ID   GP_DUGBA                Reviewed;        1551 AA.
AC   Q02004;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Envelopment polyprotein;
DE   AltName: Full=M polyprotein;
DE   Contains:
DE     RecName: Full=Mucin-like variable region;
DE   Contains:
DE     RecName: Full=GP38 {ECO:0000250|UniProtKB:Q8JSZ3};
DE   Contains:
DE     RecName: Full=Glycoprotein N {ECO:0000250|UniProtKB:Q8JSZ3};
DE              Short=Gn;
DE     AltName: Full=Glycoprotein G2;
DE   Contains:
DE     RecName: Full=Non-Structural protein M {ECO:0000250|UniProtKB:Q8JSZ3};
DE              Short=NSm;
DE   Contains:
DE     RecName: Full=Glycoprotein C {ECO:0000250|UniProtKB:Q8JSZ3};
DE              Short=Gc;
DE     AltName: Full=Glycoprotein G1;
DE   Flags: Precursor;
GN   Name=GP;
OS   Dugbe virus (isolate ArD44313) (DUGV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Nairoviridae; Orthonairovirus; Dugbe virus.
OX   NCBI_TaxID=766194;
OH   NCBI_TaxID=34610; Amblyomma variegatum (Tropical bont tick).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=72862; Hyalomma rufipes (Tick) (Hyalomma marginatum rufipes).
OH   NCBI_TaxID=72855; Hyalomma truncatum.
OH   NCBI_TaxID=34630; Rhipicephalus.
OH   NCBI_TaxID=34611; Rhipicephalus annulatus.
OH   NCBI_TaxID=60189; Rhipicephalus decoloratus (African blue tick) (Boophilus decoloratus).
OH   NCBI_TaxID=136141; Rhipicephalus geigyi.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PROTEIN SEQUENCE OF 897-905.
RX   PubMed=1387749; DOI=10.1016/0042-6822(92)90898-y;
RA   Marriott A.C., El-Ghorr A.A., Nuttall P.A.;
RT   "Dugbe Nairovirus M RNA: nucleotide sequence and coding strategy.";
RL   Virology 190:606-615(1992).
CC   -!- FUNCTION: [Glycoprotein N]: Glycoprotein N and glycoprotein C interact
CC       with each other and are present at the surface of the virion.
CC       Glycoprotein N probably locks the Gn-Gc complex in a prefusion state.
CC       Glycoprotein N and glycoprotein C are able to attach the virion to host
CC       cell receptors. This attachment induces virion internalization
CC       predominantly through clathrin-dependent endocytosis.
CC       {ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- FUNCTION: [Glycoprotein C]: Glycoprotein C and glycoprotein N interact
CC       with each other and are present at the surface of the virion (By
CC       similarity). The spikes at the surface of the virion are formed by an
CC       N-terminal extension of glycoprotein C (By similarity). Glycoprotein N
CC       and glycoprotein C are able to attach the virion to host cell receptors
CC       (By similarity). This attachment induces virion internalization
CC       predominantly through clathrin-dependent endocytosis (By similarity).
CC       Class II fusion protein that promotes fusion of viral membrane with
CC       host endosomal membrane after endocytosis of the virion (By
CC       similarity). Exposure to potassium is necessary for the conformational
CC       change leading to fusion (By similarity).
CC       {ECO:0000250|UniProtKB:A6XIP3, ECO:0000250|UniProtKB:H2AM12,
CC       ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- SUBUNIT: [Glycoprotein N]: Heterodimer with glycoprotein C; in
CC       prefusion state. {ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- SUBUNIT: [Glycoprotein C]: Heterodimer with glycoprotein N; in
CC       prefusion state (By similarity). Homotrimeric; in postfusion state (By
CC       similarity). {ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- SUBCELLULAR LOCATION: [Envelopment polyprotein]: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane
CC       {ECO:0000250|UniProtKB:Q8JSZ3}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:Q8JSZ3}. Host Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q8JSZ3}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:Q8JSZ3}. Host endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q8JSZ3}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:Q8JSZ3}. Note=Interaction between glycoprotein C
CC       and glycoprotein N is essential for proper targeting of glycoprotein C
CC       to the Golgi complex, where virion budding occurs.
