GP_BCCV
ID GP_BCCV Reviewed; 1141 AA.
AC P0DTJ0;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 1.
DT 03-AUG-2022, entry version 2.
DE RecName: Full=Envelopment polyprotein;
DE AltName: Full=Glycoprotein precursor {ECO:0000250|UniProtKB:P08668};
DE AltName: Full=M polyprotein;
DE Contains:
DE RecName: Full=Glycoprotein N {ECO:0000250|UniProtKB:P08668};
DE Short=Gn;
DE AltName: Full=Glycoprotein G1;
DE Contains:
DE RecName: Full=Glycoprotein C {ECO:0000250|UniProtKB:P08668};
DE Short=Gc;
DE AltName: Full=Glycoprotein G2;
DE Flags: Precursor;
GN Name=GP;
OS Black Creek Canal orthohantavirus (BCCV) (Black Creek Canal virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC Orthohantavirus.
OX NCBI_TaxID=1980460;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=42415; Sigmodon hispidus (Hispid cotton rat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7618284; DOI=10.1006/viro.1995.1366;
RA Ravkov E.V., Rollin P.E., Ksiazek T.G., Peters C.J., Nichol S.T.;
RT "Genetic and serologic analysis of Black Creek Canal virus and its
RT association with human disease and Sigmodon hispidus infection.";
RL Virology 210:482-489(1995).
RN [2]
RP SUBCELLULAR LOCATION (GLYCOPROTEIN N), AND SUBCELLULAR LOCATION
RP (GLYCOPROTEIN C).
RX PubMed=8995636; DOI=10.1128/jvi.71.2.1147-1154.1997;
RA Ravkov E.V., Nichol S.T., Compans R.W.;
RT "Polarized entry and release in epithelial cells of Black Creek Canal
RT virus, a New World hantavirus.";
RL J. Virol. 71:1147-1154(1997).
RN [3]
RP REVIEW.
RX PubMed=24755564; DOI=10.3390/v6041801;
RA Cifuentes-Munoz N., Salazar-Quiroz N., Tischler N.D.;
RT "Hantavirus Gn and Gc envelope glycoproteins: key structural units for
RT virus cell entry and virus assembly.";
RL Viruses 6:1801-1822(2014).
CC -!- FUNCTION: [Glycoprotein N]: Forms homotetramers with glycoprotein C at
CC the surface of the virion (By similarity). Attaches the virion to host
CC cell receptors including integrin ITGAV/ITGB3 (By similarity). This
CC attachment induces virion internalization predominantly through
CC clathrin-dependent endocytosis (By similarity). Mediates the assembly
CC and budding of infectious virus particles through its interaction with
CC the nucleocapsid protein and the viral genome (By similarity). May
CC dysregulate normal immune and endothelial cell responses through an
CC ITAM motif (By similarity). Translocates to mitochondria, binds to host
CC TUFM and recruits MAP1LC3B (By similarity). These interactions induce
CC mitochondrial autophagy and therefore destruction of host MAVS leading
CC to inhibition of type I interferon (IFN) responses (By similarity).
CC Concomitant breakdown of glycoprotein N is apparently prevented by the
CC nucleoprotein that may inhibit Gn-stimulated autophagosome-lysosome
CC fusion (By similarity). Interacts with the viral genomic RNA (By
CC similarity). {ECO:0000250|UniProtKB:P08668,
CC ECO:0000250|UniProtKB:P27312}.
CC -!- FUNCTION: [Glycoprotein C]: Forms homotetramers with glycoprotein N at
CC the surface of the virion. Attaches the virion to host cell receptors
CC including integrin ITGAV/ITGB3. This attachment induces virion
CC internalization predominantly through clathrin-dependent endocytosis.
CC Class II fusion protein that promotes fusion of viral membrane with
CC host endosomal membrane after endocytosis of the virion.
CC {ECO:0000250|UniProtKB:P08668}.
CC -!- SUBUNIT: [Glycoprotein N]: Homodimer. Homotetramer; forms
CC heterotetrameric Gn-Gc spikes in the pre-fusion conformation (By
CC similarity). Interacts (via C-terminus) with the nucleoprotein (By
CC similarity). Interacts with host TUFM; this interaction contributes to
CC the virus-induced degradation of mitochondria by autophagy, which leads
CC to degradation of host MAVS and inhibition of type I interferon (IFN)
CC responses (By similarity). Interacts with host MAP1LC3B; this
CC interaction contributes to the virus-induced degradation of
CC mitochondria by autophagy, which leads to degradation of host MAVS and
CC inhibition of type I interferon (IFN) responses (By similarity).
