ID   GAG_MLVAB               Reviewed;         235 AA.
AC   P03333;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   23-FEB-2022, entry version 111.
DE   RecName: Full=Gag polyprotein;
DE   Contains:
DE     RecName: Full=Matrix protein p15;
DE              Short=MA;
DE   Contains:
DE     RecName: Full=RNA-binding phosphoprotein p12;
DE   Contains:
DE     RecName: Full=Capsid protein p30;
DE              Short=CA;
GN   Name=gag;
OS   Abelson murine leukemia virus.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   unclassified Gammaretrovirus.
OX   NCBI_TaxID=11788;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6304726; DOI=10.1073/pnas.80.12.3623;
RA   Reddy E.P., Smith M.J., Srinivasan A.;
RT   "Nucleotide sequence of Abelson murine leukemia virus genome: structural
RT   similarity of its transforming gene product to other onc gene products with
RT   tyrosine-specific kinase activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:3623-3627(1983).
CC   -!- FUNCTION: Matrix protein p15 targets Gag and gag-pol polyproteins to
CC       the plasma membrane via a multipartite membrane binding signal, that
CC       includes its myristoylated N-terminus. Also mediates nuclear
CC       localization of the preintegration complex (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: Capsid protein p30 forms the spherical core of the virus that
CC       encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein p30]: Virion {ECO:0000305}.
CC   -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC       essential for viral particle budding. They recruit proteins of the host
CC       ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC       ESCRT-associated proteins. Gag-p12 contains one L domain: a PPXY motif
CC       which potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin
CC       ligase (Potential). {ECO:0000305}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC   -!- MISCELLANEOUS: This protein is synthesized as a Gag-Abl polyprotein.
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DR   EMBL; V01541; CAA24781.1; -; Genomic_DNA.
DR   BMRB; P03333; -.
DR   SMR; P03333; -.
DR   IntAct; P03333; 1.
DR   MINT; P03333; -.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.150.180; -; 1.
DR   InterPro; IPR000840; G_retro_matrix.
DR   InterPro; IPR036946; G_retro_matrix_sf.
DR   InterPro; IPR002079; Gag_p12.
DR   InterPro; IPR010999; Retrovr_matrix.
DR   Pfam; PF01140; Gag_MA; 1.
DR   Pfam; PF01141; Gag_p12; 1.
DR   SUPFAM; SSF47836; SSF47836; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Host-virus interaction; Lipoprotein; Myristate;
KW   Viral budding; Viral budding via the host ESCRT complexes;
KW   Viral release from host cell; Virion.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..131
FT                   /note="Matrix protein p15"
FT                   /id="PRO_0000040873"
FT   CHAIN           132..215
FT                   /note="RNA-binding phosphoprotein p12"
FT                   /id="PRO_0000040874"
FT   CHAIN           216..235
FT                   /note="Capsid protein p30"
FT                   /id="PRO_0000040875"
FT   REGION          108..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           162..165
FT                   /note="PPPY motif"
FT                   /evidence="ECO:0000255"
FT   MOTIF           162..165
FT                   /note="PPXY motif"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        108..127
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   235 AA;  25641 MW;  4D83F71D7E056C7D CRC64;
     MGQTVTTPLS LTLGHWKDVE RIAHNQSVDV KKRRWVTFCS AEWPTFNVGW PRDGTFNRDL
     ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF VHPKPPPPLP PSAPSLPLEP
     PLSTPPRSSL YPALTPSLGA KPKPQVLSDS GGPLIDLLTE DPPPYRDPRP PPSDRDGNGG
     EATPAGEAPD PSPMASRLRG RREPPVADST TSQAFPLRTG GNGQLQYWPF SSSDL