ID   GGAG_MLVF5              Reviewed;         627 AA.
AC   P0DOH0;
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   Friend murine leukemia virus (isolate 57) (FrMLV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   Murine leukemia virus.
OX   NCBI_TaxID=11796;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Friedrich R.W., Koch W., von Maydell-Livonius U., Schrewe H.,
RA   Zimmermann W.;
RL   Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases.
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=P0DOH0-1; Sequence=Displayed;
CC       Name=Gag polyprotein;
CC         IsoId=P26807-1; 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; X02794; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   SMR; P0DOH0; -.
DR   Proteomes; UP000007776; 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.
PE   3: Inferred from homology;
KW   Alternative initiation; Glycoprotein; Host cell membrane; Host membrane;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..627
FT                   /note="Glyco-Gag protein"
FT                   /id="PRO_0000441132"
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..627
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   REGION          199..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          523..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..219
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..565
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..612
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   627 AA;  70703 MW;  584990FF750EE542 CRC64;
     LGDVPRTSGA IFVARPESNH PDRFGLFGAP PLEEGYVVLV GDGRLKQFPP PSEFLLSVWN
     RSRAARLVCC SIVLCCLCLT VFLYLSENMG QTVTTPLSLT LDHWKDVERT AHNQSVEIRK
     RRWVTLCSAE WPTFNVGWPR DGTFNPDIIT QVKIKVFSSG PHGHPDQVPY IVTWEALAAD
     PPPWVKPFVH PKPPPLLLPP SAPSLPPEPP FPTPPQSSLY PALTSPLNTK PRPQVLPDSG
     GPLIDLLTED PPPYRDPGPS SSDGNGGSGE VAPTEGAPDS SPMVSRLRGR REPPVADSTT
     SQAFPLRQGG NGQFQYWPFS SSDLYNWKNN NPSFSEDPAK LTALIESVLL THQPTWDDCQ
     QLLGTLLTGE EKQRVLLEAR KAVRGEDGRP TQLPNDINDA FPLERPDWDY NTQRGRNHLV
     HYRQLLLAGL QNAGRSPTNL AKVKGITQGP NESPSAFLER LKEAYRRYTP YDPEDPGQET
     NVAMSFIWQS APDIGRKLER LEDLKSKTLG DLVREAEKIF NKRETPEERE ERIRRETEEK
     EERRRAEDEQ REKERDRRRH REMSKLLATV ISGQRQDRQG GERRRPQLDH DQCAYCKEKG
     HWARDCPKKP RGPRGPRPQA SLLTLDD