PRO_HTL1A
ID PRO_HTL1A Reviewed; 651 AA.
AC P10274;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
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.- {ECO:0000255|PROSITE-ProRule:PRU00275, ECO:0000269|PubMed:15102858};
DE Contains:
DE RecName: Full=p1;
DE Contains:
DE RecName: Full=Transframe peptide;
DE Short=TFP;
DE AltName: Full=p8;
GN Name=gag-pro; Synonyms=prt;
OS Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX NCBI_TaxID=11926;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6304725; DOI=10.1073/pnas.80.12.3618;
RA Seiki M., Hattori S., Hirayama Y., Yoshida M.C.;
RT "Human adult T-cell leukemia virus: complete nucleotide sequence of the
RT provirus genome integrated in leukemia cell DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:3618-3622(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 395-651.
RX PubMed=3021121; DOI=10.1016/s0006-291x(86)80089-4;
RA Nam S.H., Hatanaka M.;
RT "Identification of a protease gene of human T-cell leukemia virus type I
RT (HTLV-I) and its structural comparison.";
RL Biochem. Biophys. Res. Commun. 139:129-135(1986).
RN [3]
RP PROTEIN SEQUENCE OF 131-155.
RX PubMed=6280175; DOI=10.1073/pnas.79.4.1291;
RA Oroszlan S., Sarngadharan M.G., Copeland T.D., Kalyanaraman V.S.,
RA Gilden R.V., Gallo R.C.;
RT "Primary structure analysis of the major internal protein p24 of human type
RT C T-cell leukemia virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:1291-1294(1982).
RN [4]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=8416368; DOI=10.1128/jvi.67.1.196-203.1993;
RA Nam S.H., Copeland T.D., Hatanaka M., Oroszlan S.;
RT "Characterization of ribosomal frameshifting for expression of pol gene
RT products of human T-cell leukemia virus type I.";
RL J. Virol. 67:196-203(1993).
RN [5]
RP CHARACTERIZATION (PROTEASE), AND PROTEOLYTIC CLEAVAGE (GAG-PRO
RP POLYPROTEIN).
RX PubMed=10037763; DOI=10.1074/jbc.274.10.6660;
RA Louis J.M., Oroszlan S., Toezser J.;
RT "Stabilization from autoproteolysis and kinetic characterization of the
RT human T-cell leukemia virus type 1 proteinase.";
RL J. Biol. Chem. 274:6660-6666(1999).
RN [6]
RP DOMAIN (CAPSID PROTEIN P24), MUTAGENESIS OF GLY-2, AND MYRISTOYLATION AT
RP GLY-2.
RX PubMed=11333909; DOI=10.1128/jvi.75.11.5277-5287.2001;
RA Rayne F., Bouamr F., Lalanne J., Mamoun R.Z.;
RT "The NH2-terminal domain of the human T-cell leukemia virus type 1 capsid
RT protein is involved in particle formation.";
RL J. Virol. 75:5277-5287(2001).
RN [7]
RP PROTEOLYTIC CLEAVAGE (GAG-PRO POLYPROTEIN), AND MUTAGENESIS OF
RP 573-ILE--PRO-575 AND 581-VAL--LEU-584.
RX PubMed=12438640; DOI=10.1128/jvi.76.24.13101-13105.2002;
RA Heidecker G., Hill S., Lloyd P.A., Derse D.;
RT "A novel protease processing site in the transframe protein of human T-cell
RT leukemia virus type 1 PR76(gag-pro) defines the N terminus of RT.";
RL J. Virol. 76:13101-13105(2002).
RN [8]
RP REVIEW.
RX PubMed=12770819; DOI=10.1016/s1074-5521(03)00104-2;
RA Shuker S.B., Mariani V.L., Herger B.E., Dennison K.J.;
RT "Understanding HTLV-I protease.";
RL Chem. Biol. 10:373-380(2003).
RN [9]
RP FUNCTION (PROTEASE).
RX PubMed=14610163; DOI=10.1128/jvi.77.23.12392-12400.2003;
RA Alvarez E., Menendez-Arias L., Carrasco L.;
RT "The eukaryotic translation initiation factor 4GI is cleaved by different
RT retroviral proteases.";
RL J. Virol. 77:12392-12400(2003).
