GP_SFTS
ID GP_SFTS Reviewed; 1073 AA.
AC R4V2Q5; W8GRF8;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Envelopment polyprotein;
DE AltName: Full=M polyprotein;
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;
OS Dabie bandavirus (Severe fever with thrombocytopenia virus) (Huaiyangshan
OS banyangvirus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Phenuiviridae; Bandavirus; Dabie bandavirus.
OX NCBI_TaxID=1003835;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JS2012-tick01 {ECO:0000312|EMBL:AGM33042.1,
RC ECO:0000312|Proteomes:UP000246754};
RA Wu T., Guo X., Chen Y., Zhao K., Ge Y., Peng H., Cui L., Jiao Y., Shi Z.,
RA Tang F., Zhou M.;
RT "Biological and genetic characterization of SFTSV isolated from
RT Haemaphysalis longicornis tick in Jiangsu, China.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LN2012-58 {ECO:0000312|EMBL:AHK23653.1};
RA Zhang J., Yao W., Liu Y., Wang Z., Sun T., Tian J., Mao L., Sun Y., Li X.,
RA Wu W., Qi S., Li J., Liang M., Zhao Z.;
RT "SFTS virus M segment, complete genome.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION (GLYCOPROTEIN N), AND FUNCTION (GLYCOPROTEIN C).
RX PubMed=23388721; DOI=10.1128/jvi.02628-12;
RA Hofmann H., Li X., Zhang X., Liu W., Kuehl A., Kaup F., Soldan S.S.,
RA Gonzalez-Scarano F., Weber F., He Y., Poehlmann S.;
RT "Severe fever with thrombocytopenia virus glycoproteins are targeted by
RT neutralizing antibodies and can use DC-SIGN as a receptor for pH-dependent
RT entry into human and animal cell lines.";
RL J. Virol. 87:4384-4394(2013).
RN [4] {ECO:0007744|PDB:5G47}
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 563-996, GLYCOSYLATION AT
RP ASN-853; ASN-914 AND ASN-936, SUBUNIT (GLYCOPROTEIN C), AND DISULFIDE
RP BONDS.
RX PubMed=27325770; DOI=10.1073/pnas.1603827113;
RA Halldorsson S., Behrens A.J., Harlos K., Huiskonen J.T., Elliott R.M.,
RA Crispin M., Brennan B., Bowden T.A.;
RT "Structure of a phleboviral envelope glycoprotein reveals a consolidated
RT model of membrane fusion.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:7154-7159(2016).
RN [5] {ECO:0007744|PDB:5Y10, ECO:0007744|PDB:5Y11}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 20-340, DISULFIDE BONDS, AND
RP SUBUNIT.
RX PubMed=28827346; DOI=10.1073/pnas.1705176114;
RA Wu Y., Zhu Y., Gao F., Jiao Y., Oladejo B.O., Chai Y., Bi Y., Lu S.,
RA Dong M., Zhang C., Huang G., Wong G., Li N., Zhang Y., Li Y., Feng W.H.,
RA Shi Y., Liang M., Zhang R., Qi J., Gao G.F.;
RT "Structures of phlebovirus glycoprotein Gn and identification of a
RT neutralizing antibody epitope.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E7564-E7573(2017).
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 clathrin-
CC mediated endocytosis of the virion (PubMed:23388721). Plays a role in
CC the packaging of ribonucleoproteins during virus assembly (By
CC similarity). {ECO:0000250|UniProtKB:P09613,
CC ECO:0000250|UniProtKB:P21401, ECO:0000269|PubMed:23388721}.
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 (By similarity). The glycoprotein
CC protrusions are arranged on an icosahedral lattice, with T=12
CC triangulation (By similarity). They are able to attach the virion to
CC the host cell receptor CD209/DC-SIGN and to promote fusion of membranes
CC with the late endosome after clathrin-mediated endocytosis of the
CC virion (PubMed:23388721). {ECO:0000250|UniProtKB:P09613,
CC ECO:0000250|UniProtKB:P21401, ECO:0000269|PubMed:23388721}.
