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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)DescriptionActionsGraphical viewLength
Topological domaini2 – 17ExtracellularSequence analysisAdd BLAST16
Transmembranei18 – 32HelicalSequence analysisAdd BLAST15
Topological domaini33CytoplasmicSequence analysis1
Transmembranei34 – 53HelicalSequence analysisAdd BLAST20
Topological domaini54 – 58ExtracellularSequence analysis5
Topological domaini59 – 424ExtracellularSequence analysisAdd BLAST366
Transmembranei425 – 445HelicalSequence analysisAdd BLAST21
Topological domaini446 – 485CytoplasmicSequence analysisAdd BLAST40

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)DescriptionActionsGraphical viewLength
Mutagenesisi2G → A: Reduces membrane fusion activity. No effect on GP complex formation. 1 Publication1
Mutagenesisi476 – 477KK → AA: Induces transport to the cell surface in the absence of SSP. No effect on SSP binding. 1 Publication2
Mutagenesisi482 – 483RR → AA: Induces transport to the cell surface in the absence of SSP. No effect on SSP binding. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedSequence analysis
ChainiPRO_00003538502 – 485Pre-glycoprotein polyprotein GP complexAdd BLAST484
ChainiPRO_00003538512 – 58Stable signal peptideBy similarityAdd BLAST57
ChainiPRO_000003659759 – 251Glycoprotein G1By similarityAdd BLAST193
ChainiPRO_0000036598252 – 485Glycoprotein G2By similarityAdd BLAST234

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by host1 Publication1
Glycosylationi95N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi105N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi166N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi178N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi357N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi365N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi382N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi387N-linked (GlcNAc...); by hostSequence analysis1

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)DescriptionActionsGraphical viewLength
Sitei58 – 59Cleavage; by host signal peptidaseBy similarity2
Sitei251 – 252Cleavage; by host MBTPS1By similarity2

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

1485
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi90 – 94Combined sources5
Turni95 – 97Combined sources3
Beta strandi98 – 103Combined sources6
Beta strandi106 – 114Combined sources9
Turni120 – 122Combined sources3
Beta strandi123 – 128Combined sources6
Helixi129 – 135Combined sources7
Helixi139 – 151Combined sources13
Turni156 – 158Combined sources3
Beta strandi162 – 164Combined sources3
Beta strandi175 – 178Combined sources4
Helixi183 – 185Combined sources3
Helixi186 – 199Combined sources14
Beta strandi214 – 219Combined sources6
Beta strandi447 – 449Combined sources3
Beta strandi451 – 454Combined sources4
Beta strandi465 – 467Combined sources3
Turni468 – 471Combined sources4
Beta strandi480 – 482Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L0ZNMR-A445-485[»]
5EN2X-ray1.82C87-227[»]
ProteinModelPortaliP26313.
SMRiP26313.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26313.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni476 – 477Involved in ER localization2
Regioni482 – 483Involved in ER localization2

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L0ZNMR-A445-485[»]
5EN2X-ray1.82C87-227[»]
ProteinModelPortaliP26313.
SMRiP26313.
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...

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: November 2, 2016
This is version 80 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.