RN [10]
RP FUNCTION (PROTEASE), CATALYTIC ACTIVITY (PROTEASE), MUTAGENESIS OF MET-486;
RP LEU-506; ALA-508; PHE-516; ASN-545; ASN-546 AND TRP-547, AND PROTEOLYTIC
RP CLEAVAGE (GAG-PRO POLYPROTEIN).
RX PubMed=15102858; DOI=10.1074/jbc.m401868200;
RA Kadas J., Weber I.T., Bagossi P., Miklossy G., Boross P., Oroszlan S.,
RA Toezser J.;
RT "Narrow substrate specificity and sensitivity toward ligand-binding site
RT mutations of human T-cell Leukemia virus type 1 protease.";
RL J. Biol. Chem. 279:27148-27157(2004).
RN [11]
RP PROTEOLYTIC CLEAVAGE (GAG-PRO POLYPROTEIN).
RX PubMed=16682197; DOI=10.1016/j.bmcl.2006.04.056;
RA Naka H., Teruya K., Bang J.K., Aimoto S., Tatsumi T., Konno H., Nosaka K.,
RA Akaji K.;
RT "Evaluations of substrate specificity and inhibition at PR/p3 cleavage site
RT of HTLV-1 protease.";
RL Bioorg. Med. Chem. Lett. 16:3761-3764(2006).
RN [12]
RP FUNCTION (NUCLEOCAPSID PROTEIN P15-PRO).
RX PubMed=25686502; DOI=10.1016/j.bbrc.2015.02.025;
RA Qualley D.F., Sokolove V.L., Ross J.L.;
RT "Bovine leukemia virus nucleocapsid protein is an efficient nucleic acid
RT chaperone.";
RL Biochem. Biophys. Res. Commun. 458:687-692(2015).
RN [13]
RP STRUCTURE BY NMR OF 146-344.
RX PubMed=10427751; DOI=10.1023/a:1008307507462;
RA Khorasanizadeh S., Campos-Olivas R., Clark C.A., Summers M.F.;
RT "Sequence-specific 1H, 13C and 15N chemical shift assignment and secondary
RT structure of the HTLV-I capsid protein.";
RL J. Biomol. NMR 14:199-200(1999).
CC -!- FUNCTION: [Gag-Pro polyprotein]: The matrix domain targets Gag, Gag-Pro
CC and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite
CC membrane binding signal, that includes its myristoylated N-terminus.
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- FUNCTION: [Matrix protein p19]: Matrix protein.
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- FUNCTION: [Capsid protein p24]: Forms the spherical core of the virus
CC that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000305}.
CC -!- FUNCTION: [Nucleocapsid protein p15-pro]: Binds strongly to viral
CC nucleic acids and promote their aggregation. Also destabilizes the
CC nucleic acids duplexes via highly structured zinc-binding motifs.
CC {ECO:0000269|PubMed:25686502}.
CC -!- FUNCTION: [Protease]: The aspartyl protease mediates proteolytic
CC cleavages of Gag and Gag-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. Cleaves the translation
CC initiation factor eIF4G leading to the inhibition of host cap-dependent
CC translation. {ECO:0000255|PROSITE-ProRule:PRU00275,
CC ECO:0000269|PubMed:14610163, ECO:0000269|PubMed:15102858}.
CC -!- SUBUNIT: [Gag-Pro polyprotein]: Homodimer; the homodimers are part of
CC the immature particles. Interacts with human TSG101 and NEDD4; these
CC interactions are essential for budding and release of viral particles.
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- SUBUNIT: [Matrix protein p19]: Homodimer; further assembles as
CC homohexamers. {ECO:0000250|UniProtKB:P03345}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p19]: Virion
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p15-pro]: Virion
CC {ECO:0000250|UniProtKB:P03345}.
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. {ECO:0000305};
CC Name=Gag-Pro polyprotein;
CC IsoId=P10274-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P03345-1; Sequence=External;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P03362-1; Sequence=External;
CC -!- DOMAIN: [Capsid protein p24]: The capsid protein N-terminus seems to be
CC involved in Gag-Gag interactions. {ECO:0000269|PubMed:11333909}.
CC -!- DOMAIN: [Gag-Pro polyprotein]: Late-budding domains (L domains) are
CC short sequence motifs essential for viral particle release. They can
CC occur individually or in close proximity within structural proteins.
CC They interacts with sorting cellular proteins of the multivesicular
CC body (MVB) pathway. Most of these proteins are class E vacuolar protein
CC sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes.
