GP_PHV
ID GP_PHV Reviewed; 1142 AA.
AC P27315;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Envelopment polyprotein;
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 Prospect Hill virus (PHV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC Orthohantavirus.
OX NCBI_TaxID=1980485;
OH NCBI_TaxID=10058; Microtus pennsylvanicus (Meadow vole).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1840609; DOI=10.1099/0022-1317-72-8-1845;
RA Parrington M.A., Lee P.W., Kang C.Y.;
RT "Molecular characterization of the Prospect Hill virus M RNA segment: a
RT comparison with the M RNA segments of other hantaviruses.";
RL J. Gen. Virol. 72:1845-1854(1991).
RN [2]
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).
RN [3]
RP STRUCTURE BY NMR OF 548-602, AND DOMAIN (GLYCOPROTEIN N).
RX PubMed=22203819; DOI=10.3389/fmicb.2011.00251;
RA Estrada D.F., Conner M., Jeor S.C., Guzman R.N.;
RT "The Structure of the Hantavirus Zinc Finger Domain is Conserved and
RT Represents the Only Natively Folded Region of the Gn Cytoplasmic Tail.";
RL Front. Microbiol. 2:251-251(2011).
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 alpha5/ITGB1 (Probable). 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, ECO:0000305}.
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 (By similarity). Homotetramer;
CC forms 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. Host cell
CC surface {ECO:0000250|UniProtKB:P08668}. Host Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P08668}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein
CC {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 Golgi complex, where virion budding occurs.
CC {ECO:0000250|UniProtKB:P27312}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane
CC {ECO:0000250|UniProtKB:P08668}; Single-pass type I membrane protein.
CC Host cell surface {ECO:0000250|UniProtKB:P08668}. Host Golgi apparatus
CC membrane {ECO:0000250|UniProtKB:P08668}; Single-pass type I membrane
CC protein {ECO:0000250|UniProtKB:P08668}. Host endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:P08668}; Single-pass type I membrane
CC protein {ECO:0000250|UniProtKB:P08668}. Note=Budding probably takes
CC place at the host Golgi (Probable). Glycoprotein C cytoplasmic tail is
CC important for efficient Golgi localization (By similarity).
CC {ECO:0000250|UniProtKB:P08668, ECO:0000305}.
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 (PubMed:22203819).
CC {ECO:0000250|UniProtKB:P08668, ECO:0000250|UniProtKB:P0DTJ1,
CC ECO:0000250|UniProtKB:P27312, ECO:0000269|PubMed:22203819}.
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 -!- MISCELLANEOUS: This virus is non-pathogenic. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the hantavirus envelope glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; X55129; CAA38922.1; -; mRNA.
DR PIR; JQ1380; GNVUPH.
DR SMR; P27315; -.
DR PRIDE; P27315; -.
DR Proteomes; UP000242194; 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: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:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0039547; P:suppression by virus of host TRAF activity; 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; IPR016402; Envelope_glycoprot_Hantavirus.
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 PIRSF; PIRSF003945; M_poly_HantaV; 1.
DR PROSITE; PS51056; ITAM_2; 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 mitochondrion; Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host RLR pathway by virus; Inhibition of host TRAFs by virus;
KW Membrane; Metal-binding; Phosphoprotein; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral immunoevasion;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell;
KW Zinc; Zinc-finger.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1142
FT /note="Envelopment polyprotein"
FT /id="PRO_0000036818"
FT CHAIN 22..654
FT /note="Glycoprotein N"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036819"
FT CHAIN 655..1142
FT /note="Glycoprotein C"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036820"
FT TOPO_DOM 22..489
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..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..1142
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:0000269|PubMed:22203819"
FT ZN_FING 576..597
FT /note="CCHC-type 2"
FT /evidence="ECO:0000269|PubMed:22203819"
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..1142
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 CARBOHYD 139
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 31..156
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 65..162
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 114..133
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 138..143
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 180..190
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 215..253
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 411..430
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 1142 AA; 125686 MW; CD3BAD69F078C8B9 CRC64;
MSKFCLCLSL LGVLLLQVCD TRSLLELKIE CPHTVGLGQG LVIGTVDLNP VPVESVSTLK
LESSCNFDVH TSSATQQAVT KWTWEKKADT AETAKAASTT FQSKSTELNL RGLCVIPTLV
LETANKLRKT VTCYDLSCNQ TACIPTVYLI APIHTCVTTK SCLLGLGTQR IQVTYEKTYC
VSGQLVEGTC FNPIHTMALS QPSHTYDIVT IPVRCFFIAK KTNDDTLKIE KQFETILEKS
GCTAANIKGY YVCFLGATSE PIFVPTMDDF RASQILSDMA ISPHGEDHDS ALSSVSTFRI
AGKLSGKAPS TESSDTVQGV AFSGHPLYTS LSVLASKEDP VYIWSPGIIP ERNHTVCDKK
TLPLTWTGYL PLPGGIEKTT QCTIFCTLAG PGADCEAYSD TGIFNISSPT CLINRVQRFR
GAEQQIKFVC QRVDLDIVVY CNGMKKVILT KTLVIGQCIY TFTSVFSLMP GIAHSLAVEL
CVPGIHGWST IALLATFCFG WLLIPIISLV SIKIMLLFAY MCSKYSNDSK FRLLIEKVKQ
EYQKTMGSMV CEVCQQECEM AKELESHKKS CPNGMCPYCM NPTESTESAL QAHFKVCKLT
TRFQENLRKS LNPYEPKRGC YRTLSVFRYR SRCFVGLVWC ILLVLELVIW AASADTVEIK
TGWTDTAHGA GVIPLKSDLE LDFSLPSSAT YIYRRDLQNP ANEQERIPFH FQLQRQVIHA
EIQNLGHWMD GTFNLKTSFH CYGACEKYAY PWQTAKCFLE KDYEFETGWG CNPGDCPGVG
TGCTACGVYL DKLRSVGKVF KVISLKFTRR VCIQLGSEQS CKTIDSNDCL MTTSVKVCMI
GTVSKFQPGD TLLFLGPLEE GGIIFKQWCT TTCHFGDPGD IMSTPQGMQC PEHTGAFRKK
CAFATMPTCE YDGNTLSGYQ RMLATRDSFQ SFNITEPHIT SNSLEWVDPD SSLKDHINLV
VNRDVSFQDL SENPCQVGVA VSSIDGAWGS GVGFNLVCSV SLTECASFLT SIKACDAAMC
YGATTANLVR GQNTVHILGK GGHSGSKFMC CHSTECSSTG LTAAAPHLDR VTGYNVIDND
KVFDDGSPEC GVHCWFKKSG EWLMGILSGN WMVVAVLVVL LILSIFLFSL CCPRRVVHKK
SS
