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Gag polyprotein (Pr53Gag) [Cleaved into: Matrix protein p16 (MA); p2L; Capsid protein p26 (CA); p3; Nucleocapsid protein p13 (NC); p2]

 GAG_BIV29               Reviewed;         476 AA.
P19558; P19559; Q65590;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
23-MAY-2018, entry version 105.
RecName: Full=Gag polyprotein;
AltName: Full=Pr53Gag;
Contains:
RecName: Full=Matrix protein p16;
Short=MA;
Contains:
RecName: Full=p2L;
Contains:
RecName: Full=Capsid protein p26;
Short=CA;
Contains:
RecName: Full=p3;
Contains:
RecName: Full=Nucleocapsid protein p13;
Short=NC;
Contains:
RecName: Full=p2;
Name=gag;
Bovine immunodeficiency virus (strain R29) (BIV) (Bovine
immunodeficiency-like virus).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Bovine lentivirus group.
NCBI_TaxID=417296;
NCBI_TaxID=9913; Bos taurus (Bovine).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate R29-106, and Isolate R29-127;
PubMed=2183467; DOI=10.1016/0042-6822(90)90424-P;
Garvey K.J., Oberste M.S., Elser J.E., Braun M.J., Gonda M.A.;
"Nucleotide sequence and genome organization of biologically active
proviruses of the bovine immunodeficiency-like virus.";
Virology 175:391-409(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Isolate R29-Nadin;
Nadin-Davis S.A., Chang S.C., Roth J.A., Carpenter S.;
"Isolation and characterization of cDNAs encoding rev and tat of
bovine immunodeficiency-like virus.";
Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
[3]
RIBOSOMAL FRAMESHIFT, AND PROTEOLYTIC PROCESSING OF POLYPROTEIN.
STRAIN=Isolate R29-127;
PubMed=1331499;
Battles J.K., Hu M.Y., Rasmussen L., Tobin G.J., Gonda M.A.;
"Immunological characterization of the gag gene products of bovine
immunodeficiency virus.";
J. Virol. 66:6868-6877(1992).
[4]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=12414761; DOI=10.1128/CDLI.9.6.1277-1281.2002;
Lu M., Zheng L., Mitchell K., Kapil S., Wood C., Minocha H.;
"Unique epitope of bovine immunodeficiency virus gag protein spans the
cleavage site between p16(MA) and p2L.";
Clin. Diagn. Lab. Immunol. 9:1277-1281(2002).
[5]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
STRAIN=Isolate R29-127;
PubMed=14694086; DOI=10.1128/JVI.78.2.551-560.2004;
Guo X., Hu J., Whitney J.B., Russell R.S., Liang C.;
"Important role for the CA-NC spacer region in the assembly of bovine
immunodeficiency virus Gag protein.";
J. Virol. 78:551-560(2004).
[6]
FUNCTION, AND INTERACTION WITH HOST DYNLL1.
PubMed=20148896; DOI=10.1111/j.1462-5822.2010.01453.x;
Su Y., Qiao W., Guo T., Tan J., Li Z., Chen Y., Li X., Li Y., Zhou J.,
Chen Q.;
"Microtubule-dependent retrograde transport of bovine immunodeficiency
virus.";
Cell. Microbiol. 12:1098-1107(2010).
-!- FUNCTION: Matrix protein p16 forms the outer shell of the core of
the virus, lining the inner surface of the viral membrane.
{ECO:0000250}.
-!- FUNCTION: Capsid protein p26 forms the conical core of the virus
that encapsulates the genomic RNA-nucleocapsid complex.
Interaction between incoming particle-associated Gag proteins and
host dynein allows intracellular microtubule-dependent virus
transport toward the perinuclear region, prior to nucleus
translocation and integration into host genome.
{ECO:0000269|PubMed:20148896}.
-!- FUNCTION: Nucleocapsid protein p13 encapsulates and protects viral
dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc
fingers (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with host light chain cytoplasmic dynein
DYNLL1; this interaction is critical for intracellular
microtubule-dependent viral genome transport.
{ECO:0000269|PubMed:20148896}.
