GP_SFTSV
ID GP_SFTSV Reviewed; 1073 AA.
AC A0A0B5A886; F1BA47;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 19.
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;
GN Name=GP;
OS SFTS phlebovirus (isolate SFTSV/Human/China/HB29/2010) (Severe fever with
OS thrombocytopenia virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Phenuiviridae; Bandavirus; Dabie bandavirus.
OX NCBI_TaxID=992212;
OH NCBI_TaxID=44386; Haemaphysalis longicornis (Bush tick).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=21410387; DOI=10.1056/nejmoa1010095;
RA Yu X.J., Liang M.F., Zhang S.Y., Liu Y., Li J.D., Sun Y.L., Zhang L.,
RA Zhang Q.F., Popov V.L., Li C., Qu J., Li Q., Zhang Y.P., Hai R., Wu W.,
RA Wang Q., Zhan F.X., Wang X.J., Kan B., Wang S.W., Wan K.L., Jing H.Q.,
RA Lu J.X., Yin W.W., Zhou H., Guan X.H., Liu J.F., Bi Z.Q., Liu G.H., Ren J.,
RA Wang H., Zhao Z., Song J.D., He J.R., Wan T., Zhang J.S., Fu X.P.,
RA Sun L.N., Dong X.P., Feng Z.J., Yang W.Z., Hong T., Zhang Y., Walker D.H.,
RA Wang Y., Li D.X.;
RT "Fever with thrombocytopenia associated with a novel bunyavirus in China.";
RL N. Engl. J. Med. 364:1523-1532(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=25552716; DOI=10.1128/jvi.03432-14;
RA Brennan B., Li P., Zhang S., Li A., Liang M., Li D., Elliott R.M.;
RT "A reverse genetic system for severe fever with thrombocytopenia syndrome
RT virus.";
RL J. Virol. 89:3026-3037(2015).
RN [3]
RP PROTEOLYTIC CLEAVAGE (ENVELOPMENT POLYPROTEIN), SUBCELLULAR LOCATION
RP (GLYCOPROTEIN N), AND SUBCELLULAR LOCATION (GLYCOPROTEIN C).
RX PubMed=27855227; DOI=10.1371/journal.pone.0166013;
RA Plegge T., Hofmann-Winkler H., Spiegel M., Poehlmann S.;
RT "Evidence that Processing of the Severe Fever with Thrombocytopenia
RT Syndrome Virus Gn/Gc Polyprotein Is Critical for Viral Infectivity and
RT Requires an Internal Gc Signal Peptide.";
RL PLoS ONE 11:e0166013-e0166013(2016).
RN [4]
RP SUBCELLULAR LOCATION (GLYCOPROTEIN N), SUBCELLULAR LOCATION (GLYCOPROTEIN
RP C), AND FUNCTION (GLYCOPROTEIN N).
RC STRAIN=YG1;
RX PubMed=29467349; DOI=10.2220/biomedres.39.27;
RA Lundu T., Tsuda Y., Ito R., Shimizu K., Kobayashi S., Yoshii K.,
RA Yoshimatsu K., Arikawa J., Kariwa H.;
RT "Targeting of severe fever with thrombocytopenia syndrome virus structural
RT proteins to the ERGIC (endoplasmic reticulum Golgi intermediate
RT compartment) and Golgi complex.";
RL Biomed. Res. 39:27-38(2018).
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 (By similarity). Plays a role in the
CC packaging of ribonucleoproteins and polymerase during virus assembly
CC (PubMed:29467349). {ECO:0000250|UniProtKB:P09613,
CC ECO:0000250|UniProtKB:P21401, ECO:0000250|UniProtKB:R4V2Q5,
CC ECO:0000269|PubMed:29467349}.
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 (By similarity). {ECO:0000250|UniProtKB:P09613,
CC ECO:0000250|UniProtKB:P21401, ECO:0000250|UniProtKB:R4V2Q5}.
CC -!- SUBUNIT: [Glycoprotein N]: Homodimer. Heterodimer with glycoprotein C
CC (By similarity). Homotrimer (postfusion) (By similarity).
