GLYC_MOPEI
ID GLYC_MOPEI Reviewed; 489 AA.
AC P19240;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 Mopeia virus (MOPV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=11629;
OH NCBI_TaxID=10112; Mastomys natalensis (African soft-furred rat) (Praomys natalensis).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=800150;
RX PubMed=1989384; DOI=10.1016/0042-6822(91)90068-m;
RA Wilson S.M., Clegg J.C.S.;
RT "Sequence analysis of the S RNA of the African arenavirus Mopeia: an
RT unusual secondary structure feature in the intergenic region.";
RL Virology 180:543-552(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; M33879; AAC08700.1; -; Genomic_RNA.
DR PIR; A38546; VGXPMV.
DR SMR; P19240; -.
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..489
FT /note="Pre-glycoprotein polyprotein GP complex"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000353860"
FT CHAIN 2..58
FT /note="Stable signal peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000353861"
FT CHAIN 59..257
FT /note="Glycoprotein G1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000036607"
FT CHAIN 258..489
FT /note="Glycoprotein G2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000036608"
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..430
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TOPO_DOM 452..489
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 453
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 461
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 473
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 475
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 257..258
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 222
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 85..229
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 117..154
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 179..210
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 277..290
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 299..308
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 362..383
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
SQ SEQUENCE 489 AA; 55987 MW; B188EBF327E170B1 CRC64;
MGQIVTFFQE VPHILEEVMN IVLMTLSILA ILKGIYNVMT CGIIGLITFL FLCGRSCSSI
YKDNYEFFSL DLDMSSLNAT MPLSCSKNNS HHYIQVGNET GLELTLTNTS IINHKFCNLS
DAHRRNLYDK ALMSILTTFH LSIPDFNQYE AMSCDFNGGK ISVQYNLSHS NYVDAGNHCG
TIANGIMDVF RRMYWSTSLS VASDISGTQC IQTDYKYLII QNTSWEDHCM FSRPSPMGFL
SLLSQRTRNF YISRRLLGLF TWTLSDSEGN DMPGGYCLTR SMLIGLDLKC FGNTAIAKCN
QAHDEEFCDM LRLFDFNKQA ISKLRSEVQQ SINLINKAVN ALINDQLVMR NHLRDLMGIP
YCNYSKFWYL NDTRTGRTSL PKCWLVTNGS YLNETQFSTE IEQEANNMFT DMLRKEYEKR
QSTTPLGLVD LFVFSTSFYL ISVFLHLIKI PTHRHIKGKP CPKPHRLNHM AICSCGFYKQ
PGLPTQWKR