CC -!- SUBUNIT: [Glycoprotein N]: Homodimer. Heterodimer with glycoprotein C
CC (By similarity). Homotrimer (postfusion) (PubMed:27325770).
CC {ECO:0000250|UniProtKB:P09613, ECO:0000269|PubMed:27325770}.
CC -!- SUBUNIT: [Glycoprotein C]: Heterodimer with glycoprotein N.
CC {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}. 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 -!- 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 glycoprotein C and glycoprotein N.
CC {ECO:0000250|UniProtKB:P09613}.
CC -!- PTM: [Glycoprotein N]: The cytoplasmic tail is Palmitoylated.
CC {ECO:0000250|UniProtKB:P09613}.
CC -!- PTM: [Glycoprotein N]: Glycosylated. {ECO:0000250|UniProtKB:P09613}.
CC -!- PTM: [Glycoprotein C]: Palmitoylated. {ECO:0000250|UniProtKB:P09613}.
CC -!- PTM: [Glycoprotein C]: Glycosylated. {ECO:0000250|UniProtKB:P09613}.
CC -!- SIMILARITY: Belongs to the phlebovirus 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; KC473541; AGM33042.1; -; Viral_cRNA.
DR EMBL; KF887440; AHK23653.1; -; Genomic_RNA.
DR PDB; 5G47; X-ray; 2.45 A; A/B/C=563-996.
DR PDB; 5Y10; X-ray; 2.60 A; C=20-340.
DR PDB; 5Y11; X-ray; 2.10 A; C=20-340.
DR PDBsum; 5G47; -.
DR PDBsum; 5Y10; -.
DR PDBsum; 5Y11; -.
DR SMR; R4V2Q5; -.
DR Proteomes; UP000108766; Genome.
DR Proteomes; UP000246754; Genome.
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; IPR043603; Phlebo_G2_C.
DR InterPro; IPR010826; Phlebovirus_G1.
DR InterPro; IPR009878; Phlebovirus_G2_fusion.
DR Pfam; PF19019; Phlebo_G2_C; 1.
DR Pfam; PF07243; Phlebovirus_G1; 1.
DR Pfam; PF07245; Phlebovirus_G2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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; Lipoprotein; Membrane; Palmitate; Signal;
KW Transmembrane; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1073
FT /note="Envelopment polyprotein"
FT /id="PRO_0000455557"
FT CHAIN 20..562
FT /note="Glycoprotein N"
FT /id="PRO_0000455558"
FT CHAIN 563..1073
FT /note="Glycoprotein C"
FT /id="PRO_0000455559"
FT TOPO_DOM 20..453
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..535
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT TOPO_DOM 563..1036
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1037..1057
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1058..1073
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT REGION 475..521
FT /note="Golgi retention signal"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT REGION 536..562
FT /note="Internal signal sequence for glycoprotein C"
FT /evidence="ECO:0000250|UniProtKB:A0A0B5A886"
FT REGION 650..656
FT /note="Fusion loop"
FT /evidence="ECO:0000269|PubMed:27325770"
FT REGION 691..705
FT /note="Fusion loop"
FT /evidence="ECO:0000269|PubMed:27325770"
FT SITE 562..563
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:A0A0B5A886"
FT SITE 1071
FT /note="Important for glycoprotein C and glycoprotein N
FT subcellular location"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 853
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27325770"
FT CARBOHYD 914
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27325770"
FT CARBOHYD 936
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27325770"
