GAG_MPMV
ID GAG_MPMV Reviewed; 657 AA.
AC P07567; O56225;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Gag polyprotein;
DE AltName: Full=Core polyprotein;
DE AltName: Full=Pr78;
DE Contains:
DE RecName: Full=Matrix protein p10;
DE Contains:
DE RecName: Full=Phosphorylated protein pp24;
DE Contains:
DE RecName: Full=Phosphorylated protein pp18;
DE Contains:
DE RecName: Full=p12;
DE Contains:
DE RecName: Full=Capsid protein p27;
DE Contains:
DE RecName: Full=Nucleocapsid protein p14;
DE Contains:
DE RecName: Full=p4;
GN Name=gag;
OS Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11855;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RIBOSOMAL FRAMESHIFT.
RC STRAIN=Clone 6A;
RX PubMed=2421920; DOI=10.1016/0092-8674(86)90323-5;
RA Sonigo P., Barker C., Hunter E., Wain-Hobson S.;
RT "Nucleotide sequence of Mason-Pfizer monkey virus: an immunosuppressive D-
RT type retrovirus.";
RL Cell 45:375-385(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Chappey C.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 162-184; 217-250; 300-316; 526-540 AND 622-647, AND
RP PROTEOLYTIC CLEAVAGE (GAG POLYPROTEIN).
RX PubMed=3927012; DOI=10.1128/jvi.55.3.778-787.1985;
RA Henderson L.E., Sowder R., Smythers G., Benveniste R.E., Oroszlan S.;
RT "Purification and N-terminal amino acid sequence comparisons of structural
RT proteins from retrovirus-D/Washington and Mason-Pfizer monkey virus.";
RL J. Virol. 55:778-787(1985).
RN [4]
RP DOMAIN (GAG POLYPROTEIN), AND MUTAGENESIS OF 203-PRO--TYR-205 AND
RP 210-PRO--PRO-212.
RX PubMed=12915562; DOI=10.1128/jvi.77.17.9474-9485.2003;
RA Gottwein E., Bodem J., Mueller B., Schmechel A., Zentgraf H.,
RA Kraeusslich H.G.;
RT "The Mason-Pfizer monkey virus PPPY and PSAP motifs both contribute to
RT virus release.";
RL J. Virol. 77:9474-9485(2003).
RN [5]
RP STRUCTURE BY NMR OF 1-94.
RX PubMed=9312040; DOI=10.1093/emboj/16.19.5819;
RA Conte M.R., Klikova M., Hunter E., Ruml T., Matthews S.;
RT "The three-dimensional solution structure of the matrix protein from the
RT type D retrovirus, the Mason-Pfizer monkey virus, and implications for the
RT morphology of retroviral assembly.";
RL EMBO J. 16:5819-5826(1997).
RN [6] {ECO:0007744|PDB:2F76, ECO:0007744|PDB:2F77}
RP STRUCTURE BY NMR OF 1-100, MUTAGENESIS OF ARG-57, AND INTERACTION WITH HOST
RP DYNLT1 (GAG POLYPROTEIN).
RX PubMed=18647839; DOI=10.1073/pnas.0801765105;
RA Vlach J., Lipov J., Rumlova M., Veverka V., Lang J., Srb P., Knejzlik Z.,
RA Pichova I., Hunter E., Hrabal R., Ruml T.;
RT "D-retrovirus morphogenetic switch driven by the targeting signal
RT accessibility to Tctex-1 of dynein.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10565-10570(2008).
RN [7]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=24298557; DOI=10.1155/2013/984028;
RA Huang X., Cheng Q., Du Z.;
RT "A genome-wide analysis of RNA pseudoknots that stimulate efficient -1
RT ribosomal frameshifting or readthrough in animal viruses.";
RL Biomed. Res. Int. 2013:984028-984028(2013).
CC -!- FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.
CC -!- FUNCTION: [Nucleocapsid protein p14]: Nucleocapsid protein.
CC {ECO:0000305}.
CC -!- FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.
CC -!- SUBUNIT: [Gag polyprotein]: Interacts with host DYNLT1; this
CC interaction probably targets the viral polyproteins to the cytoplasmic
CC assembly site. {ECO:0000269|PubMed:18647839}.
