ID   GGAG_FSVGA              Reviewed;         425 AA.
AC   P0DOH1;
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 Gardner-Arnstein) (Ga-FeSV) (Gardner-Arnstein
OS   feline leukemia oncovirus B).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=11774;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-78.
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 78-425.
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=P0DOH1-1; Sequence=Displayed;
CC       Name=Gag polyprotein;
CC         IsoId=P03337-1; 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J02086; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; J02087; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   SMR; P0DOH1; -.
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..425
FT                   /note="Glyco-Gag protein"
FT                   /id="PRO_0000441135"
FT   TOPO_DOM        1..54
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        76..425
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   REGION          174..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..195
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..251
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00498"
SQ   SEQUENCE   425 AA;  47009 MW;  973A137FE537B1A7 CRC64;
     MSRASSGTAT GARLFGISSV LGEYRVLIGD EGAGPSRSPS EVSFSVWYRS RAARLVIVCL
     VASFLVPCLT FLIAETVMGQ TITTPLSLTL DHWSEVRARA HNQGVEVRKK KWITLCEAEW
     VMMNVGWPRE GTFSLDNISQ VEKKIFAPGP YGHPDQVPYI TTWRSLATDP PSWVRPFLPP
     PKPPTSLPQP LSPQPSAPLT SSLYPVLPKS DPPKPPVLPP DPSSPLIDLL TEEPPPYPGG
     HGPPPSGPRT PTASPIASRL RERRENPAEE SQALPLREGP NNRPQYWPFS ASDLYNWKSH
     NPPFSQDPVA LTNLIESILV THQPTWDDCQ QLLQALLTGE ERQRVLLEAR KQVPGEDGRP
     TQLPNVIDET FPLTRPNWDF ATPAGREHLR LYRQLLLAGL RGAARRPTNL AQVKQVVQGK
     EETPA