P29175 (GAG_MSVFR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gag polyprotein

Alternative name(s):
Core polyprotein

Cleaved into the following 3 chains:

1. Matrix protein p15
   Short name=MA
2. RNA-binding phosphoprotein p12
   Alternative name(s):
   pp12
3. Capsid protein p30
   Short name=CA

Gene names

Name:

gag

Organism

FBR murine osteosarcoma virus (FBR-MSV) (Finkel-Biskis-Reilly murine osteosarcoma virus)

Taxonomic identifier

11806 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Gammaretrovirus

Virus host

Mus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length	310 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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. Capsid protein p30 forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex 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.
Subcellular location	Gag polyprotein: Virion By similarity. Host cell membrane; Lipid-anchor Potential. Matrix protein p15: Virion Potential. Capsid protein p30: 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 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.
Miscellaneous	This protein is synthesized as a Gag-Fos-Fox polyprotein.

Ontologies

Keywords
Cellular component	Host cell membrane Host membrane Membrane Viral matrix protein Virion
Ligand	RNA-binding
Molecular function	Capsid protein
PTM	Lipoprotein Myristate
Gene Ontology (GO)
Biological process	virion assembly Inferred from electronic annotation. Source: InterPro
Cellular component	host cell plasma membrane 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed; by host By similarity
	Chain	2 – 310	309	Gag polyprotein		PRO_0000390817
	Chain	2 – 129	128	Matrix protein p15 Potential		PRO_0000040946
	Chain	130 – 214	85	RNA-binding phosphoprotein p12 Potential		PRO_0000040947
	Chain	215 – 310	96	Capsid protein p30 Potential		PRO_0000040948
Regions
	Motif	109 – 112	4	PTAP/PSAP motif
	Motif	128 – 132	5	LYPX(n)L motif
	Motif	161 – 164	4	PPXY motif
Sites
	Site	129 – 130	2	Cleavage; by viral protease By similarity
	Site	214 – 215	2	Cleavage; by viral protease By similarity
Amino acid modifications
	Lipidation	2	1	N-myristoyl glycine; by host By similarity

Sequences

	Sequence		Length	Mass (Da)
	P29175 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F5713E16959C5F8C	FASTA	310	33,849
	10 20 30 40 50 60 MGQTVTTPLS LTLEHWGDVQ RIASNQSVDV KKRRWVTFCS AEWPTFDVGW PQDGTFNLDI 70 80 90 100 110 120 ILQVKSKVFS PGPHGHPDQV PYIVTWEAIA YEPPPWVKPF VSPKLSPSPT APILPSGPST 130 140 150 160 170 180 QPPPRSALYP ALTPSIKPRP SKPQVLSDDG GPLIDLLTED PPPYGEQGPS SSDGDGDREE 190 200 210 220 230 240 ATSTSEIPAP SPMVSRLRGK RDPPAADSTT SRAFPLRLGG NGQKNNNPSF SEDPGKLTAL 250 260 270 280 290 300 IESVLTTHQP TWDDCQQLLG TLLTGEEKQR VLLEARKAVR GNDGRPTQMP NEVNAAFPLE 310 RPDWDYTTPE

References

[1]	"FBR murine osteosarcoma virus. II. Nucleotide sequence of the provirus reveals that the genome contains sequences acquired from two cellular genes." van Beveren C., Enami S., Curran T., Verma I.M. Virology 135:229-243(1984) [PubMed: 6203215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	K02712 Genomic DNA. Translation: AAA46573.1. Different termination.
PIR	FOMVFB. A23244.
3D structure databases
ProteinModelPortal	P29175.
SMR	P29175. Positions 2-98, 215-310.
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. [Graphical view]
Gene3D	G3DSA:1.10.150.180. G_retro_matrix_N. 1 hit.
Pfam	PF01140. Gag_MA. 1 hit. PF01141. Gag_p12. 1 hit. PF02093. Gag_p30. 1 hit. [Graphical view]
SUPFAM	SSF47943. Retrov_capsid_N. 1 hit. SSF47836. Retrovir_matrix. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GAG_MSVFR

Accession

Primary (citable) accession number: P29175

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	January 23, 2007
Last modified:	November 30, 2010
This is version 69 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program