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P03332

- GAG_MLVMS

UniProt

P03332 - GAG_MLVMS

Protein

Gag polyprotein

Gene

gag

Organism
Moloney murine leukemia virus (isolate Shinnick) (MoMLV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 4 (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.1 Publication
    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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei131 – 1322Cleavage; by viral protease p14
    Sitei215 – 2162Cleavage; by viral protease p14
    Sitei478 – 4792Cleavage; by viral protease p14

    Regions

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

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. RNA binding Source: UniProtKB-KW
    3. structural constituent of virion Source: UniProtKB-KW
    4. 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
    Short name:
    Pr65gag
    Alternative name(s):
    Core polyprotein
    Cleaved into the following 4 chains:
    Matrix protein p15
    Short name:
    MA
    Alternative name(s):
    pp12
    Capsid protein p30
    Short name:
    CA
    Nucleocapsid protein p10
    Short name:
    NC-gag
    Gene namesi
    Name:gag
    OrganismiMoloney murine leukemia virus (isolate Shinnick) (MoMLV)
    Taxonomic identifieri928306 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]
    ProteomesiUP000006625: 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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi114 – 1141P → A: Slight reduction in the number of virus-like particles produced.
    Mutagenesisi137 – 1371S → A: No effect on reverse transcription activity. 1 Publication
    Mutagenesisi148 – 1481S → A: No effect on reverse transcription activity; when associated with A-150. 1 Publication
    Mutagenesisi150 – 1501S → A: No effect on reverse transcription activity; when associated with A-148. 1 Publication
    Mutagenesisi165 – 1651Y → A: Drastic reduction in the number of virus-like particles produced. 1 Publication
    Mutagenesisi192 – 1921S → A: Complete loss of reverse transcription activity. 1 Publication
    Mutagenesisi192 – 1921S → D: Complete loss of reverse transcription activity. 1 Publication
    Mutagenesisi196 – 1961S → A: No effect on reverse transcription activity. 1 Publication
    Mutagenesisi209 – 2091S → A: Strongly reduced reverse transcription activity. 1 Publication
    Mutagenesisi209 – 2091S → D: Strongly reduced reverse transcription activity. 1 Publication
    Mutagenesisi212 – 2121S → A: No effect on reverse transcription activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by host1 Publication
    Chaini2 – 538537Gag polyproteinPRO_0000390815Add
    BLAST
    Chaini2 – 131130Matrix protein p15Sequence AnalysisPRO_0000040912Add
    BLAST
    Chaini132 – 21584RNA-binding phosphoprotein p12Sequence AnalysisPRO_0000040913Add
    BLAST
    Chaini216 – 478263Capsid protein p30Sequence AnalysisPRO_0000040914Add
    BLAST
    Chaini479 – 53860Nucleocapsid protein p10Sequence AnalysisPRO_0000040915Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by host1 Publication
    Modified residuei192 – 1921Phosphoserine; by host1 Publication

    Post-translational modificationi

    Gag polyprotein is ubiquitinated by ITCH. Gag can recruit the ubiquitin ligase Itch in an L domain-independent manner to facilitate virus release via a mechanism that involves Gag ubiquitination.
    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
    Capsid protein p30 is sumoylated; which is required for virus replication.1 Publication
    RNA-binding phosphoprotein p12 is phosphorylated on serine residues.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

    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. Capsid protein p30 interacts with mouse UBE2I and mouse PIAS4. Gag polyprotein interacts (via PPXY motif) with host NEDD4. Gag polyprotein interacts (via PSAP motif) with host TSG101. Gag polyprotein interacts (via LYPX(n)L motif) with host PDCD6IP.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Dok3Q9QZK73EBI-935477,EBI-2906753From a different organism.
    Iqgap1Q9JKF117EBI-935477,EBI-644633From a different organism.

    Protein-protein interaction databases

    IntActiP03332. 6 interactions.
    MINTiMINT-2490859.

