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

Envelope glycoprotein gp95

Gene

env

Organism
Avian leukosis virus RSA (RSV-SRA) (Rous sarcoma virus (strain Schmidt-Ruppin A))
Status
Reviewed-Annotation score:

Annotation score:4 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

The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).By similarity
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).By similarity

<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 - 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 cell membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus entry into host cell

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.G.12.1.1 the avian leukosis virus gp95 fusion protein (alv-gp95) 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:
Envelope glycoprotein gp95
Alternative name(s):
Env polyprotein
Cleaved into the following 2 chains:
Surface protein
Short name:
SU
Alternative name(s):
Glycoprotein 85
Short name:
gp85
Transmembrane protein
Short name:
TM
Alternative name(s):
Glycoprotein 37
Short name:
gp37
<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:env
<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>OrganismiAvian leukosis virus RSA (RSV-SRA) (Rous sarcoma virus (strain Schmidt-Ruppin A))
<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 identifieri269446 [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 lineageiVirusesOrterviralesRetroviridaeOrthoretrovirinaeAlpharetrovirus
<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 hostiGallus gallus (Chicken) [TaxID: 9031]
<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
  • UP000002238 <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

<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

Surface protein :
  • Virion membrane ; Peripheral membrane protein
  • Host cell membrane By similarity; Peripheral membrane protein By similarity
  • Note: The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. Both proteins are thought to be concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity).By similarity

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 domaini63 – 552ExtracellularSequence analysisAdd BLAST490
<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>Transmembranei553 – 573HelicalSequence analysisAdd BLAST21
Topological domaini574 – 606CytoplasmicSequence analysisAdd BLAST33

GO - Cellular componenti

Keywords - Cellular componenti

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

<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 ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 62Sequence analysisAdd BLAST62
<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_000023960063 – 606Envelope glycoprotein gp95Add BLAST544
ChainiPRO_000004079963 – 401Surface proteinBy similarityAdd BLAST339
ChainiPRO_0000040800402 – 606Transmembrane proteinBy similarityAdd BLAST205

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 and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi79N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi120N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi141N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi158N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi178N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi257N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi291N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi297N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi307N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi315N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi391N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi453N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi501N-linked (GlcNAc...) asparagine; by hostSequence analysis1
<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>Lipidationi565S-palmitoyl cysteine; by hostBy similarity1
Lipidationi568S-palmitoyl cysteine; by hostBy similarity1

<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. Envelope glycoproteins are synthesized as a inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R (By similarity).By similarity
The transmembrane protein is palmitoylated. Palmitoylation is necessary for glycoprotein function and infectivity (By similarity).By similarity

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>Sitei401 – 402Cleavage; by hostBy similarity2

Keywords - PTMi

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

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P03397

<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

The mature envelope protein (Env) consists of a trimer of SU-TM heterodimers attached by a labile interchain disulfide bond.By similarity

<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

Secondary structure

1606
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P03397

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

More...
SMRi
P03397

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P03397

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni418 – 438Fusion peptideAdd BLAST21
Regioni474 – 490ImmunosuppressionBy similarityAdd BLAST17

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili435 – 485Sequence analysisAdd BLAST51
Coiled coili503 – 533Sequence analysisAdd BLAST31

<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 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo (By similarity).By similarity

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

Database of Orthologous Groups

More...
OrthoDBi
VOG09000092

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005166 RSV_p95_env
IPR018154 TLV/ENV_coat_polyprotein

The PANTHER Classification System

More...
PANTHERi
PTHR10424 PTHR10424, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03708 Avian_gp85, 1 hit
PF00429 TLV_coat, 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.

