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PRO_BLVJ
ID   PRO_BLVJ                Reviewed;         571 AA.
AC   P0DOI0;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2017, sequence version 1.
DT   03-AUG-2022, entry version 10.
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 Japanese BLV-1) (BLV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX   NCBI_TaxID=11907;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2983308; DOI=10.1073/pnas.82.3.677;
RA   Sagata N., Yasunaga T., Tsuzuku-Kawamura J., Ohishi K., Ogawa Y., Ikawa Y.;
RT   "Complete nucleotide sequence of the genome of bovine leukemia virus: its
RT   evolutionary relationship to other retroviruses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:677-681(1985).
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=P0DOI0-1; Sequence=Displayed;
CC       Name=Gag polyprotein;
CC         IsoId=P03344-1; Sequence=External;
CC       Name=Gag-Pro-Pol polyprotein;
CC         IsoId=P03361-1; 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-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:P03345,
CC       ECO:0000250|UniProtKB:P10274}.
CC   -!- MISCELLANEOUS: [Isoform Gag-Pro polyprotein]: Produced by -1 ribosomal
CC       frameshifting between gag-pro. {ECO:0000305}.
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DR   EMBL; K02120; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   SMR; P0DOI0; -.
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   3: Inferred from homology;
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_0000442570"
FT   CHAIN           2..109
FT                   /note="Matrix protein p15"
FT                   /id="PRO_0000442571"
FT   CHAIN           110..322
FT                   /note="Capsid protein p24"
FT                   /id="PRO_0000442572"
FT   CHAIN           323..420
FT                   /note="Nucleocapsid protein p12-pro"
FT                   /id="PRO_0000442573"
FT   CHAIN           421..545
FT                   /note="Protease"
FT                   /id="PRO_0000442574"
FT   CHAIN           546..571
FT                   /note="p13"
FT                   /id="PRO_0000442575"
FT   REPEAT          342..362
FT   REPEAT          367..387
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:0000250|UniProtKB:P0DOI1"
FT   ACT_SITE        453
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            420..421
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03345"
FT   SITE            545..546
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"
SQ   SEQUENCE   571 AA;  61933 MW;  060F62EFADC67F55 CRC64;
     MGNSPSYNPP AGISPSDWLN LLQSAQRLNP RPSPSDFTDL KNYIHWFHKT QKKPWTFTSG
     GPTSCPPGRF GRVPLVLATL NEVLSNEGGA PGASAPEEQP PPYDPPAILP IISEGNRNRH
     RAWALRELQD IKKEIENKAP GSQVWIQTLR LAILQADPTP ADLEQLCQYI ASPVDQTAHM
     TSLTAAIAAA EAANTLQGFN PKTGTLTQQS AQPNAGDLRS QYQNLWLQAG KNLPTRPSAP
     WSTIVQGPAE SSVEFVNRLQ ISLADNLPDG VPKEPIIDSL SYANANRECQ QILQGRGPVA
     AVGQKLQACA QWAPKNKQPA LLVHTPGPKM PGPRQPAPKR PPPGPCYRCL KEGHWARDCP
     TKATGPPPGP CPICKDPSHW KRDCPTLKSK NKLIEGGLSA PQTITPITDS LSEAELECLL
     SIPLARSRPS VAVYLSGPWL QPSQNQALML VDTGAENTVL PQNWLVRDYP RIPAAVLGAG
     GVSRNRYNWL QGPLTLALKP EGPFITIPKI LVDTSDKWQI LGRDVPSRLQ ASISIPEEVR
     PPVVGVLDTP PSHIGLEHLP PPPEVPQFPL N
 
 
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