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Protein

Pre-glycoprotein polyprotein GP complex

Gene

GPC

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

Functioni

Glycoprotein G2: 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 irreversible conformational changes induced upon acidification in the endosome.UniRule annotation
Stable signal peptide (SSP): cleaved and functions as a signal peptide. In addition, it is also retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.UniRule annotation
Glycoprotein G1: interacts with the host receptor (By similarity). Mediates virus attachment to host TFRC. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis (PubMed:17287727).UniRule annotation2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi57Zinc 1UniRule annotation1 Publication1
Metal bindingi447Zinc 2; via tele nitrogenUniRule annotation1 Publication1
Metal bindingi449Zinc 2; via tele nitrogenUniRule annotation1 Publication1
Metal bindingi455Zinc 2UniRule annotation1 Publication1
Metal bindingi459Zinc 1; via pros nitrogenUniRule annotation1 Publication1
Metal bindingi467Zinc 1UniRule annotation1 Publication1
Metal bindingi469Zinc 1UniRule annotation1 Publication1
Metal bindingi485Zinc 2; via tele nitrogenUniRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processFusion 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
LigandMetal-binding, Zinc

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 complexUniRule annotation
Short name:
Pre-GP-CUniRule annotation
Cleaved into the following 3 chains:
Stable signal peptideUniRule annotation
Short name:
SSPUniRule annotation
Glycoprotein G1UniRule annotation
Short name:
GP1UniRule annotation
Glycoprotein G2UniRule annotation
Short name:
GP2UniRule annotation
Gene namesi
Name:GPCUniRule annotation
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]
Proteomesi
  • UP000127886 Componenti: Genome

Subcellular locationi

Glycoprotein G1 :
  • Virion membrane UniRule annotation; Peripheral membrane protein UniRule annotation
  • Host endoplasmic reticulum membrane UniRule annotation; Peripheral membrane protein UniRule annotation
  • Host Golgi apparatus membrane UniRule annotation; Peripheral membrane protein UniRule annotation
  • Host cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation
Glycoprotein G2 :
  • Virion membrane UniRule annotation; Single-pass membrane protein UniRule annotation
  • Host endoplasmic reticulum membrane UniRule annotation; Single-pass membrane protein UniRule annotation
  • Host Golgi apparatus membrane UniRule annotation; Single-pass membrane protein UniRule annotation
  • Host cell membrane UniRule annotation; Single-pass membrane protein UniRule annotation
  • Note: Binding to the stable signal peptide masks endogenous ER localization signals in the cytoplasmic domain of G2 to ensure that only the fully assembled, tripartite GP complex is transported for virion assembly.UniRule annotation
Stable signal peptide :
  • Virion membrane UniRule annotation; Multi-pass membrane protein UniRule annotation
  • Host endoplasmic reticulum membrane UniRule annotation; Multi-pass membrane protein UniRule annotation
  • Host Golgi apparatus membrane UniRule annotation; Multi-pass membrane protein UniRule annotation
  • Host cell membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 17ExtracellularUniRule annotationAdd BLAST16
Transmembranei18 – 32HelicalUniRule annotationAdd BLAST15
Topological domaini33CytoplasmicUniRule annotation1
Transmembranei34 – 53HelicalUniRule annotationAdd BLAST20
Topological domaini54 – 58ExtracellularUniRule annotation5
Topological domaini59 – 424ExtracellularUniRule annotationAdd BLAST366
Transmembranei425 – 445HelicalUniRule annotationAdd BLAST21
Topological domaini446 – 485CytoplasmicUniRule annotationAdd BLAST40

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host endoplasmic reticulum, Host Golgi apparatus, 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 methionineiRemoved; by hostUniRule annotation1 Publication
ChainiPRO_00003538502 – 485Pre-glycoprotein polyprotein GP complexUniRule annotationAdd BLAST484
ChainiPRO_00003538512 – 58Stable signal peptideUniRule annotationAdd BLAST57
ChainiPRO_000003659759 – 251Glycoprotein G1UniRule annotationAdd BLAST193
ChainiPRO_0000036598252 – 485Glycoprotein G2UniRule annotationAdd BLAST234

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostUniRule annotation1 Publication1
Disulfide bondi92 ↔ 226UniRule annotation1 Publication
Glycosylationi95N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi105N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication1
Disulfide bondi135 ↔ 164UniRule annotation1 Publication
Glycosylationi166N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication1
Glycosylationi178N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication1
Disulfide bondi207 ↔ 213UniRule annotation1 Publication
Disulfide bondi271 ↔ 284UniRule annotation
Disulfide bondi293 ↔ 302UniRule annotation
Disulfide bondi356 ↔ 377UniRule annotation
Glycosylationi357N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi365N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi382N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi387N-linked (GlcNAc...) asparagine; by hostUniRule annotation1

Post-translational modificationi

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.UniRule annotation
The SSP remains stably associated with the GP complex following cleavage by signal peptidase and plays crucial roles in the trafficking of GP through the secretory pathway.UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei58 – 59Cleavage; by host signal peptidaseUniRule annotation2
Sitei251 – 252Cleavage; by host MBTPS1UniRule annotation2

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Myristate

PTM databases

iPTMnetiP26313

Interactioni

Subunit structurei

Glycoprotein G1: homotetramer; disulfide-linked (By similarity). Interacts with host TFRC (PubMed:17287727). Glycoprotein G2: homotetramer. GP2 homotetramers bind through ionic interactions with GP1 homotetramers to form the GP complex together with the stable signal peptide. The GP-C polyprotein interacts with the host protease MBTPS1/SKI-1 resulting in the polyprotein processing.UniRule annotation2 Publications

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 plays a role in ER location. It also contains a zinc-binding domain that allows SSP retention in the GPC complex by accepting 'Cys-57' from SSP as the fourth ligand.UniRule annotation1 Publication

Sequence similaritiesi

Belongs to the arenaviridae GPC protein family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

HAMAPiMF_04084 ARENA_GPC, 1 hit
InterProiView protein in InterPro
IPR001535 Arena_glycoprot
PfamiView protein in Pfam
PF00798 Arena_glycoprot, 2 hits
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

Similar proteinsi

Entry informationi

Entry nameiGLYC_JUNIN
AccessioniPrimary (citable) accession number: P26313
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 19, 2004
Last modified: April 25, 2018
This is version 87 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome
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Main funding by: National Institutes of Health