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Protein

Pre-glycoprotein polyprotein GP complex

Gene

GPC

Organism
Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 annotation1 Publication
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 annotation1 Publication
Glycoprotein G1: interacts with the host receptor (By similarity). Mediates virus attachment to host receptor alpha-dystroglycan DAG1. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis (PubMed:9851928).UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi57Zinc 1UniRule annotation1
Metal bindingi461Zinc 2; via tele nitrogenUniRule annotation1
Metal bindingi463Zinc 2; via tele nitrogenUniRule annotation1
Metal bindingi469Zinc 2UniRule annotation1
Metal bindingi473Zinc 1; via pros nitrogenUniRule annotation1
Metal bindingi481Zinc 1UniRule annotation1
Metal bindingi483Zinc 1UniRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>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

Transport Classification Database

More...
TCDBi
1.G.8.1.1 the arenavirus fusion protein (av-fp) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GPCUniRule annotation
Synonyms:GP-C
Ordered Locus Names:Segment S
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiLymphocytic choriomeningitis virus (strain Armstrong) (LCMV)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri11624 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesArenaviridaeMammarenavirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiHomo sapiens (Human) [TaxID: 9606]
Mesocricetus auratus (Golden hamster) [TaxID: 10036]
Mus musculus (Mouse) [TaxID: 10090]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000121528 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome
  • UP000002474 Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Glycoprotein G1 :
Glycoprotein G2 :
Stable signal peptide :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini2 – 17ExtracellularUniRule annotationAdd BLAST16
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei18 – 32HelicalUniRule annotationAdd BLAST15
Topological domaini33CytoplasmicUniRule annotation1
Transmembranei34 – 53HelicalUniRule annotationAdd BLAST20
Topological domaini54 – 58ExtracellularUniRule annotation5
Topological domaini59 – 438ExtracellularUniRule annotationAdd BLAST380
Transmembranei439 – 459HelicalUniRule annotationAdd BLAST21
Topological domaini460 – 498CytoplasmicUniRule annotationAdd BLAST39

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host endoplasmic reticulum, Host Golgi apparatus, Host membrane, Membrane, Viral envelope protein, Virion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi12P → A: 99% loss of virus infectivity. 1 Publication1
Mutagenesisi12P → G: 96% loss of virus infectivity. 1 Publication1
Mutagenesisi16D → A: More than 99% loss of infectivity; when associated with A-17. 1 Publication1
Mutagenesisi16D → K: More than 99% loss of infectivity; when associated with K-17. 1 Publication1
Mutagenesisi17E → A: More than 99% loss of infectivity; when associated with A-16. 1 Publication1
Mutagenesisi17E → K: More than 99% loss of infectivity; when associated with K-16. 1 Publication1
Mutagenesisi20N → A: 99% loss of infectivity. 1 Publication1
Mutagenesisi20N → K: 91% loss of infectivity. 1 Publication1
Mutagenesisi20N → Q: 98% loss of infectivity. 1 Publication1
Mutagenesisi33K → A: More than 99% loss of infectivity. 1 Publication1
Mutagenesisi33K → D: More than 99% loss of infectivity. 1 Publication1
Mutagenesisi37N → A: 97% loss of infectivity. 1 Publication1
Mutagenesisi37N → K: 92% loss of infectivity. 1 Publication1
Mutagenesisi37N → Q: 7% loss of infectivity. 1 Publication1
Mutagenesisi49F → A: More than 99% loss of infectivity. 1 Publication1
Mutagenesisi49F → L: 95% loss of ionfectivity. 1 Publication1
Mutagenesisi54G → A: More than 99% loss of infectivity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; by hostUniRule annotation
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003562552 – 498Pre-glycoprotein polyprotein GP complexUniRule annotationAdd BLAST497
ChainiPRO_00003562562 – 58Stable signal peptideUniRule annotationAdd BLAST57
ChainiPRO_000003660359 – 265Glycoprotein G1UniRule annotationAdd BLAST207
ChainiPRO_0000036604266 – 498Glycoprotein G2UniRule annotationAdd BLAST233

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine; by hostUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi85N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi92 ↔ 239UniRule annotation
Glycosylationi95N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi114N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi123 ↔ 160UniRule annotation
Glycosylationi124N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi171N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi184 ↔ 220UniRule annotation
Glycosylationi232N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi285 ↔ 298UniRule annotation
Disulfide bondi307 ↔ 316UniRule annotation
Disulfide bondi370 ↔ 391UniRule annotation
Glycosylationi371N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi396N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi401N-linked (GlcNAc...) asparagine; by hostUniRule annotation1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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 annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei58 – 59Cleavage; by host signal peptidaseUniRule annotation2
Sitei265 – 266Cleavage; by host MBTPS1UniRule annotation2

