PRO_SRV1
ID PRO_SRV1 Reviewed; 912 AA.
AC P04024;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Gag-Pro polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p10;
DE Contains:
DE RecName: Full=Phosphorylated protein pp24;
DE Contains:
DE RecName: Full=Phosphorylated protein pp18;
DE Contains:
DE RecName: Full=p12;
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:P07570};
DE Contains:
DE RecName: Full=Protease 17 kDa {ECO:0000250|UniProtKB:P07570};
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
DE Contains:
DE RecName: Full=Protease 13 kDa {ECO:0000250|UniProtKB:P07570};
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
DE Contains:
DE RecName: Full=G-patch peptide {ECO:0000250|UniProtKB:P07570};
GN Name=pro; Synonyms=prt;
OS Simian retrovirus SRV-1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11942;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3006247; DOI=10.1126/science.3006247;
RA Power M.D., Marx P.A., Bryant M.L., Gardner M.B., Barr P.J., Luciw P.A.;
RT "Nucleotide sequence of SRV-1, a type D simian acquired immune deficiency
RT syndrome retrovirus.";
RL Science 231:1567-1572(1986).
RN [2]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=24298557; DOI=10.1155/2013/984028;
RA Huang X., Cheng Q., Du Z.;
RT "A genome-wide analysis of RNA pseudoknots that stimulate efficient -1
RT ribosomal frameshifting or readthrough in animal viruses.";
RL Biomed. Res. Int. 2013:984028-984028(2013).
CC -!- FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.
CC -!- FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein.
CC {ECO:0000305}.
CC -!- FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.
CC -!- FUNCTION: [Protease 17 kDa]: 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.
CC {ECO:0000250|UniProtKB:P07570, ECO:0000255|PROSITE-ProRule:PRU00275}.
CC -!- FUNCTION: [Protease 13 kDa]: 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.
CC {ECO:0000250|UniProtKB:P07570, ECO:0000255|PROSITE-ProRule:PRU00275}.
CC -!- FUNCTION: [G-patch peptide]: Enhances the activity of the reverse
CC transcriptase. May be part of the mature RT.
CC {ECO:0000250|UniProtKB:P07570}.
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:P07570};
CC -!- SUBUNIT: [Protease 17 kDa]: Homodimer. {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBUNIT: [G-patch peptide]: Interacts with the reverse
CC transcriptase/ribonuclease H. {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBUNIT: [Nucleocapsid protein-dUTPase]: Homotrimer.
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protease 13 kDa]: Virion
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBCELLULAR LOCATION: [Protease 17 kDa]: Virion
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag-Pro polyprotein;
CC IsoId=P04024-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P04022-1; Sequence=External;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P04025-1; 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 Phosphorylated protein pp24 and phosphorylated protein pp18 contains
CC two L domains: a PTAP/PSAP motif which interacts with the UEV domain of
CC TSG101, and a PPXY motif which binds to the WW domains of the ubiquitin
CC ligase NEDD4. Both motifs contribute to viral release. The PSAP motif
CC acts as an additional L domain and promotes the efficient release of
CC the virions but requires an intact PPPY motif to perform its function.
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- DOMAIN: [Protease 17 kDa]: The glycine-rich G-patch domain (GPD) is
CC present at the C-terminus of the protease from which it is then
CC detached by the protease itself. {ECO:0000250|UniProtKB:P07570}.
CC -!- PTM: [Protease 17 kDa]: Released by autocatalytic processing. The
CC protease can undergo further autoprocessing to yield 2 shorter but
CC enzymatically active forms of 12 kDa and 13 kDa without the GDP domain.
CC {ECO:0000250|UniProtKB:P07570}.
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:0000250|UniProtKB:P07570}.
CC -!- MISCELLANEOUS: [Isoform Gag-Pro polyprotein]: Produced by -1 ribosomal
CC frameshifting between gag-pro. {ECO:0000305|PubMed:24298557}.
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; M11841; AAA47731.1; -; Genomic_RNA.
DR BMRB; P04024; -.
DR SMR; P04024; -.
DR MEROPS; A02.009; -.
DR PRIDE; P04024; -.
DR Proteomes; UP000007228; 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:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
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; IPR000467; G_patch_dom.