FT DISULFID 26..49
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 143..156
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 180..327
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 206..216
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 258..305
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 266..303
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 274..280
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 287..292
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 349..352
FT /evidence="ECO:0000303|PubMed:28827346"
FT DISULFID 356..424
FT /evidence="ECO:0000303|PubMed:28827346"
FT DISULFID 376..381
FT /evidence="ECO:0000303|PubMed:28827346"
FT DISULFID 563..604
FT /evidence="ECO:0000269|PubMed:27325770"
FT DISULFID 576..586
FT /evidence="ECO:0000269|PubMed:27325770"
FT DISULFID 629..725
FT /evidence="ECO:0000269|PubMed:27325770"
FT DISULFID 644..841
FT /evidence="ECO:0000269|PubMed:27325770"
FT DISULFID 650..698
FT /evidence="ECO:0000269|PubMed:27325770"
FT DISULFID 656..705
FT /evidence="ECO:0000269|PubMed:27325770"
FT DISULFID 660..687
FT /evidence="ECO:0000269|PubMed:27325770"
FT DISULFID 691..696
FT /evidence="ECO:0000269|PubMed:27325770"
FT DISULFID 778..793
FT /evidence="ECO:0000269|PubMed:27325770"
FT DISULFID 809..823
FT /evidence="ECO:0000269|PubMed:27325770"
FT DISULFID 908..978
FT /evidence="ECO:0000269|PubMed:27325770"
FT DISULFID 918..921
FT /evidence="ECO:0000269|PubMed:27325770"
FT DISULFID 943..974
FT /evidence="ECO:0000269|PubMed:27325770"
FT VARIANT 343..346
FT /note="EQRL -> VQRI (in strain: LN2012-58)"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 491
FT /note="M -> I (in strain: LN2012-58)"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 507
FT /note="R -> G (in strain: LN2012-58)"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 556..557
FT /note="AI -> VM (in strain: LN2012-58)"
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 1073 AA; 116935 MW; F9E7A015B2C4A2B3 CRC64;
MMKVIWFSSL ICFVIQCSGD SGPIICAGPI HSNKSADIPH LLGYSEKICQ IDRLIHVSSW
LRNHSQFQGY VGQRGGRSQV SYYPAENSYS RWSGLLSPCD ADWLGMLVVK KAKGSDMIVP
GPSYKGKVFF ERPTFDGYVG WGCGSGKSRT ESGELCSSDS GTSSGLLPSD RVLWIGDVAC
QPMTPIPEET FLELKSFSQS EFPDICKIDG IVFNQCEGES LPQPFDVAWM DVGHSHKIIM
REHKTKWVQE SSSKDFVCYK EGTGPCSESE EKTCKTSGSC RGDMQFCKVA GCEHGEEASE
AKCRCSLVHK PGEVVVSYGG MRVRPKCYGF SRMMATLEVN QPEQRLGQCT GCHLECINGG
VRLITLTSEL KSATVCASHF CSSATSGKKS TEIQFHSGSL VGKTAIHVKG ALVDGTEFTF
EGSCMFPDGC DAVDCTFCRE FLKNPQCYPA KKWLFIIIVI LLGYAGLMLL TNVLKAIGIW
GSWVIAPVKL MFAIIKKLMR TVSCLMRKLM DRGRQVIHEE IGENREGNQD DVRIEMARPR
RVRHWMYSPV ILTILAIGLA ESCDEMVHAD SKLVSCRQGS GNMKECVTTG RALLPAVNPG
QEACLHFTAP GSPDSKCLKI KVKRINLKCK KSSSYFVPDA RSRCTSVRRC RWAGDCQSGC
PPHFTSNSFS DDWAGKMDRA GLGFSGCSDG CGGAACGCFN AAPSCIFWRK WVENPHGIIW
KVSPCAAWVP SAVIELTMPS GEVRTFHPMS GIPTQVFKGV SVTYLGSDME VSGLTDLCEI
EELKSKKLAL APCNQAGMGV VGKVGEIQCS SEESARTIKK DGCIWNADLV GIELRVDDAV
CYSKITSVEA VANYSAIPTT IGGLRFERSH DSQGKISGSP LDITAIRGSF SVNYRGLRLS
LSEITATCTG EVTNVSGCYS CMTGAKVSIK LHSSKNSTAH VRCKGDETAF SVLEGVHSYT
VSLSFDHAVV DEQCQLNCGG HESQVTLKGN LIFLDVPKFV DGSYMQTYHS TVPTGANIPS
PTDWLNALFG NGLSRWILGV IGVLLGGLAL FFMIMSLFKL GTKQVFRSRT KLA