CC Matrix protein p19 contains two L domains: a PTAP/PSAP motif which
CC interacts with the UEV domain of TSG101, and a PPXY motif which binds
CC to the WW domains of the ubiquitin ligase NEDD4.
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages by the viral
CC protease yield mature proteins. The polyprotein is cleaved during and
CC after budding, this process is termed maturation. The protease is
CC autoproteolytically processed at its N- and C-termini.
CC {ECO:0000269|PubMed:10037763, ECO:0000269|PubMed:12438640,
CC ECO:0000269|PubMed:15102858, ECO:0000269|PubMed:16682197}.
CC -!- PTM: [Matrix protein p19]: Phosphorylation of the matrix protein p19 by
CC MAPK1 seems to play a role in budding. {ECO:0000250|UniProtKB:P03345}.
CC -!- PTM: [Gag-Pro polyprotein]: Myristoylated (PubMed:11333909).
CC Myristoylation of the matrix (MA) domain mediates the transport and
CC binding of Gag polyproteins to the host plasma membrane and is required
CC for the assembly of viral particles (By similarity).
CC {ECO:0000250|UniProtKB:P03345, ECO:0000269|PubMed:11333909}.
CC -!- MISCELLANEOUS: HTLV-1 lineages are divided in four clades, A
CC (Cosmopolitan), B (Central African group), C (Melanesian group) and D
CC (New Central African group). {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Gag-Pro polyprotein]: Produced by -1 ribosomal
CC frameshifting at the gag-pro genes boundary.
CC {ECO:0000269|PubMed:8416368}.
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DR EMBL; J02029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M13810; AAA46206.1; ALT_SEQ; Genomic_RNA.
DR PIR; A24817; PNLJH1.
DR PDB; 6W6Q; X-ray; 2.10 A; A/B=450-565.
DR PDB; 6W6R; X-ray; 2.05 A; A/B=450-565.
DR PDB; 6W6S; X-ray; 2.29 A; A/B=450-565.
DR PDBsum; 6W6Q; -.
DR PDBsum; 6W6R; -.
DR PDBsum; 6W6S; -.
DR BMRB; P10274; -.
DR SMR; P10274; -.
DR BindingDB; P10274; -.
DR ChEMBL; CHEMBL3346; -.
DR MEROPS; A02.012; -.
DR iPTMnet; P10274; -.
DR Proteomes; UP000007683; Genome.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
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 GO; GO:0039604; P:suppression by virus of host translation; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Capsid protein; Direct protein sequencing;
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; Phosphoprotein; Protease;
KW Reference proteome; Repeat; Ribosomal frameshifting; Viral nucleoprotein;
KW Virion; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255"
FT CHAIN 2..651
FT /note="Gag-Pro polyprotein"
FT /id="PRO_0000259788"
FT CHAIN 2..130
FT /note="Matrix protein p19"
FT /id="PRO_0000259789"
FT CHAIN 131..344
FT /note="Capsid protein p24"
FT /id="PRO_0000259790"
FT CHAIN 345..449
FT /note="Nucleocapsid protein p15-pro"
FT /id="PRO_0000259791"
FT CHAIN 450..574
FT /note="Protease"
FT /id="PRO_0000259792"
FT PEPTIDE 575..582
FT /note="p1"
FT /id="PRO_0000259793"
FT CHAIN 583..651
FT /note="Transframe peptide"
FT /id="PRO_0000259794"
FT DOMAIN 476..554
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT ZN_FING 355..372
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 378..395
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 93..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 118..121
FT /note="PPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P03345"
FT MOTIF 124..127
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000250|UniProtKB:P03345"
FT COMPBIAS 95..126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 481
FT /note="For protease activity; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT SITE 130..131
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:10037763"
FT SITE 344..345
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:10037763"
FT SITE 449..450
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:10037763"
FT SITE 574..575
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:10037763,
FT ECO:0000269|PubMed:16682197"
FT SITE 582..583
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000303|PubMed:15102858"
FT MOD_RES 105
FT /note="Phosphoserine; by host MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P03345"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:11333909"
FT VARIANT 440..441
FT /note="LP -> FL"
FT VARIANT 569
FT /note="R -> G"
FT VARIANT 592
FT /note="E -> Q"
FT VARIANT 626
FT /note="G -> E"
FT MUTAGEN 2
FT /note="G->A: Complete loss of myristoylation the
FT polyprotein. The concomitent loss of binding to the host
FT cell membrane impairs the formation of viral particles."
