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GLYC_LATVB
ID   GLYC_LATVB              Reviewed;         515 AA.
AC   Q8B121; Q8B116;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 67.
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   Latino mammarenavirus (isolate Rat/Bolivia/MARU 1924/1965) (LATV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX   NCBI_TaxID=45221;
OH   NCBI_TaxID=56210; Calomys callosus (Large vesper mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12504568; DOI=10.1006/viro.2002.1695;
RA   Archer A.M., Rico-Hesse R.;
RT   "High genetic divergence and recombination in Arenaviruses from the
RT   Americas.";
RL   Virology 304:274-281(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12207889; DOI=10.1016/s0006-291x(02)02053-3;
RA   Charrel R.N., Feldmann H., Fulhorst C.F., Khelifa R., de Chesse R.,
RA   de Lamballerie X.;
RT   "Phylogeny of New World arenaviruses based on the complete coding sequences
RT   of the small genomic segment identified an evolutionary lineage produced by
RT   intrasegmental recombination.";
RL   Biochem. Biophys. Res. Commun. 296:1118-1124(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=18602020; DOI=10.1016/j.mib.2008.06.001;
RA   Charrel R.N., de Lamballerie X., Emonet S.;
RT   "Phylogeny of the genus Arenavirus.";
RL   Curr. Opin. Microbiol. 11:362-368(2008).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH HOST DAG1.
RX   PubMed=11967329; DOI=10.1128/jvi.76.10.5140-5146.2002;
RA   Spiropoulou C.F., Kunz S., Rollin P.E., Campbell K.P., Oldstone M.B.;
RT   "New World arenavirus clade C, but not clade A and B viruses, utilizes
RT   alpha-dystroglycan as its major receptor.";
RL   J. Virol. 76:5140-5146(2002).
CC   -!- FUNCTION: [Glycoprotein G1]: Interacts with the host receptor (By
CC       similarity). Mediates virus attachment to host receptor alpha-
CC       dystroglycan DAG1. This attachment induces virion internalization
CC       predominantly through clathrin- and caveolin-independent endocytosis
CC       (PubMed:11967329). {ECO:0000255|HAMAP-Rule:MF_04084,
CC       ECO:0000269|PubMed:11967329}.
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   -!- 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; AF485259; AAN09940.1; -; Genomic_RNA.
DR   EMBL; AF512830; AAN32959.1; -; Genomic_RNA.
DR   RefSeq; YP_001936021.1; NC_010758.1.
DR   SMR; Q8B121; -.
DR   GeneID; 6334523; -.
DR   KEGG; vg:6334523; -.
DR   Proteomes; UP000009262; 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; 1.
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; Reference proteome; Transmembrane;
KW   Transmembrane helix; 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..515
FT                   /note="Pre-glycoprotein polyprotein GP complex"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT                   /id="PRO_0000361596"
FT   CHAIN           2..58
FT                   /note="Stable signal peptide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT                   /id="PRO_0000361597"
FT   CHAIN           59..280
FT                   /note="Glycoprotein G1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT                   /id="PRO_0000361598"
FT   CHAIN           281..515
FT                   /note="Glycoprotein G2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT                   /id="PRO_0000361599"
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..453
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   TRANSMEM        454..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   TOPO_DOM        475..515
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         476
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   BINDING         478
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   BINDING         484
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   BINDING         488
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="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   BINDING         498
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            280..281
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        75
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        386
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   CARBOHYD        416
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   DISULFID        87..255
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   DISULFID        300..313
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   DISULFID        322..331
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   DISULFID        385..406
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   VARIANT         269
FT                   /note="P -> S"
SQ   SEQUENCE   515 AA;  59232 MW;  9A247EC412383128 CRC64;
     MGQVIGFFQS LPEIINEALN IALICVALLA TIKGMVNIWK SGLIQLLFFL TLAGRSCSHS
     FTIGRFHEFQ SVTVNFTQFM SYAPSSCSVN NTHHYFKGPQ NTTWGLELTL TNESMINITN
     SMRVFTNIHH NVTNCVQNIS EHEGVLKWLL ETMHLSISKP GKHIAPVMCE RQKGLLIEYN
     LTMTKDHHPN YWNQVLYGLA KLLGSSKRLW FGACNKADCQ MQSDHQHIKC NYSNCKGYTS
     FKYLIIQNTT WENHCEYNHL NTIHLLMSPI GQSFITRRLQ AFLTWTLSDA LGNDLPGGYC
     LEQWAVVWFG IKCFDNTAMA KCNQNHDSEF CDMLRLFDYN RNAIQSLNDQ SQARLNLLTN
     TINSLVSDNL LMKNKLRELM NVPYCNYTRF WFINDTKNGR HTLPQCWLVS DGSYLNETRF
     RTQWLSESNS LYTEMLTEEY EKRQGRTPLS LVDLCFWSTL FYISTLFAHL VGFPTHRHLI
     GEGCPKPHRL TGSGICSCGH YGIPGKPVRW TKMSR
 
 
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