P03337 (GAG_FSVGA) 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

Feline sarcoma virus (strain Gardner-Arnstein) (Ga-FeSV) (Gardner-Arnstein feline leukemia oncovirus B)

Taxonomic identifier

11774 [NCBI]

Taxonomic lineage

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

Virus host

Felidae (cat family) [TaxID: 9681]

Protein attributes

Sequence length	425 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. Matrix protein p15 contains one L domain: a PTAP/PSAP motif, which potentially interacts with the UEV domain of TSG101. RNA-binding phosphoprotein p12 contains one L domain: a PPXY motif which potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase. 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-Fes 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
	Chain	1 – 425	425	Gag polyprotein		PRO_0000390800
	Propeptide	1 – 77	77	Leader peptide Potential		PRO_0000040843
	Chain	78 – 204	127	Matrix protein p15 Potential		PRO_0000040844
	Chain	205 – 274	70	RNA-binding phosphoprotein p12 Potential		PRO_0000040845
	Chain	275 – 425	151	Capsid protein p30 Potential		PRO_0000040846
Regions
	Motif	195 – 198	4	PTAP/PSAP motif
	Motif	234 – 237	4	PPXY motif
Sites
	Site	204 – 205	2	Cleavage; by viral protease By similarity
	Site	274 – 275	2	Cleavage; by viral protease By similarity
Amino acid modifications
	Lipidation	79	1	N-myristoyl glycine; by host By similarity

Sequences

	Sequence		Length	Mass (Da)
	P03337 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 973A137FE537B1A7	FASTA	425	47,009
	10 20 30 40 50 60 MSRASSGTAT GARLFGISSV LGEYRVLIGD EGAGPSRSPS EVSFSVWYRS RAARLVIVCL 70 80 90 100 110 120 VASFLVPCLT FLIAETVMGQ TITTPLSLTL DHWSEVRARA HNQGVEVRKK KWITLCEAEW 130 140 150 160 170 180 VMMNVGWPRE GTFSLDNISQ VEKKIFAPGP YGHPDQVPYI TTWRSLATDP PSWVRPFLPP 190 200 210 220 230 240 PKPPTSLPQP LSPQPSAPLT SSLYPVLPKS DPPKPPVLPP DPSSPLIDLL TEEPPPYPGG 250 260 270 280 290 300 HGPPPSGPRT PTASPIASRL RERRENPAEE SQALPLREGP NNRPQYWPFS ASDLYNWKSH 310 320 330 340 350 360 NPPFSQDPVA LTNLIESILV THQPTWDDCQ QLLQALLTGE ERQRVLLEAR KQVPGEDGRP 370 380 390 400 410 420 TQLPNVIDET FPLTRPNWDF ATPAGREHLR LYRQLLLAGL RGAARRPTNL AQVKQVVQGK EETPA

References

[1]	"Nucleotide sequences of feline sarcoma virus long terminal repeats and 5' leaders show extensive homology to those of other mammalian retroviruses." Hampe A., Gobet M., Even J., Sherr C.J., Galibert F. J. Virol. 45:466-472(1983) [PubMed: 6296453] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-78.
[2]	"Nucleotide sequences of feline retroviral oncogenes (v-fes) provide evidence for a family of tyrosine-specific protein kinase genes." Hampe A., Laprevotte I., Galibert F., Fedele L.A., Sherr C.J. Cell 30:775-785(1982) [PubMed: 6183005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 78-425.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J02086 Genomic RNA. No translation available. J02087 Genomic RNA. Translation: AAA43041.1.
PIR	FOMVGC. A03934.
3D structure databases
ProteinModelPortal	P03337.
SMR	P03337. Positions 79-175, 275-405.
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_FSVGA

Accession

Primary (citable) accession number: P03337

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 30, 2010
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program