FT /evidence="ECO:0000269|PubMed:11333909"
FT MUTAGEN 486
FT /note="M->A,D,N: Complete loss of protease activity."
FT /evidence="ECO:0000269|PubMed:15102858"
FT MUTAGEN 486
FT /note="M->I: Almost no effect on protease activity."
FT /evidence="ECO:0000269|PubMed:15102858"
FT MUTAGEN 486
FT /note="M->V: Decrease in protease activity."
FT /evidence="ECO:0000269|PubMed:15102858"
FT MUTAGEN 506
FT /note="L->G: Complete loss of protease activity."
FT /evidence="ECO:0000269|PubMed:15102858"
FT MUTAGEN 508
FT /note="A->I: Decrease in protease activity."
FT /evidence="ECO:0000269|PubMed:15102858"
FT MUTAGEN 516
FT /note="F->Q: Complete loss of protease activity."
FT /evidence="ECO:0000269|PubMed:15102858"
FT MUTAGEN 545
FT /note="N->T: Almost complete loss of protease activity."
FT /evidence="ECO:0000269|PubMed:15102858"
FT MUTAGEN 546
FT /note="N->P: Almost complete loss of protease activity."
FT /evidence="ECO:0000269|PubMed:15102858"
FT MUTAGEN 547
FT /note="W->V: Almost complete loss of protease activity."
FT /evidence="ECO:0000269|PubMed:15102858"
FT MUTAGEN 573..575
FT /note="ILP->TAG: Complete loss of cleavage between protease
FT and p1."
FT /evidence="ECO:0000269|PubMed:12438640"
FT MUTAGEN 581..584
FT /note="VLGL->GAGA: Complete loss of cleavage between p1 and
FT the transframe peptide."
FT /evidence="ECO:0000269|PubMed:12438640"
FT CONFLICT 547
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:6W6R"
FT STRAND 461..467
FT /evidence="ECO:0007829|PDB:6W6R"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:6W6R"
FT STRAND 474..480
FT /evidence="ECO:0007829|PDB:6W6R"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:6W6R"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:6W6R"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:6W6R"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:6W6R"
FT STRAND 510..521
FT /evidence="ECO:0007829|PDB:6W6R"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:6W6R"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:6W6R"
FT STRAND 540..545
FT /evidence="ECO:0007829|PDB:6W6R"
FT HELIX 552..557
FT /evidence="ECO:0007829|PDB:6W6R"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:6W6R"
SQ SEQUENCE 651 AA; 71558 MW; 8BDE487979495D59 CRC64;
MGQIFSRSAS PIPRPPRGLA AHHWLNFLQA AYRLEPGPSS YDFHQLKKFL KIALETPARI
CPINYSLLAS LLPKGYPGRV NEILHILIQT QAQIPSRPAP PPPSSPTHDP PDSDPQIPPP
YVEPTAPQVL PVMHPHGAPP NHRPWQMKDL QAIKQEVSQA APGSPQFMQT IRLAVQQFDP
TAKDLQDLLQ YLCSSLVASL HHQQLDSLIS EAETRGITGY NPLAGPLRVQ ANNPQQQGLR
REYQQLWLAA FAALPGSAKD PSWASILQGL EEPYHAFVER LNIALDNGLP EGTPKDPILR
SLAYSNANKE CQKLLQARGH TNSPLGDMLR ACQTWTPKDK TKVLVVQPKK PPPNQPCFRC
GKAGHWSRDC TQPRPPPGPC PLCQDPTHWK RDCPRLKPTI PEPEPEEDAL LLDLPADIPH
PKNLHRGGGL TSPPTLQQVL PNQDPASILP VIPLDPARRP VIKAQVDTQT SHPKTIEALL
DTGADMTVLP IALFSSNTPL KNTSVLGAGG QTQDHFKLTS LPVLIRLPFR TTPIVLTSCL
VDTKNNWAII GRDALQQCQG VLYLPEAKRP PVILPIQAPA VLGLEHLPRP PEISQFPLNQ
NASRPCNTWS GRPWRQAISN PTPGQGITQY SQLKRPMEPG DSSTTCGPLT L
