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P32594

- GAG_MSVMT

UniProt

P32594 - GAG_MSVMT

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Protein
Gag polyprotein
Gene
gag
Organism
Moloney murine sarcoma virus (strain ts110) (MoMSV)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

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.
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.
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 elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization By similarity.

Sites

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

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW
  2. structural constituent of virion Source: UniProtKB-KW

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

RNA-binding, Viral nucleoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
Gag polyprotein
Alternative name(s):
Core polyprotein
Cleaved into the following 3 chains:
Matrix protein p15
Short name:
MA
Alternative name(s):
pp12
Capsid protein p30
Short name:
CA
Gene namesi
Name:gag
OrganismiMoloney murine sarcoma virus (strain ts110) (MoMSV)
Taxonomic identifieri31691 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostiMus musculus (Mouse) [TaxID: 10090]

Subcellular locationi

Chain Gag polyprotein : Virion By similarity. Host cell membrane; Lipid-anchor Reviewed prediction
Chain Matrix protein p15 : Virion Reviewed prediction
Chain Capsid protein p30 : Virion Reviewed prediction

GO - Cellular componenti

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

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by host By similarity
Chaini2 – 468467Gag polyprotein
PRO_0000390819Add
BLAST
Chaini2 – 131130Matrix protein p15 Reviewed prediction
PRO_0000040953Add
BLAST
Chaini132 – 21584RNA-binding phosphoprotein p12 Reviewed prediction
PRO_0000040954Add
BLAST
Chaini216 – 468253Capsid protein p30 Reviewed prediction
PRO_0000040955Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by host By 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.

Keywords - PTMi

Lipoprotein, Myristate

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.

Structurei

3D structure databases

ProteinModelPortaliP32594.
SMRiP32594. Positions 2-98, 216-346, 352-382.

Family & Domainsi

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.

Family and domain databases

Gene3Di1.10.150.180. 1 hit.
1.10.375.10. 1 hit.
InterProiIPR000840. G_retro_matrix_N.
IPR002079. Gag_p12.
IPR003036. Gag_P30.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
[Graphical view]
PfamiPF01140. Gag_MA. 1 hit.
PF01141. Gag_p12. 1 hit.
PF02093. Gag_p30. 1 hit.
[Graphical view]
SUPFAMiSSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P32594-1 [UniParc]FASTAAdd to Basket

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MGQTVTTPLS LTLDHWKDVE RIAHNQSVDV KKRRWVTFCS AEWPTFNVGW    50
PRDGTFNRDL ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF 100
VHPKPPPPLL PSAPSLPLEP PLSTPPQSSL YPALTPSLGA KPKPQVLSDS 150
GGPLIDLLTE DPPPYRDPRP PPSDRDGDSG EATPAGEAPD PSPMASRLRG 200
RREPPVADST TSQAFPLRTG GNGQLQYWPF SSSDLYNWKS NNPSFSEDPG 250
KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR 300
PTQLPNEVDA AFPLERPDWE YTTQAGRNHL VHYRQLLIAG LQNAGRSPTN 350
LAKVKGITQG PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ 400
SAPDIGRKLE RLEDLRNKTL GDLVREAERI FNKRETPEER EERIRREREE 450
KEERHAPKLP WLFLIISP 468
Length:468
Mass (Da):52,681
Last modified:January 23, 2007 - v3
Checksum:iAF4F795F5D69824F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M96854 Genomic DNA. No translation available.
PIRiA42745. FOMVMU.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M96854 Genomic DNA. No translation available.
PIRi A42745. FOMVMU.

3D structure databases

ProteinModelPortali P32594.
SMRi P32594. Positions 2-98, 216-346, 352-382.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.10.150.180. 1 hit.
1.10.375.10. 1 hit.
InterProi IPR000840. G_retro_matrix_N.
IPR002079. Gag_p12.
IPR003036. Gag_P30.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
[Graphical view ]
Pfami PF01140. Gag_MA. 1 hit.
PF01141. Gag_p12. 1 hit.
PF02093. Gag_p30. 1 hit.
[Graphical view ]
SUPFAMi SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Moloney murine sarcoma virus MuSVts110 DNA: cloning, nucleotide sequence, and gene expression."
    Huai L., Chiocca S.M., Gilbreth M.A., Ainsworth J.R., Bishop L.A., Murphy E.C. Jr.
    J. Virol. 66:5329-5337(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiGAG_MSVMT
AccessioniPrimary (citable) accession number: P32594
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein is probably translated as a Gag-Mos polyprotein.

External Data

Dasty 3

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