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Gag polyprotein [Cleaved into: Matrix protein p15 (MA); Capsid protein p24 (CA); Nucleocapsid protein p12-gag]

 GAG_BLVAU               Reviewed;         392 AA.
P25058;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
20-DEC-2017, sequence version 4.
23-MAY-2018, entry version 98.
RecName: Full=Gag polyprotein;
Contains:
RecName: Full=Matrix protein p15;
Short=MA;
Contains:
RecName: Full=Capsid protein p24;
Short=CA;
Contains:
RecName: Full=Nucleocapsid protein p12-gag;
Name=gag;
Bovine leukemia virus (isolate Australian) (BLV).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Deltaretrovirus.
NCBI_TaxID=11903;
NCBI_TaxID=9913; Bos taurus (Bovine).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2167927; DOI=10.1099/0022-1317-71-8-1737;
Coulston J., Naif H., Brandon R., Kumar S., Khan S., Daniel R.C.W.,
Lavin M.F.;
"Molecular cloning and sequencing of an Australian isolate of proviral
bovine leukaemia virus DNA: comparison with other isolates.";
J. Gen. Virol. 71:1737-1746(1990).
[2]
RIBOSOMAL FRAMESHIFT.
PubMed=6094258;
Sagata N., Yasunaga T., Ikawa Y.;
"Identification of a potential protease-coding gene in the genomes of
bovine leukemia and human T-cell leukemia viruses.";
FEBS Lett. 178:79-82(1984).
[3]
DOMAIN LATE-BUDDING, AND MUTAGENESIS OF 100-PRO--TYR-103.
PubMed=12134053; DOI=10.1128/JVI.76.16.8485-8493.2002;
Wang H., Norris K.M., Mansky L.M.;
"Analysis of bovine leukemia virus gag membrane targeting and late
domain function.";
J. Virol. 76:8485-8493(2002).
[4]
FUNCTION (NUCLEOCAPSID PROTEIN P12-GAG).
PubMed=25686502; DOI=10.1016/j.bbrc.2015.02.025;
Qualley D.F., Sokolove V.L., Ross J.L.;
"Bovine leukemia virus nucleocapsid protein is an efficient nucleic
acid chaperone.";
Biochem. Biophys. Res. Commun. 458:687-692(2015).
[5]
STRUCTURE BY NMR OF 1-109.
PubMed=8670827;
Matthews S., Miklhailov M., Burny A., Roy P.;
"The solution structure of the bovine leukaemia virus matrix protein
and similarity with lentiviral matrix proteins.";
EMBO J. 15:3267-3274(1996).
-!- FUNCTION: Gag polyprotein: The matrix domain targets Gag, Gag-Pro
and Gag-Pro-Pol polyproteins to the plasma membrane via a
multipartite membrane binding signal, that includes its
myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.
-!- FUNCTION: Matrix protein p15: Matrix protein.
{ECO:0000250|UniProtKB:P03345}.
-!- FUNCTION: Capsid protein p24: Forms the spherical core of the
virus that encapsulates the genomic RNA-nucleocapsid complex.
{ECO:0000250|UniProtKB:P03345}.
-!- FUNCTION: Nucleocapsid protein p12-gag: Binds strongly to viral
nucleic acids and promote their aggregation. Also destabilizes the
nucleic acids duplexes via highly structured zinc-binding motifs.
{ECO:0000269|PubMed:25686502}.
-!- SUBUNIT: Gag polyprotein: Homodimer; the homodimers are part of
the immature particles. Gag polyprotein: Interacts with host
NEDD4; these interactions are essential for budding and release of
viral particles. Matrix protein p15: Homodimer; further assembles
as homohexamers. {ECO:0000250|UniProtKB:P03345}.
-!- SUBCELLULAR LOCATION: Matrix protein p15: Virion
{ECO:0000250|UniProtKB:P03345}.