CC       {ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane
CC       {ECO:0000250|UniProtKB:Q8JSZ3}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q8JSZ3}. Host Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q8JSZ3}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- SUBCELLULAR LOCATION: [Non-Structural protein M]: Host Golgi apparatus
CC       membrane {ECO:0000250|UniProtKB:Q8JSZ3}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- PTM: [Envelopment polyprotein]: Specific enzymatic cleavage by host
CC       MBTPS1/S1P/SKI-1 endopeptidase yield glycoprotein N. Specific enzymatic
CC       cleavages by host furin-like protease and MBTPS1/S1P endopeptidase
CC       yield GP38. {ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- PTM: [Glycoprotein N]: Glycosylated. {ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- PTM: [Glycoprotein C]: Glycosylated. {ECO:0000250|UniProtKB:Q8JSZ3}.
CC   -!- SIMILARITY: Belongs to the nairovirus envelope glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; M94133; AAA42974.1; -; Genomic_RNA.
DR   PIR; A43364; A43364.
DR   SMR; Q02004; -.
DR   GlyCosmos; Q02004; 9 sites, No reported glycans.
DR   Proteomes; UP000000278; 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:0016020; C: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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019049; P:virus-mediated perturbation of host defense response; IEA:InterPro.
DR   Gene3D; 1.10.8.1320; -; 2.
DR   InterPro; IPR048791; Gc_C_bunya.
DR   InterPro; IPR048801; Gn_nairovirus.
DR   InterPro; IPR048529; GP38_nairovirus.
DR   InterPro; IPR002532; Hanta_Gc_N.
DR   InterPro; IPR048796; NSm_dom_nairovirus.
DR   Pfam; PF20682; Hanta_Gc_C; 1.
DR   Pfam; PF01561; Hanta_Gc_N; 1.
DR   Pfam; PF20726; Nairovirus_Gn; 1.
DR   Pfam; PF07948; Nairovirus_GP38; 1.
DR   Pfam; PF20728; Nairovirus_NSm; 1.
PE   1: Evidence at protein level;
KW   Clathrin-mediated endocytosis of virus by host;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
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; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW   Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW   Virus endocytosis by host; Virus entry into host cell.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..1551
FT                   /note="Envelopment polyprotein"
FT                   /id="PRO_0000036802"
FT   CHAIN           18..105
FT                   /note="Mucin-like variable region"
FT                   /id="PRO_0000369248"
FT   CHAIN           106..374
FT                   /note="GP38"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT                   /id="PRO_0000434912"
FT   CHAIN           375..662
FT                   /note="Glycoprotein N"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000036804"
FT   CHAIN           694..896
FT                   /note="Non-Structural protein M"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT                   /id="PRO_0000434913"
FT   CHAIN           897..1551
FT                   /note="Glycoprotein C"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000036805"
FT   TOPO_DOM        18..546
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        547..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        568..675
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   TRANSMEM        676..696
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        697..704
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   TRANSMEM        705..725
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        726..823
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   TRANSMEM        824..844
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        845..1451
