Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pre-glycoprotein polyprotein GP complex

Gene

GPC

Organism
Junin mammarenavirus (JUNV) (Junn mammarenavirus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Stable signal peptide (SSP) is cleaved but is apparently retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational cleavage of GP1 and GP2, glycoprotein transport to the cell plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion (By similarity).By similarity
Glycoprotein G1 mediates virus attachment to host TFRC. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis.1 Publication
Glycoprotein G2 is a class I viral fusion protein, that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversable conformational changes induced upon acidification in the endosome (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus endocytosis by host, Virus entry into host cell

Protein family/group databases

TCDBi1.G.8.1.2. the arenavirus fusion protein (av-fp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-glycoprotein polyprotein GP complex
Cleaved into the following 3 chains:
Stable signal peptide
Short name:
SSP
Glycoprotein G1
Short name:
GP1
Glycoprotein G2
Short name:
GP2
Gene namesi
Name:GPC
Synonyms:GP-C
OrganismiJunin mammarenavirus (JUNV) (Junn mammarenavirus)
Taxonomic identifieri11619 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesArenaviridaeMammarenavirus
Virus hostiAkodon azarae (Azara's grass mouse) [TaxID: 29095]
Bolomys [TaxID: 10080]
Calomys laucha (Small vesper mouse) [TaxID: 56211]
Calomys musculinus (Drylands vesper mouse) [TaxID: 56212]
Homo sapiens (Human) [TaxID: 9606]

Subcellular locationi

Glycoprotein G2 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1716ExtracellularSequence analysisAdd
BLAST
Transmembranei18 – 3215HelicalSequence analysisAdd
BLAST
Topological domaini33 – 331CytoplasmicSequence analysis
Transmembranei34 – 5320HelicalSequence analysisAdd
BLAST
Topological domaini54 – 585ExtracellularSequence analysis
Topological domaini59 – 424366ExtracellularSequence analysisAdd
BLAST
Transmembranei425 – 44521HelicalSequence analysisAdd
BLAST
Topological domaini446 – 48540CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21G → A: Reduces membrane fusion activity. No effect on GP complex formation. 1 Publication
Mutagenesisi476 – 4772KK → AA: Induces transport to the cell surface in the absence of SSP. No effect on SSP binding. 1 Publication
Mutagenesisi482 – 4832RR → AA: Induces transport to the cell surface in the absence of SSP. No effect on SSP binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedSequence analysis
Chaini2 – 485484Pre-glycoprotein polyprotein GP complexPRO_0000353850Add
BLAST
Chaini2 – 5857Stable signal peptideBy similarityPRO_0000353851Add
BLAST
Chaini59 – 251193Glycoprotein G1By similarityPRO_0000036597Add
BLAST
Chaini252 – 485234Glycoprotein G2By similarityPRO_0000036598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by host1 Publication
Glycosylationi95 – 951N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi105 – 1051N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi166 – 1661N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi178 – 1781N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi357 – 3571N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi365 – 3651N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi382 – 3821N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi387 – 3871N-linked (GlcNAc...); by hostSequence analysis

Post-translational modificationi

Cleavage by signal peptidase releases the stable signal peptide, which stays associated to the glycoprotein complex through interaction with glycoprotein G2.
Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei58 – 592Cleavage; by host signal peptidaseBy similarity
Sitei251 – 2522Cleavage; by host MBTPS1By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Myristate

Interactioni

Subunit structurei

Glycoprotein G1 is a homotrimer; disulfide-linked. Glycoprotein G2 is a homotrimer. GP2 homotrimers bind with GP1 homotrimers to form, with the stable signal peptide, the GP-complex. Interacts with host TFRC. GP-complex interacts with protein Z, which interacts with ribonucleocapsid; these interactions supposely induce virion budding (By similarity).By similarity

Structurei

Secondary structure

1
485
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi90 – 945Combined sources
Turni95 – 973Combined sources
Beta strandi98 – 1036Combined sources
Beta strandi106 – 1149Combined sources
Turni120 – 1223Combined sources
Beta strandi123 – 1286Combined sources
Helixi129 – 1357Combined sources
Helixi139 – 15113Combined sources
Turni156 – 1583Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi175 – 1784Combined sources
Helixi183 – 1853Combined sources
Helixi186 – 19914Combined sources
Beta strandi214 – 2196Combined sources
Beta strandi447 – 4493Combined sources
Beta strandi451 – 4544Combined sources
Beta strandi465 – 4673Combined sources
Turni468 – 4714Combined sources
Beta strandi480 – 4823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L0ZNMR-A445-485[»]
5EN2X-ray1.82C87-227[»]
ProteinModelPortaliP26313.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26313.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni476 – 4772Involved in ER localization
Regioni482 – 4832Involved in ER localization

Domaini

The cytoplasmic domain of GP2 binds to the SSP.By similarity

Sequence similaritiesi

Belongs to the arenaviridae GPC protein family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR001535. Arena_glycoprot.
[Graphical view]
PfamiPF00798. Arena_glycoprot. 2 hits.
[Graphical view]
PIRSFiPIRSF004028. GPC_ArenaV. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26313-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQFISFMQE IPTFLQEALN IALVAVSLIA IIKGVVNLYK SGLFQFFVFL
60 70 80 90 100
ALAGRSCTEE AFKIGLHTEF QTVSFSMVGL FSNNPHDLPL LCTLNKSHLY
110 120 130 140 150
IKGGNASFKI SFDDIAVLLP EYDVIIQHPA DMSWCSKSDD QIWLSQWFMN
160 170 180 190 200
AVGHDWYLDP PFLCRNRTKT EGFIFQVNTS KTGINENYAK KFKTGMHHLY
210 220 230 240 250
REYPDSCLDG KLCLMKAQPT SWPLQCPLDH VNTLHFLTRG KNIQLPRRSL
260 270 280 290 300
KAFFSWSLTD SSGKDTPGGY CLEEWMLVAA KMKCFGNTAV AKCNLNHDSE
310 320 330 340 350
FCDMLRLFDY NKNAIKTLND ETKKQVNLMG QTINALISDN LLMKNKIREL
360 370 380 390 400
MSVPYCNYTK FWYVNHTLSG QHSLPRCWLI KNNSYLNISD FRNDWILESD
410 420 430 440 450
FLISEMLSKE YSDRQGKTPL TLVDICFWST VFFTASLFLH LVGIPTHRHI
460 470 480
RGEACPLPHR LNSLGGCRCG KYPNLKKPTV WRRGH
Length:485
Mass (Da):55,607
Last modified:July 19, 2004 - v2
Checksum:iEE57D860FDD17F05
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10072 Genomic RNA. Translation: BAA00964.2.
PIRiJT0978. VGXPJV.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10072 Genomic RNA. Translation: BAA00964.2.
PIRiJT0978. VGXPJV.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L0ZNMR-A445-485[»]
5EN2X-ray1.82C87-227[»]
ProteinModelPortaliP26313.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi1.G.8.1.2. the arenavirus fusion protein (av-fp) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP26313.

Family and domain databases

InterProiIPR001535. Arena_glycoprot.
[Graphical view]
PfamiPF00798. Arena_glycoprot. 2 hits.
[Graphical view]
PIRSFiPIRSF004028. GPC_ArenaV. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular organization of Junin virus S RNA: complete nucleotide sequence, relationship with other members of the Arenaviridae and unusual secondary structures."
    Ghiringhelli P.D., Rivera-Pomar R.V., Lozano M.E., Grau O., Romanowski V.
    J. Gen. Virol. 72:2129-2141(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: MC2.
  2. Romanowski V.
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 43-51; 58-80 AND 143.
  3. "The signal peptide of the Junin arenavirus envelope glycoprotein is myristoylated and forms an essential subunit of the mature G1-G2 complex."
    York J., Romanowski V., Lu M., Nunberg J.H.
    J. Virol. 78:10783-10792(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, MYRISTOYLATION, MUTAGENESIS OF GLY-2.
  4. "Role of the stable signal peptide and cytoplasmic domain of G2 in regulating intracellular transport of the Junin virus envelope glycoprotein complex."
    Agnihothram S.S., York J., Nunberg J.H.
    J. Virol. 80:5189-5198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 476-LYS-LYS-477 AND 482-ARG-ARG-483.
  5. "Transferrin receptor 1 is a cellular receptor for New World haemorrhagic fever arenaviruses."
    Radoshitzky S.R., Abraham J., Spiropoulou C.F., Kuhn J.H., Nguyen D., Li W., Nagel J., Schmidt P.J., Nunberg J.H., Andrews N.C., Farzan M., Choe H.
    Nature 446:92-96(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST TFRC.
  6. "Involvement of cellular proteins in Junin arenavirus entry."
    Martinez M.G., Forlenza M.B., Candurra N.A.
    Biotechnol. J. 4:866-870(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiGLYC_JUNIN
AccessioniPrimary (citable) accession number: P26313
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 19, 2004
Last modified: March 16, 2016
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.