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Gag polyprotein (Core polyprotein) (Pr78) [Cleaved into: Matrix protein p10; Phosphorylated protein pp24; Phosphorylated protein pp18; p12; Capsid protein p27; Nucleocapsid protein p14; p4]

 GAG_MPMV                Reviewed;         657 AA.
P07567; O56225;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 136.
RecName: Full=Gag polyprotein;
AltName: Full=Core polyprotein;
AltName: Full=Pr78;
Contains:
RecName: Full=Matrix protein p10;
Contains:
RecName: Full=Phosphorylated protein pp24;
Contains:
RecName: Full=Phosphorylated protein pp18;
Contains:
RecName: Full=p12;
Contains:
RecName: Full=Capsid protein p27;
Contains:
RecName: Full=Nucleocapsid protein p14;
Contains:
RecName: Full=p4;
Name=gag;
Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus).
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae;
Betaretrovirus.
NCBI_TaxID=11855;
NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RIBOSOMAL FRAMESHIFT.
STRAIN=Clone 6A;
PubMed=2421920; DOI=10.1016/0092-8674(86)90323-5;
Sonigo P., Barker C., Hunter E., Wain-Hobson S.;
"Nucleotide sequence of Mason-Pfizer monkey virus: an
immunosuppressive D-type retrovirus.";
Cell 45:375-385(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Chappey C.;
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 162-184; 217-250; 300-316; 526-540 AND 622-647,
AND PROTEOLYTIC CLEAVAGE (GAG POLYPROTEIN).
PubMed=3927012;
Henderson L.E., Sowder R., Smythers G., Benveniste R.E., Oroszlan S.;
"Purification and N-terminal amino acid sequence comparisons of
structural proteins from retrovirus-D/Washington and Mason-Pfizer
monkey virus.";
J. Virol. 55:778-787(1985).
[4]
DOMAIN (GAG POLYPROTEIN), AND MUTAGENESIS OF 203-PRO--TYR-205 AND
210-PRO--PRO-212.
PubMed=12915562;
Gottwein E., Bodem J., Mueller B., Schmechel A., Zentgraf H.,
Kraeusslich H.G.;
"The Mason-Pfizer monkey virus PPPY and PSAP motifs both contribute to
virus release.";
J. Virol. 77:9474-9485(2003).
[5]
STRUCTURE BY NMR OF 1-94.
PubMed=9312040; DOI=10.1093/emboj/16.19.5819;
Conte M.R., Klikova M., Hunter E., Ruml T., Matthews S.;
"The three-dimensional solution structure of the matrix protein from
the type D retrovirus, the Mason-Pfizer monkey virus, and implications
for the morphology of retroviral assembly.";
EMBO J. 16:5819-5826(1997).
[6] {ECO:0000244|PDB:2F76, ECO:0000244|PDB:2F77}
STRUCTURE BY NMR OF 1-100, MUTAGENESIS OF ARG-57, AND INTERACTION WITH
HOST DYNLT1 (GAG POLYPROTEIN).
PubMed=18647839; DOI=10.1073/pnas.0801765105;
Vlach J., Lipov J., Rumlova M., Veverka V., Lang J., Srb P.,
Knejzlik Z., Pichova I., Hunter E., Hrabal R., Ruml T.;
"D-retrovirus morphogenetic switch driven by the targeting signal
accessibility to Tctex-1 of dynein.";
Proc. Natl. Acad. Sci. U.S.A. 105:10565-10570(2008).
[7]
RIBOSOMAL FRAMESHIFT.
PubMed=24298557; DOI=10.1155/2013/984028;
Huang X., Cheng Q., Du Z.;
"A genome-wide analysis of RNA pseudoknots that stimulate efficient -1
ribosomal frameshifting or readthrough in animal viruses.";
Biomed. Res. Int. 2013:984028-984028(2013).
-!- FUNCTION: Matrix protein p10: Matrix protein. {ECO:0000305}.
-!- FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein.
{ECO:0000305}.
-!- FUNCTION: Capsid protein p27: capsid protein. {ECO:0000305}.
-!- SUBUNIT: Gag polyprotein: Interacts with host DYNLT1; this
interaction probably targets the viral polyproteins to the
cytoplasmic assembly site. {ECO:0000269|PubMed:18647839}.
