Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P03332

- GAG_MLVMS

UniProt

P03332 - GAG_MLVMS

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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. 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
Complete GO annotation...

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 endosome Source: UniProtKB-KW
  2. host cell plasma membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
  4. viral nucleocapsid Source: UniProtKB-KW
Complete GO annotation...

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

        10         20         30         40         50
MGQTVTTPLS LTLGHWKDVE RIAHNQSVDV KKRRWVTFCS AEWPTFNVGW
60 70 80 90 100
PRDGTFNRDL ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF
110 120 130 140 150
VHPKPPPPLP PSAPSLPLEP PRSTPPRSSL YPALTPSLGA KPKPQVLSDS
160 170 180 190 200
GGPLIDLLTE DPPPYRDPRP PPSDRDGNGG EATPAGEAPD PSPMASRLRG
210 220 230 240 250
RREPPVADST TSQAFPLRAG GNGQLQYWPF SSSDLYNWKN NNPSFSEDPG
260 270 280 290 300
KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR
310 320 330 340 350
PTQLPNEVDA AFPLERPDWD YTTQAGRNHL VHYRQLLLAG LQNAGRSPTN
360 370 380 390 400
LAKVKGITQG PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ
410 420 430 440 450
SAPDIGRKLE RLEDLKNKTL GDLVREAEKI FNKRETPEER EERIRRETEE
460 470 480 490 500
KEERRRTEDE QKEKERDRRR HREMSKLLAT VVSGQKQDRQ GGERRRSQLD
510 520 530
RDQCAYCKEK GHWAKDCPKK PRGPRGPRPQ TSLLTLDD
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 29, 2014
This is version 126 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