GAG_MMTVB
ID GAG_MMTVB Reviewed; 591 AA.
AC P10258;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Gag polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p10;
DE Contains:
DE RecName: Full=Phosphorylated protein pp21;
DE Contains:
DE RecName: Full=Protein p3;
DE Contains:
DE RecName: Full=Protein p8;
DE Contains:
DE RecName: Full=Protein n;
DE Contains:
DE RecName: Full=Capsid protein p27;
DE Contains:
DE RecName: Full=Nucleocapsid protein p14;
GN Name=gag;
OS Mouse mammary tumor virus (strain BR6) (MMTV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11758;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RIBOSOMAL FRAMESHIFT.
RX PubMed=3027377; DOI=10.1128/jvi.61.2.480-490.1987;
RA Moore R., Dixon M., Smith R., Peters G., Dickson C.;
RT "Complete nucleotide sequence of a milk-transmitted mouse mammary tumor
RT virus: two frameshift suppression events are required for translation of
RT gag and pol.";
RL J. Virol. 61:480-490(1987).
RN [2]
RP SUBCELLULAR LOCATION (MATRIX PROTEIN P10), SUBCELLULAR LOCATION (CAPSID
RP PROTEIN P27), AND SUBCELLULAR LOCATION (NUCLEOCAPSID PROTEIN P14).
RX PubMed=205999; DOI=10.1016/0042-6822(78)90420-8;
RA Cardiff R.D., Puentes M.J., Young L.J., Smith G.H., Teramoto Y.A.,
RA Altrock B.W., Pratt T.S.;
RT "Serological and biochemical characterization of the mouse mammary tumor
RT virus with localization of p10.";
RL Virology 85:157-167(1978).
RN [3]
RP PROTEOLYTIC CLEAVAGE (GAG POLYPROTEIN).
RX PubMed=1331110; DOI=10.1016/s0021-9258(18)35956-8;
RA Menendez-Arias L., Young M., Oroszlan S.;
RT "Purification and characterization of the mouse mammary tumor virus
RT protease expressed in Escherichia coli.";
RL J. Biol. Chem. 267:24134-24139(1992).
RN [4] {ECO:0007744|PDB:4ZV5}
RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 2-92, MYRISTOYLATION AT GLY-2,
RP AND SUBUNIT (MATRIX PROTEIN P10).
RX PubMed=26728401; DOI=10.1186/s12977-015-0235-8;
RA Dolezal M., Zabransky A., Dostal J., Vanek O., Brynda J., Lepsik M.,
RA Hadravova R., Pichova I.;
RT "Myristoylation drives dimerization of matrix protein from mouse mammary
RT tumor virus.";
RL Retrovirology 13:2-2(2016).
CC -!- FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.
CC -!- FUNCTION: [Nucleocapsid protein p14]: Binds strongly to viral nucleic
CC acids and promotes their aggregation. Also destabilizes the nucleic
CC acids duplexes via highly structured zinc-binding motifs.
CC {ECO:0000305}.
CC -!- FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.
CC -!- SUBUNIT: [Matrix protein p10]: Homodimer; when myristoylated.
CC {ECO:0000269|PubMed:26728401}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p10]: Virion
CC {ECO:0000269|PubMed:205999}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27]: Virion
CC {ECO:0000269|PubMed:205999}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion
CC {ECO:0000269|PubMed:205999}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag polyprotein;
CC IsoId=P10258-1; Sequence=Displayed;
CC Name=Gag-Pro polyprotein;
CC IsoId=P10271-1; Sequence=External;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P03365-1; 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 Gag-p27 contains one L domain: a PTAP/PSAP motif, which interacts with
CC the UEV domain of TSG101. {ECO:0000305}.
CC -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. {ECO:0000269|PubMed:1331110}.
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:0000269|PubMed:26728401}.
CC -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC translation. {ECO:0000269|PubMed:3027377}.
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DR EMBL; M15122; AAA46543.1; -; Genomic_RNA.
DR PIR; A26795; FOMVMM.
