GAG_FLV
ID GAG_FLV Reviewed; 506 AA.
AC P10262; Q85560;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 3.
DT 02-JUN-2021, entry version 106.
DE RecName: Full=Gag polyprotein;
DE AltName: Full=Core polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p15;
DE Short=MA;
DE Contains:
DE RecName: Full=RNA-binding phosphoprotein p12;
DE AltName: Full=pp12;
DE Contains:
DE RecName: Full=Capsid protein p30;
DE Short=CA;
DE Contains:
DE RecName: Full=Nucleocapsid protein p10-Gag;
DE Short=NC-gag;
GN Name=gag;
OS Feline leukemia virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11768;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND ALTERNATIVE INITIATION.
RX PubMed=6328019; DOI=10.1128/jvi.50.3.884-894.1984;
RA Laprevotte I., Hampe A., Sherr C.J., Galibert F.;
RT "Nucleotide sequence of the gag gene and gag-pol junction of feline
RT leukemia virus.";
RL J. Virol. 50:884-894(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rickard subgroup A;
RX PubMed=9696797; DOI=10.1128/jvi.72.9.7048-7056.1998;
RA Chen H., Bechtel M.K., Shi Y., Phipps A., Mathes L.E., Hayes K.A.,
RA Roy-Burman P.;
RT "Pathogenicity induced by feline leukemia virus, Rickard strain, subgroup A
RT plasmid DNA (pFRA).";
RL J. Virol. 72:7048-7056(1998).
CC -!- FUNCTION: [Gag polyprotein]: Plays a role in budding and is processed
CC by the viral protease during virion maturation outside the cell. During
CC budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-
CC like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to
CC Gag binding host factors. Interaction with HECT ubiquitin ligases
CC probably links the viral protein to the host ESCRT pathway and
CC facilitates release. {ECO:0000250|UniProtKB:P03332}.
CC -!- FUNCTION: [Matrix protein p15]: Targets Gag and gag-pol polyproteins to
CC the plasma membrane via a multipartite membrane binding signal, that
CC includes its myristoylated N-terminus. Also mediates nuclear
CC localization of the pre-integration complex.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- FUNCTION: [RNA-binding phosphoprotein p12]: Constituent of the pre-
CC integration complex (PIC) which tethers the latter to mitotic
CC chromosomes. {ECO:0000250|UniProtKB:P03332}.
CC -!- FUNCTION: [Capsid protein p30]: Forms the spherical core of the virion
CC that encapsulates the genomic RNA-nucleocapsid complex.
CC {ECO:0000250|UniProtKB:P03336}.
CC -!- FUNCTION: [Nucleocapsid protein p10-Gag]: Involved in the packaging and
CC encapsidation of two copies of the genome. Binds with high affinity to
CC conserved elements within the packaging signal, located near the 5'-end
CC of the genome. This binding is dependent on genome dimerization.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- SUBUNIT: [Capsid protein p30]: Homohexamer; further associates as
CC homomultimer (By similarity). The virus core is composed of a lattice
CC formed from hexagonal rings, each containing six capsid monomers (By
CC similarity). {ECO:0000250|UniProtKB:P03355}.
CC -!- SUBUNIT: [Gag polyprotein]: Interacts (via PPXY motif) with host NEDD4
CC (By similarity). Interacts (via PSAP motif) with host TSG101 (By
CC similarity). Interacts (via LYPX(n)L motif) with host PDCD6IP (By
CC similarity). {ECO:0000250|UniProtKB:P03355, ECO:0000255|PROSITE-
CC ProRule:PRU00405}.
CC -!- SUBCELLULAR LOCATION: [Gag polyprotein]: Virion
CC {ECO:0000250|UniProtKB:P03332}. Host cell membrane
CC {ECO:0000250|UniProtKB:P03332}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P03332}. Host late endosome membrane
CC {ECO:0000250|UniProtKB:P03332}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular body
CC {ECO:0000250|UniProtKB:P26807}. Note=These locations are probably
CC linked to virus assembly sites. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p30]: Virion
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p10-Gag]: Virion
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- SUBCELLULAR LOCATION: [RNA-binding phosphoprotein p12]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P03332}. Note=Localizes to the host cytoplasm
CC early in infection and binds to the mitotic chromosomes later on.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Gag polyprotein;
CC IsoId=P10262-1; Sequence=Displayed;
CC Name=Glyco-Gag protein;
CC IsoId=P0DOH3-1; Sequence=External;
CC -!- DOMAIN: [Gag polyprotein]: Late-budding domains (L domains) are short
CC sequence motifs essential for viral particle release. They can occur
CC individually or in close proximity within structural proteins. They
CC interacts with sorting cellular proteins of the multivesicular body
CC (MVB) pathway. Most of these proteins are class E vacuolar protein
CC sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes.