-!- INTERACTION:
P63172:DYNLT1 (xeno); NbExp=2; IntAct=EBI-15717123, EBI-1176455;
-!- SUBCELLULAR LOCATION: Matrix protein p10: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein p27: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p14: Virion
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=3;
Name=Gag polyprotein;
IsoId=P07567-1; Sequence=Displayed;
Note=Produced by conventional translation.
{ECO:0000305|PubMed:2421920, ECO:0000305|PubMed:24298557};
Name=Gag-Pro polyprotein;
IsoId=P07570-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting between gag-pro.
{ECO:0000305|PubMed:2421920, ECO:0000305|PubMed:24298557};
Name=Gag-Pro-Pol polyprotein;
IsoId=P07572-1; Sequence=External;
Note=Produced by -1 ribosomal frameshiftings between gag-pro and
pro-pol. {ECO:0000305|PubMed:2421920,
ECO:0000305|PubMed:24298557};
-!- DOMAIN: Gag polyprotein: Late-budding domains (L domains) are
short sequence motifs essential for viral particle release. They
can occur individually or in close proximity within structural
proteins. They interacts with sorting cellular proteins of the
multivesicular body (MVB) pathway. Most of these proteins are
class E vacuolar protein sorting factors belonging to ESCRT-I,
ESCRT-II or ESCRT-III complexes. Phosphorylated protein pp24 and
phosphorylated protein pp18 contains two L domains: a PTAP/PSAP
motif which interacts with the UEV domain of TSG101, and a PPXY
motif which binds to the WW domains of the ubiquitin ligase NEDD4.
Both motifs contribute to viral release. The PSAP motif acts as an
additional L domain and promotes the efficient release of the
virions but requires an intact PPPY motif to perform its function.
{ECO:0000269|PubMed:12915562}.
-!- PTM: Gag polyprotein: Myristoylated. Myristoylation of the matrix
(MA) domain mediates the transport and binding of Gag polyproteins
to the host plasma membrane and is required for the assembly of
viral particles. {ECO:0000250|UniProtKB:P10258}.
-!- PTM: Gag polyprotein: Specific enzymatic cleavages in vivo yield
mature proteins. {ECO:0000269|PubMed:3927012}.
-----------------------------------------------------------------------
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EMBL; M12349; AAA47710.1; -; Genomic_RNA.
EMBL; AF033815; AAC82573.1; -; Genomic_RNA.
PIR; A25839; FOLJMP.
RefSeq; NP_056893.1; NC_001550.1. [P07567-1]
PDB; 1BAX; NMR; -; A=1-94.
PDB; 1CL4; NMR; -; A=546-605.
PDB; 2F76; NMR; -; X=2-100.
PDB; 2F77; NMR; -; X=1-100.
PDB; 2KGF; NMR; -; A=300-439.
PDB; 2LPY; NMR; -; A=2-118.
PDB; 2MV4; NMR; -; A=2-118.
PDB; 4ARD; EM; 7.00 A; A/B=318-433.
PDB; 5LDL; NMR; -; A=2-118.
PDB; 5LMY; NMR; -; A=2-118.
PDBsum; 1BAX; -.
PDBsum; 1CL4; -.
PDBsum; 2F76; -.
PDBsum; 2F77; -.
PDBsum; 2KGF; -.
PDBsum; 2LPY; -.
PDBsum; 2MV4; -.
PDBsum; 4ARD; -.
PDBsum; 5LDL; -.
PDBsum; 5LMY; -.
ProteinModelPortal; P07567; -.
SMR; P07567; -.
DIP; DIP-45130N; -.
ELM; P07567; -.
IntAct; P07567; 1.
GeneID; 2746974; -.
KEGG; vg:2746974; -.
OrthoDB; VOG090001BU; -.
EvolutionaryTrace; P07567; -.
PMAP-CutDB; P07567; -.
Proteomes; UP000008870; Genome.
Proteomes; UP000105838; Genome.
GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.150.490; -; 1.
Gene3D; 1.10.375.10; -; 1.
InterPro; IPR003322; B_retro_matrix.
InterPro; IPR038124; B_retro_matrix_sf.
InterPro; IPR000721; Gag_p24.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF02337; Gag_p10; 1.
Pfam; PF00607; Gag_p24; 1.