CC {ECO:0000250|UniProtKB:P03518, ECO:0000250|UniProtKB:P09613}.
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:0000269|PubMed:27855227, ECO:0000269|PubMed:29467349}; Single-pass
CC type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host
CC endoplasmic reticulum membrane {ECO:0000269|PubMed:27855227,
CC ECO:0000269|PubMed:29467349}; 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:0000269|PubMed:27855227}.
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:0000269|PubMed:27855227, ECO:0000269|PubMed:29467349}; Single-pass
CC type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host
CC endoplasmic reticulum membrane {ECO:0000269|PubMed:27855227,
CC ECO:0000269|PubMed:29467349}; 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:0000269|PubMed:27855227}.
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:0000269|PubMed:27855227}.
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}.
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DR EMBL; HM745931; ADZ04471.1; -; Viral_cRNA.
DR EMBL; KP202164; AJD86039.1; -; Genomic_RNA.
DR RefSeq; YP_006504094.1; NC_018138.1.
DR GeneID; 13231111; -.
DR KEGG; vg:13231111; -.
DR Proteomes; UP000117954; Genome.
DR Proteomes; UP000201130; 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 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-virus interaction; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; 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_0000455554"
FT CHAIN 20..562
FT /note="Glycoprotein N"
FT /id="PRO_0000455555"
FT CHAIN 563..1073
FT /note="Glycoprotein C"
FT /id="PRO_0000455556"
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:P09613"
FT REGION 650..656
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT REGION 691..705
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT SITE 562..563
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000269|PubMed:27855227"
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:0000255"
FT CARBOHYD 914
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 936
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 26..49
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 143..156
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 180..327
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 206..216
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 258..305
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 287..292
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 349..352
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 356..424
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 376..381
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 563..604
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 576..586
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 629..725
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 644..841
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 650..698
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 656..705
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 660..687
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 691..696
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 778..793
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 809..823
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 908..978
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 918..921
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 943..974
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT CONFLICT 321
FT /note="M -> T (in Ref. 1; ADZ04471)"
FT /evidence="ECO:0000305"
FT CONFLICT 962
FT /note="S -> R (in Ref. 1; ADZ04471)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1073 AA; 116636 MW; 612D80CA07722F4A CRC64;
MMKVIWFSSL ICLVIQCSGD SGPIICAGPI HSNKSAGIPH LLGYSEKICQ IDRLIHVSSW
LRNHSQFQGY VGQRGGRSQV SYYPAENSYS RWSGLLSPCD ADWLGMLVVK KAKESDMIVP
GPSYKGKVFF ERPTFDGYVG WGCGSGKSRT ESGELCSSDS GTSSGLLPSD RVLWIGDVAC
QPMTPIPEET FLELKSFSQS EFPDICKIDG IVFNQCEGES LPQPFDVAWM DVGHSHKIIM
REHKTKWVQE SSSKDFVCYK EGTGPCSESE EKACKTSGSC RGDMQFCKVA GCEHGEEASE
AKCRCSLVHK PGEVVVSYGG MRVRPKCYGF SRMMATLEVN PPEQRIGQCT GCHLECINGG
VRLITLTSEL RSATVCASHF CSSASSGKKS TEIHFHSGSL VGKTAIHVKG ALVDGTEFTF
EGSCMFPDGC DAVDCTFCRE FLKNPQCYPA KKWLFIIIVI LLGYAGLMLL TNVLKAIGVW
GSWVIAPVKL MFAIIKKLMR TVSCLVGKLM DRGRQVIHEE IGENGEGNQD DVRIEMARPR
RVRHWMYSPV ILTILAIGLA EGCDEMVHAD SKLVSCRQGS GNMKECITTG 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 SVLEGVHSYI
VSLSFDHAVV DEQCQLNCGG HESQVTLKGN LIFLDVPKFV DGSYMQTYHS TVPTGANIPS
PTDWLNALFG NGLSRWILGV IGVLLGGLAL FFLIMFLLKL GTKQVFRSRT KLA
