PRO_SMRVH
ID PRO_SMRVH Reviewed; 998 AA.
AC P21407;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Gag-Pro polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p19;
DE Contains:
DE RecName: Full=Core protein p16;
DE Contains:
DE RecName: Full=Capsid protein p35;
DE AltName: Full=Capsid protein p34;
DE Contains:
DE RecName: Full=Probable 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 Squirrel monkey retrovirus (SMRV-H) (SMRV-HLB).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11856;
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 319-346, AND
RP PROTEOLYTIC CLEAVAGE (GAG-PRO POLYPROTEIN).
RX PubMed=3201749; DOI=10.1016/s0042-6822(88)90109-2;
RA Oda T., Ikeda S., Watanabe S., Hatsushika M., Akiyama K., Mitsunobu F.;
RT "Molecular cloning, complete nucleotide sequence, and gene structure of the
RT provirus genome of a retrovirus produced in a human lymphoblastoid cell
RT line.";
RL Virology 167:468-476(1988).
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. Nucleocapsid protein-dUTPase: Homotrimer.
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBUNIT: [Probable nucleocapsid protein-dUTPase]: Homotrimer.
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p35]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Probable 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=P21407-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P21411-1; Sequence=External;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P03364-1; 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-p35 contains one L domain: a PTAP/PSAP motif, which interacts with
CC the UEV domain of TSG101. {ECO:0000305}.
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: [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:0000305|PubMed:3201749}.
CC -!- MISCELLANEOUS: [Isoform Gag-Pro polyprotein]: Produced by -1 ribosomal
CC frameshifting between gag-pro. {ECO:0000305|PubMed:24298557}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA66452.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; M23385; AAA66452.1; ALT_INIT; Genomic_RNA.
DR PIR; B31827; PRLJHD.
DR RefSeq; NP_041260.2; NC_001514.1.
DR SMR; P21407; -.
DR GeneID; 1491963; -.
DR KEGG; vg:1491963; -.
DR Proteomes; UP000007223; 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; 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 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.
PE 1: Evidence at protein level;
KW Aspartyl protease; Capsid protein; Direct protein sequencing; DNA-binding;
KW Hydrolase; Lipoprotein; Magnesium; Myristate; Nucleotide metabolism;
KW Protease; Ribosomal frameshifting; Viral matrix protein;
KW Viral nucleoprotein; Virion.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255"
FT CHAIN 2..998
FT /note="Gag-Pro polyprotein"
FT /id="PRO_0000199553"
FT CHAIN 2..163
FT /note="Matrix protein p19"
FT /id="PRO_0000443199"
FT CHAIN 164..318
FT /note="Core protein p16"
FT /id="PRO_0000443200"
FT CHAIN 319..585
FT /note="Capsid protein p35"
FT /id="PRO_0000443201"
FT CHAIN 586..842
FT /note="Probable nucleocapsid protein-dUTPase"
FT /id="PRO_0000443202"
FT CHAIN 843..998
FT /note="Protease 17 kDa"
FT /id="PRO_0000443203"
FT CHAIN 843..960
FT /note="Protease 13 kDa"
FT /id="PRO_0000443204"
FT PEPTIDE 961..998
FT /note="G-patch peptide"
FT /id="PRO_0000443205"
FT DOMAIN 863..939
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 950..996
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REGION 115..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..366
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 868
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT SITE 163..164
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000305|PubMed:3201749"
FT SITE 318..319
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000305|PubMed:3201749"
FT SITE 585..586
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000305|PubMed:3201749"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 998 AA; 108735 MW; FAF6CE7DF50AA024 CRC64;
MGQASSHSEN DLFISHLKES LKVRRIRVRK KDLVSFFSFI FKTCPWFPQE GSIDSRVWGR
VGDCLNDYYR VFGPETIPIT TFNYYNLIRD VLTNQSDSPD IQRLCKEGHK ILISHSRPPS
RQAPVTITTS EKASSRPPSR APSTCPSVAI DIGSHDTGQS SLYPNLATLT DPPIQSPHSR
AHTPPQHLPL LANSKTLHNS GSQDDQLNPA DQADLEEAAA QYNNPDWPQL TNTPALPPFR
PPSYVSTAVP PVAVAAPVLH APTSGVPGSP TAPNLPGVAL AKPSGPIDET VSLLDGVKTL
VTKLSDLALL PPAGVMAFPV TRSQGQVSSN TTGRASPHPD THTIPEEEEA DSGESDSEDD
EEESSEPTEP TYTHSYKRLN LKTIEKIKTA VANYGPTAPF TVALVESLSE RWLTPSDWFF
LSRAALSGGD NILWKSEYED ISKQFAERTR VRPPPKDGPL KIPGASPYQN NDKQAQFPPG
LLTQIQSAGL KAWKRLPQKG AATTSLAKIR QGPDESYSDF VSRLQETADR LFGSGESESS
FVKHLAYENA NPACQSAIRP FRQKELSTMS PLLWYCSAHA VGLAIGAALQ NLAPAQLLEP
RPAFAIIVTN PAIFQETAPK KIQPPTQLPT QPNAPQASLI KNLGPTTKCP RCKKGFHWAS
ECRSRLDING QPIIKQGNLE QGPAPGPHYR DELRGFTVHP PIPPANPCPP SNQPRRYVTD
LWRATAGSAG LDLCTTTDTI LTTQNSPLTL PVGIYGPLPP QTFGLILAEP ALPSKGIQVL
PGILDNDFEG EIHIILSTTK DLVTIPKGTR LAQIVILPLQ QINSNFHKPY RGASAPGSSD
VYWVQQISQQ RPTLKLKLNG KLFSGILDTG ADATVISYTH WPRNWPLTTV ATHLRGIGQA
TNPQQSAQML KWEDSEGNNG HITPYVLPNL PVNLWGRDIL SQMKLVMCSP NDTVMTQMLS
QGYLPGQGLG KNNQGITQPI TITPKKDKTG LGFHQNLP
