GAG_BIV29
ID GAG_BIV29 Reviewed; 476 AA.
AC P19558; P19559; Q65590;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 23-FEB-2022, entry version 113.
DE RecName: Full=Gag polyprotein;
DE AltName: Full=Pr53Gag;
DE Contains:
DE RecName: Full=Matrix protein p16;
DE Short=MA;
DE Contains:
DE RecName: Full=p2L;
DE Contains:
DE RecName: Full=Capsid protein p26;
DE Short=CA;
DE Contains:
DE RecName: Full=p3;
DE Contains:
DE RecName: Full=Nucleocapsid protein p13;
DE Short=NC;
DE Contains:
DE RecName: Full=p2;
GN Name=gag;
OS Bovine immunodeficiency virus (strain R29) (BIV) (Bovine
OS immunodeficiency-like virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=417296;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate R29-106, and Isolate R29-127;
RX PubMed=2183467; DOI=10.1016/0042-6822(90)90424-p;
RA Garvey K.J., Oberste M.S., Elser J.E., Braun M.J., Gonda M.A.;
RT "Nucleotide sequence and genome organization of biologically active
RT proviruses of the bovine immunodeficiency-like virus.";
RL Virology 175:391-409(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Isolate R29-Nadin;
RA Nadin-Davis S.A., Chang S.C., Roth J.A., Carpenter S.;
RT "Isolation and characterization of cDNAs encoding rev and tat of bovine
RT immunodeficiency-like virus.";
RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP RIBOSOMAL FRAMESHIFT, AND PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RC STRAIN=Isolate R29-127;
RX PubMed=1331499; DOI=10.1128/jvi.66.12.6868-6877.1992;
RA Battles J.K., Hu M.Y., Rasmussen L., Tobin G.J., Gonda M.A.;
RT "Immunological characterization of the gag gene products of bovine
RT immunodeficiency virus.";
RL J. Virol. 66:6868-6877(1992).
RN [4]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=12414761; DOI=10.1128/cdli.9.6.1277-1281.2002;
RA Lu M., Zheng L., Mitchell K., Kapil S., Wood C., Minocha H.;
RT "Unique epitope of bovine immunodeficiency virus gag protein spans the
RT cleavage site between p16(MA) and p2L.";
RL Clin. Diagn. Lab. Immunol. 9:1277-1281(2002).
RN [5]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RC STRAIN=Isolate R29-127;
RX PubMed=14694086; DOI=10.1128/jvi.78.2.551-560.2004;
RA Guo X., Hu J., Whitney J.B., Russell R.S., Liang C.;
RT "Important role for the CA-NC spacer region in the assembly of bovine
RT immunodeficiency virus Gag protein.";
RL J. Virol. 78:551-560(2004).
RN [6]
RP FUNCTION, AND INTERACTION WITH HOST DYNLL1.
RX PubMed=20148896; DOI=10.1111/j.1462-5822.2010.01453.x;
RA Su Y., Qiao W., Guo T., Tan J., Li Z., Chen Y., Li X., Li Y., Zhou J.,
RA Chen Q.;
RT "Microtubule-dependent retrograde transport of bovine immunodeficiency
RT virus.";
RL Cell. Microbiol. 12:1098-1107(2010).
CC -!- FUNCTION: Matrix protein p16 forms the outer shell of the core of the
CC virus, lining the inner surface of the viral membrane. {ECO:0000250}.
CC -!- FUNCTION: Capsid protein p26 forms the conical core of the virus that
CC encapsulates the genomic RNA-nucleocapsid complex. Interaction between
CC incoming particle-associated Gag proteins and host dynein allows
CC intracellular microtubule-dependent virus transport toward the
CC perinuclear region, prior to nucleus translocation and integration into
CC host genome. {ECO:0000269|PubMed:20148896}.
