ID   GAG_MSVMO               Reviewed;         538 AA.
AC   P03334;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Gag polyprotein;
DE   AltName: Full=Core polyprotein;
DE   Contains:
DE     RecName: Full=Matrix protein p15;
DE              Short=MA;
DE   Contains:
DE     RecName: Full=RNA-binding phosphoprotein p12;
DE     AltName: Full=pp12;
DE   Contains:
DE     RecName: Full=Capsid protein p30;
DE              Short=CA;
DE   Contains:
DE     RecName: Full=Nucleocapsid protein p10-gag;
DE              Short=NC-gag;
GN   Name=gag;
OS   Moloney murine sarcoma virus (MoMSV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=11809;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (PROVIRUS).
RX   PubMed=6170110; DOI=10.1126/science.6170110;
RA   Reddy E.P., Smith M.J., Aaronson S.A.;
RT   "Complete nucleotide sequence and organization of the Moloney murine
RT   sarcoma virus genome.";
RL   Science 214:445-450(1981).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONE 124 CIRCULAR).
RX   PubMed=6173134; DOI=10.1016/0092-8674(81)90364-0;
RA   van Beveren C., van Straaten F., Galleshaw J.A., Verma I.M.;
RT   "Nucleotide sequence of the genome of a murine sarcoma virus.";
RL   Cell 27:97-108(1981).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-17, AND MYRISTOYLATION AT GLY-2.
RX   PubMed=6340098; DOI=10.1073/pnas.80.2.339;
RA   Henderson L.E., Krutzsch H.C., Oroszlan S.;
RT   "Myristyl amino-terminal acylation of murine retrovirus proteins: an
RT   unusual post-translational proteins modification.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:339-343(1983).
CC   -!- FUNCTION: [Gag polyprotein]: Plays a role in budding and is processed
CC       by the viral protease during virion maturation outside the cell. During
CC       budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-
CC       like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to
CC       Gag binding host factors. Interaction with HECT ubiquitin ligases
CC       probably links the viral protein to the host ESCRT pathway and
CC       facilitates release. {ECO:0000250|UniProtKB:P03332}.
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 pre-integration complex.
CC       {ECO:0000250|UniProtKB:P03332}.
CC   -!- FUNCTION: [RNA-binding phosphoprotein p12]: Constituent of the pre-
CC       integration complex (PIC) which tethers the latter to mitotic
CC       chromosomes. {ECO:0000250|UniProtKB:P03332}.
CC   -!- FUNCTION: [Capsid protein p30]: Forms the spherical core of the virion
CC       that encapsulates the genomic RNA-nucleocapsid complex.
CC       {ECO:0000250|UniProtKB:P03332}.
CC   -!- FUNCTION: [Nucleocapsid protein p10-gag]: Involved in the packaging and
CC       encapsidation of two copies of the genome. Binds with high affinity to
CC       conserved UCUG elements within the packaging signal, located near the
CC       5'-end of the genome. This binding is dependent on genome dimerization.
CC       {ECO:0000250|UniProtKB:P03332}.
CC   -!- SUBUNIT: [Gag polyprotein]: Interacts (via PPXY motif) with host NEDD4
CC       (By similarity). Interacts (via PSAP motif) with host TSG101 (By
CC       similarity). Interacts (via LYPX(n)L motif) with host PDCD6IP (By
CC       similarity). {ECO:0000250|UniProtKB:P03332}.
CC   -!- SUBUNIT: [Capsid protein p30]: Homohexamer. Further associates as
CC       homomultimer (By similarity). The virus core is composed of a lattice
CC       formed from hexagonal rings, each containing six capsid monomers (By
CC       similarity). Interacts with mouse UBE2I and mouse PIAS4 (By
CC       similarity). {ECO:0000250|UniProtKB:P03332,
CC       ECO:0000250|UniProtKB:P03336}.
CC   -!- SUBCELLULAR LOCATION: [Gag polyprotein]: Virion {ECO:0000250}. Host
CC       cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein p30]: Virion {ECO:0000305}.
