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Entry version 121 (13 Nov 2019)
Sequence version 3 (24 Jul 2007)
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Protein

MLV-related proviral Env polyprotein

Gene
N/A
Organism
Mus musculus (Mouse)
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

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

Caution

This polyprotein is encoded by an endogenous retrovirus expressed in some mouse strains. Multiple sequences are present in different regions of the genome, probably reflecting the different sites of integration of the exogenous retrovirus.Curated

<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

<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

LigandMetal-binding, Zinc

<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:
MLV-related proviral Env polyprotein
Cleaved into the following 2 chains:
Surface protein
Short name:
SU
Transmembrane protein
Short name:
TM
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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: Unplaced

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

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 domaini33 – 581ExtracellularSequence analysisAdd BLAST549
<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>Transmembranei582 – 602HelicalSequence analysisAdd BLAST21
Topological domaini603 – 641CytoplasmicSequence analysisAdd BLAST39

Keywords - Cellular componenti

Cell 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 – 32Sequence analysisAdd BLAST32
<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_000002118633 – 440Surface proteinBy similarityAdd BLAST408
ChainiPRO_0000295257441 – 641Transmembrane proteinBy similarityAdd BLAST201

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>Glycosylationi43N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi58N-linked (GlcNAc...) asparagineSequence analysis1
<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 bondi109 ↔ 126By similarity
Disulfide bondi118 ↔ 131By similarity
Glycosylationi297N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi307 ↔ 534Interchain (between SU and TM chains, or C-337 with C-558); in linked formBy similarity
Disulfide bondi307 ↔ 310By similarity
Glycosylationi336N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi337 ↔ 391By similarity
Disulfide bondi356 ↔ 368By similarity
Glycosylationi369N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi398 ↔ 411By similarity
Disulfide bondi526 ↔ 533By similarity
<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>Lipidationi601S-palmitoyl cysteineBy 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 an 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. The R-peptide is released from the C-terminus of the cytoplasmic tail of the TM protein upon particle formation as a result of proteolytic cleavage by the viral protease. Cleavage of this peptide is required for TM to become fusogenic (By similarity).By similarity
The CXXC motif is highly conserved across a broad range of retroviral envelope proteins. It is thought to participate in the formation of a labile disulfide bond possibly with the CX6CC motif present in the transmembrane protein. Isomerization of the intersubunit disulfide bond to an SU intrachain disulfide bond is thought to occur upon receptor recognition in order to allow membrane fusion (By similarity).By similarity
The transmembrane protein is palmitoylated.By similarity
The R-peptide is palmitoylated.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>Sitei440 – 441CleavageBy similarity2

Keywords - PTMi

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

Proteomic databases

The CPTAC Assay portal

More...
CPTACi
non-CPTAC-3575

Encyclopedia of Proteome Dynamics

More...
EPDi
P10404

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P10404

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P10404

PeptideAtlas

More...
PeptideAtlasi
P10404

PRoteomics IDEntifications database

More...
PRIDEi
P10404

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P10404

PTM databases

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P10404

<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

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P10404, 1 interactor

<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

1641
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P10404

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

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>Regioni443 – 463Fusion peptideBy similarityAdd BLAST21
Regioni509 – 525ImmunosuppressionBy 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 coili471 – 520Sequence analysisAdd BLAST50
Coiled coili530 – 566Sequence analysisAdd BLAST37

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi307 – 310CXXCBy similarity4
Motifi526 – 534CX6CCBy similarity9
Motifi626 – 629YXXL motif; contains endocytosis signalBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi230 – 279Pro-richAdd BLAST50

<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 YXXL motif is involved in determining the exact site of viral release at the surface of infected mononuclear cells and promotes endocytosis.
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

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P10404

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.90.310.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008981 FMuLV_rcpt-bd
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
PF00429 TLV_coat, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49830 SSF49830, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

P10404-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEGPAFSKPL KDKINPWGPL IVLGILIRAG VSVQHDSPHQ VFNVTWRVTN
60 70 80 90 100
LMTGQTANAT SLLGTMTDAF PKLYFDLCDL IGDDWDETGL GCRTPGGRKR
110 120 130 140 150
ARTFDFYVCP GHTVPTGCGG PREGYCGKWG CETTGQAYWK PSSSWDLISL
160 170 180 190 200
KRRNTPQNQG PCYDSSAVSS DIKGATPGGR CNPLVLEFTD AGKKASWDGP
210 220 230 240 250
KVWGLRLYRS TGTDPVTRFS LTRQVLNIGP RVPIGPNPVI TDQLPPSRPV
260 270 280 290 300
QIMLPRPPQP PPPGAASIVP ETAPPSQQPG TGDRLLNLVD GAYQALNLTS
310 320 330 340 350
PDKTQECWLC LVAGPPYYEG VAVLGTYSNH TSAPANCSVA SQHKLTLSEV
360 370 380 390 400
TGQGLCVGAV PKTHQALCNT TQKTSDGSYY LAAPAGTIWA CNTGLTPCLS
410 420 430 440 450
TTVLDLTTDY CVLVELWPKV TYHSPGYVYG QFERKTKYKR EPVSLTLALL
460 470 480 490 500
LGGLTMGGIA AGVGTGTTAL VATKQFEQLQ AAIHTDLGAL EKSVSALEKS
510 520 530 540 550
LTSLSEVVLQ NRRGLDLLFL KEGGLCAALK EECCFYADHT GVVRDSMAKL
560 570 580 590 600
RERLNQRQKL FESGQGWFEG LFNRSPWFTT LISTIMGPLI ILLLILLFGP
610 620 630 640
CILNRLVQFV KDRISVVQAL VLTQQYHQLK SIDPEEVESR E
Length:641
Mass (Da):69,613
Last modified:July 24, 2007 - v3
<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:iC39BF1C2F7B4063F
GO

