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Protein

Gag polyprotein

Gene

gag

Organism
AKV murine leukemia virus (AKR (endogenous) murine leukemia virus)
Status
Reviewed-Annotation score: Annotation score: 4 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 (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
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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri501 – 518CCHC-typePROSITE-ProRule annotationAdd BLAST18

GO - Molecular functioni

GO - Biological processi

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
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
OrganismiAKV murine leukemia virus (AKR (endogenous) murine leukemia virus)
Taxonomic identifieri11791 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
Proteomesi
  • UP000008875 Componenti: Genome

Subcellular locationi

Gag polyprotein :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00003908062 – 537Gag polyproteinAdd BLAST536
ChainiPRO_00000408762 – 129Matrix protein p15Sequence analysisAdd BLAST128
ChainiPRO_0000040877130 – 214RNA-binding phosphoprotein p12Sequence analysisAdd BLAST85
ChainiPRO_0000040878215 – 477Capsid protein p30Sequence analysisAdd BLAST263
ChainiPRO_0000040879478 – 537Nucleocapsid protein p10Sequence analysisAdd BLAST60

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1
Modified residuei191Phosphoserine; by hostBy similarity1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei129 – 130Cleavage; by viral protease p14By similarity2
Sitei214 – 215Cleavage; by viral protease p14By similarity2
Sitei477 – 478Cleavage; by viral protease p14By similarity2

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

Protein-protein interaction databases

IntActiP03336. 1 interactor.
MINTiMINT-8387356.

Structurei

Secondary structure

1537
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi216 – 218Combined sources3
Beta strandi222 – 226Combined sources5
Helixi231 – 239Combined sources9
Turni244 – 246Combined sources3
Helixi248 – 261Combined sources14
Helixi266 – 276Combined sources11
Helixi279 – 291Combined sources13
Beta strandi298 – 300Combined sources3
Helixi304 – 310Combined sources7
Helixi323 – 344Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U7KX-ray1.85A/B/C/D/E/F215-345[»]
2Y4ZX-ray2.00A215-346[»]
3BP9X-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/X/Y215-346[»]
ProteinModelPortaliP03336.
SMRiP03336.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03336.

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili437 – 478Sequence analysisAdd BLAST42

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi109 – 112PTAP/PSAP motif4
Motifi128 – 132LYPX(n)L motif5
Motifi161 – 164PPXY motif4

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 motif 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)DescriptionActionsGraphical viewLength
Zinc fingeri501 – 518CCHC-typePROSITE-ProRule annotationAdd BLAST18

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.
IPR002079. Gag_p12.
IPR003036. Gag_P30.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
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.

P03336-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQTVTTPLS LTLEHWEDVQ RIASNQSVDV KKRRWVTFCS AEWPTFGVGW
60 70 80 90 100
PQDGTFNLDI ILQVKSKVFS PGPHGHPDQV PYIVTWEAIA YEPPPWVKPF
110 120 130 140 150
VSPKLSPSPT APILPSGPST QPPPRSALYP ALTPSIKPRP SKPQVLSDNG
160 170 180 190 200
GPLIDLLSED PPPYGGQGLS SSDGDGDREE ATSTSEIPAP SPIVSRLRGK
210 220 230 240 250
RDPPAADSTT SRAFPLRLGG NGQLQYWPFS SSDLYNWKNN NPSFSEDPGK
260 270 280 290 300
LTALIESVLT THQPTWDDCQ QLLGTLLTGE EKQRVLLEAR KAVRGNDGRP
310 320 330 340 350
TQLPNEVDAA FPLERPDWDY TTQRGRNHLV LYRQLLLAGL QNAGRSPTNL
360 370 380 390 400
AKVKGITQGP NESPSAFLER LKEAYRRYTP YDPEDPGQET NVSMSFIWQS
410 420 430 440 450
APDIGRKLER LEDLKSKTLG DLVREAERIF NKRETPEERE ERVRRETEEK
460 470 480 490 500
EERRRAEEEQ KEKERDRRRH REMSKLLATV VSGQRQDRQG GERRRPQLDK
510 520 530
DQCAYCKEKG HWAKDCPKKP RGPRGPRPQT SLLTLDD
Length:537
Mass (Da):60,558
Last modified:January 23, 2007 - v3
Checksum:iD35C4AD89B17CF93
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01998 Genomic RNA. Translation: AAB03090.1.
PIRiA03933. FOMVGV.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01998 Genomic RNA. Translation: AAB03090.1.
PIRiA03933. FOMVGV.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U7KX-ray1.85A/B/C/D/E/F215-345[»]
2Y4ZX-ray2.00A215-346[»]
3BP9X-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/X/Y215-346[»]
ProteinModelPortaliP03336.
SMRiP03336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP03336. 1 interactor.
MINTiMINT-8387356.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP03336.

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.
IPR002079. Gag_p12.
IPR003036. Gag_P30.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiGAG_MLVAV
AccessioniPrimary (citable) accession number: P03336
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 113 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

3D-structure, Complete proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.