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GLYC_PIARV
ID   GLYC_PIARV              Reviewed;         503 AA.
AC   P03540;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 100.
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   Pichinde mammarenavirus (PICV) (Pichind mammarenavirus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX   NCBI_TaxID=2169993;
OH   NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=530178; Nephelomys albigularis (Tomes's rice rat) (Oryzomys albigularis).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6492264; DOI=10.1128/jvi.52.3.897-904.1984;
RA   Auperin D.D., Romanowski V., Galinski M., Bishop D.H.L.;
RT   "Sequencing studies of pichinde arenavirus S RNA indicate a novel coding
RT   strategy, an ambisense viral S RNA.";
RL   J. Virol. 52:897-904(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2435460; DOI=10.1007/978-3-642-71683-6_2;
RA   Bishop D.H.L., Auperin D.D.;
RT   "Arenavirus gene structure and organization.";
RL   Curr. Top. Microbiol. Immunol. 133:5-17(1987).
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; K02734; AAA46824.1; -; Genomic_RNA.
DR   EMBL; M16735; AAA46827.1; -; Genomic_RNA.
DR   PIR; A04149; QQXPGP.
DR   RefSeq; YP_138543.1; NC_006447.1.
DR   SMR; P03540; -.
DR   GeneID; 5075743; -.
DR   KEGG; vg:5075743; -.
DR   Proteomes; UP000201514; 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   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..503
FT                   /note="Pre-glycoprotein polyprotein GP complex"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT                   /id="PRO_0000353862"
FT   CHAIN           2..58
FT                   /note="Stable signal peptide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT                   /id="PRO_0000353863"
FT   CHAIN           59..273
FT                   /note="Glycoprotein G1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT                   /id="PRO_0000036609"
FT   CHAIN           274..503
FT                   /note="Glycoprotein G2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT                   /id="PRO_0000036610"
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..446
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   TOPO_DOM        468..503
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         469
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   BINDING         471
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   BINDING         477
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   BINDING         481
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   BINDING         489
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   BINDING         491
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            273..274
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        67
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        379
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        404
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   CARBOHYD        409
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   DISULFID        86..248
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   DISULFID        293..306
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   DISULFID        315..324
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT   DISULFID        378..399
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
SQ   SEQUENCE   503 AA;  57279 MW;  17740E092B450044 CRC64;
     MGQIVTLIQS IPEVLQEVFN VALIIVSVLC IVKGFVNLMR CGLFQLVTFL ILSGRSCDSM
     MIDRRHNLTH VEFNLTRMFD NLPQSCSKNN THHYYKGPSN TTWGIELTLT NTSIANETSG
     NFSNIGSLGY GNISNCDRTR EAGHTLKWLL NELHFNVLHV TRHIGARCKT VEGAGVLIQY
     NLTVGDRGGE VGRHLIASLA QIIGDPKIAW VGKCFNNCSG DTCRLTNCEG GTHYNFLIIQ
     NTTWENHCTY TPMATIRMAL QRTAYSSVSR KLLGFFTWDL SDSSGQHVPG GYCLEQWAII
     WAGIKCFDNT VMAKCNKDHN EEFCDTMRLF DFNQNAIKTL QLNVENSLNL FKKTINGLIS
     DSLVIRNSLK QLAKIPYCNY TKFWYINDTI TGRHSLPQCW LVHNGSYLNE THFKNDWLWE
     SQNLYNEMLM KEYEERQGKT PLALTDICFW SLVFYTITVF LHIVGIPTHR HIIGDGCPKP
     HRITRNSLCS CGYYKYQRNL TNG
 
 
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