DR RefSeq; NP_056882.1; NC_001503.1.
DR PDB; 4ZV5; X-ray; 1.57 A; A/B=2-92.
DR PDB; 5HYB; X-ray; 1.94 A; A/B=2-92.
DR PDB; 5I27; X-ray; 2.05 A; A/B=6-92.
DR PDBsum; 4ZV5; -.
DR PDBsum; 5HYB; -.
DR PDBsum; 5I27; -.
DR SMR; P10258; -.
DR iPTMnet; P10258; -.
DR GeneID; 1491864; -.
DR KEGG; vg:1491864; -.
DR Proteomes; UP000228400; Genome.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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 Pfam; PF00098; zf-CCHC; 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; DNA-binding; Host-virus interaction;
KW Lipoprotein; Metal-binding; Myristate; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; 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:0000255"
FT CHAIN 2..591
FT /note="Gag polyprotein"
FT /id="PRO_0000442465"
FT CHAIN 2..99
FT /note="Matrix protein p10"
FT /id="PRO_0000040920"
FT CHAIN 100..195
FT /note="Phosphorylated protein pp21"
FT /id="PRO_0000040921"
FT CHAIN 196..228
FT /note="Protein p3"
FT /id="PRO_0000040922"
FT CHAIN 229..254
FT /note="Protein p8"
FT /id="PRO_0000040923"
FT CHAIN 255..269
FT /note="Protein n"
FT /id="PRO_0000040924"
FT CHAIN 270..496
FT /note="Capsid protein p27"
FT /id="PRO_0000040925"
FT CHAIN 497..591
FT /note="Nucleocapsid protein p14"
FT /id="PRO_0000040926"
FT ZN_FING 525..542
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 552..569
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 151..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 305..308
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000305"
FT SITE 99..100
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:1331110"
FT SITE 195..196
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:1331110"
FT SITE 228..229
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:1331110"
FT SITE 254..255
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:1331110"
FT SITE 269..270
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:1331110"
FT SITE 496..497
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:1331110"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000269|PubMed:26728401"
FT TURN 5..8
FT /evidence="ECO:0007829|PDB:5HYB"
FT HELIX 9..21
FT /evidence="ECO:0007829|PDB:5HYB"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:5HYB"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:5HYB"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:5HYB"
FT HELIX 54..71
FT /evidence="ECO:0007829|PDB:5HYB"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:5HYB"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:5HYB"
SQ SEQUENCE 591 AA; 66269 MW; 8A5C2212460864A5 CRC64;
MGVSGSKGQK LFVSVLQRLL SERGLHVKES SAIEFYQFLI KVSPWFPEEG GLNLQDWKRV
GREMKRYAAE HGTDSIPKQA YPIWLQLREI LTEQSDLVLL SAEAKSVTEE ELEEGLTGLL
STSSQEKTYG TRGTAYAEID TEVDKLSEHI YDEPYEEKEK ADKNEEKDHV RKIKKVVQRK
ENSEGKRKEK DSKAFLATDW NDDDLSPEDW DDLEEQAAHY HDDDELILPV KRKVVKKKPQ
ALRRKPLPPV GFAGAMAEAR EKGDLTFTFP VVFMGESDED DTPVWEPLPL KTLKELQSAV
RTMGPSAPYT LQVVDMVASQ WLTPSDWHQT ARATLSPGDY VLWRTEYEEK SKEMVQKAAG
KRKGKVSLDM LLGTGQFLSP SSQIKLSKDV LKDVTTNAVL AWRAIPPPGV KKTVLAGLKQ
GNEESYETFI SRLEEAVYRM MPRGEGSDIL IKQLAWENAN SLCQDLIRPI RKTGTIQDYI
RACLDASPAV VQGMAYAAAM RGQKYSTFVK QTYGGGKGGQ GAEGPVCFSC GKTGHIRKDC
KDEKGSKRAP PGLCPRCKKG YHWKSECKSK FDKDGNPLPP LETNAENSKN L
