GGAG_MLVFP
ID GGAG_MLVFP Reviewed; 626 AA.
AC P0DOH6;
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 PVC-211) (FrMLV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=11798;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1620621; DOI=10.1093/nar/20.12.3249;
RA Remington M.P., Hoffman P.M., Ruscetti S.K., Masuda M.;
RT "Complete nucleotide sequence of a neuropathogenic variant of Friend murine
RT leukemia virus PVC-211.";
RL Nucleic Acids Res. 20:3249-3249(1992).
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=P0DOH6-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P26805-1; 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; M93134; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0DOH6; -.
DR Proteomes; UP000007777; 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; Glycoprotein; Host cell membrane; Host membrane;
KW Membrane; Metal-binding; Transmembrane; Transmembrane helix; Zinc;
KW Zinc-finger.
FT CHAIN 1..626
FT /note="Glyco-Gag protein"
FT /id="PRO_0000441140"
FT TOPO_DOM 1..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 68..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 199..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 COMPBIAS 199..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"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 626 AA; 70658 MW; D028F9FB7B2DE890 CRC64;
LGDVPGTSGA IFVARPESNY PDRFGLFGAP PLEEGYVILV GDGRLKRFPP PSEFLLSVWS
RSRAARPVCC SIVLCCFCLT VFLYLSENMG QTATTPLSLT LDHWKDVERT AHNQSVEVRK
RRWVTFCSAE WPTFNVGWPR DGTFNPDIIT QVKIKVFSPG PHGHPDQVPY IVTWEALAVD
PPPWVKPFVH PKPPLLLPPS APSLPPEPPL STPPQSSLYP ALTSPLNTKP RPQVLPDSGG
PLIDLLTEDP PPYRDPGPPS PDGKGDSGEV APTEGAPDSS PMVSRLRGRR EPPVADSTTS
QAFPLRLGGN GQFQYWPFSS SDLYNWKNNN PSFSEDPGKL TALIESVLLT HQPTWDDCQQ
LLGTLLTGEE KQRVLLEARK AVRGEDGRPT QLPNDINDAF PLERPDWDYN TQRGRNHLVH
YRQLLLAGLQ NAGRSPTNLA KVKGITQGPN ESPSAFLERL KEAYRRYTPY DPEDPGQETN
VSMSFIWQSA PDIGRKLERL EDLKNKTLGD LVREAEKIFN KRETPEEREE RVRRETEEKE
ERRRAEDERR EKERDRRRHR EMSKLLATVV SGQRQDRQGG ERRRPQLDHD QCAYCKEKGH
WARDCPKKPR GPRGPRPQAS LLTLDD
