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Protein Tat

 A0A1L7E4A9_9HIV1        Unreviewed;        99 AA.
A0A1L7E4A9;
15-MAR-2017, integrated into UniProtKB/TrEMBL.
15-MAR-2017, sequence version 1.
31-JAN-2018, entry version 7.
RecName: Full=Protein Tat {ECO:0000256|HAMAP-Rule:MF_04079, ECO:0000256|RuleBase:RU003311, ECO:0000256|SAAS:SAAS00396010};
AltName: Full=Transactivating regulatory protein {ECO:0000256|HAMAP-Rule:MF_04079};
Name=tat {ECO:0000256|HAMAP-Rule:MF_04079,
ECO:0000313|EMBL:APU07403.1};
Human immunodeficiency virus 1.
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Primate lentivirus group.
NCBI_TaxID=11676 {ECO:0000313|EMBL:APU07403.1};
NCBI_TaxID=9606; Homo sapiens (Human).
[1] {ECO:0000313|EMBL:APU07403.1}
NUCLEOTIDE SEQUENCE.
STRAIN=CH427.PL.011608.A2.1 {ECO:0000313|EMBL:APU04154.1},
CH427.PL.011608.A2.10 {ECO:0000313|EMBL:APU04163.1},
CH427.PL.011608.A2.2 {ECO:0000313|EMBL:APU04172.1},
CH427.PL.011608.A2.3 {ECO:0000313|EMBL:APU04181.1},
CH427.PL.011608.A2.4 {ECO:0000313|EMBL:APU04190.1},
CH427.PL.011608.A2.5 {ECO:0000313|EMBL:APU04199.1},
CH427.PL.011608.A2.6 {ECO:0000313|EMBL:APU04208.1},
CH427.PL.011608.A2.7 {ECO:0000313|EMBL:APU04217.1},
CH427.PL.011608.A2.8 {ECO:0000313|EMBL:APU04226.1},
CH427.PL.011608.A2.9 {ECO:0000313|EMBL:APU04235.1},
CH427.PL.011608.BE.1 {ECO:0000313|EMBL:APU04244.1},
CH427.PL.011608.UT.1 {ECO:0000313|EMBL:APU04253.1},
CH427.PL.011608.UT.10 {ECO:0000313|EMBL:APU04262.1},
CH427.PL.011608.UT.2 {ECO:0000313|EMBL:APU04271.1},
CH427.PL.011608.UT.3 {ECO:0000313|EMBL:APU04280.1},
CH427.PL.011608.UT.4 {ECO:0000313|EMBL:APU04289.1},
CH427.PL.011608.UT.5 {ECO:0000313|EMBL:APU04298.1},
CH427.PL.011608.UT.6 {ECO:0000313|EMBL:APU04306.1},
CH427.PL.011608.UT.7 {ECO:0000313|EMBL:APU04315.1},
CH427.PL.011608.UT.8 {ECO:0000313|EMBL:APU04324.1},
CH427.PL.011608.UT.9 {ECO:0000313|EMBL:APU04333.1},
CH427_SGA.600.1 {ECO:0000313|EMBL:APU07262.1},
CH427_SGA.600.11 {ECO:0000313|EMBL:APU07277.1},
CH427_SGA.600.12 {ECO:0000313|EMBL:APU07285.1},
CH427_SGA.600.13 {ECO:0000313|EMBL:APU07292.1},
CH427_SGA.600.14 {ECO:0000313|EMBL:APU07300.1},
CH427_SGA.600.15 {ECO:0000313|EMBL:APU07308.1},
CH427_SGA.600.16 {ECO:0000313|EMBL:APU07316.1},
CH427_SGA.600.18 {ECO:0000313|EMBL:APU07324.1},
CH427_SGA.600.19 {ECO:0000313|EMBL:APU07332.1},