CC {ECO:0000250|UniProtKB:P08668, ECO:0000250|UniProtKB:P0DTJ1}.
CC -!- SUBUNIT: [Glycoprotein C]: Homodimer. Homotetramer; forms
CC heterotetrameric Gn-Gc spikes in the pre-fusion conformation.
CC Homotrimer; forms homotrimer in the post-fusion conformation at acidic
CC pH (By similarity). Interacts (via C-terminus) with the nucleoprotein
CC (By similarity). {ECO:0000250|UniProtKB:P08668,
CC ECO:0000250|UniProtKB:P27312}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane
CC {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein
CC {ECO:0000305}. Host cell surface {ECO:0000269|PubMed:8995636}. Host
CC Golgi apparatus membrane {ECO:0000250|UniProtKB:P08668}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P08668}. Host endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P08668}. Host mitochondrion
CC {ECO:0000250|UniProtKB:P08668}. Note=Interaction between glycoprotein N
CC and glycoprotein C is essential for proper targeting of glycoprotein N
CC to the host plasma membrane, where virion budding occurs.
CC {ECO:0000305|PubMed:8995636}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane
CC {ECO:0000250|UniProtKB:P08668}; Single-pass type I membrane protein
CC {ECO:0000305}. Host cell surface {ECO:0000269|PubMed:8995636}. Host
CC Golgi apparatus membrane {ECO:0000250|UniProtKB:P08668}; Single-pass
CC type I membrane protein {ECO:0000250|UniProtKB:P08668}. Host
CC endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P08668}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:P08668}.
CC Note=Budding probably takes place at the host plasma membrane
CC (Probable). Glycoprotein C cytoplasmic tail is important for efficient
CC Golgi localization (By similarity). {ECO:0000250|UniProtKB:P08668,
CC ECO:0000305|PubMed:8995636}.
CC -!- DOMAIN: [Glycoprotein N]: The YxxL motif at the C-terminus is
CC indispensable for the interaction with MAP1LC3B and for the Gn-mediated
CC induction of mitochondrial autophagy (By similarity). The cytoplasmic
CC tail is involved in the inhibition of the host innate immune response
CC (By similarity). The C-terminus of the cytoplasmic tail is involved in
CC binding to the viral genome and the nucleocapsid (By similarity).
CC Contains 2 contiguous zinc-fingers (By similarity).
CC {ECO:0000250|UniProtKB:P08668, ECO:0000250|UniProtKB:P0DTJ1,
CC ECO:0000250|UniProtKB:P27312, ECO:0000250|UniProtKB:Q9E006}.
CC -!- DOMAIN: [Glycoprotein C]: The C-terminus is necessary for proper
CC localization in the Golgi (By similarity). The cytoplasmic tail is
CC involved in binding to the nucleocapsid (By similarity).
CC {ECO:0000250|UniProtKB:P27312}.
CC -!- PTM: [Envelopment polyprotein]: Envelope polyprotein precursor is
CC quickly cleaved in vivo just after synthesis, presumably by host signal
CC peptidase. {ECO:0000250|UniProtKB:P08668}.
CC -!- SIMILARITY: Belongs to the hantavirus envelope glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; L39950; -; NOT_ANNOTATED_CDS; Genomic_RNA.
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:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0039547; P:suppression by virus of host TRAF activity; IEA:UniProtKB-KW.
DR GO; GO:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR002532; Hanta_Gc.
DR InterPro; IPR002534; Hanta_Gn.
DR InterPro; IPR012316; ITAM_motif_hantavir-typ.
DR Pfam; PF01567; Hanta_G1; 1.
DR Pfam; PF01561; Hanta_G2; 1.
DR Pfam; PF10538; ITAM_Cys-rich; 1.
DR PROSITE; PS51056; ITAM_2; 1.
