GAG_HTL3P
ID GAG_HTL3P Reviewed; 422 AA.
AC Q09T00;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Gag polyprotein;
DE AltName: Full=Pr53Gag;
DE Contains:
DE RecName: Full=Matrix protein p19;
DE Short=MA;
DE Contains:
DE RecName: Full=Capsid protein p24;
DE Short=CA;
DE Contains:
DE RecName: Full=Nucleocapsid protein p15-gag;
DE Short=NC-gag;
GN Name=gag;
OS Human T-cell leukemia virus 3 (strain Pyl43) (HTLV-3).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX NCBI_TaxID=406769;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16973592; DOI=10.1128/jvi.00799-06;
RA Calattini S., Chevalier S.A., Duprez R., Afonso P., Froment A., Gessain A.,
RA Mahieux R.;
RT "Human T-cell lymphotropic virus type 3: complete nucleotide sequence and
RT characterization of the human tax3 protein.";
RL J. Virol. 80:9876-9888(2006).
CC -!- FUNCTION: Matrix protein p19 targets Gag, Gag-Pro and Gag-Pro-Pol
CC polyproteins to the plasma membrane via a multipartite membrane binding
CC signal, that includes its myristoylated N-terminus. Also mediates
CC nuclear localization of the preintegration complex (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Capsid protein p24 forms the conical core of the virus that
CC encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
CC -!- FUNCTION: Nucleocapsid protein p15 is involved in the packaging and
CC encapsidation of two copies of the genome. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with human TSG101. This interaction is essential for
CC budding and release of viral particles (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p15-gag]: Virion
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
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=Q09T00-1; Sequence=Displayed;
CC Name=Gag-Pro polyprotein;
CC IsoId=Q09SZ9-1; Sequence=External;
CC Name=Gag-Pol polyprotein;
CC IsoId=Q4U0X6-1; Sequence=External;
CC -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC essential for viral particle release. They can occur individually or in
CC close proximity within structural proteins. They interacts with sorting
CC cellular proteins of the multivesicular body (MVB) pathway. Most of
CC these proteins are class E vacuolar protein sorting factors belonging
CC to ESCRT-I, ESCRT-II or ESCRT-III complexes. Matrix protein p19
CC contains two L domains: a PTAP/PSAP motif which interacts with the UEV
CC domain of TSG101, and a PPXY motif which binds to the WW domains of
CC HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages by the viral protease yield mature
CC proteins. The polyprotein is cleaved during and after budding, this
CC process is termed maturation (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC translation.
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DR EMBL; DQ462191; ABF18959.1; -; Genomic_DNA.
DR SMR; Q09T00; -.
DR Proteomes; UP000007684; Genome.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016032; P:viral process; IEA:InterPro.
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 3: Inferred from homology;
KW Capsid protein; Host-virus interaction; Lipoprotein; Metal-binding;
KW Myristate; Phosphoprotein; Repeat; Ribosomal frameshifting;
KW Viral nucleoprotein; Virion; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..123
FT /note="Matrix protein p19"
FT /evidence="ECO:0000250"
FT /id="PRO_0000260469"
FT CHAIN 124..337
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000260470"
FT CHAIN 338..422
FT /note="Nucleocapsid protein p15-gag"
FT /evidence="ECO:0000250"
FT /id="PRO_0000260471"
FT ZN_FING 349..366
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 372..389
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 93..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 98..101
FT /note="PTAP/PSAP motif"
FT MOTIF 109..112
FT /note="PPXY motif"
FT COMPBIAS 95..117
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 123..124
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 337..338
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 422 AA; 46938 MW; CFEA583A47B1D331 CRC64;
MGKTYSSPVN PIPKAPKGLA IHHWLNFLQA AYRLQPGPSE FDFHQLRKFL KLAIKTPVWL
NPINYSVLAR LIPKNYPGRV HEIVAILIQE TPAREAPPSA PPADDPQKPP PYPEHAQVEP
QCLPVLHPHG APATHRPWQM KDLQAIKQEV SSSAPGSPQF MQTVRLAVQQ FDPTAKDLHD
LLQYLCSSLV ASLHHQQLET LIAQAETQGI TGYNPLAGPL RVQANNPNQQ GLRREYQNLW
LSAFSALPGN TKDPTWAAIL QGPEEPFCSF VERLNVALDN GLPEGTPKDP ILRSLAYSNA
NKECQKLLQA RGQTNSPLGE MLRACQTWTP RDKNKILMIQ PKKTPPPNQP CFRCGQAGHW
SRDCKQPRPP PGPCPLCQDP AHWKQDCPQL KADTKGSEDL LLDLPCEASH VRERKNSSGG
ED
