ID   GGAG_MLVCB              Reviewed;         624 AA.
AC   P0DOH4;
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   Cas-Br-E murine leukemia virus.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   Murine leukemia virus.
OX   NCBI_TaxID=11792;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1840655; DOI=10.1093/nar/19.7.1707;
RA   Perryman S.M., McAtee F.J., Portis J.L.;
RT   "Complete nucleotide sequence of the neurotropic murine retrovirus CAS-BR-
RT   E.";
RL   Nucleic Acids Res. 19:1707-1707(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=P0DOH4-1; Sequence=Displayed;
CC       Name=Gag polyprotein;
CC         IsoId=P27460-1; 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; X57540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0DOH4; -.
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; Glycoprotein; Host cell membrane; Host membrane;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..624
FT                   /note="Glyco-Gag protein"
FT                   /id="PRO_0000441138"
FT   TOPO_DOM        1..63
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        64..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..624
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   REGION          200..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..562
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..609
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"
FT   CARBOHYD        478
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   624 AA;  70325 MW;  747D2C8B4D415905 CRC64;
     LGDVPGTSGA VFVARPESKS PDRFGLFGAP PLEEGYVILV GDENLKQFPP PSKFLPSVWN
     RSRAARLVCC SIVLCCLCLA VFLYWSENMG QTVTTPLSLT LDHWKDVERT AHNQSVDVKK
     RRWVTFCSVE WPTFNVGWPQ DGTFNRDIIT QVKIKVFSPG PHGHPDQVPY IVTWEALAFD
     PPPWVKPFVH PKPPLPPSAP SLLPEPPLST SPRSSLYPAL TPSLGAKPKP QVLPDSGGPL
     IDLLTEDPPP YRDPGPPPSD RDRDDGEAAP AGEAPDPSPM ASRLRGRREL PVADSTTSQA
     FPLRSGGNGQ LQYWPFSSSD LYNWKNNNPS FSEDPGKLTA LIESVLLTHQ PTWDDCQQLL
     GTLLTGEEKQ RVLLEARKAV RGEDGRPTQL PNEINDAFPL ERPDWDYNTQ RGRNHLVLYR
     QLLLAGLQNA GRSPTNLAKV KGITQGPNES PSAFLERLKE AYRRYTPYDP EDPGQETNVS
     MSFIWQSAPD IGRKLERLED LKSKTLGDLV REAEKIFNKR ETPEEREERI KRETEEKEER
     RRAEDEQKEK ERDRRRHREM SKLLATVVSG QKQDRQGGER RRPQLDKDQC AYCKEKGHWA
     KDCPKKPRGP RGPRPQTSLL ALDD