GAG_BLVAU
ID GAG_BLVAU Reviewed; 392 AA.
AC P25058;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 4.
DT 23-FEB-2022, entry version 108.
DE RecName: Full=Gag 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-gag;
GN Name=gag;
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).
RN [4]
RP FUNCTION (NUCLEOCAPSID PROTEIN P12-GAG).
RX PubMed=25686502; DOI=10.1016/j.bbrc.2015.02.025;
RA Qualley D.F., Sokolove V.L., Ross J.L.;
RT "Bovine leukemia virus nucleocapsid protein is an efficient nucleic acid
RT chaperone.";
RL Biochem. Biophys. Res. Commun. 458:687-692(2015).
RN [5]
RP STRUCTURE BY NMR OF 1-109.
RX PubMed=8670827; DOI=10.1002/j.1460-2075.1996.tb00691.x;
RA Matthews S., Miklhailov M., Burny A., Roy P.;
RT "The solution structure of the bovine leukaemia virus matrix protein and
RT similarity with lentiviral matrix proteins.";
RL EMBO J. 15:3267-3274(1996).
CC -!- FUNCTION: [Gag polyprotein]: The matrix domain targets Gag, Gag-Pro and
CC 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:P03345}.
CC -!- FUNCTION: [Nucleocapsid protein p12-gag]: 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:0000269|PubMed:25686502}.
CC -!- SUBUNIT: [Gag polyprotein]: Homodimer; the homodimers are part of the
CC immature particles. Interacts with host NEDD4; these interactions are
CC 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-gag]: Virion
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag polyprotein;
CC IsoId=P25058-1; Sequence=Displayed;
CC Name=Gag-Pro polyprotein;
CC IsoId=P0DOI1-1; 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:0000269|PubMed:12134053}.
CC -!- DOMAIN: [Capsid protein p24]: The capsid protein N-terminus seems to be
CC involved in Gag-Gag interactions. {ECO:0000250|UniProtKB:P03345}.
CC -!- PTM: [Gag 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.
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- PTM: [Gag 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 -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC translation. {ECO:0000269|PubMed:6094258}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA00543.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D00647; BAA00543.1; ALT_FRAME; Genomic_DNA.
DR PIR; JQ0554; FOLJGA.
DR SMR; P25058; -.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IDA:UniProtKB.
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: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 InterPro; IPR003139; D_retro_matrix.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_N.
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; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Capsid protein; Host-virus interaction; Lipoprotein; Metal-binding;
KW Myristate; Phosphoprotein; Repeat; 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..392
FT /note="Gag polyprotein"
FT /id="PRO_0000442550"
FT CHAIN 2..109
FT /note="Matrix protein p15"
FT /id="PRO_0000040830"
FT CHAIN 110..323
FT /note="Capsid protein p24"
FT /id="PRO_0000040831"
FT CHAIN 324..392
FT /note="Nucleocapsid protein p12-gag"
FT /id="PRO_0000040832"
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:0000269|PubMed:12134053"
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 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 392 AA; 42862 MW; 4CC4D5A79C9C87B9 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 KN
