ID   GGAG_FSVMD              Reviewed;         536 AA.
AC   P0DOH2;
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 McDonough).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=11778;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6582485; DOI=10.1073/pnas.81.1.85;
RA   Hampe A., Gobet M., Sherr C.J., Galibert F.;
RT   "Nucleotide sequence of the feline retroviral oncogene v-fms shows
RT   unexpected homology with oncogenes encoding tyrosine-specific protein
RT   kinases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:85-89(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=P0DOH2-1; Sequence=Displayed;
CC       Name=Gag polyprotein;
CC         IsoId=P03340-1; 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; K01643; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   SMR; P0DOH2; -.
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..536
FT                   /note="Glyco-Gag protein"
FT                   /id="PRO_0000441136"
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..536
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   REGION          174..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..250
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..520
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   536 AA;  60235 MW;  FBBC80D612AC8702 CRC64;
     MSGASSGTAT GARLFGISSV LGEYRVLIGD EGAGPSRSPS EVSFSVWYRS RAARLVILCL
     VASFLVPCLT FLIAETVMGQ TVTTPPSLTL DHWSEVRTRA HNQGIEVRKK KWITLCEAEW
     VMMNVGWPRE GTPPLDNTSQ VEKRIFAPGP HGHPDQVPYI TTWRSLATDP PSWVRPFLPP
     PKPPTPLPQP LSPQPSAPPT SSLYPVLPKT NPPKPPVLPP DPSSPLIDLL TEEPPPYPGG
     HGPPPSGLRT PAASPIASRL RERRENPAEE SQALPLREGP NNRPQYWPFS ASDLYNWKLH
     NPPFSQDPVA LTNLIESILV THQPTWDDCQ QLLQALLTAE ERQRVLLEAR KQVPGEDGRP
     TQLPNVIDEA FPLTRPNWDF ATPAGREHLR LYRQLLLAGL RGAARRPTNL AQVKQVVQGK
     EETPASFLER LKEAYRMYTP YDPEDPGQAA SVILSFIYQS SPDIRNKLQR LEGLQGFTLS
     DLLKEAEKIY NKRETPEERE ERLWQRQEER DKKRHKEMTK VLATVVTQNR NKDREE