ID PRO_MMTVB Reviewed; 860 AA.
AC P10271;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 2.
DT 24-JAN-2024, entry version 111.
DE RecName: Full=Gag-Pro 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-dUTPase;
DE Short=NC-dUTPase;
DE EC=3.6.1.23 {ECO:0000250|UniProtKB:P11283};
DE Contains:
DE RecName: Full=Protease;
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275, ECO:0000269|PubMed:1331110};
GN Name=gag-pro;
OS Mouse mammary tumor virus (strain BR6) (MMTV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus;
OC Mouse mammary tumor virus.
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-PRO POLYPROTEIN), CHARACTERIZATION (PROTEASE),
RP SUBUNIT (PROTEASE), CATALYTIC ACTIVITY (PROTEASE), ACTIVITY REGULATION
RP (PROTEASE), AND BIOPHYSICOCHEMICAL PROPERTIES (PROTEASE).
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).
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 -!- FUNCTION: [Protease]: The aspartyl protease mediates proteolytic
CC cleavages of Gag and Gag-Pol polyproteins during or shortly after the
CC release of the virion from the plasma membrane. Cleavages take place as
CC an ordered, step-wise cascade to yield mature proteins. This process is
CC called maturation. Displays maximal activity during the budding process
CC just prior to particle release from the cell. {ECO:0000255|PROSITE-
CC ProRule:PRU00275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;
CC Evidence={ECO:0000250|UniProtKB:P11283};
CC -!- ACTIVITY REGULATION: [Protease]: Inhibited by pepstatin A.
CC {ECO:0000269|PubMed:1331110}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4-6 for protease. {ECO:0000269|PubMed:1331110};
CC -!- SUBUNIT: [Matrix protein p10]: Homodimer; when myristoylated (By
CC similarity). {ECO:0000250|UniProtKB:P10258}.
CC -!- SUBUNIT: [Protease]: Homodimer (PubMed:1331110).
CC {ECO:0000269|PubMed:1331110}.
CC -!- SUBUNIT: [Nucleocapsid protein-dUTPase]: NC-dUTPase is a homotrimer (By
CC similarity). {ECO:0000250|UniProtKB:P10258}.
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-dUTPase]: Virion
CC {ECO:0000269|PubMed:205999}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag-Pro polyprotein;
CC IsoId=P10271-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P10258-1; Sequence=External;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P03365-1; Sequence=External;
CC -!- DOMAIN: [Gag-Pro polyprotein]: Late-budding domains (L domains) are
CC short sequence motifs essential for viral particle release. They can
CC occur individually or in close proximity within structural proteins.
CC They interacts with sorting cellular proteins of the multivesicular
CC body (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: [Protease]: Released by autocatalytic processing.
CC {ECO:0000269|PubMed:1331110}.
CC -!- PTM: [Gag-Pro 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:0000250|UniProtKB:P10258}.
CC -!- PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. {ECO:0000269|PubMed:1331110}.
CC -!- MISCELLANEOUS: [Isoform Gag-Pro polyprotein]: Produced by -1 ribosomal
CC frameshifting between gag-pro. {ECO:0000269|PubMed:3027377}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA46541.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M15122; AAA46541.1; ALT_FRAME; Genomic_RNA.
DR PIR; B26795; PRMVMM.
DR SMR; P10271; -.
DR MEROPS; A02.010; -.
DR Proteomes; UP000228400; Genome.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0016032; P:viral process; IEA:InterPro.
DR CDD; cd05482; HIV_retropepsin_like; 1.
DR CDD; cd07557; trimeric_dUTPase; 1.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR Gene3D; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1.
DR Gene3D; 1.10.150.490; Retroviral GAG p10 protein; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR003322; B_retro_matrix.
DR InterPro; IPR038124; B_retro_matrix_sf.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR034170; Retropepsin-like_cat_dom.
DR InterPro; IPR018061; Retropepsins.
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 PANTHER; PTHR40389; ENDOGENOUS RETROVIRUS GROUP K MEMBER 24 GAG POLYPROTEIN-RELATED; 1.
DR PANTHER; PTHR40389:SF3; IGE-BINDING PROTEIN; 1.
DR Pfam; PF00692; dUTPase; 1.
DR Pfam; PF02337; Gag_p10; 1.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR Pfam; PF14787; zf-CCHC_5; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF51283; dUTPase-like; 1.
DR SUPFAM; SSF47836; Retroviral matrix proteins; 1.
DR SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR SUPFAM; SSF47943; Retrovirus capsid protein, N-terminal core domain; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 2.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Capsid protein; DNA-binding; Hydrolase; Lipoprotein;
KW Magnesium; Metal-binding; Myristate; Protease; Reference proteome;
KW Ribosomal frameshifting; Viral matrix protein; Viral nucleoprotein; Virion;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255"
FT CHAIN 2..859
FT /note="Gag-Pro polyprotein"
FT /id="PRO_0000199549"
FT CHAIN 2..99
FT /note="Matrix protein p10"
FT /id="PRO_0000442484"
FT CHAIN 100..195
FT /note="Phosphorylated protein pp21"
FT /id="PRO_0000442485"
FT CHAIN 196..228
FT /note="Protein p3"
FT /id="PRO_0000442486"
FT CHAIN 229..254
FT /note="Protein p8"
FT /id="PRO_0000442487"
FT CHAIN 255..269
FT /note="Protein n"
FT /id="PRO_0000442488"
FT CHAIN 270..496
FT /note="Capsid protein p27"
FT /id="PRO_0000442489"
FT CHAIN 497..745
FT /note="Nucleocapsid protein-dUTPase"
FT /id="PRO_0000442490"
FT CHAIN 746..860
FT /note="Protease"
FT /id="PRO_0000442491"
FT DOMAIN 766..841
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT ZN_FING 525..542
FT /note="CCHC-type"
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 572..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 305..308
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 581..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 771
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
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 SITE 745..746
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:0000250|UniProtKB:P10258"
SQ SEQUENCE 860 AA; 95409 MW; 025DA3826F544C9A 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 LVKGQSPSPA
QKGDGVKGSG LNPEAPPFTI HDLPRGTPGS AGLDLSSQKD LILSLEDGVS LVPTLVKGTL
PEGTTGLIIG RSSNYKKGLE VLPGVIDSDF QGEIKVMVKA AKNAVIIHKG ERIAQLLLLP
YLKLPNPVIK EERGSEGFGS TSHVHWVQEI SDSRPMLHIY LNGRRFLGLL DTGADKTCIA
GRDWPANWPI HQTESSLQGL GMACGVARSS QPLRWQHEDK SGIIHPFVIP TLPFTLWGRD
IMKDIKVRLM TDSPDDSQDL
//