    Structurei

    Secondary structure

    1
    538
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 147
    Helixi16 – 2510
    Helixi32 – 409
    Helixi43 – 464
    Helixi58 – 6811
    Helixi77 – 793
    Helixi80 – 9112
    Turni356 – 3605
    Helixi361 – 3633
    Helixi364 – 37815
    Beta strandi494 – 4963
    Beta strandi501 – 5033
    Beta strandi505 – 5073
    Beta strandi510 – 5123
    Helixi514 – 5163
    Beta strandi518 – 5203
    Beta strandi522 – 5243

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A6BNMR-B492-531[»]
    1BM4NMR-A352-382[»]
    1MN8X-ray1.00A/B/C/D1-99[»]
    1U6PNMR-A479-534[»]
    1WWDNMR-A479-534[»]
    1WWENMR-A479-534[»]
    1WWFNMR-A479-534[»]
    1WWGNMR-A479-534[»]
    ProteinModelPortaliP03332.
    SMRiP03332. Positions 2-98, 216-347, 352-382, 479-534.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03332.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni345 – 39349Interaction with mouse PIAS4Add
    BLAST
    Regioni430 – 4356Interaction with mouse UBE2I

    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 interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase. PPXY motif is essential for virus egress. Matrix protein p15 contains one L domain: a PTAP/PSAP motif, which 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 motif which interacts with PDCD6IP. Both PSAP and LYPX(n)L domains might play little to no role in budding and possibly drive residual virus release.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform Pr65gag (identifier: P03332-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGQTVTTPLS LTLGHWKDVE RIAHNQSVDV KKRRWVTFCS AEWPTFNVGW    50
    PRDGTFNRDL ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF 100
    VHPKPPPPLP PSAPSLPLEP PRSTPPRSSL YPALTPSLGA KPKPQVLSDS 150
    GGPLIDLLTE DPPPYRDPRP PPSDRDGNGG EATPAGEAPD PSPMASRLRG 200
    RREPPVADST TSQAFPLRAG GNGQLQYWPF SSSDLYNWKN NNPSFSEDPG 250
    KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR 300
    PTQLPNEVDA AFPLERPDWD YTTQAGRNHL VHYRQLLLAG LQNAGRSPTN 350
    LAKVKGITQG PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ 400
    SAPDIGRKLE RLEDLKNKTL GDLVREAEKI FNKRETPEER EERIRRETEE 450
    KEERRRTEDE QKEKERDRRR HREMSKLLAT VVSGQKQDRQ GGERRRSQLD 500
    RDQCAYCKEK GHWAKDCPKK PRGPRGPRPQ TSLLTLDD 538
    Length:538
    Mass (Da):60,858
    Last modified:January 23, 2007 - v4
    Checksum:i8A7652439B464495
    GO
    Isoform Pr80gag (identifier: Q8UN02-1) [UniParc]FASTAAdd to Basket

    Also known as: GlycoGag

    The sequence of this isoform can be found in the external entry Q8UN02.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by an upstream CUG initiation codon.

    Length:626
    Mass (Da):70,503
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02255 Genomic RNA. Translation: AAB59942.1.
    AF033811 Genomic RNA. Translation: AAC82566.1.
    PIRiA03930. FOMV1M.
    RefSeqiNP_057934.1. NC_001501.1.

    Genome annotation databases

    GeneIDi1491870.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02255 Genomic RNA. Translation: AAB59942.1 .
    AF033811 Genomic RNA. Translation: AAC82566.1 .
    PIRi A03930. FOMV1M.
    RefSeqi NP_057934.1. NC_001501.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A6B NMR - B 492-531 [» ]
    1BM4 NMR - A 352-382 [» ]
    1MN8 X-ray 1.00 A/B/C/D 1-99 [» ]
    1U6P NMR - A 479-534 [» ]
    1WWD NMR - A 479-534 [» ]
    1WWE NMR - A 479-534 [» ]
    1WWF NMR - A 479-534 [» ]
    1WWG NMR - A 479-534 [» ]
    ProteinModelPortali P03332.
    SMRi P03332. Positions 2-98, 216-347, 352-382, 479-534.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P03332. 6 interactions.
    MINTi MINT-2490859.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1491870.

