PRO_MMTVC
ID PRO_MMTVC Reviewed; 860 AA.
AC Q9IZT2;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
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:0000269|PubMed:8091672};
DE Contains:
DE RecName: Full=Protease;
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
GN Name=gag-pro;
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 RIBOSOMAL 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-PRO 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 PROTEIN SEQUENCE OF 497-512 AND 744-745, RIBOSOMAL FRAMESHIFT, SUBUNIT
RP (NUCLEOCAPSID PROTEIN-DUTPASE), FUNCTION (NUCLEOCAPSID PROTEIN-DUTPASE),
RP AND COFACTOR (NUCLEOCAPSID PROTEIN-DUTPASE).
RX PubMed=8091672; DOI=10.1006/viro.1994.1547;
RA Bergman A.C., Bjornberg O., Nord J., Nyman P.O., Rosengren A.M.;
RT "The protein p30, encoded at the gag-pro junction of mouse mammary tumor
RT virus, is a dUTPase fused with a nucleocapsid protein.";
RL Virology 204:420-424(1994).
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: [Nucleocapsid protein-dUTPase]: NC-dUTPase has dUTPase
CC activity, thereby preventing incorporation of uracil into DNA.
CC {ECO:0000305|PubMed:8091672}.
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:0000269|PubMed:8091672};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Magnesium ions are required for NC-dUTPase activity.
CC {ECO:0000305|PubMed:8091672};
CC -!- ACTIVITY REGULATION: [Protease]: Inhibited by pepstatin A.
CC {ECO:0000250|UniProtKB:P10271}.
CC -!- SUBUNIT: [Matrix protein p10]: Homodimer; when myristoylated.
CC {ECO:0000305}.
CC -!- SUBUNIT: [Protease]: Homodimer (By similarity).
CC {ECO:0000250|UniProtKB:P10258}.
CC -!- SUBUNIT: [Nucleocapsid protein-dUTPase]: NC-dUTPase is a homotrimer
CC (PubMed:8091672). {ECO:0000269|PubMed:8091672}.
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-dUTPase]: Virion
CC {ECO:0000250|UniProtKB:P10258}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag-Pro polyprotein;
CC IsoId=Q9IZT2-1; Sequence=Displayed;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P11283-1; Sequence=External;
CC Name=Gag polyprotein;
CC IsoId=P11284-1; 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:0000250|UniProtKB:P10271}.
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:0000269|PubMed:2542570}.
CC -!- PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. {ECO:0000269|PubMed:2542570}.
CC -!- MISCELLANEOUS: [Isoform Gag-Pro polyprotein]: Produced by -1 ribosomal
CC frameshifting between gag-pro. {ECO:0000269|PubMed:3035577,
CC ECO:0000269|PubMed:8091672}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF228552; AAF31473.1; -; Genomic_DNA.
DR EMBL; M16766; AAA66623.1; -; Genomic_RNA.
DR BMRB; Q9IZT2; -.
DR SMR; Q9IZT2; -.
DR MEROPS; A02.010; -.
DR iPTMnet; Q9IZT2; -.
DR Proteomes; UP000006540; 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; 1.10.150.490; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 2.70.40.10; -; 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; IPR000721; Gag_p24_N.
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 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 SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
DR SUPFAM; SSF57756; SSF57756; 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; Direct protein sequencing; DNA-binding;
KW Hydrolase; Lipoprotein; Magnesium; Metal-binding; Myristate;
KW Phosphoprotein; Protease; Reference proteome; Repeat;
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..860
FT /note="Gag-Pro polyprotein"
FT /id="PRO_0000403622"
FT CHAIN 2..99
FT /note="Matrix protein p10"
FT /id="PRO_0000403623"
FT CHAIN 100..195
FT /note="Phosphorylated protein pp21"
FT /id="PRO_0000403624"
FT CHAIN 196..228
FT /note="Protein p3"
FT /id="PRO_0000403625"
FT CHAIN 229..254
FT /note="Protein p8"
FT /id="PRO_0000403626"
FT CHAIN 255..269
FT /note="Protein n"
FT /id="PRO_0000403627"
FT CHAIN 270..496
FT /note="Capsid protein p27"
FT /id="PRO_0000403628"
FT CHAIN 497..745
FT /note="Nucleocapsid protein-dUTPase"
FT /id="PRO_0000403629"
FT CHAIN 746..860
FT /note="Protease"
FT /id="PRO_0000403630"
FT DOMAIN 766..841
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
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 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..605
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: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:0000269|PubMed:2542570"
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 ECO:0000269|PubMed:8091672"
FT SITE 745..746
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:8091672"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000269|PubMed:2542570"
FT VARIANT 523
FT /note="E -> K"
SQ SEQUENCE 860 AA; 95593 MW; EC4015AAA30F0797 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 SRLEEAVYRM MPRGEGSDIL IKQLAWENAN SLCQDLIRPM RKTGTMQDYI
RACLDASPAV VQGMAYAAAM RGQKYSTFVK QTYGGGKGGQ GSEGPVCFSC GKTGHIKRDC
KEEKGSKRAP PGLCPRCKKG YHWKSECKSK FDKDGNPLPP LETNAENSKN LVKGQSPSPT
QKGDKGKDSG LNPEAPPFTI HDLPRGTPGS AGLDLSSQKD LILSLEDGVS LVPTLVKGTL
PEGTTGLIIG RSSNYKKGLE VLPGVIDSDF QGEIKVMVKA AKNAVIIHKG ERIAQLLLLP
YLKLPNPIIK EERGSEGFGS TSHVHWVQEI SDSRPMLHIS LNGRRFLGLL DTGADKTCIA
GRDWPANWPI HQTESSLQGL GMACGVARSS QPLRWQHEDK SGIIHPFVIP TLPFTLWGRD
IMKEIKVRLM TDSPDDSQDL