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1452..1472
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1473..1551
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          24..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            105..106
FT                   /note="Cleavage; by host furin-like protease"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   SITE            374..375
FT                   /note="Cleavage; by host MBTPS1/SKI-1 protease"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   SITE            662..663
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   SITE            694..695
FT                   /note="Cleavage; by host protease"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   SITE            849..850
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   SITE            896..897
FT                   /note="Cleavage; by host protease"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   SITE            924
FT                   /note="Involved in fusion with the host membrane"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   SITE            1221
FT                   /note="Involved in fusion with the host membrane"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   SITE            1336
FT                   /note="Involved in fusion with the host membrane"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        413
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   CARBOHYD        848
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1201
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1258
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1420
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT   DISULFID        1023..1216
FT                   /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
SQ   SEQUENCE   1551 AA;  173355 MW;  7C1654C63895C620 CRC64;
     MSKRVLIIAV VVYLVFTTQN QITGNHTTIN SSSPSTTEAS STPTVSRTPQ TTTTSTAVST
     TITATTTPTA SWTTQSQYFN KTTQHHWREE TMISRNPTVL DRQSRASSVR ELLNTKFLML
     LGFIPKGEVN HLENACNREG KNCTELILKE RIARFFSETE KESCYNTYLE KHLRSVSPEV
     SLTPYRVLGL REDILLKEID RRIIRFETDS QRVTCLSASL LKPDVFIREQ RIDAKPSNGP
     KIVPVDSVAC MNLEANVDVR SNKLVIQSLM TTVKISLKNC KVVVNSRQCI HQQTGSGVIK
     VPKFEKQQGG TWSSYIAGVY TATIDLLDEN NQNCKLFTEC IVKGRELVKG QSELKSFNIE
     VLLPRVMKTR RKLLAVTDGS TECNSGTQLI EGKSIEVHKQ DIGGPGKKLT ICNGTSVLDV
     PLDEGHGCYT INVITSKRAC RPKNSKLQCS IDKELKPCDS GKCLSISQKG AGHIKVSRGK
     TILITECKEH CQIPVPTGKG DIMVDCSGGR QHYLEVNIVD IHCPNTKFLG GIMLYFCRMS
     SRPTVALLLG IWIGCGYILT CIFSFLLYHL ILFFANCIKQ CRKKGERLGE ICVKCEQQTV
     NLMDQELHDL NCNFNLCPYC CNRMSDEGMS RHVGKCPKRL ERLNEIELYL TTSECLCLSV
     CYQLLISVGI FLKRTTWLVV LLVLLGLAIS PVQGAPTEVS NVKQDGDYSI CYFIFGCLVT
     AALLLKVKRT NSNGIVVVVD SFGRCPYCNE FTDSLFEEVL HDTLCSLCVC PFCEKQALDL
     VTLEEHVKEC YKVATRKDIF KILGRKFTNA LVRREKLFTT GLQLFINKTN VVVFALIMCF
     LLLLTGHNAS AFDSGDLPDG VWEESSQLVK SCTQFCYIEE DVCYCPAEDG VGRKLLFFNG
     LQNSVKRLSD SHKLLTSVSI DAPWGRINVE STWKPTLAAS NIAMSWSSTD IKGEKVILSG
     RSTSIIKLKE KTGVMWKLVG SGLASEKKKP FRFPIMDFAQ VYNSVFQYIT GDRLLSEWPK
     AVCTGDCPHR CGCQTSTCMA KECHTQECVS THMVLGIGTG CTCCGMDVER PFNKYLGVKW
     STEYLRTEVL VCVEVTEEER HCEIVEAGTR FNIGPITITI SDPQNIGSKL PESLMTVQEI
     DDSNFVDIMH VGNVISADNS CRLQSCTHGS AVTTRFTALT ALIKDDHSSG LNLAVLDPKV
     NSSWLSWEGC DMDYYCNVGD WPTCTYTGVV TQKLREFLKL DQHRKRLHTT LSFSLKKNLS
     KRSHTSVRLE GKTVTRMEVK VTALIEVDGM ELHSKTIRLS GIRLTGLKCS GCFSCTSGIS
     CSVNAKLTSP DEFTLHLRST SPNVVVAETS IIARKGPSAT TSRFKVFSVR DTKKICFEVV
     EREYCKDCTP DELTTCTGVE LEPTKDILLE HRGTIVQHQN DTCKSKIDCW SNSISSFASG
     IGDFFKHYIG SIAVGVLGTV LPFALLILFF IYGDKMLWPF KVFCRPCRRC CRKNEGYNKL
     AEEEELRDII RKFSKSGELI NKDAKDKRTL ARLFMSDNPK LKKEKKLSEI A
//