ID   GGAG_MLVFF              Reviewed;         626 AA.
AC   P0DOH5;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2017, sequence version 1.
DT   02-JUN-2021, entry version 12.
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   Friend murine leukemia virus (isolate FB29) (FrMLV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   Murine leukemia virus.
OX   NCBI_TaxID=11797;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1762923; DOI=10.1093/nar/19.24.6950;
RA   Perryman S., Nishio J., Chesebro B.;
RT   "Complete nucleotide sequence of Friend murine leukemia virus, strain
RT   FB29.";
RL   Nucleic Acids Res. 19:6950-6950(1991).
CC   -!- FUNCTION: Plays a role in viral particle release. Presumably acts by
CC       facilitating the fission of the virion bud at the cell surface. May
CC       prevent the antiviral activity of murine APOBEC3.
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=P0DOH5-1; Sequence=Displayed;
CC       Name=Gag polyprotein;
CC         IsoId=P26806-1; 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; Z11128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0DOH5; -.
DR   Proteomes; UP000008877; Genome.
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; 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; Coiled coil; Glycoprotein; Host cell membrane;
KW   Host membrane; Membrane; Metal-binding; Transmembrane; Transmembrane helix;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..626
FT                   /note="Glyco-Gag protein"
FT                   /id="PRO_0000441139"
FT   TOPO_DOM        1..66
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        67..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..626
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   ZN_FING         590..607
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          198..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          522..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          526..566
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        198..215
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..564
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..611
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   626 AA;  70523 MW;  81E46D70416EC60D CRC64;
     LGDVPGTSGA IFVARPESNH PDRFGLFGAP PLEEGYVVLV GDRGLKRFPP PSEFLLSVWN
     RSRAARLVCC SIVLCCLCLT VFLYLSENMG QAVTTPLSLT LDHWKDVERT AHNLSVEVRK
     RRWVTFCSAE WPTFNVGWPR DGTFNPDIIT QVKIKVFSPG PHGHPDQVPY IVTWEAIAVD
     PPPWVRPFVH PKPPLSLPPS APSLPPEPPL STPPQSSLYP ALTSPLNTKP RPQVLPDSGG
     PLIDLLTEDP PPYRDPGPPS PDGNGDSGEV APTEGAPDPS PMVSRLRGRK EPPVADSTTS
     QAFPLRLGGN GQYQYWPFSS SDLYNWKNNN PSFSEDPAKL TALIESVLLT HQPTWDDCQQ
     LLGTLLTGEE KQRVLLEARK AVRGEDGRPT QLPNDINDAF PLERPDWDYN TQRGRNHLVH
     YRQLLLAGLQ NAGRSPTNLA KVKGITQGPN ESPSAFLERL KEAYRRYTPY DPEDPGQETN
     VAMSFIWQSA PDIGRKLERL EDLKSKTLGD LVREAEKIFN KRETPEEREE RIRRETEEKE
     ERRRAEDVQR EKERDRRRHR EMSKLLATVV SGQRQDRQGG ERRRPQLDHD QCAYCKEKGH
     WARDCPKKPR GPRGPRPQAS LLTLDD