CC -!- FUNCTION: Nucleocapsid protein p13 encapsulates and protects viral
CC dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc
CC fingers (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with host light chain cytoplasmic dynein DYNLL1;
CC this interaction is critical for intracellular microtubule-dependent
CC viral genome transport. {ECO:0000269|PubMed:20148896}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p16]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p26]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p13]: Virion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=This strategy of translation probably allows the virus to
CC modulate the quantity of each viral protein.;
CC Name=Gag polyprotein;
CC IsoId=P19558-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=P19560-1; Sequence=External;
CC -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC essential for viral particle budding. They recruit proteins of the host
CC ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC ESCRT-associated proteins. Gag polyprotein contains one L domain: a
CC PTAP/PSAP motif, which interacts with the UEV domain of TSG101 (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: The sequence shown is that of isolate R29-127.
CC -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC translation.
CC -!- SIMILARITY: Belongs to the bovine lentivirus group gag polyprotein
CC family. {ECO:0000305}.
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DR EMBL; M32690; AAA91270.1; -; Genomic_RNA.
DR EMBL; L04974; AAA42763.1; -; Genomic_DNA.
DR PIR; A34742; FOLJBT.
DR RefSeq; NP_040562.1; NC_001413.1.
DR SMR; P19558; -.
DR GeneID; 1489970; -.
DR KEGG; vg:1489970; -.
DR PRO; PR:P19558; -.
DR GO; GO:0043657; C:host cell; IEA:GOC.
DR GO; GO:0019013; C:viral nucleocapsid; 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:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-KW.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00098; zf-CCHC; 2.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 1: Evidence at protein level;
KW Capsid protein; Cytoplasmic inwards viral transport;
KW Host-virus interaction; Metal-binding;
KW Microtubular inwards viral transport; Repeat; Ribosomal frameshifting;
KW Viral budding; Viral budding via the host ESCRT complexes;
KW Viral matrix protein; Viral nucleoprotein; Viral release from host cell;
KW Virion; Virion maturation; Virus entry into host cell; Zinc; Zinc-finger.
FT CHAIN 1..476
FT /note="Gag polyprotein"
FT /id="PRO_0000272319"
FT CHAIN 1..126
FT /note="Matrix protein p16"
FT /evidence="ECO:0000255"
FT /id="PRO_0000038763"
FT PEPTIDE 127..148
FT /note="p2L"
FT /id="PRO_0000272320"
FT CHAIN 149..367
FT /note="Capsid protein p26"
FT /evidence="ECO:0000255"
FT /id="PRO_0000038764"
FT PEPTIDE 368..392
FT /note="p3"
FT /id="PRO_0000272321"
FT CHAIN 393..?
FT /note="Nucleocapsid protein p13"
FT /evidence="ECO:0000255"
FT /id="PRO_0000038765"
FT CHAIN ?..476
FT /note="p2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000272322"
FT ZN_FING 403..420
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 421..438
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 130..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 468..471
FT /note="PTAP/PSAP motif"
FT COMPBIAS 130..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 126..127
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255"
FT SITE 148..149
FT /note="Cleavage; by viral protease"
FT SITE 367..368
FT /note="Cleavage; by viral protease"
FT SITE 392..393
FT /note="Cleavage; by viral protease"
FT VARIANT 17
FT /note="P -> L (in strain: Isolate R29-106 and Isolate R29-
FT Nadin)"
FT VARIANT 67
FT /note="N -> D (in strain: Isolate R29-Nadin)"
FT VARIANT 71
FT /note="R -> K (in strain: Isolate R29-Nadin)"
FT VARIANT 116..117
FT /note="AD -> TE (in strain: Isolate R29-Nadin)"
FT VARIANT 117
FT /note="D -> E (in strain: Isolate R29-106)"
FT VARIANT 180
FT /note="V -> I (in strain: Isolate R29-Nadin)"
FT VARIANT 416
FT /note="R -> K (in strain: Isolate R29-Nadin)"
SQ 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