-!- SUBCELLULAR LOCATION: Matrix protein p16: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein p26: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p13: Virion
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Comment=This strategy of translation probably allows the virus
to modulate the quantity of each viral protein.;
Name=Gag polyprotein;
IsoId=P19558-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Gag-Pol polyprotein;
IsoId=P19560-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting at the gag-pol genes
boundary.;
-!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
essential for viral particle budding. They recruit proteins of the
host ESCRT machinery (Endosomal Sorting Complex Required for
Transport) or ESCRT-associated proteins. Gag polyprotein contains
one L domain: a PTAP/PSAP motif, which interacts with the UEV
domain of TSG101 (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: The sequence shown is that of isolate R29-127.
-!- SIMILARITY: Belongs to the bovine lentivirus group gag polyprotein
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M32690; AAA91270.1; -; Genomic_RNA.
EMBL; L04974; AAA42763.1; -; Genomic_DNA.
PIR; A34742; FOLJBT.
RefSeq; NP_040562.1; NC_001413.1.
ProteinModelPortal; P19558; -.
SMR; P19558; -.
PRIDE; P19558; -.
GeneID; 1489970; -.
KEGG; vg:1489970; -.
PRO; PR:P19558; -.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-KW.
GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.375.10; -; 1.
InterPro; IPR000721; Gag_p24.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF00607; Gag_p24; 1.
Pfam; PF00098; zf-CCHC; 2.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50158; ZF_CCHC; 2.
1: Evidence at protein level;
Capsid protein; Cytoplasmic inwards viral transport;
Host-virus interaction; Metal-binding;
Microtubular inwards viral transport; Repeat; Ribosomal frameshifting;
Viral budding; Viral budding via the host ESCRT complexes;
Viral matrix protein; Viral nucleoprotein;
Viral release from host cell; Virion; Virion maturation;
Virus entry into host cell; Zinc; Zinc-finger.
CHAIN 1 476 Gag polyprotein.
/FTId=PRO_0000272319.
CHAIN 1 126 Matrix protein p16. {ECO:0000255}.
/FTId=PRO_0000038763.
PEPTIDE 127 148 p2L.
/FTId=PRO_0000272320.
CHAIN 149 367 Capsid protein p26. {ECO:0000255}.
/FTId=PRO_0000038764.
PEPTIDE 368 392 p3.
/FTId=PRO_0000272321.
CHAIN 393 ? Nucleocapsid protein p13. {ECO:0000255}.
/FTId=PRO_0000038765.
CHAIN ? 476 p2. {ECO:0000255}.
/FTId=PRO_0000272322.
ZN_FING 403 420 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 421 438 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
MOTIF 468 471 PTAP/PSAP motif.
SITE 126 127 Cleavage; by viral protease.
{ECO:0000255}.
SITE 148 149 Cleavage; by viral protease.
SITE 367 368 Cleavage; by viral protease.
SITE 392 393 Cleavage; by viral protease.
VARIANT 17 17 P -> L (in strain: Isolate R29-106 and
Isolate R29-Nadin).
VARIANT 67 67 N -> D (in strain: Isolate R29-Nadin).
VARIANT 71 71 R -> K (in strain: Isolate R29-Nadin).
VARIANT 116 117 AD -> TE (in strain: Isolate R29-Nadin).
VARIANT 117 117 D -> E (in strain: Isolate R29-106).
VARIANT 180 180 V -> I (in strain: Isolate R29-Nadin).
VARIANT 416 416 R -> K (in strain: Isolate R29-Nadin).
SEQUENCE 476 AA; 53440 MW; FAA896BD684255FF CRC64;
MKRRELEKKL RKVRVTPQQD KYYTIGNLQW AIRMINLMGI KCVCDEECSA AEVALIITQF
SALDLENSPI RGKEEVAIKN TLKVFWSLLA GYKPESTETA LGYWEAFTYR EREARADKEG
EIKSIYPSLT QNTQNKKQTS NQTNTQSLPA ITTQDGTPRF DPDLMKQLKI WSDATERNGV
DLHAVNILGV ITANLVQEEI KLLLNSTPKW RLDVQLIESK VREKENAHRT WKQHHPEAPK
TDEIIGKGLS SAEQATLISV ECRETFRQWV LQAAMEVAQA KHATPGPINI HQGPKEPYTD
FINRLVAALE GMAAPETTKE YLLQHLSIDH ANEDCQSILR PLGPNTPMEK KLEACRVVGS
QKSKMQFLVA AMKEMGIQSP IPAVLPHTPE AYASQTSGPE DGRRCYGCGK TGHLKRNCKQ
QKCYHCGKPG HQARNCRSKN GKCSSAPYGQ RSQPQNNFHQ SNMSSVTPSA PPLILD


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