ID   GGAG_FLV                Reviewed;         580 AA.
AC   P0DOH3;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2017, sequence version 1.
DT   02-JUN-2021, entry version 11.
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 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].
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).
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=P0DOH3-1; Sequence=Displayed;
CC       Name=Gag polyprotein;
CC         IsoId=P10262-1; 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; K01803; AAA43055.1; -; Genomic_RNA.
DR   SMR; P0DOH3; -.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 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; 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; Glycoprotein; Host cell membrane; Host membrane;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..580
FT                   /note="Glyco-Gag protein"
FT                   /id="PRO_0000441137"
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..580
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   REGION          171..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..580
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"
FT   CARBOHYD        572
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   580 AA;  65195 MW;  10F8C3775B37042C CRC64;
     MSGASSGTAI GAHLFGVSPE YRVLIGDGGA GPSKSLSEVS FSVWYRSRAA RLVILCLVAS
     FLVPCLTFLI AEAVMGQTVT TPLSLTLDHW SEVRARAHNQ GVEVRKKKWI TLCEAEWVMM
     NVGWPREGTF SLDNISQVEK KIFAPGPHGH PDQVPYITTW RSLATDPPSW VRPFLPPPKP
     PTPLPQPLSP QPSAPLTSSL YPVVPKPDPP KPPVLPPDPS SPLIDLLTEE PPPYPGGHGP
     PPSGPRTPAA SPIASRLRER RENPAEESQA LPLREGPNNR PQYWPFSASD LYNWKSHNPP
     FSQDPVALTN LIESILVTHQ PTWDDCQQLL QALLTGEERQ RVLLEARKQV PGEDGRPTQL
     PNVIDETFPL TRPNWDFATP AGREHLRLYR QLLLAGLRGA ARRPTNLAQV KQVVQGKEET
     PAAFLERLKE AYRMYTPYDP EDPGQAASVI LSFIYQSSPD IRNKLQRLEG LQGFTLSDLL
     KEAEKIYNKR ETPEEREERL WQRQEERDKK RHKEMTKVLA TVVAQNRDKD REENKLGDQR
     KIPLGKDQCA YCKEKGHWVR DCPKRPRKKP ANSTLLNLED