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; PF01585; G-patch; 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 SMART; SM00443; G_patch; 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; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Capsid protein; Coiled coil; DNA-binding; Hydrolase;
KW Lipoprotein; Magnesium; Metal-binding; Myristate; Nucleotide metabolism;
KW Protease; Repeat; Ribosomal frameshifting; Viral matrix protein;
KW Viral nucleoprotein; Virion; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT CHAIN 2..912
FT /note="Gag-Pro polyprotein"
FT /id="PRO_0000199551"
FT CHAIN 2..100
FT /note="Matrix protein p10"
FT /id="PRO_0000443206"
FT CHAIN 101..217
FT /note="Phosphorylated protein pp24"
FT /id="PRO_0000443207"
FT PROPEP 101..162
FT /evidence="ECO:0000305"
FT /id="PRO_0000443208"
FT CHAIN 163..217
FT /note="Phosphorylated protein pp18"
FT /id="PRO_0000443209"
FT CHAIN 218..300
FT /note="p12"
FT /id="PRO_0000443210"
FT CHAIN 301..526
FT /note="Capsid protein p27"
FT /id="PRO_0000443211"
FT CHAIN 527..760
FT /note="Nucleocapsid protein-dUTPase"
FT /id="PRO_0000443212"
FT CHAIN 761..912
FT /note="Protease 17 kDa"
FT /id="PRO_0000443213"
FT CHAIN 761..874
FT /note="Protease 13 kDa"
FT /id="PRO_0000443214"
FT PEPTIDE 875..912
FT /note="G-patch peptide"
FT /id="PRO_0000443215"
FT DOMAIN 781..857
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 868..912
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 548..565
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 113..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 217..258
FT /evidence="ECO:0000255"
FT MOTIF 203..206
FT /note="PPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P07570"
FT MOTIF 211..214
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000250|UniProtKB:P07570"
FT COMPBIAS 113..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 786
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT SITE 100..101
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 162..163
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 217..218
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 300..301
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 526..527
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 760..761
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07570"
FT SITE 874..875
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07570"
SQ SEQUENCE 912 AA; 100774 MW; A56E7599FF0B8ED6 CRC64;
MGQELSQHER YVEQLKQALK TRGVKVKYAD LLKFFDFVKD TCPWFPQEGT IDIKRWRRVG
DCFQDYYNTF GPEKVPVTAF SYWNLIKELI DKKEVNPQVM AAVAQTEEIL KTSSHTELTT
KPSQNPDLDL ISLDSDDEGA KGSSLKDKNL SCTKKPKRFP VLLTAQTSAD PEDPNPSEVD
WDGLEDEAAK YHNPDWPPFL TRPPPYNKAT PSAPTVMAVV NPKEELKEKI AQLEEQIKLE
ELHQALISKL QKLKTGNETV TSPETAGGFS RTPHWPGQHI PKGKCCASRE KEEQTPKDIF
PVTETVDGQG QAWRHHNGFD FTVIKELKTA ASQYGATAPY TLAIVESVAD NWLTPTDWNT
LVRAVLSGGD HLLWKSEFFE NCRETAKRNQ QAGNGWDFDM LTGSGNYSST DAQMQYDPGL
FAQIQAAATK AWRKLPVKGD PGASLTGVKQ GPDEPFADFV HRLITTAGRI FGSAEAGVDY
VKQLAYENAN PACQAAIRPY RKKTDLTGYI RLCSDIGPSY QQGLAMAAAF SGQTVKDFLN
NKNKEKGGCC FKCGRKGHFA KNCHEHIHNN SETKAPGLCP RCKRGKHWAN ECKSKTDSQG
NPLPPHQGNR TEGPAPGPET SLWGGQLCSS QQKQPISKLT RATPGSAGLD LSSTSHTVLT
PEMGPQALST GIYGPLPPNT FGLILGRSSI TIKGLQVYPG VIDNDYTGEI KIMAKAVNNI
VTVPQGNRIA QLILLPLIET DNKVQQPYRG QGSFGSSDIY WVQPITCQKP SLTLWLDDKM
FTGLIDTGAD VTIIKLEDWP PNWPITDTLT NLRGIGQSNN PKQSSKYLTW RDKENNSGLI
KPFVIPNLPV NLWGRDLLSQ MKIMMCSPSD IVTAQMLAQG YSPGKGLGKN ENGILHPIPN
QGQFDKKGFG NF