CH427_SGA.600.2 {ECO:0000313|EMBL:APU07340.1},
CH427_SGA.600.20 {ECO:0000313|EMBL:APU07348.1},
CH427_SGA.600.21 {ECO:0000313|EMBL:APU07356.1},
CH427_SGA.600.22 {ECO:0000313|EMBL:APU07363.1},
CH427_SGA.600.24 {ECO:0000313|EMBL:APU07371.1},
CH427_SGA.600.25 {ECO:0000313|EMBL:APU07379.1},
CH427_SGA.600.26 {ECO:0000313|EMBL:APU07387.1},
CH427_SGA.600.27 {ECO:0000313|EMBL:APU07395.1},
CH427_SGA.600.29 {ECO:0000313|EMBL:APU07403.1},
CH427_SGA.600.3 {ECO:0000313|EMBL:APU07410.1},
CH427_SGA.600.30 {ECO:0000313|EMBL:APU07418.1},
CH427_SGA.600.31 {ECO:0000313|EMBL:APU07426.1},
CH427_SGA.600.32 {ECO:0000313|EMBL:APU07434.1},
CH427_SGA.600.33 {ECO:0000313|EMBL:APU07442.1},
CH427_SGA.600.35 {ECO:0000313|EMBL:APU07450.1},
CH427_SGA.600.36 {ECO:0000313|EMBL:APU07458.1},
CH427_SGA.600.37 {ECO:0000313|EMBL:APU07466.1},
CH427_SGA.600.39 {ECO:0000313|EMBL:APU07473.1},
CH427_SGA.600.4 {ECO:0000313|EMBL:APU07481.1},
CH427_SGA.600.6 {ECO:0000313|EMBL:APU07489.1},
CH427_SGA.600.7 {ECO:0000313|EMBL:APU07497.1},
CH427_SGA.600.8 {ECO:0000313|EMBL:APU07505.1},
CH427_SGA.600.9 {ECO:0000313|EMBL:APU07513.1},
CH492.CV.020608.UT.3 {ECO:0000313|EMBL:APU04504.1},
CH492.CV.020608.UT.9 {ECO:0000313|EMBL:APU04558.1},
CH492.PL.031108.A2.13 {ECO:0000313|EMBL:APU04603.1},
CH492.PL.031108.A2.14 {ECO:0000313|EMBL:APU04612.1},
CH492.PL.031108.A2.15 {ECO:0000313|EMBL:APU04621.1},
CH492.PL.031108.A2.16 {ECO:0000313|EMBL:APU04630.1},
CH492.PL.031108.BE.14 {ECO:0000313|EMBL:APU04782.1},
CH492.PL.031108.BE.4 {ECO:0000313|EMBL:APU04809.1},
CH492.PL.031108.BE.5 {ECO:0000313|EMBL:APU04818.1},
CH492.PL.031108.UT.3 {ECO:0000313|EMBL:APU04917.1},
CH492_SGA.1H1 {ECO:0000313|EMBL:APU07671.1},
CH492_SGA.1H8 {ECO:0000313|EMBL:APU07694.1},
CH492_SGA.2B7 {ECO:0000313|EMBL:APU07710.1},
CH492_SGA.2B8 {ECO:0000313|EMBL:APU07718.1},
CH492_SGA.2F5 {ECO:0000313|EMBL:APU07758.1}, and
CH492_SGA.2G12 {ECO:0000313|EMBL:APU07773.1};
PubMed=28069935;
Iyer S.S., Bibollet-Ruche F., Sherrill-Mix S., Learn G.H.,
Plenderleith L., Smith A.G., Barbian H.J., Russell R.M., Gondim M.V.,
Bahari C.Y., Shaw C.M., Li Y., Decker T., Haynes B.F., Shaw G.M.,
Sharp P.M., Borrow P., Hahn B.H.;
"Resistance to type 1 interferons is a major determinant of HIV-1
transmission fitness.";
Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2017).