-!- SUBCELLULAR LOCATION: Capsid protein p24: Virion
{ECO:0000250|UniProtKB:P03345}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p12-gag: Virion
{ECO:0000250|UniProtKB:P03345}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=3;
Name=Gag polyprotein;
IsoId=P25058-1; Sequence=Displayed;
Note=Produced by conventional translation.
{ECO:0000269|PubMed:6094258};
Name=Gag-Pro polyprotein;
IsoId=P0DOI1-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting between gag-pro.
{ECO:0000269|PubMed:6094258};
Name=Gag-Pro-Pol polyprotein;
IsoId=P25059-1; Sequence=External;
Note=Produced by -1 ribosomal frameshiftings between gag-pro and
pro-pol. {ECO:0000269|PubMed:6094258};
-!- DOMAIN: Gag polyprotein: Late-budding domains (L domains) are
short sequence motifs essential for viral particle release. They
can occur individually or in close proximity within structural
proteins. They interacts with sorting cellular proteins of the
multivesicular body (MVB) pathway. Most of these proteins are
class E vacuolar protein sorting factors belonging to ESCRT-I,
ESCRT-II or ESCRT-III complexes. Matrix protein p15 contains one L
domain: a PPXY motif which binds to the WW domains of the
ubiquitin ligase NEDD4. {ECO:0000269|PubMed:12134053}.
-!- DOMAIN: Capsid protein p24: The capsid protein N-terminus seems to
be involved in Gag-Gag interactions.
{ECO:0000250|UniProtKB:P03345}.
-!- PTM: Gag polyprotein: Specific enzymatic cleavages by the viral
protease yield mature proteins. The polyprotein is cleaved during
and after budding, this process is termed maturation.
{ECO:0000250|UniProtKB:P03345}.
-!- PTM: Gag polyprotein: Myristoylated. Myristoylation of the matrix
(MA) domain mediates the transport and binding of Gag polyproteins
to the host plasma membrane and is required for the assembly of
viral particles. {ECO:0000250|UniProtKB:P03345}.
-!- SEQUENCE CAUTION:
Sequence=BAA00543.1; Type=Frameshift; Positions=193, 229; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; D00647; BAA00543.1; ALT_FRAME; Genomic_DNA.
PIR; JQ0554; FOLJGA.
ProteinModelPortal; P25058; -.
SMR; P25058; -.
PRIDE; P25058; -.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IDA:UniProtKB.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.185.10; -; 1.
Gene3D; 1.10.375.10; -; 1.
InterPro; IPR003139; D_retro_matrix.
InterPro; IPR036989; D_retro_matrix_sf.
InterPro; IPR000721; Gag_p24.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF02228; Gag_p19; 1.
Pfam; PF00607; Gag_p24; 1.
Pfam; PF00098; zf-CCHC; 1.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
Capsid protein; Host-virus interaction; Lipoprotein; Metal-binding;
Myristate; Phosphoprotein; Repeat; Ribosomal frameshifting;
Viral budding; Viral budding via the host ESCRT complexes;
Viral matrix protein; Viral nucleoprotein;
Viral release from host cell; Virion; Zinc; Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000255}.
CHAIN 2 392 Gag polyprotein.
/FTId=PRO_0000442550.
CHAIN 2 109 Matrix protein p15.
/FTId=PRO_0000040830.
CHAIN 110 323 Capsid protein p24.
/FTId=PRO_0000040831.
CHAIN 324 392 Nucleocapsid protein p12-gag.
/FTId=PRO_0000040832.
REPEAT 342 362
REPEAT 367 387
ZN_FING 345 362 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 370 387 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
MOTIF 100 103 PPXY motif.
{ECO:0000269|PubMed:12134053}.
SITE 109 110 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03345}.
SITE 323 324 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03345}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000255}.
MUTAGEN 100 103 PPPY->AAAA: Greatly reduced release of
new viral particles.
{ECO:0000269|PubMed:12134053}.
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


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