ProDom; PD004265; B_retro_matrix_N; 1.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF57756; SSF57756; 2.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
3D-structure; Capsid protein; Coiled coil; Complete proteome;
Direct protein sequencing; Host-virus interaction; Lipoprotein;
Metal-binding; Myristate; Phosphoprotein; Repeat;
Ribosomal frameshifting; Viral budding;
Viral budding via the host ESCRT complexes; Viral matrix protein;
Viral nucleoprotein; Viral release from host cell; Virion; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000305}.
CHAIN 2 657 Gag polyprotein.
/FTId=PRO_0000443122.
CHAIN 2 100 Matrix protein p10.
/FTId=PRO_0000040940.
CHAIN 101 216 Phosphorylated protein pp24.
/FTId=PRO_0000040941.
PROPEP 101 161 {ECO:0000305}.
/FTId=PRO_0000443123.
CHAIN 162 216 Phosphorylated protein pp18.
/FTId=PRO_0000443124.
CHAIN 217 299 p12.
/FTId=PRO_0000040942.
CHAIN 300 525 Capsid protein p27.
/FTId=PRO_0000040943.
CHAIN 526 621 Nucleocapsid protein p14.
/FTId=PRO_0000040944.
CHAIN 622 657 p4.
/FTId=PRO_0000040945.
ZN_FING 547 564 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 576 593 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
COILED 216 257 {ECO:0000255}.
MOTIF 202 205 PPXY motif.
{ECO:0000269|PubMed:12915562}.
MOTIF 210 213 PTAP/PSAP motif.
{ECO:0000269|PubMed:12915562}.
SITE 100 101 Cleavage; by viral protease.
{ECO:0000269|PubMed:3927012}.
SITE 162 163 Cleavage; by viral protease.
{ECO:0000269|PubMed:3927012}.
SITE 216 217 Cleavage; by viral protease.
{ECO:0000269|PubMed:3927012}.
SITE 299 300 Cleavage; by viral protease.
{ECO:0000269|PubMed:3927012}.
SITE 525 526 Cleavage; by viral protease.
{ECO:0000269|PubMed:3927012}.
SITE 621 622 Cleavage; by viral protease.
{ECO:0000269|PubMed:3927012}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250|UniProtKB:P10258}.
MUTAGEN 57 57 R->F: Redirects assembly from host
cytoplasm to plasma membrane. Loss of
interaction with host DYNLT1.
{ECO:0000269|PubMed:18647839}.
MUTAGEN 203 205 PPY->GAA: 80% loss of virus release.
{ECO:0000269|PubMed:12915562}.
MUTAGEN 210 211 PS->AG: 30% loss of virus release.
{ECO:0000269|PubMed:12915562}.
HELIX 3 5 {ECO:0000244|PDB:5LMY}.
HELIX 7 20 {ECO:0000244|PDB:2F76}.
TURN 21 23 {ECO:0000244|PDB:2F76}.
HELIX 28 41 {ECO:0000244|PDB:2F76}.
TURN 46 48 {ECO:0000244|PDB:2LPY}.
HELIX 52 70 {ECO:0000244|PDB:2F76}.
TURN 72 74 {ECO:0000244|PDB:2F77}.
HELIX 78 93 {ECO:0000244|PDB:2F76}.
HELIX 98 101 {ECO:0000244|PDB:2LPY}.
HELIX 103 106 {ECO:0000244|PDB:2LPY}.
STRAND 112 115 {ECO:0000244|PDB:2LPY}.
STRAND 301 305 {ECO:0000244|PDB:2KGF}.
STRAND 311 315 {ECO:0000244|PDB:2KGF}.
HELIX 320 332 {ECO:0000244|PDB:2KGF}.
HELIX 338 348 {ECO:0000244|PDB:2KGF}.
HELIX 354 364 {ECO:0000244|PDB:2KGF}.
HELIX 368 391 {ECO:0000244|PDB:2KGF}.
STRAND 396 398 {ECO:0000244|PDB:2KGF}.
TURN 399 401 {ECO:0000244|PDB:2KGF}.
STRAND 404 406 {ECO:0000244|PDB:2KGF}.
HELIX 408 414 {ECO:0000244|PDB:2KGF}.
HELIX 417 430 {ECO:0000244|PDB:2KGF}.
STRAND 596 599 {ECO:0000244|PDB:1CL4}.
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


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