GLYC_MACHU
ID GLYC_MACHU Reviewed; 496 AA.
AC Q6IUF7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
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 Machupo virus (MACV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=11628;
OH NCBI_TaxID=56210; Calomys callosus (Large vesper mouse).
OH NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Hajjaj A., Chain P.S.G., Smith K.L., Imbro P.M., Malfatti S.A.;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Jahrling P.B., Geisbert J., Ibrahim M.S.;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Milazzo M.L., Cajimat M.N.B., Rollin P.E., Dodsley N.A., Nichol S.T.,
RA Bowen M.D., Ksiazek T.G., Fulhorst C.F.;
RT "Genetic diversity of Machupo virus (family Arenaviridae): implications for
RT synthetic antibody therapy for Bolivian hemorrhagic fever.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND INTERACTION WITH HOST TFRC.
RX PubMed=17287727; DOI=10.1038/nature05539;
RA Radoshitzky S.R., Abraham J., Spiropoulou C.F., Kuhn J.H., Nguyen D.,
RA Li W., Nagel J., Schmidt P.J., Nunberg J.H., Andrews N.C., Farzan M.,
RA Choe H.;
RT "Transferrin receptor 1 is a cellular receptor for New World haemorrhagic
RT fever arenaviruses.";
RL Nature 446:92-96(2007).
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 (By
CC similarity). Mediates virus attachment to host TFRC. This attachment
CC induces virion internalization predominantly through clathrin-mediated
CC endocytosis (PubMed:17287727). {ECO:0000255|HAMAP-Rule:MF_04084,
CC ECO:0000269|PubMed:17287727}.
CC -!- SUBUNIT: [Glycoprotein G1]: Homotetramer; disulfide-linked (By
CC similarity). Interacts with host TFRC (PubMed:17287727).
CC {ECO:0000255|HAMAP-Rule:MF_04084, ECO:0000269|PubMed:17287727}.
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; AY624355; AAT45081.1; -; Genomic_RNA.
DR EMBL; AY924202; AAX99327.1; -; Genomic_RNA.
DR SMR; Q6IUF7; -.
DR Proteomes; UP000009263; 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: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; 2.
DR PIRSF; PIRSF004028; GPC_ArenaV; 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 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..496
FT /note="Pre-glycoprotein polyprotein GP complex"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000361600"
FT CHAIN 2..58
FT /note="Stable signal peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000361601"
FT CHAIN 59..262
FT /note="Glycoprotein G1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000361602"
FT CHAIN 263..496
FT /note="Glycoprotein G2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000361603"
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..435
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TOPO_DOM 457..496
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 458
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 460
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="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 470
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 478
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 480
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 496
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 262..263
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 83
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 137
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 178
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 376
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 CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 92..237
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 135..164
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 207..213
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 282..295
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 304..313
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 367..388
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
SQ SEQUENCE 496 AA; 57041 MW; 3899C19FD1988793 CRC64;
MGQLISFFQE IPVFLQEALN IALVAVSLIA VIKGIINLYK SGLFQFIFFL LLAGRSCSDG
TFKIGLHTEF QSVTLTMQRL LANHSNELPS LCMLNNSFYY MKGGVNTFLI RVSDISVLMK
EHDVSIYEPE DLGNCLNKSD SSWAIHWFSN ALGHDWLMDP PMLCRNKTKK EGSNIQFNIS
KADDVRVYGK KIRNGMRHLF RGFHDPCEEG KKCYLTINQC GDPSSFDYCG MDHLSKCQFD
HVNTLHFLVR SKTHLNFERS LKAFFSWSLT DSSGKDMPGG YCLEEWMLIA AKMKCFGNTA
VAKCNQNHDS EFCDMLRLFD YNKNAIKTLN DESKKEINLL SQTVNALISD NLLMKNKIKE
LMSIPYCNYT KFWYVNHTLT GQHTLPRCWL IRNGSYLNTS EFRNDWILES DHLISEMLSK
EYAERQGKTP ITLVDICFWS TVFFTASLFL HLVGIPTHRH LKGEACPLPH KLDSFGGCRC
GKYPRLRKPT IWHKRH
