PRO_BLVAU
ID PRO_BLVAU Reviewed; 571 AA.
AC P0DOI1;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Gag-Pro polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p15;
DE Short=MA;
DE Contains:
DE RecName: Full=Capsid protein p24;
DE Short=CA;
DE Contains:
DE RecName: Full=Nucleocapsid protein p12-pro;
DE Contains:
DE RecName: Full=Protease;
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
DE Contains:
DE RecName: Full=p13;
OS Bovine leukemia virus (isolate Australian) (BLV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX NCBI_TaxID=11903;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2167927; DOI=10.1099/0022-1317-71-8-1737;
RA Coulston J., Naif H., Brandon R., Kumar S., Khan S., Daniel R.C.W.,
RA Lavin M.F.;
RT "Molecular cloning and sequencing of an Australian isolate of proviral
RT bovine leukaemia virus DNA: comparison with other isolates.";
RL J. Gen. Virol. 71:1737-1746(1990).
RN [2]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=6094258; DOI=10.1016/0014-5793(84)81244-2;
RA Sagata N., Yasunaga T., Ikawa Y.;
RT "Identification of a potential protease-coding gene in the genomes of
RT bovine leukemia and human T-cell leukemia viruses.";
RL FEBS Lett. 178:79-82(1984).
RN [3]
RP DOMAIN LATE-BUDDING, AND MUTAGENESIS OF 100-PRO--TYR-103.
RX PubMed=12134053; DOI=10.1128/jvi.76.16.8485-8493.2002;
RA Wang H., Norris K.M., Mansky L.M.;
RT "Analysis of bovine leukemia virus gag membrane targeting and late domain
RT function.";
RL J. Virol. 76:8485-8493(2002).
CC -!- FUNCTION: [Gag-Pro polyprotein]: The matrix domain targets Gag, Gag-Pro
CC and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite
CC membrane binding signal, that includes its myristoylated N-terminus.
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- FUNCTION: [Matrix protein p15]: Matrix protein.
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- FUNCTION: [Capsid protein p24]: Forms the spherical core of the virus
CC that encapsulates the genomic RNA-nucleocapsid complex.
CC {ECO:0000250|UniProtKB:P10274}.
CC -!- FUNCTION: [Nucleocapsid protein p12-pro]: Binds strongly to viral
CC nucleic acids and promote their aggregation. Also destabilizes the
CC nucleic acids duplexes via highly structured zinc-binding motifs.
CC {ECO:0000250|UniProtKB:P10274}.
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 -!- SUBUNIT: [Gag-Pro polyprotein]: Homodimer; the homodimers are part of
CC the immature particles. Interacts with human TSG101 and NEDD4; these
CC interactions are essential for budding and release of viral particles.
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- SUBUNIT: [Matrix protein p15]: Homodimer; further assembles as
CC homohexamers. {ECO:0000250|UniProtKB:P03345}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p12-pro]: Virion
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag-Pro polyprotein;
CC IsoId=P0DOI1-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P25058-1; Sequence=External;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P25059-1; 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 Matrix protein p15 contains one L domain: a PPXY motif which binds to
CC the WW domains of the ubiquitin ligase NEDD4.
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages by the viral
CC protease yield mature proteins. The polyprotein is cleaved during and
CC after budding, this process is termed maturation. The protease is
CC autoproteolytically processed at its N- and C-termini.
CC {ECO:0000250|UniProtKB:P10274}.
CC -!- PTM: Gag polyprotein: Myristoylated. Myristoylation of the matrix (MA)
CC domain mediates the transport and binding of Gag polyproteins to the
CC host plasma membrane and is required for the assembly of viral
CC particles. {ECO:0000250|UniProtKB:P03345,
CC ECO:0000250|UniProtKB:P10274}.
CC -!- MISCELLANEOUS: [Isoform Gag-Pro polyprotein]: Produced by -1 ribosomal
CC frameshifting between gag-pro. {ECO:0000269|PubMed:6094258,
CC ECO:0000305}.
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DR EMBL; D00647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0DOI1; -.
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:0003676; F:nucleic acid binding; IEA:InterPro.
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:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR InterPro; IPR003139; D_retro_matrix.
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; 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; PF02228; Gag_p19; 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; SSF57756; SSF57756; 1.
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; Host-virus interaction; Hydrolase;
KW Lipoprotein; Metal-binding; Myristate; Phosphoprotein; Protease; 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:0000255"
FT CHAIN 2..571
FT /note="Gag-Pro polyprotein"
FT /id="PRO_0000442564"
FT CHAIN 2..109
FT /note="Matrix protein p15"
FT /id="PRO_0000442565"
FT CHAIN 110..323
FT /note="Capsid protein p24"
FT /id="PRO_0000442566"
FT CHAIN 324..419
FT /note="Nucleocapsid protein p12-pro"
FT /id="PRO_0000442567"
FT CHAIN 420..544
FT /note="Protease"
FT /id="PRO_0000442568"
FT CHAIN 545..571
FT /note="p13"
FT /id="PRO_0000442569"
FT REPEAT 342..362
FT REPEAT 367..387
FT DOMAIN 447..525
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT ZN_FING 345..362
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 370..387
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT MOTIF 100..103
FT /note="PPXY motif"
FT /evidence="ECO:0000269|PubMed:12134053"
FT ACT_SITE 452
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT SITE 109..110
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03345"
FT SITE 323..324
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03345"
FT SITE 419..420
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03345"
FT SITE 544..545
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03345"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255"
FT MUTAGEN 100..103
FT /note="PPPY->AAAA: Greatly reduced release of new viral
FT particles."
FT /evidence="ECO:0000269|PubMed:12134053"
SQ SEQUENCE 571 AA; 62261 MW; 68890E386172F54F CRC64;
MGNSPSYNPP AGISPSDWLN LLQSAQRLNP RPSPSDFTDL KNYIHWFHKT QKKPWTFTSG
GPASCPPGKF GRVPLVLATL NEVLSNDEGA PGASAPEEQP PPYDPPAVLP IISEGNRNRH
RAWALRELQD IKKEIENKAP GSQVWIQTLR LAILQADPTP ADLEQLCQYI ASPVDQTAHM
TSLTAAIAAE AANTLQGFNP KMGTLTQQSA QPNAGDLRSQ YQNLWLQAWK NLPTRPSVQP
WSTIVQGPAE SYVEFVNRLQ ISLADNLPDG VPKEPIIDSL SYANANKECQ QILQGRGLVA
APVGQKLQAC AHWAPKTKQP AILVHTPGPK MPGPRQPAPK RPPPGPCYRC LKEGHWARDC
PTKTTGPPPG PCPICKDPSH WKRDCPTLKS KKLIEGGPSA PQIITPITDS LSEAELECLL
SIPLARSRPS VAVYLSGPWL QPSQNQALML VDTGAENTVL PQNWLVRDYP RTPAAVLGAG
GISRNRYNWL QGPLTLALKP EGPFITIPKI LVDTFDKWQI LGRDVLSRLQ ASISIPEEVH
PPVVGVLDAP PSHIGLEHLP PPPEVPQFPL N
