PRO_HTL3P
ID PRO_HTL3P Reviewed; 584 AA.
AC Q09SZ9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Gag-Pro polyprotein;
DE AltName: Full=Pr76Gag-Pro;
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-pro;
DE Short=NC';
DE Short=NC-pro;
DE Contains:
DE RecName: Full=Protease;
DE Short=PR;
DE EC=3.4.23.-;
DE Contains:
DE RecName: Full=p1;
DE Contains:
DE RecName: Full=Transframe peptide;
DE Short=TFP;
DE AltName: Full=p8;
DE AltName: Full=pX;
GN Name=gag-pro;
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 -!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of Gag,
CC Gag-Pro and Gag-Pro-Pol polyproteins during or shortly after the
CC release of the virion from the plasma membrane. Cleavages take place as
CC an ordered, step-wise cascade to yield mature proteins. This process is
CC called maturation. Displays maximal activity during the budding process
CC just prior to particle release from the cell. Hydrolyzes host EIF4GI in
CC order to shut off the capped cellular mRNA translation. The resulting
CC inhibition of cellular protein synthesis serves to ensure maximal viral
CC gene expression and to evade host immune response (By similarity).
CC {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-pro]: 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-Pro polyprotein;
CC IsoId=Q09SZ9-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=Q09T00-1; 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 -!- DOMAIN: The capsid protein N-terminus seems to be involved in Gag-Gag
CC interactions. {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. The protease is autoproteolytically
CC processed at its N- and C-termini (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Gag-Pro polyprotein]: Produced by -1 ribosomal
CC frameshifting at the gag-pro genes boundary.
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DR EMBL; DQ462191; ABF18960.1; ALT_SEQ; Genomic_DNA.
DR SMR; Q09SZ9; -.
DR Proteomes; UP000007684; Genome.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR003139; D_retro_matrix.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_N.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR018061; Retropepsins.
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; PF00077; RVP; 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; SSF50630; SSF50630; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Capsid protein;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus;
KW Host gene expression shutoff by virus; Host-virus interaction; Hydrolase;
KW Lipoprotein; Metal-binding; Myristate; Protease; Repeat;
KW Ribosomal frameshifting; Viral nucleoprotein; Virion; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..584
FT /note="Gag-Pro polyprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000260480"
FT CHAIN 2..123
FT /note="Matrix protein p19"
FT /evidence="ECO:0000250"
FT /id="PRO_0000260481"
FT CHAIN 124..337
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000260482"
FT CHAIN 338..430
FT /note="Nucleocapsid protein p15-pro"
FT /evidence="ECO:0000250"
FT /id="PRO_0000260483"
FT CHAIN 431..553
FT /note="Protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000260484"
FT PEPTIDE 554..561
FT /note="p1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000260485"
FT CHAIN 562..584
FT /note="Transframe peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000260486"
FT DOMAIN 457..535
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
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 REGION 564..584
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 ACT_SITE 462
FT /note="For protease activity; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
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 SITE 430..431
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 553..554
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 561..562
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 584 AA; 64519 MW; DB0109FF41AA2C3B 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 VRERKNLLRG
GGLTSPRTIL PLIPLSQQRQ PILHVQVSFS NTSPVGVQAL LDTGADITVL PAYLCPPDSN
LQDTTVLGAG GPSTSKFKIL PRPVHIHLPF RKQPVTLTSC LIDTNDQWTI LGRDALQQCQ
SSLYLADQPS SVLPVQTPKL IGLEHLPPPP EVSQFPLNRS ASRP
