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P26806

- GAG_MLVFF

UniProt

P26806 - GAG_MLVFF

Protein

Gag polyprotein

Gene

gag

Organism
Friend murine leukemia virus (isolate FB29) (FrMLV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Gag polyprotein plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably link the viral protein to the host ESCRT pathway and facilitate release By similarity.By similarity
    Matrix protein p15 targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex By similarity.By similarity
    Capsid protein p30 forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex.By similarity
    Nucleocapsid protein p10 is involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei131 – 1322Cleavage; by viral protease p14By similarity
    Sitei215 – 2162Cleavage; by viral protease p14By similarity
    Sitei478 – 4792Cleavage; by viral protease p14By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri502 – 51918CCHC-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. RNA binding Source: UniProtKB-KW
    2. structural constituent of virion Source: UniProtKB-KW
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. viral budding via host ESCRT complex Source: UniProtKB-KW
    2. viral release from host cell Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, Viral budding, Viral budding via the host ESCRT complexes, Virus exit from host cell

    Keywords - Ligandi

    Metal-binding, RNA-binding, Viral nucleoprotein, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gag polyprotein
    Alternative name(s):
    Core polyprotein
    Cleaved into the following 4 chains:
    Gene namesi
    Name:gag
    OrganismiFriend murine leukemia virus (isolate FB29) (FrMLV)
    Taxonomic identifieri11797 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]
    ProteomesiUP000008877: Genome

    Subcellular locationi

    Chain Gag polyprotein : Virion By similarity. Host cell membrane Curated; Lipid-anchor Curated. Host late endosome membrane Curated; Lipid-anchor Curated. Host endosomehost multivesicular body By similarity
    Note: These locations are probably linked to virus assembly sites.By similarity

    GO - Cellular componenti

    1. host cell late endosome membrane Source: UniProtKB-SubCell
    2. host cell plasma membrane Source: UniProtKB-SubCell
    3. host multivesicular body Source: UniProtKB-SubCell
    4. membrane Source: UniProtKB-KW
    5. viral nucleocapsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host cell membrane, Host endosome, Host membrane, Membrane, Viral matrix protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by hostBy similarity
    Chaini2 – 538537Gag polyproteinBy similarityPRO_0000390812Add
    BLAST
    Chaini2 – 131130Matrix protein p15Sequence AnalysisPRO_0000040900Add
    BLAST
    Chaini132 – 21584RNA-binding phosphoprotein p12Sequence AnalysisPRO_0000040901Add
    BLAST
    Chaini216 – 478263Capsid protein p30Sequence AnalysisPRO_0000040902Add
    BLAST
    Chaini479 – 53860Nucleocapsid protein p10Sequence AnalysisPRO_0000040903Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
    Modified residuei192 – 1921Phosphoserine; by hostBy similarity

    Post-translational modificationi

    Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation By similarity.By similarity
    RNA-binding phosphoprotein p12 is phosphorylated on serine residues.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein

    Interactioni

    Subunit structurei

    Capsid protein p30 is a homohexamer, that further associates as homomultimer. The virus core is composed of a lattice formed from hexagonal rings, each containing six capsid monomers By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP26806.
    SMRiP26806. Positions 2-98, 216-346, 352-382, 479-534.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili438 – 47841Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi111 – 1144PTAP/PSAP motif
    Motifi130 – 1345LYPX(n)L motif
    Motifi162 – 1654PPXY motif

    Domaini

    Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. RNA-binding phosphoprotein p12 contains one L domain: a PPXY motif which potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase. Matrix protein p15 contains one L domain: a PTAP/PSAP motif, which potentially interacts with the UEV domain of TSG101. The junction between the matrix protein p15 and RNA-binding phosphoprotein p12 also contains one L domain: a LYPX(n)L which potentially interacts with PDCD6IP By similarity.By similarity

    Sequence similaritiesi

    Contains 1 CCHC-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri502 – 51918CCHC-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Family and domain databases