CC   -!- DOMAIN: [Gag polyprotein]: Late-budding domains (L domains) are short
CC       sequence motifs essential for viral particle budding. They recruit
CC       proteins of the host ESCRT machinery (Endosomal Sorting Complex
CC       Required for Transport) or ESCRT-associated proteins. RNA-binding
CC       phosphoprotein p12 contains one L domain: a PPXY motif which interacts
CC       with the WW domain 3 of NEDD4 E3 ubiquitin ligase. PPXY motif is
CC       essential for virus egress. Matrix protein p15 contains one L domain: a
CC       PTAP/PSAP motif, which interacts with the UEV domain of TSG101. The
CC       junction between the matrix protein p15 and RNA-binding phosphoprotein
CC       p12 also contains one L domain: a LYPX(n)L motif which interacts with
CC       PDCD6IP. Both PSAP and LYPX(n)L domains might play little to no role in
CC       budding and possibly drive residual virus release.
CC       {ECO:0000250|UniProtKB:P03332}.
CC   -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral
CC       protease yield mature proteins. The protease is released by
CC       autocatalytic cleavage. The polyprotein is cleaved during and after
CC       budding, this process is termed maturation.
CC       {ECO:0000250|UniProtKB:P03332}.
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DR   EMBL; J02266; AAA46499.1; -; Genomic_RNA.
DR   EMBL; V01185; CAA24507.1; -; Genomic_DNA.
DR   PIR; A94261; FOMVM.
DR   RefSeq; NP_057858.1; NC_001502.1.
DR   BMRB; P03334; -.
DR   SMR; P03334; -.
DR   ELM; P03334; -.
DR   iPTMnet; P03334; -.
DR   GeneID; 1491884; -.
DR   KEGG; vg:1491884; -.
DR   OrthoDB; 3221at10239; -.
DR   Proteomes; UP000108184; Genome.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.10.150.180; Gamma-retroviral matrix domain; 1.
DR   Gene3D; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 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   PANTHER; PTHR33166:SF1; CORE SHELL PROTEIN GAG P30 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR33166; GAG_P30 DOMAIN-CONTAINING PROTEIN; 1.
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; Retroviral matrix proteins; 1.
DR   SUPFAM; SSF47943; Retrovirus capsid protein, N-terminal core domain; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   1: Evidence at protein level;
KW   Capsid protein; Direct protein sequencing; Host cell membrane;
KW   Host membrane; Host-virus interaction; Lipoprotein; Membrane;
KW   Metal-binding; Myristate; 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:0000250"
FT   CHAIN           2..538
FT                   /note="Gag polyprotein"
FT                   /id="PRO_0000390818"
FT   CHAIN           2..131
FT                   /note="Matrix protein p15"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040949"
FT   CHAIN           132..215
FT                   /note="RNA-binding phosphoprotein p12"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040950"
FT   CHAIN           216..478
FT                   /note="Capsid protein p30"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040951"
FT   CHAIN           479..538
FT                   /note="Nucleocapsid protein p10-gag"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040952"
FT   ZN_FING         502..519
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          111..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           111..114
FT                   /note="PTAP/PSAP motif"
FT   MOTIF           130..134
FT                   /note="LYPX(n)L motif"
FT   MOTIF           162..165
FT                   /note="PPXY motif"
FT   COMPBIAS        111..127
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..476
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            131..132
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   SITE            215..216
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   SITE            478..479
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000269|PubMed:6340098"
FT   VARIANT         519
FT                   /note="R -> K (in clone 124)"
SQ   SEQUENCE   538 AA;  61209 MW;  D78326F3B5701E56 CRC64;
     MGQTVTTPLS LTLDHWKDVE RLAHNQSVDV KKRRWVTFCS AEWPTFNVGW PRDGTFNRDL
     ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF VHPKPPPPLL PSAPSLPLEP
     PLSTPPQSSL YPALTPSLGA KPKPQVLSDS GGPLIDLLTE DPPPYRDPRP PPSDRDGDSG
     EATPAGEAPD PSPMASRLRG RREPPVADST TSQAFPLRTG GNGQLQYWPF SSSDLYNWKN
     NNPSFSEDPG KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR
     PTQLPNEVDA AFPLERPDWE YTTQAGRNHL VHYRQLLIAG LQNAGRSPTN LAKVKGITQG
     PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ SAPDIGRKLE RLEDLRNKTL
     GDLVREAERI FNKRETPEER EERIRREREE KEERRRTEDE QKEKERDRRR HREMSRLLAT
     VVSGQRQDRQ EGERRRSQLD CDQCTYCEEQ GHWAKDCPRR PRGPRGPRPQ TSLLTLDD
//