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P14077

- GAG_HTL1M

UniProt

P14077 - GAG_HTL1M

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Protein

Gag polyprotein

Gene

gag

Organism
Human T-cell leukemia virus 1 (strain Japan MT-2 subtype A) (HTLV-1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Matrix protein p19 targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex (By similarity).By similarity
Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex.By similarity
Nucleocapsid protein p15 is involved in the packaging and encapsidation of two copies of the genome.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei130 – 1312Cleavage; by viral proteaseBy similarity
Sitei344 – 3452Cleavage; by viral proteaseBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri355 – 37218CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri378 – 39518CCHC-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. nucleic acid binding Source: InterPro
  2. structural molecule activity Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

Metal-binding, Viral nucleoprotein, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Gag polyprotein
Alternative name(s):
Pr53Gag
Cleaved into the following 3 chains:
Matrix protein p19
Short name:
MA
Capsid protein p24
Short name:
CA
Gene namesi
Name:gag
OrganismiHuman T-cell leukemia virus 1 (strain Japan MT-2 subtype A) (HTLV-1)
Taxonomic identifieri11928 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeDeltaretrovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

GO - Cellular componenti

  1. viral nucleocapsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by host
Chaini2 – 429428Gag polyproteinPRO_0000259773Add
BLAST
Chaini2 – 130129Matrix protein p19By similarityPRO_0000038817Add
BLAST
Chaini131 – 344214Capsid protein p24By similarityPRO_0000038818Add
BLAST
Chaini345 – 42985Nucleocapsid protein p15-gagBy similarityPRO_0000038819Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by host1 Publication
Modified residuei105 – 1051Phosphoserine; by host MAPK1By similarity

Post-translational modificationi

Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation (By similarity).By similarity
Phosphorylation of the matrix protein p19 by MAPK1 seems to play a role in budding.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

Interacts with human TSG101 and NEDD4. These interactions are essential for budding and release of viral particles (By similarity).By similarity

Structurei

Secondary structure

1
429
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi136 – 1383Combined sources
Helixi148 – 15912Combined sources
Beta strandi160 – 1634Combined sources
Helixi166 – 17712Combined sources
Helixi182 – 1909Combined sources
Helixi195 – 21622Combined sources
Beta strandi217 – 2193Combined sources
Helixi227 – 2315Combined sources
Helixi238 – 25215Combined sources
Turni254 – 2574Combined sources
Turni261 – 2633Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G03NMR-A131-264[»]
ProteinModelPortaliP14077.
SMRiP14077. Positions 1-344.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14077.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi118 – 1214PPXY motif
Motifi124 – 1274PTAP/PSAP motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi95 – 14450Pro-richAdd
BLAST

Domaini

Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. Matrix protein p19 contains two L domains: a PTAP/PSAP motif which interacts with the UEV domain of TSG101, and a PPXY motif which binds to the WW domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases, like NEDD4 (By similarity).By similarity
The capsid protein N-terminus seems to be involved in Gag-Gag interactions.By similarity

Sequence similaritiesi

Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri355 – 37218CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri378 – 39518CCHC-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Family and domain databases

Gene3Di1.10.1200.30. 1 hit.
1.10.185.10. 1 hit.
1.10.375.10. 1 hit.
4.10.60.10. 1 hit.
InterProiIPR003139. D_retro_matrix_N.
IPR000721. Gag_p24.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF02228. Gag_p19. 1 hit.
PF00607. Gag_p24. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
SMARTiSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50158. ZF_CCHC. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by ribosomal frameshifting. Align

Note: This strategy of translation probably allows the virus to modulate the quantity of each viral protein.

Isoform Gag polyprotein (identifier: P14077-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGQIFSRSAS PIPRPPRGLA AHHWLNFLQA AYRLEPGPSS YDFHQLKKFL
60 70 80 90 100
KIALETPVWI CPINYSLLAS LLPKGYPGRV NEILHILIQT QAQIPSRPAP
110 120 130 140 150
PPPSSPTHDP PDSDPQIPPP YVEPTAPQVL PVMHPHGAPP NHRPWQMKDL
160 170 180 190 200
QAIKQEVSQA APGSPQFMQT IRLAVQQFDP TAKDLQDLLQ YLCSSLVASL
210 220 230 240 250
HHQQLDSLIS EAETRGITSY NPLAGPLRVQ ANNPQQQGLR REYQQLWLAA
260 270 280 290 300
FAALPGSAKD PSWASILQGL EEPYHAFVER LNIALDNGLP EGTPKDPILR
310 320 330 340 350
SLAYSNANKE CQKLLQARGH TNSPLGDMLR ACQTWTPKDK TKVLVVQPKK
360 370 380 390 400
PPPNQPCFRC GKAGHWSRDC TQPRPPPGPC PLCQDPTHWK RDCPRLKPTI
410 420
PEPEPEEDAL LLDLPADIPH PKNSIGGEV

Note: Produced by conventional translation.

Length:429
Mass (Da):47,585
Last modified:January 23, 2007 - v3
Checksum:iEF5201C934EF0291
GO
Isoform Gag-Pro polyprotein (identifier: P14077-2)

Sequence is not available

Note: Produced by -1 ribosomal frameshifting at the gag-pro genes boundary.

Length:
Mass (Da):
Isoform Gag-Pol polyprotein (identifier: P14077-3)

Sequence is not available

Note: Produced by -1 ribosomal frameshifting at the gag-pol genes boundary.

Length:
Mass (Da):

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15951 Genomic RNA. Translation: CAA34075.1.
PIRiS06073.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15951 Genomic RNA. Translation: CAA34075.1 .
PIRi S06073.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G03 NMR - A 131-264 [» ]
ProteinModelPortali P14077.
SMRi P14077. Positions 1-344.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P14077.

Family and domain databases

Gene3Di 1.10.1200.30. 1 hit.
1.10.185.10. 1 hit.
1.10.375.10. 1 hit.
4.10.60.10. 1 hit.
InterProi IPR003139. D_retro_matrix_N.
IPR000721. Gag_p24.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR001878. Znf_CCHC.
[Graphical view ]
Pfami PF02228. Gag_p19. 1 hit.
PF00607. Gag_p24. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view ]
SMARTi SM00343. ZnF_C2HC. 2 hits.
[Graphical view ]
SUPFAMi SSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEi PS50158. ZF_CCHC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of the core (gag) gene from HTLV-1 isolate MT-2."
    Gray G.S., Bartman T., White M.
    Nucleic Acids Res. 17:7998-7998(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Antibodies to an NH2-terminal myristoyl glycine moiety can detect NH2-terminal myristoylated proteins in the retrovirus-infected cells."
    Shoji S., Tashiro A., Furuishi K., Takenaka O., Kida Y., Horiuchi S., Funakoshi T., Kubota Y.
    Biochem. Biophys. Res. Commun. 162:724-732(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2.
  3. "Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein."
    Cornilescu C.C., Bouamr F., Yao X., Carter C., Tjandra N.
    J. Mol. Biol. 306:783-797(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 131-264.

Entry informationi

Entry nameiGAG_HTL1M
AccessioniPrimary (citable) accession number: P14077
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 101 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

HTLV-1 lineages are divided in four clades, A (Cosmopolitan), B (Central African group), C (Melanesian group) and D (New Central African group).

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3