CC -!- INTERACTION:
CC P07567; P63172: DYNLT1; Xeno; NbExp=2; IntAct=EBI-15717123, EBI-1176455;
CC -!- SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag polyprotein;
CC IsoId=P07567-1; Sequence=Displayed;
CC Name=Gag-Pro polyprotein;
CC IsoId=P07570-1; Sequence=External;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P07572-1; Sequence=External;
CC -!- DOMAIN: [Gag polyprotein]: Late-budding domains (L domains) are short
CC sequence motifs essential for viral particle release. They can occur
CC individually or in close proximity within structural proteins. They
CC interacts with sorting cellular proteins of the multivesicular body
CC (MVB) pathway. Most of these proteins are class E vacuolar protein
CC sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes.
CC Phosphorylated protein pp24 and phosphorylated protein pp18 contains
CC two L domains: a PTAP/PSAP motif which interacts with the UEV domain of
CC TSG101, and a PPXY motif which binds to the WW domains of the ubiquitin
CC ligase NEDD4. Both motifs contribute to viral release. The PSAP motif
CC acts as an additional L domain and promotes the efficient release of
CC the virions but requires an intact PPPY motif to perform its function.
CC {ECO:0000269|PubMed:12915562}.
CC -!- PTM: [Gag polyprotein]: Myristoylated. Myristoylation of the matrix
CC (MA) domain mediates the transport and binding of Gag polyproteins to
CC the host plasma membrane and is required for the assembly of viral
CC particles. {ECO:0000250|UniProtKB:P10258}.
CC -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. {ECO:0000269|PubMed:3927012}.
CC -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC translation. {ECO:0000305|PubMed:2421920, ECO:0000305|PubMed:24298557}.
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DR EMBL; M12349; AAA47710.1; -; Genomic_RNA.
DR EMBL; AF033815; AAC82573.1; -; Genomic_RNA.
DR PIR; A25839; FOLJMP.
DR RefSeq; NP_056893.1; NC_001550.1. [P07567-1]
DR PDB; 1BAX; NMR; -; A=1-94.
DR PDB; 1CL4; NMR; -; A=546-605.
DR PDB; 2F76; NMR; -; X=2-100.
DR PDB; 2F77; NMR; -; X=1-100.
DR PDB; 2KGF; NMR; -; A=300-439.
DR PDB; 2LPY; NMR; -; A=2-118.
DR PDB; 2MV4; NMR; -; A=2-118.
DR PDB; 4ARD; EM; 7.00 A; A/B=318-433.
DR PDB; 5LDL; NMR; -; A=2-118.
DR PDB; 5LMY; NMR; -; A=2-118.
DR PDBsum; 1BAX; -.
DR PDBsum; 1CL4; -.
DR PDBsum; 2F76; -.
DR PDBsum; 2F77; -.
DR PDBsum; 2KGF; -.
DR PDBsum; 2LPY; -.
DR PDBsum; 2MV4; -.
DR PDBsum; 4ARD; -.
DR PDBsum; 5LDL; -.
DR PDBsum; 5LMY; -.
DR BMRB; P07567; -.
DR SMR; P07567; -.
DR DIP; DIP-45130N; -.
DR ELM; P07567; -.
DR IntAct; P07567; 1.
DR GeneID; 2746974; -.
DR KEGG; vg:2746974; -.
DR EvolutionaryTrace; P07567; -.
DR Proteomes; UP000008870; Genome.
DR Proteomes; UP000105838; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.490; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR InterPro; IPR003322; B_retro_matrix.
