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Gag polyprotein (Core polyprotein) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10 (NC-gag)]

 GAG_FSVMD               Reviewed;         459 AA.
P03340;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
30-AUG-2017, sequence version 2.
30-AUG-2017, entry version 89.
RecName: Full=Gag polyprotein;
AltName: Full=Core polyprotein;
Contains:
RecName: Full=Matrix protein p15;
Short=MA;
Contains:
RecName: Full=RNA-binding phosphoprotein p12;
AltName: Full=pp12;
Contains:
RecName: Full=Capsid protein p30;
Short=CA;
Contains:
RecName: Full=Nucleocapsid protein p10;
Short=NC-gag;
Name=gag;
Feline sarcoma virus (strain McDonough).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Gammaretrovirus.
NCBI_TaxID=11778;
NCBI_TaxID=9681; Felidae (cat family).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6582485; DOI=10.1073/pnas.81.1.85;
Hampe A., Gobet M., Sherr C.J., Galibert F.;
"Nucleotide sequence of the feline retroviral oncogene v-fms shows
unexpected homology with oncogenes encoding tyrosine-specific protein
kinases.";
Proc. Natl. Acad. Sci. U.S.A. 81:85-89(1984).
-!- 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).
{ECO:0000250}.
-!- FUNCTION: 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).
{ECO:0000250}.
-!- FUNCTION: Capsid protein p30 forms the spherical core of the
virion that encapsulates the genomic RNA-nucleocapsid complex.
{ECO:0000250}.
-!- SUBUNIT: 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). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Gag polyprotein: Virion {ECO:0000250}. Host
cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Matrix protein p15: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein p30: Virion {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Gag polyprotein;
IsoId=P03340-1; Sequence=Displayed;
Name=Glyco-Gag protein;
IsoId=P0DOH2-1; Sequence=External;
-!- DOMAIN: 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). {ECO:0000250}.
-!- PTM: 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). {ECO:0000250}.
-!- MISCELLANEOUS: This protein is synthesized as a Gag-Fms
polyprotein.
-!- CAUTION: This gag polyprotein encodes a truncated nucleoprotein.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA43045.1; Type=Erroneous gene model prediction; Evidence={ECO:0000250|UniProtKB:P03336};
-----------------------------------------------------------------------
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EMBL; K01643; AAA43045.1; ALT_SEQ; Genomic_RNA.
PIR; A03938; FOMVMD.
ProteinModelPortal; P03340; -.
ELM; P03340; -.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-KW.
Gene3D; 1.10.150.180; -; 1.
Gene3D; 1.10.375.10; -; 1.
InterPro; IPR000840; G_retro_matrix.
InterPro; IPR002079; Gag_p12.
InterPro; IPR003036; Gag_P30.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
Pfam; PF01140; Gag_MA; 1.
Pfam; PF01141; Gag_p12; 1.
Pfam; PF02093; Gag_p30; 1.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
3: Inferred from homology;
Alternative initiation; Capsid protein; Host cell membrane;
Host membrane; Host-virus interaction; Lipoprotein; Membrane;
Myristate; RNA-binding; Viral budding;
Viral budding via the host ESCRT complexes; Viral matrix protein;
Viral nucleoprotein; Virion; Virus exit from host cell.
INIT_MET 1 1 Removed; by host.
{ECO:0000250|UniProtKB:P03336}.
CHAIN 2 459 Gag polyprotein.
/FTId=PRO_0000390802.
CHAIN 2 127 Matrix protein p15. {ECO:0000255}.
/FTId=PRO_0000040852.
CHAIN 128 197 RNA-binding phosphoprotein p12.
{ECO:0000255}.
/FTId=PRO_0000040853.
CHAIN 198 445 Capsid protein p30. {ECO:0000255}.
/FTId=PRO_0000040854.
CHAIN 446 459 Nucleocapsid protein p10. {ECO:0000255}.
/FTId=PRO_0000040855.
MOTIF 118 121 PTAP/PSAP motif.
MOTIF 126 130 LYPX(n)L motif.
MOTIF 157 160 PPXY motif.
SITE 127 128 Cleavage; by viral protease.
{ECO:0000250}.
SITE 197 198 Cleavage; by viral protease.
{ECO:0000250}.
SITE 445 446 Cleavage; by viral protease.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
SEQUENCE 459 AA; 52197 MW; A10AAF4A18E75305 CRC64;
MGQTVTTPPS LTLDHWSEVR TRAHNQGIEV RKKKWITLCE AEWVMMNVGW PREGTPPLDN
TSQVEKRIFA PGPHGHPDQV PYITTWRSLA TDPPSWVRPF LPPPKPPTPL PQPLSPQPSA
PPTSSLYPVL PKTNPPKPPV LPPDPSSPLI DLLTEEPPPY PGGHGPPPSG LRTPAASPIA
SRLRERRENP AEESQALPLR EGPNNRPQYW PFSASDLYNW KLHNPPFSQD PVALTNLIES
ILVTHQPTWD DCQQLLQALL TAEERQRVLL EARKQVPGED GRPTQLPNVI DEAFPLTRPN
WDFATPAGRE HLRLYRQLLL AGLRGAARRP TNLAQVKQVV QGKEETPASF LERLKEAYRM
YTPYDPEDPG QAASVILSFI YQSSPDIRNK LQRLEGLQGF TLSDLLKEAE KIYNKRETPE
EREERLWQRQ EERDKKRHKE MTKVLATVVT QNRNKDREE


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