    Miscellaneous databases

    EvolutionaryTracei P03332.

    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. "Nucleotide sequence of Moloney murine leukaemia virus."
      Shinnick T.M., Lerner R.A., Sutcliffe J.G.
      Nature 293:543-548(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] (CLONE PMLV-1).
    2. Chappey C.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Myristyl amino-terminal acylation of murine retrovirus proteins: an unusual post-translational proteins modification."
      Henderson L.E., Krutzsch H.C., Oroszlan S.
      Proc. Natl. Acad. Sci. U.S.A. 80:339-343(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-31, MYRISTOYLATION AT GLY-2.
    4. "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 479-529.
    5. "Phosphorylated serine residues and an arginine-rich domain of the moloney murine leukemia virus p12 protein are required for early events of viral infection."
      Yueh A., Goff S.P.
      J. Virol. 77:1820-1829(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-192, MUTAGENESIS OF SER-137; SER-148; SER-150; SER-192; SER-196; SER-209 AND SER-212.
    6. "Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with Nedd4 ubiquitin ligases during budding."
      Segura-Morales C., Pescia C., Chatellard-Causse C., Sadoul R., Bertrand E., Basyuk E.
      J. Biol. Chem. 280:27004-27012(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MOUSE NEDD4; TSG101 AND PDCD6IP/ALIX, MUTAGENESIS OF TYR-165.
    7. "Interaction of moloney murine leukemia virus capsid with Ubc9 and PIASy mediates SUMO-1 addition required early in infection."
      Yueh A., Leung J., Bhattacharyya S., Perrone L.A., de los Santos K., Pu S.-Y., Goff S.P.
      J. Virol. 80:342-352(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBE2I AND PIAS4, SUMOYLATION.
    8. "Characterization of the murine leukemia virus protease and its comparison with the human immunodeficiency virus type 1 protease."
      Feher A., Boross P., Sperka T., Miklossy G., Kadas J., Bagossi P., Oroszlan S., Weber I.T., Tozser J.
      J. Gen. Virol. 87:1321-1330(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
    9. "Late domain-independent rescue of a release-deficient Moloney murine leukemia virus by the ubiquitin ligase Itch."
      Jadwin J.A., Rudd V., Sette P., Challa S., Bouamr F.
      J. Virol. 84:704-715(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Three-dimensional 1H NMR structure of the nucleocapsid protein NCp10 of Moloney murine leukemia virus."
      Demene H., Jullian N., Morellet N., de Rocquigny H., Cornille F., Maigret B., Roques B.P.
      J. Biomol. NMR 4:153-170(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 492-531.
    11. "Solution structures of human immunodeficiency virus type 1 (HIV-1) and moloney murine leukemia virus (MoMLV) capsid protein major-homology-region peptide analogs by NMR spectroscopy."
      Clish C.B., Peyton D.H., Barklis E.
      Eur. J. Biochem. 257:69-77(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 352-382.
    12. "Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins."
      Riffel N., Harlos K., Iourin O., Rao Z., Kingsman A., Stuart D., Fry E.
      Structure 10:1627-1636(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 1-99.
    13. "Structural basis for packaging the dimeric genome of Moloney murine leukaemia virus."
      D'Souza V., Summers M.F.
      Nature 431:586-590(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 479-534.
    14. "Composition and sequence-dependent binding of RNA to the nucleocapsid protein of Moloney murine leukemia virus."
      Dey A., York D., Smalls-Mantey A., Summers M.F.
      Biochemistry 44:3735-3744(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 479-534.

    Entry informationi

    Entry nameiGAG_MLVMS
    AccessioniPrimary (citable) accession number: P03332
    Secondary accession number(s): Q9WJP4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 125 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3