GP_PUUMU
ID GP_PUUMU Reviewed; 236 AA.
AC Q09120;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=M polyprotein;
DE Contains:
DE RecName: Full=Glycoprotein C {ECO:0000250|UniProtKB:P08668};
DE Short=Gc;
DE AltName: Full=Glycoprotein G2;
DE Flags: Fragment;
GN Name=GP;
OS Puumala virus (strain Udmurtia/894CG/91).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC Orthohantavirus.
OX NCBI_TaxID=39003;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=447135; Myodes glareolus (Bank vole) (Clethrionomys glareolus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8113763; DOI=10.1099/0022-1317-75-2-405;
RA Plyusnin A., Vapalahti O., Ulfves K., Lehvaeslaiho H., Apekina N.,
RA Gavrilovskaya I., Blinov V., Vaheri A.;
RT "Sequences of wild Puumala virus genes show a correlation of genetic
RT variation with geographic origin of the strains.";
RL J. Gen. Virol. 75:405-409(1994).
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).
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 C]: Homodimer. Homotetramer; forms
CC heterotetrameric Gn-Gc spikes in the pre-fusion conformation (By
CC similarity). Homotrimer; forms homotrimer in the post-fusion
CC conformation at acidic pH (By similarity). Interacts (via C-terminus)
CC with the nucleoprotein (By similarity). {ECO:0000250|UniProtKB:P08668,
CC ECO:0000250|UniProtKB:P27312, ECO:0000250|UniProtKB:P41266}.
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:0000250|UniProtKB:P08668}. 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 -!- 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: [Envelope glycoprotein]: Envelope polyprotein precursor is quickly
CC 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; Z21509; CAA79722.1; -; Genomic_RNA.
DR SMR; Q09120; -.
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: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: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 Pfam; PF01561; Hanta_G2; 1.
PE 3: Inferred from homology;
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; Phosphoprotein; Repeat; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT CHAIN <1..236
FT /note="Envelope glycoprotein"
FT /id="PRO_0000232520"
FT CHAIN <1..236
FT /note="Glycoprotein C"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036834"
FT TOPO_DOM <1..202
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 219..236
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT REGION 219..231
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P41266"
FT DISULFID 67..97
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 90..142
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 107..112
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 143..148
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 182..186
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT NON_TER 1
SQ SEQUENCE 236 AA; 25556 MW; C70267CC53328C37 CRC64;
CQFDGNTISG YKRMIATKDS FQSFNVTEPH ISASALEWID PDSSLRDHIN VIVSRDLSFQ
DLSETPCQID LSTASIDGAW GSGVGFNLVC TVSLTECSAF LTSIKACDAA MCYGSTTANL
VRGQNTIHIV GKGGHSGSKF MCCHDTKCST TGLVAAAPHL DRVTGYNQAD SDKIFDDGAP
ECGMSCWFKK SGEWILGVLN GNWMVVAVLI ALLILSILLF TLCCPRRPSY RKEHKP
