GAG_MMTVC
ID GAG_MMTVC Reviewed; 591 AA.
AC P11284; Q9IZT1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 133.
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 C3H) (MMTV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11759;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10982330; DOI=10.1128/jvi.74.19.8876-8883.2000;
RA Hook L.M., Agafonova Y., Ross S.R., Turner S.J., Golovkina T.V.;
RT "Genetics of mouse mammary tumor virus-induced mammary tumors: linkage of
RT tumor induction to the gag gene.";
RL J. Virol. 74:8876-8883(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 359-591 AND 857-970, AND RIBOSOMAL
RP FRAMESHIFT.
RX PubMed=3035577; DOI=10.1073/pnas.84.12.4298;
RA Jacks T., Townsley K., Varmus H.E., Majors J.;
RT "Two efficient ribosomal frameshifting events are required for synthesis of
RT mouse mammary tumor virus gag-related polyproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:4298-4302(1987).
RN [3]
RP PROTEIN SEQUENCE OF 2-58; 65-116; 194-218; 227-241; 251-252; 270-276 AND
RP 362-591, PROTEOLYTIC CLEAVAGE (GAG POLYPROTEIN), AND MYRISTOYLATION AT
RP GLY-2.
RX PubMed=2542570; DOI=10.1128/jvi.63.6.2543-2549.1989;
RA Hizi A., Henderson L.E., Copeland T.D., Sowder R.C., Krutzsch H.C.,
RA Oroszlan S.;
RT "Analysis of gag proteins from mouse mammary tumor virus.";
RL J. Virol. 63:2543-2549(1989).
RN [4]
RP STRUCTURE BY NMR OF 523-543 AND 550-580.
RX PubMed=10677209; DOI=10.1021/bi9922493;
RA Klein D.J., Johnson P.E., Zollars E.S., De Guzman R.N., Summers M.F.;
RT "The NMR structure of the nucleocapsid protein from the mouse mammary tumor
RT virus reveals unusual folding of the C-terminal zinc knuckle.";
RL Biochemistry 39:1604-1612(2000).
CC -!- FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.
CC -!- FUNCTION: [Nucleocapsid protein p14]: Binds strongly to viral nucleic
CC acids and promote 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:0000250|UniProtKB:P10258}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p10]: Virion
CC {ECO:0000250|UniProtKB:P10258}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27]: Virion
CC {ECO:0000250|UniProtKB:P10258}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion
CC {ECO:0000250|UniProtKB:P10258}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag polyprotein;
CC IsoId=P11284-1; Sequence=Displayed;
CC Name=Gag-Pro polyprotein;
CC IsoId=Q9IZT2-1; Sequence=External;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P11283-1; 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]: 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:2542570}.
CC -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. {ECO:0000269|PubMed:2542570}.
CC -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC translation. {ECO:0000269|PubMed:3035577}.
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DR EMBL; AF228552; AAF31472.1; -; Genomic_DNA.
DR EMBL; M16766; AAA66623.1; -; Genomic_RNA.
DR PIR; A29029; A29029.
DR PDB; 1DSQ; NMR; -; A=523-543.
DR PDB; 1DSV; NMR; -; A=550-580.
DR PDBsum; 1DSQ; -.
DR PDBsum; 1DSV; -.
DR BMRB; P11284; -.
DR SMR; P11284; -.
DR ELM; P11284; -.
DR iPTMnet; P11284; -.
DR EvolutionaryTrace; P11284; -.
DR Proteomes; UP000006540; 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; Direct protein sequencing; DNA-binding;
KW Host-virus interaction; Lipoprotein; Metal-binding; Myristate;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW 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:0000269|PubMed:2542570"
FT CHAIN 2..591
FT /note="Gag polyprotein"
FT /id="PRO_0000442466"
FT CHAIN 2..99
FT /note="Matrix protein p10"
FT /id="PRO_0000040927"
FT CHAIN 100..195
FT /note="Phosphorylated protein pp21"
FT /id="PRO_0000040928"
FT CHAIN 196..228
FT /note="Protein p3"
FT /id="PRO_0000040929"
FT CHAIN 229..254
FT /note="Protein p8"
FT /id="PRO_0000040930"
FT CHAIN 255..269
FT /note="Protein n"
FT /id="PRO_0000040931"
FT CHAIN 270..496
FT /note="Capsid protein p27"
FT /id="PRO_0000040932"
FT CHAIN 497..591
FT /note="Nucleocapsid protein p14"
FT /id="PRO_0000040933"
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 154..193
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:2542570"
FT SITE 195..196
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:2542570"
FT SITE 228..229
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:2542570"
FT SITE 254..255
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P10258"
FT SITE 269..270
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:2542570"
FT SITE 496..497
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:2542570"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000269|PubMed:2542570"
FT VARIANT 523
FT /note="K -> E"
FT CONFLICT 106
FT /note="S -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="V -> M (in Ref. 1; AAF31472)"
FT /evidence="ECO:0000305"
FT TURN 528..530
FT /evidence="ECO:0007829|PDB:1DSQ"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:1DSQ"
FT TURN 537..541
FT /evidence="ECO:0007829|PDB:1DSQ"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:1DSV"
FT STRAND 559..562
FT /evidence="ECO:0007829|PDB:1DSV"
FT TURN 564..566
FT /evidence="ECO:0007829|PDB:1DSV"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:1DSV"
FT HELIX 573..575
FT /evidence="ECO:0007829|PDB:1DSV"
SQ SEQUENCE 591 AA; 66351 MW; 8F9E3C05D6F7B9AC CRC64;
MGVSGSKGQK LFVSVLQRLL SERGLHVKES SAIEFYQFLI KVSPWFPEEG GLNLQDWKRV
GREMKKYAAE HGTDSIPKQA YPIWLQLREI LTEQSDLVLL SAEAKSVTEE ELEEGLTGLL
SASSQEKTYG TRGTAYAEID TEVDKLSEHI YDEPYEEKEK ADKNEEKDHV RKVKKIVQRK
ENSEHKRKEK DQKAFLATDW NNDDLSPEDW DDLEEQAAHY HDDDELILPV KRKVDKKKPL
ALRRKPLPPV GFAGAMAEAR EKGDLTFTFP VVFMGESDDD DTPVWEPLPL KTLKELQSAV
RTMGPSAPYT LQVVDMVASQ WLTPSDWHQT ARATLSPGDY VLWRTEYEEK SKETVQKTAG
KRKGKVSLDM LLGTGQFLSP SSQIKLSKDV LKDVTTNAVL AWRAIPPPGV KKTVLAGLKQ
GNEESYETFI SRLEEAVYRV MPRGEGSDIL IKQLAWENAN SLCQDLIRPM RKTGTMQDYI
RACLDASPAV VQGMAYAAAM RGQKYSTFVK QTYGGGKGGQ GSKGPVCFSC GKTGHIKRDC
KEEKGSKRAP PGLCPRCKKG YHWKSECKSK FDKDGNPLPP LETNAENSKN L