P03397-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEAVIKAFLT GYPGKTSKKD SKEKPLATSK KDPEKTPLLP TRVNYILIIG
60 70 80 90 100
VLVLCEVTGV RADVHLLEQP GNLWITWANR TGQTDFCLST QSATSPFQTC
110 120 130 140 150
LIGIPSPISE GDFKGYVSDN CTTLGTDRLV SSADFTGGPD NSTTLTYRKV
160 170 180 190 200
SCLLLKLNVS MWDEPHELQL LGSQSLPNIT NIAQISGITG GCVGFRPQGV
210 220 230 240 250
PWYLGWSRQE ATRFLLRHPS FSKSTEPFTV VTADRHNLFM GSEYCGAYGY
260 270 280 290 300
RFWNMYNCSQ VGRQYRCGNA RSPRPGLPEI QCTRRGGKWV NQSQEINESE
310 320 330 340 350
PFSFTVNCTA SSLGNASGCC GKAGTILPGK WVDSTQGSFT KPKALPPAIF
360 370 380 390 400
LICGDRAWQG IPSRPVGGPC YLGKLTMLAP KHTDILKVLV NSSRTGIRRK
410 420 430 440 450
RSTSHLDDTC SDEVQLWGPT ARIFASILAP GVAAAQALRE IERLACWSVK
460 470 480 490 500
QANLTTSLLG DLLDDVTSIR HAVLQNRAAI DFLLLAHGHG CEDVAGMCCF
510 520 530 540 550
NLSDHSESIQ KKFQLMKEHV NKIGVDSDPI GSWLRGLFGG IGEWAVHLLK
560 570 580 590 600
GLLLGLVVIL LLVVCLPCLL QIVCGNIRKM INNSISYHTE YKKLQKACGQ

PESRIV
Length:606
Mass (Da):66,325
Last modified:September 27, 2004 - v2
<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:i4A87F20967FFF6F3
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 conflicti381K → N in AAA42564 (PubMed:6292477).Curated1
Sequence conflicti388V → I (PubMed:6292477).Curated1
Sequence conflicti390V → A (PubMed:6292477).Curated1
Sequence conflicti403T → V in AAA42564 (PubMed:6292477).Curated1
Sequence conflicti434A → R in AAA91268 (PubMed:1311072).Curated1
Sequence conflicti439R → K in AAA42564 (PubMed:6292477).Curated1
Sequence conflicti458L → F in AAA91268 (PubMed:1311072).Curated1
Sequence conflicti505H → Q (PubMed:6253794).Curated1
Sequence conflicti505H → Q (PubMed:6298633).Curated1
Sequence conflicti529P → L (PubMed:6253794).Curated1
Sequence conflicti529P → L (PubMed:6298633).Curated1
Sequence conflicti572 – 573IV → ML (PubMed:6253794).Curated2
Sequence conflicti572 – 573IV → ML (PubMed:6298633).Curated2
Sequence conflicti577I → R (PubMed:6253794).Curated1
Sequence conflicti577I → R (PubMed:6298633).Curated1
Sequence conflicti598C → Y in AAA42564 (PubMed:6292477).Curated1

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
V01169 Genomic RNA Translation: CAA24494.1
L29199 Genomic DNA Translation: AAA42562.1
K00928 Genomic RNA Translation: AAA42564.1
M37980 Genomic RNA Translation: AAA91268.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B38017 VCFV37
S35427

NCBI Reference Sequences

More...
RefSeqi
NP_040548.1, NC_001408.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1491907

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:1491907

<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
V01169 Genomic RNA Translation: CAA24494.1
L29199 Genomic DNA Translation: AAA42562.1
K00928 Genomic RNA Translation: AAA42564.1
M37980 Genomic RNA Translation: AAA91268.1
PIRiB38017 VCFV37
S35427
RefSeqiNP_040548.1, NC_001408.1

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
1XNLNMR-A418-445[»]
4JPRX-ray2.00A452-522[»]
5H9CX-ray1.78A452-522[»]
ProteinModelPortaliP03397
SMRiP03397
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi1.G.12.1.1 the avian leukosis virus gp95 fusion protein (alv-gp95) family

Proteomic databases

PRIDEiP03397

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1491907
KEGGivg:1491907

Phylogenomic databases

OrthoDBiVOG09000092

Miscellaneous databases

EvolutionaryTraceiP03397

Family and domain databases

InterProiView protein in InterPro
IPR005166 RSV_p95_env
IPR018154 TLV/ENV_coat_polyprotein
PANTHERiPTHR10424 PTHR10424, 1 hit
PfamiView protein in Pfam
PF03708 Avian_gp85, 1 hit
PF00429 TLV_coat, 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 nameiENV_RSVSA
<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: P03397
Secondary accession number(s): Q03803, Q85500
<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 21, 1986
Last sequence update: September 27, 2004
Last modified: June 20, 2018
This is version 105 of the entry and version 2 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again