ID   GGAG_FSVST              Reviewed;         371 AA.
AC   P0DOG9;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2017, sequence version 1.
DT   02-JUN-2021, entry version 10.
DE   RecName: Full=Glyco-Gag protein;
DE   AltName: Full=Gross cell surface antigen;
DE   AltName: Full=glycosylated Pr80 gag;
DE            Short=gPr80 Gag;
DE            Short=gag-gPr80;
OS   Feline sarcoma virus (strain Snyder-Theilen).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=11780;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-75.
RX   PubMed=6296453; DOI=10.1128/jvi.45.1.466-472.1983;
RA   Hampe A., Gobet M., Even J., Sherr C.J., Galibert F.;
RT   "Nucleotide sequences of feline sarcoma virus long terminal repeats and 5'
RT   leaders show extensive homology to those of other mammalian retroviruses.";
RL   J. Virol. 45:466-472(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 75-371.
RX   PubMed=6183005; DOI=10.1016/0092-8674(82)90282-3;
RA   Hampe A., Laprevotte I., Galibert F., Fedele L.A., Sherr C.J.;
RT   "Nucleotide sequences of feline retroviral oncogenes (v-fes) provide
RT   evidence for a family of tyrosine-specific protein kinase genes.";
RL   Cell 30:775-785(1982).
CC   -!- FUNCTION: Plays a role in viral particle release. Presumably acts by
CC       facilitating the fission of the virion bud at the cell surface.
CC       {ECO:0000250|UniProtKB:P0DOG8}.
CC   -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000250|UniProtKB:P0DOG8,
CC       ECO:0000255}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P0DOG8}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Glyco-Gag protein;
CC         IsoId=P0DOG9-1; Sequence=Displayed;
CC       Name=Gag polyprotein;
CC         IsoId=P03338-1; Sequence=External;
CC   -!- PTM: Glycosylated by host. {ECO:0000250|UniProtKB:P0DOG8}.
CC   -!- PTM: Cleaved by host near the middle of the molecule, releasing the c-
CC       terminal half containing capsid and nucleoprotein domains op GAG.
CC       {ECO:0000250|UniProtKB:P0DOG8}.
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DR   EMBL; J02088; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   SMR; P0DOG9; -.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019068; P:virion assembly; IEA:InterPro.
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   Pfam; PF01140; Gag_MA; 1.
DR   Pfam; PF01141; Gag_p12; 1.
DR   Pfam; PF02093; Gag_p30; 1.
DR   SUPFAM; SSF47836; SSF47836; 1.
DR   SUPFAM; SSF47943; SSF47943; 1.
PE   3: Inferred from homology;
KW   Alternative initiation; Glycoprotein; Host cell membrane; Host membrane;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..371
FT                   /note="Glyco-Gag protein"
FT                   /id="PRO_0000441134"
FT   TOPO_DOM        1..51
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..371
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   REGION          171..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..192
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..248
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   371 AA;  40830 MW;  5842DCC63483F420 CRC64;
     MSGASSGTAI GAHLFGVSPE YRVLIGDEGA GPSKSLSEVS FSVWYRSRAA RLVILCLVAS
     FLVPCLTFLI AEAVMGQTVT TPLSLTLDHW SEVRARAHNQ GVEVRKKKWI TLCKAEWVMM
     NVGWPREGTF SLDNISQVKK KIFAPGPHGH PDQVPYITTW RSLATDPPSW VRPFLPPPKP
     PTPLPQPLSP QPSAPLTSSL YPVVPKPDPP KPPVLPPDPS SPLIDLLTEE PPPYPGGHGP
     PPSGPRTPAA SPIVSRLRER RENPAEESQA LPLREGPNNR PQYWPFSASD LYNWKSHNPP
     FSQDPVALTN LIESILVTHQ PTWDDCQQLL QALLTGEERQ RVLLEARKQV PGEDGRPTQL
     PNVIDETFPL T