_G1.
DR InterPro; IPR009878; Phlebovirus_G2_fusion.
DR InterPro; IPR009879; Phlebovirus_NSM.
DR Pfam; PF19019; Phlebo_G2_C; 1.
DR Pfam; PF07243; Phlebovirus_G1; 1.
DR Pfam; PF07245; Phlebovirus_G2; 1.
DR Pfam; PF07246; Phlebovirus_NSM; 1.
DR PIRSF; PIRSF003961; M_poly_PhleboV; 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 endoplasmic reticulum; Host Golgi apparatus; Host membrane;
KW Host-virus interaction; Membrane; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell;
KW Viral attachment to host entry receptor;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1313
FT /note="Envelopment polyprotein"
FT /id="PRO_0000247008"
FT CHAIN 18..270
FT /note="NSm-Gn protein"
FT /id="PRO_0000036844"
FT CHAIN 271..809
FT /note="Glycoprotein N"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036845"
FT CHAIN 810..1313
FT /note="Glycoprotein C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036846"
FT TOPO_DOM 18..712
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 713..733
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 734..791
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT TOPO_DOM 810..1278
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1279..1299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1300..1313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 250..270
FT /note="Internal signal sequence for glycoprotein N"
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT REGION 731..773
FT /note="Golgi retention signal"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT REGION 769..773
FT /note="Important for correct targeting of the glycoproteins
FT to the Golgi complex but not for heterodimerization"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT REGION 793..809
FT /note="Internal signal sequence for glycoprotein C"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT REGION 896..902
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT REGION 938..949
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT COILED 178..237
FT /evidence="ECO:0000255"
FT SITE 271..272
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT SITE 809..810
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT SITE 1311
FT /note="Important for glycoprotein C and glycoprotein N
FT subcellular location"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1154
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT CARBOHYD 1243
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 303..312
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 352..362
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 373..404
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 394..407
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 432..579
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 450..460
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 501..557
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 525..536
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 543..548
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 602..605
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 609..679
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 629..634
FT /evidence="ECO:0000250|UniProtKB:P03518"
FT DISULFID 810..850
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 823..832
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 875..971
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 890..1084
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 896..944
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 902..951
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 907..933
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 937..942
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 1053..1066
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 1148..1220
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 1158..1161
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 1168..1202
FT /evidence="ECO:0000250|UniProtKB:P21401"
SQ SEQUENCE 1313 AA; 146375 MW; 72072F27735A74A2 CRC64;
MIFTILNVLT RAMLVMSMYS LTTWDSTSRN DMCFSNDSPL EGLVYYWETH SKRHDYKKQE
SQRCRVGDSD KKMITNVTII SLISEIQKSI SELSLSCVND DNSTGQVLTF NGLEDTIRGD
YIVDCVTGLY QSDIGVGVGL GRTHHGHQQM KNKAVVIDEK ERMISLLETQ QSENDIKMQV
LMSEIEQLKN QLSKKRNERG QEKRDAEKVM SDLMARNSDL RKHNDILTAE ISQMKNKNTI
QRNKNTVSTT VVPAILSVAL LSSSVAPIIA APPDSPMINP WPHAKNRVGT GMYKYDENDD
SGCRPIRYGV SCIGFDFMLK MDKYPFFNAF IGHKTPLESF ADKIIEKEEE TCEIGTNKEF
KCFEERAYIK GTCPTNINAV HYIDNKGKLR YVKCKENLEM TEDCAFCRKI KKKAGQSVQV
QKTSVPLQDA ICQENSDTYS GPKIPFKGVC KIGLIKYKEC KFKTSSYETV SFITLKEKGK
IYIEHLMLKN IEVVTNVSFV CYEHVGQDEQ EVEHRALKRV SVNDCKIVDN SKQKICTGDH
VFCEKYDCST SYPDVTCIHA PGSGPLYINL MGSWIKPQCV GYERVLVDRE VKQPLLAPEQ
NCDTCVSECL DEGVHIKSTG FEITSAVACS HGSCISAHQE PSTSVIVPYP GLLASVGGRI
GIHLSHTSDS ASVHMVVVCP PRDSCAAHNC LLCYHGILNY QCHSTLSAIL TSFLLILFIY
TVFSVTTNIL YVLRLIPKQL KSPVGWLKLF INWLLTALRI KTRNVMRRIN QRIGWVDHHD
VERPRHREPM RRFKTTLLLT LIMMTGGNAC SNTVVANSKQ TRCVQEGSNT KCSITATITL
RAGVIGAESC FIIKGPMENQ QKTISIKTIS SETVCREGSS FWTSLYIPSC LSSRRCHLVG
DCVGNKCQSW RDDQLSREFS GVKDNHIMNE NKCFEQCGAI GCGCFNINPS CLYVHAYLKS
ARNEAVRVFS CSDWVHRVSF EVKGPDGETE LVTLGSPGTK FLNWGTLSLS LDAEGISGTN
SISFLESSKG GFALYDEGYN EIPREGFLGE IRCSSESAAI SAHKSCIRAP GLIKYKPMTD
QIECTASLVD PFAIFLKGSL PQTRNGQTFT STKDKKTVQA FTNGAIKALL SINLDDHEIV
FINKVKNCDA TFLNVSGCYS CDYGAHVCVK VKSSESADFF AESEDKTTVL SFPIQSGTHD
YCQVLHFQKP LVDERLSYSC GSEPKLIVIK GTLVCMGVYD FRNKTGGSST VVNPSEGAWS
ISNWFSGLLD WLGGPMKAIL KILGFIAIGI VCFVLFMILI RIAVNSINIK KKN
