Gag polyprotein - AKV murine leukemia virus

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P03336 (GAG_MLVAV) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Gag polyprotein

Alternative name(s):
Core polyprotein

Cleaved into the following 4 chains:

Matrix protein p15
Short name=MA
RNA-binding phosphoprotein p12
Alternative name(s):
pp12
Capsid protein p30
Short name=CA
Nucleocapsid protein p10
Short name=NC-gag

Gene names

Name:

gag

Organism

AKV murine leukemia virus (AKR (endogenous) murine leukemia virus) [Complete proteome]

Taxonomic identifier

11791 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Gammaretrovirus › Murine leukemia virus

Virus host

Mus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length	537 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. 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.
Subunit structure	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. Ref.2
Subcellular location	Gag polyprotein: Virion By similarity. Host cell membrane; Lipid-anchor Potential. Host late endosome membrane; Lipid-anchor Potential. Host endosome › host multivesicular body By similarity. Note: These locations are probably linked to virus assembly sites By similarity. Matrix protein p15: Virion Potential. Capsid protein p30: Virion Potential. Nucleocapsid protein p10: Virion Potential.
Domain	Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. 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.
Post-translational modification	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. RNA-binding phosphoprotein p12 is phosphorylated on serine residues By similarity.
Sequence similarities	Contains 1 CCHC-type zinc finger.

Ontologies

Keywords
Cellular component	Host cell membrane Host endosome Host membrane Membrane Viral matrix protein Virion
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding RNA-binding Viral nucleoprotein Zinc
Molecular function	Capsid protein
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	virion assembly Inferred from electronic annotation. Source: InterPro
Cellular component	host cell late endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell host multivesicular body Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-KW viral capsid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW structural molecule activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed; by host By similarity

Chain

2 – 537

536

Gag polyprotein

PRO_0000390806

Chain

2 – 129

128

Matrix protein p15 Potential

PRO_0000040876

Chain

130 – 214

RNA-binding phosphoprotein p12 Potential

PRO_0000040877

Chain

215 – 477

263

Capsid protein p30 Potential

PRO_0000040878

Chain

478 – 537

Nucleocapsid protein p10 Potential

PRO_0000040879

Regions

Zinc finger

501 – 518

CCHC-type

Coiled coil

437 – 478

Potential

Motif

109 – 112

PTAP/PSAP motif

Motif

128 – 132

LYPX(n)L motif

Motif

161 – 164

PPXY motif

Sites

Site

129 – 130

Cleavage; by viral protease p14 By similarity

Site

214 – 215

Cleavage; by viral protease p14 By similarity

Site

477 – 478

Cleavage; by viral protease p14 By similarity

Amino acid modifications

Modified residue

191

Phosphoserine; by host By similarity

Lipidation

N-myristoyl glycine; by host By similarity

Secondary structure

537

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P03336 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D35C4AD89B17CF93
Show »

FASTA

537

60,558

        10         20         30         40         50         60 
MGQTVTTPLS LTLEHWEDVQ RIASNQSVDV KKRRWVTFCS AEWPTFGVGW PQDGTFNLDI 

        70         80         90        100        110        120 
ILQVKSKVFS PGPHGHPDQV PYIVTWEAIA YEPPPWVKPF VSPKLSPSPT APILPSGPST 

       130        140        150        160        170        180 
QPPPRSALYP ALTPSIKPRP SKPQVLSDNG GPLIDLLSED PPPYGGQGLS SSDGDGDREE 

       190        200        210        220        230        240 
ATSTSEIPAP SPIVSRLRGK RDPPAADSTT SRAFPLRLGG NGQLQYWPFS SSDLYNWKNN 

       250        260        270        280        290        300 
NPSFSEDPGK LTALIESVLT THQPTWDDCQ QLLGTLLTGE EKQRVLLEAR KAVRGNDGRP 

       310        320        330        340        350        360 
TQLPNEVDAA FPLERPDWDY TTQRGRNHLV LYRQLLLAGL QNAGRSPTNL AKVKGITQGP 

       370        380        390        400        410        420 
NESPSAFLER LKEAYRRYTP YDPEDPGQET NVSMSFIWQS APDIGRKLER LEDLKSKTLG 

       430        440        450        460        470        480 
DLVREAERIF NKRETPEERE ERVRRETEEK EERRRAEEEQ KEKERDRRRH REMSKLLATV 

       490        500        510        520        530 
VSGQRQDRQG GERRRPQLDK DQCAYCKEKG HWAKDCPKKP RGPRGPRPQT SLLTLDD

« Hide

References

[1]	"Nucleotide sequence of AKV murine leukemia virus." Herr W. J. Virol. 49:471-478(1984) [PubMed: 6319746] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Consideration of the three-dimensional structure of core shells (capsids) in spherical retroviruses." Nermut M.V., Mulloy B. Micron 38:462-470(2007) [PubMed: 17223564] [Abstract] Cited for: SUBUNIT.
[3]	"High-resolution structure of a retroviral capsid hexameric amino-terminal domain." Mortuza G.B., Haire L.F., Stevens A., Smerdon S.J., Stoye J.P., Taylor I.A. Nature 431:481-485(2004) [PubMed: 15386017] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 215-345.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J01998 Genomic RNA. Translation: AAB03090.1.

PIR

FOMVGV. A03933.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U7K	X-ray	1.85	A/B/C/D/E/F	215-345	[»]
2Y4Z	X-ray	2.00	A	215-346	[»]
3BP9	X-ray	2.60	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/X/Y	215-346	[»]

ProteinModelPortal

P03336.

SMR

P03336. Positions 2-98, 215-345, 351-381, 478-533.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000840. G_retro_matrix_N.
IPR002079. Gag_p12.
IPR003036. Gag_p30.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR013084. Znf_CCH_retrovir.
IPR001878. Znf_CCHC.
[Graphical view]

Gene3D

G3DSA:1.10.150.180. G_retro_matrix_N. 1 hit.
G3DSA:4.10.60.10. Znf_CCH_retrovir. 1 hit.

Pfam

PF01140. Gag_MA. 1 hit.
PF01141. Gag_p12. 1 hit.
PF02093. Gag_p30. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]

SMART

SM00343. ZnF_C2HC. 1 hit.
[Graphical view]

SUPFAM

SSF47943. Retrov_capsid_N. 1 hit.
SSF47836. Retrovir_matrix. 1 hit.

PROSITE

PS50158. ZF_CCHC. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GAG_MLVAV

Accession

Primary (citable) accession number: P03336

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 4 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents