GLYC_LASSG
ID GLYC_LASSG Reviewed; 490 AA.
AC P17332;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Pre-glycoprotein polyprotein GP complex {ECO:0000255|HAMAP-Rule:MF_04084};
DE Short=Pre-GP-C {ECO:0000255|HAMAP-Rule:MF_04084};
DE Contains:
DE RecName: Full=Stable signal peptide {ECO:0000255|HAMAP-Rule:MF_04084};
DE Short=SSP {ECO:0000255|HAMAP-Rule:MF_04084};
DE Contains:
DE RecName: Full=Glycoprotein G1 {ECO:0000255|HAMAP-Rule:MF_04084};
DE Short=GP1 {ECO:0000255|HAMAP-Rule:MF_04084};
DE Contains:
DE RecName: Full=Glycoprotein G2 {ECO:0000255|HAMAP-Rule:MF_04084};
DE Short=GP2 {ECO:0000255|HAMAP-Rule:MF_04084};
GN Name=GPC {ECO:0000255|HAMAP-Rule:MF_04084}; Synonyms=GP-C;
OS Lassa virus (strain GA391) (LASV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=11621;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=10112; Mastomys natalensis (African soft-furred rat) (Praomys natalensis).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2042397; DOI=10.1016/0168-1702(91)90015-n;
RA Clegg J.C.S., Wilson S.M., Oram J.D.;
RT "Nucleotide sequence of the S RNA of Lassa virus (Nigerian strain) and
RT comparative analysis of arenavirus gene products.";
RL Virus Res. 18:151-164(1991).
CC -!- FUNCTION: [Glycoprotein G2]: Class I viral fusion protein that directs
CC fusion of viral and host endosomal membranes, leading to delivery of
CC the nucleocapsid into the cytoplasm. Membrane fusion is mediated by
CC irreversible conformational changes induced upon acidification in the
CC endosome. {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- FUNCTION: Stable signal peptide (SSP): cleaved and functions as a
CC signal peptide. In addition, it is also retained as the third component
CC of the GP complex. The SSP is required for efficient glycoprotein
CC expression, post-translational maturation cleavage of GP1 and GP2,
CC glycoprotein transport to the cell surface plasma membrane, formation
CC of infectious virus particles, and acid pH-dependent glycoprotein-
CC mediated cell fusion. {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- FUNCTION: [Glycoprotein G1]: Interacts with the host receptor.
CC {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- SUBUNIT: [Glycoprotein G1]: Homotetramer; disulfide-linked.
CC {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- SUBUNIT: [Glycoprotein G2]: Homotetramer. GP2 homotetramers bind
CC through ionic interactions with GP1 homotetramers to form the GP
CC complex together with the stable signal peptide. The GP-C polyprotein
CC interacts with the host protease MBTPS1/SKI-1 resulting in the
CC polyprotein processing. {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein G1]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein G2]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Note=Binding to the stable signal
CC peptide masks endogenous ER localization signals in the cytoplasmic
CC domain of G2 to ensure that only the fully assembled, tripartite GP
CC complex is transported for virion assembly. {ECO:0000255|HAMAP-
CC Rule:MF_04084}.
CC -!- SUBCELLULAR LOCATION: [Stable signal peptide]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- DOMAIN: The cytoplasmic domain of GP2 plays a role in ER location. It
CC also contains a zinc-binding domain that allows SSP retention in the
CC GPC complex by accepting a cysteine from SSP as the fourth ligand.
CC {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. GP-C
CC polyprotein is cleaved in the endoplasmic reticulum by the host
CC protease MBTPS1. Only cleaved glycoprotein is incorporated into
CC virions. {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- PTM: The SSP remains stably associated with the GP complex following
CC cleavage by signal peptidase and plays crucial roles in the trafficking
CC of GP through the secretory pathway. {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- SIMILARITY: Belongs to the arenaviridae GPC protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04084}.
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DR EMBL; X52400; CAA36645.1; -; Genomic_RNA.
DR PIR; A43492; A43492.
DR SMR; P17332; -.
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:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
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-UniRule.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
DR Gene3D; 2.20.28.180; -; 1.
DR HAMAP; MF_04084; ARENA_GPC; 1.
DR InterPro; IPR001535; Arena_glycoprot.
DR InterPro; IPR043015; Arena_glycoprot_zinc-bd.
DR Pfam; PF00798; Arena_glycoprot; 1.
DR PIRSF; PIRSF004028; GPC_ArenaV; 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 cell membrane; Host endoplasmic reticulum; Host Golgi apparatus;
KW Host membrane; Host-virus interaction; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell; Zinc.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CHAIN 2..490
FT /note="Pre-glycoprotein polyprotein GP complex"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000353852"
FT CHAIN 2..58
FT /note="Stable signal peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000353853"
FT CHAIN 59..258
FT /note="Glycoprotein G1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000036599"
FT CHAIN 259..490
FT /note="Glycoprotein G2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000036600"
FT TOPO_DOM 2..17
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TRANSMEM 18..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TOPO_DOM 33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TOPO_DOM 54..58
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TOPO_DOM 59..431
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TOPO_DOM 453..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 454
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 456
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 462
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 466
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 474
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 476
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT SITE 58..59
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT SITE 258..259
FT /note="Cleavage; by host MBTPS1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 85..230
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 117..154
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 179..211
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 278..291
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 300..309
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 363..384
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
SQ SEQUENCE 490 AA; 55839 MW; F1E775E219C766B8 CRC64;
MGQIVTFFQE VPHVIEEVMN IVLIALSILA ILKGLYNVAT CGLIGLVTFL LLSGRSCSLI
YKGTYELQTL ELNMETLNMT MPLSCTKNNS HHYIRVGNET GLELTLTNTS ILNHKFCNLS
DAHKRNLYDH SLMSIISTFH LSIPNFNQYE AMSCDFNGGK ITVQYNLSHS FAVDAAGHCG
TLANGVLQTF MRMAWGGSYI ALDSGRGNWD CIMTSYQYLI IQNTTWDDHC QFSRPSPIGY
LGLLSQRTRD IYISRRLLGT FTWTLSDSEG NETPGGYCLT RWMLIEAELK CFGNTAVAKC
NEKHDEEFCD MLRLFDFNKQ AIRRLKTEAQ MSIQLINKAV NALINDQLIM KNHLRDIMGI
PYCNYSRYWY LNHTSTGKTS LPRCWLISNG SYLNETKFSD DIEQQADNMI TEMLQKEYID
RQGKTPLGLV DLFVFSTSFY LISIFLHLVK IPTHRHIVGK PCPKPHRLNH MGICSCGLYK
QPGVPVRWKR
