GAG_HTL1C
ID GAG_HTL1C Reviewed; 429 AA.
AC P14076; O56229;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 120.
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 1 (isolate Caribbea HS-35 subtype A) (HTLV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX NCBI_TaxID=11927;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2899128; DOI=10.1099/0022-1317-69-7-1695;
RA Malik K.T.A., Even J., Karpas A.;
RT "Molecular cloning and complete nucleotide sequence of an adult T cell
RT leukaemia virus/human T cell leukaemia virus type I (ATLV/HTLV-I) isolate
RT of Caribbean origin: relationship to other members of the ATLV/HTLV-I
RT subgroup.";
RL J. Gen. Virol. 69:1695-1710(1988).
CC -!- FUNCTION: [Gag polyprotein]: The matrix domain targets Gag, Gag-Pro and
CC 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.
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- FUNCTION: [Nucleocapsid protein p15-gag]: 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:0000250|UniProtKB:P03345}.
CC -!- SUBUNIT: [Gag polyprotein]: Homodimer; the homodimers are part of the
CC 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-gag]: 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 polyprotein;
CC IsoId=P14076-1; Sequence=Displayed;
CC Name=Gag-Pro polyprotein;
CC IsoId=P14074-1; Sequence=External;
CC Name=Gag-Pol polyprotein;
CC IsoId=P14078-1; Sequence=External;
CC -!- DOMAIN: [Gag polyprotein]: Late-budding domains (L domains) are short
CC sequence motifs essential for viral particle release. They can occur
CC individually or in close proximity within structural proteins. They
CC interacts with sorting cellular proteins of the multivesicular body
CC (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 -!- DOMAIN: [Capsid protein p24]: The capsid protein N-terminus seems to be
CC involved in Gag-Gag interactions. {ECO:0000250|UniProtKB:P03345}.
CC -!- DOMAIN: [Nucleocapsid protein p15-gag]: The C-terminus is acidic.
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- PTM: [Gag 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.
CC {ECO:0000250|UniProtKB:P03345}.
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 polyprotein]: Ubiquitinated by host NEDD4.
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- PTM: [Gag polyprotein]: Myristoylated. Myristoylation of the matrix
CC (MA) domain mediates the transport and binding of Gag polyproteins to
CC the host plasma membrane and is required for the assembly of viral
CC particles. {ECO:0000250|UniProtKB:P03345}.
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 polyprotein]: Produced by conventional
CC translation. {ECO:0000250|UniProtKB:P03345}.
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DR EMBL; D13784; BAA02929.1; -; Genomic_DNA.
DR EMBL; AF033817; AAC82579.1; -; Genomic_DNA.
DR PIR; A28136; FOLJCN.
DR RefSeq; NP_057862.1; NC_001436.1.
DR BMRB; P14076; -.
DR SMR; P14076; -.
DR PRIDE; P14076; -.
DR GeneID; 1491934; -.
DR KEGG; vg:1491934; -.
DR Proteomes; UP000001061; Genome.
DR Proteomes; UP000110593; 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; Disulfide bond; Host-virus interaction; Lipoprotein;
KW Metal-binding; Myristate; Phosphoprotein; Reference proteome; Repeat;
KW Ribosomal frameshifting; Ubl conjugation; Viral nucleoprotein; Virion;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255"
FT CHAIN 2..429
FT /note="Gag polyprotein"
FT /id="PRO_0000259772"
FT CHAIN 2..130
FT /note="Matrix protein p19"
FT /id="PRO_0000038814"
FT CHAIN 131..344
FT /note="Capsid protein p24"
FT /id="PRO_0000038815"
FT CHAIN 345..429
FT /note="Nucleocapsid protein p15-gag"
FT /id="PRO_0000038816"
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..142
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 SITE 130..131
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03345"
FT SITE 344..345
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03345"
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"
FT DISULFID 61
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P03345"
SQ SEQUENCE 429 AA; 47514 MW; CFBF686497B738EC CRC64;
MGQIFSRSAS PIPRPPRGLA AHHWLNFLQA AYRLEPGPSS YDFHQLKKFL KIALETPVWI
CPINYSLLAS LLPKGYPGRV NEILHILIQT QAQIPSRPAP PPPSSSTHDP PDSDPQIPPP
YVEPTAPQVL PVMHPHGAPP NHRPWQMKDL QAIKQEVSQA APGSPQFMQT IRLAVQQFDP
TAKDLQDLLQ YLCSSLVASL HHQQLDSLIS EAETRGITGY NPLAGPLRVQ ANNPQQQGLR
REYQQLWLAA FAALPGSAKD PSWASILQGL EEPYHAFVER LNIALDNGLP EGTPKDPILR
SLAYSNANKE CQKLLQARGH TNSPLGDMLR ACQAWTPKDK TKVLVVQPKK PPPNQPCFRC
GKAGHWSRDC TQPRPPPGPC PLCQDPTHWK RDCPRLKPTI PEPEPEEDAL LLDLPADIPH
PKNSIGGEV