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Myristate

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P09991

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Glycoprotein G1: homotetramer; disulfide-linked (By similarity). Interacts with host DAG1 (PubMed:9851928). 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 (By similarity). GP-complex interacts with protein Z, which interacts with ribonucleocapsid; these interactions may induce virion budding (PubMed:17581989).UniRule annotation3 Publications

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P09991

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P09991

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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 a cysteine from SSP as the fourth ligand.UniRule annotation

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the arenaviridae GPC protein family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

Database of Orthologous Groups

More...
OrthoDBi
VOG0900016T

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_04084 ARENA_GPC, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001535 Arena_glycoprot

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00798 Arena_glycoprot, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF004028 GPC_ArenaV, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P09991-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGQIVTMFEA LPHIIDEVIN IVIIVLIVIT GIKAVYNFAT CGIFALISFL
60 70 80 90 100
LLAGRSCGMY GLKGPDIYKG VYQFKSVEFD MSHLNLTMPN ACSANNSHHY
110 120 130 140 150
ISMGTSGLEL TFTNDSIISH NFCNLTSAFN KKTFDHTLMS IVSSLHLSIR
160 170 180 190 200
GNSNYKAVSC DFNNGITIQY NLTFSDAQSA QSQCRTFRGR VLDMFRTAFG
210 220 230 240 250
GKYMRSGWGW TGSDGKTTWC SQTSYQYLII QNRTWENHCT YAGPFGMSRI
260 270 280 290 300
LLSQEKTKFF TRRLAGTFTW TLSDSSGVEN PGGYCLTKWM ILAAELKCFG
310 320 330 340 350
NTAVAKCNVN HDAEFCDMLR LIDYNKAALS KFKEDVESAL HLFKTTVNSL
360 370 380 390 400
ISDQLLMRNH LRDLMGVPYC NYSKFWYLEH AKTGETSVPK CWLVTNGSYL
410 420 430 440 450
NETHFSDQIE QEADNMITEM LRKDYIKRQG STPLALMDLL MFSTSAYLVS
460 470 480 490
IFLHLVKIPT HRHIKGGSCP KPHRLTNKGI CSCGAFKVPG VKTVWKRR
Length:498
Mass (Da):56,131
Last modified:July 1, 1989 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i11737E3555122CE6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti177A → R in AAA46256 (PubMed:3259346).1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti176D → N in strain: Isolate Armstrong 53b. 1
Natural varianti260F → L in strain: Isolate CTL- and Isolate Armstrong-derived variant Cl13. 1
Natural varianti313A → E in strain: Isolate Armstrong 53b and Isolate Armstrong-derived variant Cl13. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M20869 Genomic RNA Translation: AAA46256.1
AY847350 Genomic RNA Translation: AAX49341.1
DQ361065 Genomic RNA Translation: ABC96001.2

Protein sequence database of the Protein Information Resource

More...
PIRi
A28920 VGXPLA
B26345 VGXPLM

NCBI Reference Sequences

More...
RefSeqi
NP_694851.1, NC_004294.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
956591

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:956591

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20869 Genomic RNA Translation: AAA46256.1
AY847350 Genomic RNA Translation: AAX49341.1
DQ361065 Genomic RNA Translation: ABC96001.2
PIRiA28920 VGXPLA
B26345 VGXPLM
RefSeqiNP_694851.1, NC_004294.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5JWDX-ray2.50C392-400[»]
5JWEX-ray2.40P/Q/R/S92-101[»]
ProteinModelPortaliP09991
SMRiP09991
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi1.G.8.1.1 the arenavirus fusion protein (av-fp) family

Proteomic databases

PRIDEiP09991

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi956591
KEGGivg:956591

Phylogenomic databases

OrthoDBiVOG0900016T

Family and domain databases

HAMAPiMF_04084 ARENA_GPC, 1 hit
InterProiView protein in InterPro
IPR001535 Arena_glycoprot
PfamiView protein in Pfam
PF00798 Arena_glycoprot, 1 hit
PIRSFiPIRSF004028 GPC_ArenaV, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGLYC_LYCVA
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P09991
Secondary accession number(s): Q27V72, Q49K87
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 10, 2018
This is version 96 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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