DR InterPro; IPR038124; B_retro_matrix_sf.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_N.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF02337; Gag_p10; 1.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF57756; SSF57756; 2.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Coiled coil; Direct protein sequencing;
KW Host-virus interaction; Lipoprotein; Metal-binding; Myristate;
KW Phosphoprotein; Repeat; Ribosomal frameshifting; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral matrix protein;
KW Viral nucleoprotein; Viral release from host cell; Virion; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000305"
FT CHAIN 2..657
FT /note="Gag polyprotein"
FT /id="PRO_0000443122"
FT CHAIN 2..100
FT /note="Matrix protein p10"
FT /id="PRO_0000040940"
FT CHAIN 101..216
FT /note="Phosphorylated protein pp24"
FT /id="PRO_0000040941"
FT PROPEP 101..161
FT /evidence="ECO:0000305"
FT /id="PRO_0000443123"
FT CHAIN 162..216
FT /note="Phosphorylated protein pp18"
FT /id="PRO_0000443124"
FT CHAIN 217..299
FT /note="p12"
FT /id="PRO_0000040942"
FT CHAIN 300..525
FT /note="Capsid protein p27"
FT /id="PRO_0000040943"
FT CHAIN 526..621
FT /note="Nucleocapsid protein p14"
FT /id="PRO_0000040944"
FT CHAIN 622..657
FT /note="p4"
FT /id="PRO_0000040945"
FT ZN_FING 547..564
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 576..593
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 113..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 216..257
FT /evidence="ECO:0000255"
FT MOTIF 202..205
FT /note="PPXY motif"
FT /evidence="ECO:0000269|PubMed:12915562"
FT MOTIF 210..213
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000269|PubMed:12915562"
FT COMPBIAS 113..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 100..101
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:3927012"
FT SITE 162..163
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:3927012"
FT SITE 216..217
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:3927012"
FT SITE 299..300
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:3927012"
FT SITE 525..526
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:3927012"
FT SITE 621..622
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:3927012"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:P10258"
FT MUTAGEN 57
FT /note="R->F: Redirects assembly from host cytoplasm to
FT plasma membrane. Loss of interaction with host DYNLT1."
FT /evidence="ECO:0000269|PubMed:18647839"
FT MUTAGEN 203..205
FT /note="PPY->GAA: 80% loss of virus release."
FT /evidence="ECO:0000269|PubMed:12915562"
FT MUTAGEN 210..211
FT /note="PS->AG: 30% loss of virus release."
FT /evidence="ECO:0000269|PubMed:12915562"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:5LMY"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:2F76"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:2F76"
FT HELIX 28..41
FT /evidence="ECO:0007829|PDB:2F76"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:2LPY"
FT HELIX 52..70
FT /evidence="ECO:0007829|PDB:2F76"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:2F77"
FT HELIX 78..93
FT /evidence="ECO:0007829|PDB:2F76"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:2LPY"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:2LPY"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:2LPY"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:2KGF"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:2KGF"
FT HELIX 320..332
FT /evidence="ECO:0007829|PDB:2KGF"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:2KGF"
FT HELIX 354..364
FT /evidence="ECO:0007829|PDB:2KGF"
FT HELIX 368..391
FT /evidence="ECO:0007829|PDB:2KGF"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:2KGF"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:2KGF"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:2KGF"
FT HELIX 408..414
FT /evidence="ECO:0007829|PDB:2KGF"
FT HELIX 417..430
FT /evidence="ECO:0007829|PDB:2KGF"
FT STRAND 596..599
FT /evidence="ECO:0007829|PDB:1CL4"
SQ SEQUENCE 657 AA; 73110 MW; 301888B033BC3061 CRC64;
MGQELSQHER YVEQLKQALK TRGVKVKYAD LLKFFDFVKD TCPWFPQEGT IDIKRWRRVG
DCFQDYYNTF GPEKVPVTAF SYWNLIKELI DKKEVNPQVM AAVAQTEEIL KSNSQTDLTK
TSQNPDLDLI SLDSDDEGAK SSSLQDKGLS STKKPKRFPV LLTAQTSKDP EDPNPSEVDW
DGLEDEAAKY HNPDWPPFLT RPPPYNKATP SAPTVMAVVN PKEELKEKIA QLEEQIKLEE
LHQALISKLQ KLKTGNETVT HPDTAGGLSR TPHWPGQHIP KGKCCASREK EEQIPKDIFP
VTETVDGQGQ AWRHHNGFDF AVIKELKTAA SQYGATAPYT LAIVESVADN WLTPTDWNTL
VRAVLSGGDH LLWKSEFFEN CRDTAKRNQQ AGNGWDFDML TGSGNYSSTD AQMQYDPGLF
AQIQAAATKA WRKLPVKGDP GASLTGVKQG PDEPFADFVH RLITTAGRIF GSAEAGVDYV
KQLAYENANP ACQAAIRPYR KKTDLTGYIR LCSDIGPSYQ QGLAMAAAFS GQTVKDFLNN
KNKEKGGCCF KCGKKGHFAK NCHEHAHNNA EPKVPGLCPR CKRGKHWANE CKSKTDNQGN
PIPPHQGNGW RGQPQAPKQA YGAVSFVPAN KNNPFQSLPE PPQEVQDWTS VPPPTQY