CC RNA-binding phosphoprotein p12 contains one L domain: a PPXY motif
CC which potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin
CC ligase. PPXY motif is essential for virus egress. Matrix protein p15
CC contains one L domain: a PTAP/PSAP motif, which potentially interacts
CC with the UEV domain of TSG101. The junction between the matrix protein
CC p15 and RNA-binding phosphoprotein p12 also contains one L domain: a
CC LYPX(n)L motif which potentially interacts with PDCD6IP. Both PSAP and
CC LYPX(n)L domains might play little to no role in budding and possibly
CC drive residual virus release. contains. {ECO:0000250|UniProtKB:P03332}.
CC -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral
CC protease yield mature proteins. The protease is released by
CC autocatalytic cleavage. The polyprotein is cleaved during and after
CC budding, this process is termed maturation.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- PTM: RNA-binding phosphoprotein p12 is phosphorylated on serine
CC residues. {ECO:0000250|UniProtKB:P03332}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA43054.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF052723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; K01803; AAA43054.1; ALT_INIT; Genomic_RNA.
DR SMR; P10262; -.
DR Proteomes; UP000118006; Genome.
DR GO; GO:0044185; C:host cell late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.180; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR InterPro; IPR000840; G_retro_matrix.
DR InterPro; IPR036946; G_retro_matrix_sf.
DR InterPro; IPR002079; Gag_p12.
DR InterPro; IPR003036; Gag_P30.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF01140; Gag_MA; 1.
DR Pfam; PF01141; Gag_p12; 1.
DR Pfam; PF02093; Gag_p30; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Alternative initiation; Capsid protein; Host cell membrane; Host cytoplasm;
KW Host endosome; Host membrane; Host-virus interaction; Lipoprotein;
KW Membrane; Metal-binding; Myristate; Phosphoprotein; RNA-binding;
KW Viral budding; Viral budding via the host ESCRT complexes;
KW Viral matrix protein; Viral nucleoprotein; Viral release from host cell;
KW Virion; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255"
FT CHAIN 2..506
FT /note="Gag polyprotein"
FT /id="PRO_0000390798"
FT CHAIN 2..127
FT /note="Matrix protein p15"
FT /id="PRO_0000040837"
FT CHAIN 128..197
FT /note="RNA-binding phosphoprotein p12"
FT /id="PRO_0000040838"
FT CHAIN 198..445
FT /note="Capsid protein p30"
FT /id="PRO_0000040839"
FT CHAIN 446..506
FT /note="Nucleocapsid protein p10-Gag"
FT /id="PRO_0000040840"
FT ZN_FING 473..490
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 97..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 118..121
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT MOTIF 126..130
FT /note="LYPX(n)L motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT MOTIF 157..160
FT /note="PPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT COMPBIAS 97..118
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 127..128
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT SITE 197..198
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT SITE 445..446
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255"
FT VARIANT 5
FT /note="I -> V"
FT /evidence="ECO:0000305|PubMed:6328019"
FT VARIANT 74
FT /note="Y -> H"
FT /evidence="ECO:0000305|PubMed:6328019"
FT VARIANT 130
FT /note="L -> V"
FT /evidence="ECO:0000305|PubMed:6328019"
FT VARIANT 133
FT /note="S -> P"
FT /evidence="ECO:0000305|PubMed:6328019"
FT VARIANT 175
FT /note="T -> A"
FT /evidence="ECO:0000305|PubMed:6328019"
FT VARIANT 460
FT /note="S -> N"
FT /evidence="ECO:0000305|PubMed:6328019"
FT VARIANT 505
FT /note="G -> E"
FT /evidence="ECO:0000305|PubMed:6328019"
SQ SEQUENCE 506 AA; 57527 MW; D18569C69A6DEF6F CRC64;
MGQTITTPLS LTLDHWSEVR ARAHNQGVEV RKKKWITLCE AEWVMMNVGW PREGTFSLDN
ISQVEKKIFA PGPYGHPDQV PYITTWRSLA TDPPSWVRPF LPPPKPPTPL PQPLSPQPSA
PLTSSLYPVL PKSDPPKPPV LPPDPSSPLI DLLTEEPPPY PGGHGPPPSG PRTPTASPIA
SRLRERRENP AEESQALPLR EGPNNRPQYW PFSASDLYNW KSHNPPFSQD PVALTNLIES
ILVTHQPTWD DCQQLLQALL TGEERQRVLL EARKQVPGED GRPTQLPNVI DETFPLTRPN
WDFATPAGRE HLRLYRQLLL AGLRGAARRP TNLAQVKQVV QGKEETPAAF LERLKEAYRM
YTPYDPEDPG QAASVILSFI YQSSPDIRNK LQRLEGLQGF TLSDLLKEAE KIYNKRETPE
EREERLWQRQ EERDKKRHKE MTKVLATVVA QNRDKDREES KLGDQRKIPL GKDQCAYCKE
KGHWVRDCPK RPRKKPANST LLNLGD
