GGAG_MLVAV
ID GGAG_MLVAV Reviewed; 625 AA.
AC P0DOG8;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 1.
DT 02-JUN-2021, entry version 13.
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 AKV murine leukemia virus (AKR (endogenous) murine leukemia virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=11791;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6319746; DOI=10.1128/jvi.49.2.471-478.1984;
RA Herr W.;
RT "Nucleotide sequence of AKV murine leukemia virus.";
RL J. Virol. 49:471-478(1984).
RN [2]
RP GLYCOSYLATION.
RX PubMed=6997511; DOI=10.1128/jvi.35.1.41-51.1980;
RA Edwards S.A., Fan H.;
RT "Sequence relationship of glycosylated and unglycosylated gag polyproteins
RT of Moloney murine leukemia virus.";
RL J. Virol. 35:41-51(1980).
RN [3]
RP ALTERNATIVE INITIATION.
RX PubMed=2538626; DOI=10.1016/0022-2836(89)90347-1;
RA Prats A.C., De Billy G., Wang P., Darlix J.L.;
RT "CUG initiation codon used for the synthesis of a cell surface antigen
RT coded by the murine leukemia virus.";
RL J. Mol. Biol. 205:363-372(1989).
RN [4]
RP CLEAVAGE BY HOST, AND SUBCELLULAR LOCATION.
RX PubMed=9188605; DOI=10.1128/jvi.71.7.5355-5360.1997;
RA Fujisawa R., McAtee F.J., Zirbel J.H., Portis J.L.;
RT "Characterization of glycosylated Gag expressed by a neurovirulent murine
RT leukemia virus: identification of differences in processing in vitro and in
RT vivo.";
RL J. Virol. 71:5355-5360(1997).
RN [5]
RP INITIATION WITH LEUCINE.
RX PubMed=15510226; DOI=10.1371/journal.pbio.0020366;
RA Schwab S.R., Shugart J.A., Horng T., Malarkannan S., Shastri N.;
RT "Unanticipated antigens: translation initiation at CUG with leucine.";
RL PLoS Biol. 2:E366-E366(2004).
RN [6]
RP FUNCTION.
RX PubMed=17267509; DOI=10.1128/jvi.01538-06;
RA Low A., Datta S., Kuznetsov Y., Jahid S., Kothari N., McPherson A., Fan H.;
RT "Mutation in the glycosylated gag protein of murine leukemia virus results
RT in reduced in vivo infectivity and a novel defect in viral budding or
RT release.";
RL J. Virol. 81:3685-3692(2007).
RN [7]
RP FUNCTION.
RX PubMed=20702647; DOI=10.1128/jvi.01023-10;
RA Kolokithas A., Rosenke K., Malik F., Hendrick D., Swanson L.,
RA Santiago M.L., Portis J.L., Hasenkrug K.J., Evans L.H.;
RT "The glycosylated Gag protein of a murine leukemia virus inhibits the
RT antiretroviral function of APOBEC3.";
RL J. Virol. 84:10933-10936(2010).
RN [8]
RP FUNCTION.
RX PubMed=22828015; DOI=10.1186/1742-4690-9-58;
RA Nitta T., Lee S., Ha D., Arias M., Kozak C.A., Fan H.;
RT "Moloney murine leukemia virus glyco-gag facilitates xenotropic murine
RT leukemia virus-related virus replication through human APOBEC3-independent
RT mechanisms.";
RL Retrovirology 9:58-58(2012).
RN [9]
RP FUNCTION.
RX PubMed=23671100; DOI=10.1073/pnas.1217399110;
RA Stavrou S., Nitta T., Kotla S., Ha D., Nagashima K., Rein A.R., Fan H.,
RA Ross S.R.;
RT "Murine leukemia virus glycosylated Gag blocks apolipoprotein B editing
RT complex 3 and cytosolic sensor access to the reverse transcription
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:9078-9083(2013).
RN [10]
RP FUNCTION.
RX PubMed=25505062; DOI=10.1128/jvi.03330-14;
RA Rosales Gerpe M.C., Renner T.M., Belanger K., Lam C., Aydin H.,
RA Langlois M.A.;
RT "N-linked glycosylation protects gammaretroviruses against deamination by
RT APOBEC3 proteins.";
RL J. Virol. 89:2342-2357(2015).
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 (PubMed:17267509, PubMed:22828015). May prevent the antiviral activity
CC of murine APOBEC3 (PubMed:25505062, PubMed:23671100, PubMed:20702647).
CC {ECO:0000269|PubMed:17267509, ECO:0000269|PubMed:20702647,
CC ECO:0000269|PubMed:22828015, ECO:0000269|PubMed:23671100,
CC ECO:0000269|PubMed:25505062}.
CC -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255,
CC ECO:0000269|PubMed:17267509, ECO:0000269|PubMed:9188605}; Single-pass
CC membrane protein {ECO:0000269|PubMed:9188605}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Glyco-Gag protein;
CC IsoId=P0DOG8-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P03336-1; Sequence=External;
CC -!- PTM: Glycosylated by host (PubMed:6997511).
CC {ECO:0000269|PubMed:6997511}.
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 (PubMed:9188605). {ECO:0000269|PubMed:9188605}.
CC -!- CAUTION: The protein uses an unusual AUG start codon with leucine.
CC {ECO:0000269|PubMed:15510226}.
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; J01998; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0DOG8; -.
DR Proteomes; UP000008875; 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 1: Evidence at protein level;
KW Alternative initiation; Glycoprotein; Host cell membrane; Host membrane;
KW Membrane; Transmembrane; Transmembrane helix.
FT CHAIN 1..625
FT /note="Glyco-Gag protein"
FT /id="PRO_0000441131"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9188605"
FT TRANSMEM 67..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..625
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9188605"
FT REGION 195..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..217
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..610
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 479
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 625 AA; 70051 MW; 305A6E2751D8A4E0 CRC64;
LGDVSEASGA RWVAQSVSPS PDRFGLFGAP PLSEGYVVLL GDERSKPSPP PSEFLLSVFR
RNRAARLVCL SIVLSFVCSL LFWTASKNMG QTVTTPLSLT LEHWEDVQRI ASNQSVDVKK
RRWVTFCSAE WPTFGVGWPQ DGTFNLDIIL QVKSKVFSPG PHGHPDQVPY IVTWEAIAYE
PPPWVKPFVS PKLSPSPTAP ILPSGPSTQP PPRSALYPAL TPSIKPRPSK PQVLSDNGGP
LIDLLSEDPP PYGGQGLSSS DGDGDREEAT STSEIPAPSP IVSRLRGKRD PPAADSTTSR
AFPLRLGGNG QLQYWPFSSS DLYNWKNNNP SFSEDPGKLT ALIESVLTTH QPTWDDCQQL
LGTLLTGEEK QRVLLEARKA VRGNDGRPTQ LPNEVDAAFP LERPDWDYTT QRGRNHLVLY
RQLLLAGLQN AGRSPTNLAK VKGITQGPNE SPSAFLERLK EAYRRYTPYD PEDPGQETNV
SMSFIWQSAP DIGRKLERLE DLKSKTLGDL VREAERIFNK RETPEEREER VRRETEEKEE
RRRAEEEQKE KERDRRRHRE MSKLLATVVS GQRQDRQGGE RRRPQLDKDQ CAYCKEKGHW
AKDCPKKPRG PRGPRPQTSL LTLDD