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 varianti22V → I. 1
Natural varianti24G → R. 1
Natural varianti153R → G. 1
Natural varianti157Q → R. 1
Natural varianti268I → T. 1
Natural varianti280G → E. 1
Natural varianti339V → A. 1
Natural varianti349E → K. 1
Natural varianti358G → R. 1
Natural varianti434R → K. 1
Natural varianti458G → D. 1
Natural varianti491E → K. 1
Natural varianti514G → R. 1
Natural varianti524G → R. 1
Natural varianti531E → K. 1
Natural varianti546S → N. 1
Natural varianti548A → T. 1
Natural varianti552E → K. 1
Natural varianti636E → K. 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
AY219544 Genomic DNA Translation: AAO37244.2
AY219545 Genomic DNA Translation: AAO37246.2
AY219546 Genomic DNA Translation: AAO37248.2
AY219547 Genomic DNA Translation: AAO37250.2
AY219548 Genomic DNA Translation: AAO37252.2
AY219550 Genomic DNA Translation: AAO37255.2
AY219551 Genomic DNA Translation: AAO37257.2
AY219554 Genomic DNA Translation: AAO37261.2
AY219557 Genomic DNA Translation: AAO37265.2
AY219558 Genomic DNA Translation: AAO37267.2
AY219564 Genomic DNA Translation: AAO37279.2
AY219566 Genomic DNA Translation: AAO37283.2
AY219567 Genomic DNA Translation: AAO37285.2
M11301 mRNA Translation: AAA37561.1

NCBI Reference Sequences

More...
RefSeqi
XP_017173509.1, XM_017318020.1
XP_017176706.1, XM_017321217.1
XP_017176707.1, XM_017321218.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
105246904
108168376

Keywords - Coding sequence diversityi

Polymorphism

<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
AY219544 Genomic DNA Translation: AAO37244.2
AY219545 Genomic DNA Translation: AAO37246.2
AY219546 Genomic DNA Translation: AAO37248.2
AY219547 Genomic DNA Translation: AAO37250.2
AY219548 Genomic DNA Translation: AAO37252.2
AY219550 Genomic DNA Translation: AAO37255.2
AY219551 Genomic DNA Translation: AAO37257.2
AY219554 Genomic DNA Translation: AAO37261.2
AY219557 Genomic DNA Translation: AAO37265.2
AY219558 Genomic DNA Translation: AAO37267.2
AY219564 Genomic DNA Translation: AAO37279.2
AY219566 Genomic DNA Translation: AAO37283.2
AY219567 Genomic DNA Translation: AAO37285.2
M11301 mRNA Translation: AAA37561.1
RefSeqiXP_017173509.1, XM_017318020.1
XP_017176706.1, XM_017321217.1
XP_017176707.1, XM_017321218.1

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
4JGSX-ray2.20A/B/C/D/E/F/G/H/I469-564[»]
SMRiP10404
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP10404, 1 interactor

PTM databases

SwissPalmiP10404

Proteomic databases

CPTACinon-CPTAC-3575
EPDiP10404
jPOSTiP10404
MaxQBiP10404
PeptideAtlasiP10404
PRIDEiP10404
TopDownProteomicsiP10404

Genome annotation databases

GeneIDi105246904
108168376

Phylogenomic databases

InParanoidiP10404

Family and domain databases

Gene3Di3.90.310.10, 1 hit
InterProiView protein in InterPro
IPR008981 FMuLV_rcpt-bd
IPR018154 TLV/ENV_coat_polyprotein
PANTHERiPTHR10424 PTHR10424, 1 hit
PfamiView protein in Pfam
PF00429 TLV_coat, 2 hits
SUPFAMiSSF49830 SSF49830, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiENV1_MOUSE
<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: P10404
Secondary accession number(s): Q78N71
, Q78N73, Q78N94, Q80SW7, Q80SW8, Q80SY0, Q80SY1, Q811M9, Q811N4
<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 24, 2007
Last modified: November 13, 2019
This is version 121 of the entry and version 3 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 programChordata 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
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