    Gene3Di1.10.150.180. 1 hit.
    1.10.375.10. 1 hit.
    4.10.60.10. 1 hit.
    InterProiIPR000840. G_retro_matrix_N.
    IPR002079. Gag_p12.
    IPR003036. Gag_P30.
    IPR008919. Retrov_capsid_N.
    IPR010999. Retrovr_matrix_N.
    IPR001878. Znf_CCHC.
    [Graphical view]
    PfamiPF01140. Gag_MA. 1 hit.
    PF01141. Gag_p12. 1 hit.
    PF02093. Gag_p30. 1 hit.
    PF00098. zf-CCHC. 1 hit.
    [Graphical view]
    SMARTiSM00343. ZnF_C2HC. 1 hit.
    [Graphical view]
    SUPFAMiSSF47836. SSF47836. 1 hit.
    SSF47943. SSF47943. 1 hit.
    SSF57756. SSF57756. 1 hit.
    PROSITEiPS50158. ZF_CCHC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P26806-1 [UniParc]FASTAAdd to Basket

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    MGQAVTTPLS LTLDHWKDVE RTAHNLSVEV RKRRWVTFCS AEWPTFNVGW    50
    PRDGTFNPDI ITQVKIKVFS PGPHGHPDQV PYIVTWEAIA VDPPPWVRPF 100
    VHPKPPLSLP PSAPSLPPEP PLSTPPQSSL YPALTSPLNT KPRPQVLPDS 150
    GGPLIDLLTE DPPPYRDPGP PSPDGNGDSG EVAPTEGAPD PSPMVSRLRG 200
    RKEPPVADST TSQAFPLRLG GNGQYQYWPF SSSDLYNWKN NNPSFSEDPA 250
    KLTALIESVL LTHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGEDGR 300
    PTQLPNDIND AFPLERPDWD YNTQRGRNHL VHYRQLLLAG LQNAGRSPTN 350
    LAKVKGITQG PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVAMSFIWQ 400
    SAPDIGRKLE RLEDLKSKTL GDLVREAEKI FNKRETPEER EERIRRETEE 450
    KEERRRAEDV QREKERDRRR HREMSKLLAT VVSGQRQDRQ GGERRRPQLD 500
    HDQCAYCKEK GHWARDCPKK PRGPRGPRPQ ASLLTLDD 538
    Length:538
    Mass (Da):60,929
    Last modified:January 23, 2007 - v3
    Checksum:i2E652DDB9E0D4A3C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti501 – 5011H → R AA sequence (PubMed:6267042)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11128 Genomic DNA. Translation: CAA77478.1.
    PIRiS70394.
    RefSeqiNP_040332.1. NC_001362.1.

    Genome annotation databases

    GeneIDi1491876.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11128 Genomic DNA. Translation: CAA77478.1 .
    PIRi S70394.
    RefSeqi NP_040332.1. NC_001362.1.

    3D structure databases

    ProteinModelPortali P26806.
    SMRi P26806. Positions 2-98, 216-346, 352-382, 479-534.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1491876.

    Family and domain databases

    Gene3Di 1.10.150.180. 1 hit.
    1.10.375.10. 1 hit.
    4.10.60.10. 1 hit.
    InterProi IPR000840. G_retro_matrix_N.
    IPR002079. Gag_p12.
    IPR003036. Gag_P30.
    IPR008919. Retrov_capsid_N.
    IPR010999. Retrovr_matrix_N.
    IPR001878. Znf_CCHC.
    [Graphical view ]
    Pfami PF01140. Gag_MA. 1 hit.
    PF01141. Gag_p12. 1 hit.
    PF02093. Gag_p30. 1 hit.
    PF00098. zf-CCHC. 1 hit.
    [Graphical view ]
    SMARTi SM00343. ZnF_C2HC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47836. SSF47836. 1 hit.
    SSF47943. SSF47943. 1 hit.
    SSF57756. SSF57756. 1 hit.
    PROSITEi PS50158. ZF_CCHC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence of Friend murine leukemia virus, strain FB29."
      Perryman S., Nishio J., Chesebro B.
      Nucleic Acids Res. 19:6950-6950(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Primary structure of the low molecular weight nucleic acid-binding proteins of murine leukemia viruses."
      Henderson L.E., Copeland T.D., Sowder R.C., Smythers G.W., Oroszlan S.
      J. Biol. Chem. 256:8400-8406(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 479-512.

    Entry informationi

    Entry nameiGAG_MLVFF
    AccessioniPrimary (citable) accession number: P26806
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 107 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3