GP_DUGBA
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 03-AUG-2022, entry version 101.
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.
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 C and glycoprotein N interact with each other
CC and are present at the surface of the virion. They are able to attach
CC the virion to a cell receptor and to promote fusion of membranes after
CC endocytosis of the virion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Glycoprotein C and Glycoprotein N interact with each other.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}. Host Golgi apparatus
CC membrane {ECO:0000305}; Single-pass type I membrane protein
CC {ECO:0000305}. Host endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}. Note=Interaction
CC between Glycoprotein C and Glycoprotein N is essential for proper
CC targeting of Glycoprotein C to the Golgi complex, where virion budding
CC occurs. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}. Host Golgi apparatus
CC membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins
CC including Glycoprotein C and Glycoprotein N.
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 PRIDE; Q02004; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
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 GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR002532; Hanta_Gc.
DR InterPro; IPR012487; Nairovirus_M.
DR Pfam; PF01561; Hanta_G2; 1.
DR Pfam; PF07948; Nairovirus_M; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing;
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; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Virion; 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..95
FT /note="Mucin-like variable region"
FT /id="PRO_0000369248"
FT CHAIN 96..374
FT /note="GP38"
FT /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT /id="PRO_0000434912"
FT CHAIN 371..893
FT /note="Glycoprotein N"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036804"
FT CHAIN 698..896
FT /note="Non-Structural protein M"
FT /evidence="ECO:0000250|UniProtKB:Q8JSZ3"
FT /id="PRO_0000434913"
FT CHAIN 894..1551
FT /note="Glycoprotein C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036805"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 676..696
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 705..725
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 824..844
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1452..1472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 24..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 370..371
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 893..894
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
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:0000255"
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:0000255"
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