PE 3: Inferred from homology;
KW Activation of host autophagy by virus; 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 mitochondrion; Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host MAVS by virus; Inhibition of host RLR pathway by virus;
KW Inhibition of host TRAFs by virus; Membrane; Metal-binding; Phosphoprotein;
KW Repeat; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Viral immunoevasion;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell; Zinc; Zinc-finger.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1141
FT /note="Envelopment polyprotein"
FT /id="PRO_0000455194"
FT CHAIN 19..654
FT /note="Glycoprotein N"
FT /id="PRO_0000455195"
FT CHAIN 655..1141
FT /note="Glycoprotein C"
FT /id="PRO_0000455196"
FT TOPO_DOM 19..483
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..633
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 634..654
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 655..1110
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1111..1131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1132..1141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 617..640
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT ZN_FING 551..571
FT /note="CCHC-type 1"
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT ZN_FING 576..597
FT /note="CCHC-type 2"
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT REGION 522..539
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT REGION 594..611
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT REGION 598..609
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT REGION 617..631
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT REGION 763..783
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:P41266"
FT REGION 1127..1141
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT MOTIF 621..624
FT /note="YxxL"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT SITE 654..655
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT MOD_RES 621
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 634
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 933
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 30..158
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 64..164
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 113..135
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 140..145
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 182..192
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 217..253
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 242..357
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 382..441
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 386..395
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 458..481
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 741..776
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 745..783
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 757..890
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 771..901
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 786..909
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 812..821
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 829..838
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 869..873
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 975..1005
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 998..1050
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 1015..1020
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 1051..1056
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 1090..1094
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
SQ SEQUENCE 1141 AA; 125597 MW; 999276B9A2756D2F CRC64;
MGRLYLIVLG VLITATAGFP RSVHELKIEC PHTVVLGQGY VTGSVELGFI ALDQVTDLKI
ESSCSFDHHA APTTTQNFTQ LKWAKTASTT DTTNAAETTF ESKSTEVHLK GVCTIPSNVL
DGPSRPVTGR KTVVCYDLAC NQTHCQPTVH LLAPIQTCMS VRSCMISLLA SRIQVVYEKT
YCVTGQLIEG LCFNPVPNLA LTQPGHTYDT FTLPITCFLV AKKGANLKIA VELEKLTTKT
GCAENALQAY YICFIGQHSE PLTVPMLEDY RSAEIFTRIM MNPKGEDHDM EQSSQGALRI
VGPIKGKVPP TETSDTVQGI AFAGLPMYSS FSSLVRKAEP EYLFSPGIIA ESNHSSCDKK
TLPLTWRGFL SMSGEIERIT GCNVFCTLAG PGASCEAYSE NGIFNISSPT CLVNKVQKFR
GSEQRINFIS QRIDQDVIVY CNGQKKVILT KTLVIGQCIY TFTSIFSLIP SVAHSLAVEL
CVPGIHGWAT IALVITFCFG WLLIPTTTMV VLKCLRLLTY SCSHYSTESK FKVILEKVKV
EYQKTMGSMV CDICHHECET AKELESHKKS CADGQCPYCM TITEATESAL QAHYAVCKLT
GRFHEALKKS LKKPEVQRGC YRTLGVFRYK SRCYVGLVWM CLLTLELIVW AASADTPLLE
PGWSDTAHGV GDIPMKTDLE LDFAIPSSSS YSYRRRLVNP ANSDETVPFH FQLERQVIHA
EIQSLGHWMD ATFNIISAFH CYGECKKYSY PWQTAKCFFE KDYQYETSWS CNPPDCPGVG
TGCTACGIYL DKLKSVGKAY KVITLKYARK VCIQLGTEQT CKNIDVNDCL VTSSIKVCMI
GTISKFQPGD TLLFLGPLEE GGLVLKQWCT TTCSFGDPGD IMSTTSGMRC PEHTGSFRKI
CGFATTPVCE YQGNTVSGFK RLMATKDSFQ SFNVSEVHIT TTKLEWSDPD SNIKDHINLI
LNRDVSFQDL SDNPCKVDLS TQAIDGAWGS GVGFTLTCIV GLTECSSFMT SIKVCDMAMC
YGASVVNLVR GSNTVKIVGK GGHSGSTFRC CHDKDCTSNG LLASAPHLER VTGFNQIDSD
KVYDDGAPPC SIKCWFAKSG EWLLGILNGN WVVVAVLVII LLISIFLFSF FCPIRSHKKQ
L