-!- FUNCTION: Extracellular circulating Tat can be endocytosed by
surrounding uninfected cells via the binding to several surface
receptors such as CD26, CXCR4, heparan sulfate proteoglycans
(HSPG) or LDLR. Neurons are rarely infected, but they internalize
Tat via their LDLR. Through its interaction with nuclear HATs, Tat
is potentially able to control the acetylation-dependent cellular
gene expression. Modulates the expression of many cellular genes
involved in cell survival, proliferation or in coding for
cytokines or cytokine receptors. Tat plays a role in T-cell and
neurons apoptosis. Tat induced neurotoxicity and apoptosis
probably contribute to neuroAIDS. Circulating Tat also acts as a
chemokine-like and/or growth factor-like molecule that binds to
specific receptors on the surface of the cells, affecting many
cellular pathways. In the vascular system, Tat binds to
ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of
endothelial cells and competes with bFGF for heparin-binding
sites, leading to an excess of soluble bFGF. {ECO:0000256|HAMAP-
Rule:MF_04079}.
-!- SUBUNIT: Interacts with host CCNT1. Associates with the P-TEFb
complex composed at least of Tat, P-TEFb (CDK9 and CCNT1), TAR
RNA, RNA Pol II. Recruits the HATs CREBBP, TAF1/TFIID, EP300, PCAF
and GCN5L2. Interacts with host KAT5/Tip60; this interaction
targets the latter to degradation. Interacts with the host
deacetylase SIRT1. Interacts with host capping enzyme RNGTT; this
interaction stimulates RNGTT. Binds to host KDR, and to the host
integrins ITGAV/ITGB3 and ITGA5/ITGB1. Interacts with host
KPNB1/importin beta-1 without previous binding to KPNA1/importin
alpha-1. Interacts with EIF2AK2. Interacts with host nucleosome
assembly protein NAP1L1; this interaction may be required for the
transport of Tat within the nucleus, since the two proteins
interact at the nuclear rim. Interacts with host C1QBP/SF2P32;
this interaction involves lysine-acetylated Tat. Interacts with
the host chemokine receptors CCR2, CCR3 and CXCR4. Interacts with
host DPP4/CD26; this interaction may trigger an anti-proliferative
effect. Interacts with host LDLR. Interacts with the host
extracellular matrix metalloproteinase MMP1. Interacts with host
PRMT6; this interaction mediates Tat's methylation. Interacts
with, and is ubiquitinated by MDM2/Hdm2. Interacts with host PSMC3
and HTATIP2. Interacts with STAB1; this interaction may overcome
SATB1-mediated repression of IL2 and IL2RA (interleukin) in T
cells by binding to the same domain than HDAC1. Interacts (when
acetylated) with human CDK13, thereby increasing HIV-1 mRNA
splicing and promoting the production of the doubly spliced HIV-1
protein Nef.Interacts with host TBP; this interaction modulates
the activity of transcriptional pre-initiation complex. Interacts
with host RELA. {ECO:0000256|HAMAP-Rule:MF_04079}.
-!- SUBCELLULAR LOCATION: Host nucleus, host nucleolus
{ECO:0000256|HAMAP-Rule:MF_04079}. Host cytoplasm
{ECO:0000256|HAMAP-Rule:MF_04079}. Secreted {ECO:0000256|HAMAP-
Rule:MF_04079}. Note=Probably localizes to both nuclear and
nucleolar compartments. Nuclear localization is mediated through
the interaction of the nuclear localization signal with importin
KPNB1. Secretion occurs through a Golgi-independent pathway. Tat
is released from infected cells to the extracellular space where
it remains associated to the cell membrane, or is secreted into
the cerebrospinal fluid and sera. Extracellular Tat can be
endocytosed by surrounding uninfected cells via binding to several
receptors depending on the cell type. {ECO:0000256|HAMAP-
Rule:MF_04079}.
-!- DOMAIN: The Arg-rich RNA-binding region binds the TAR RNA. This
region also mediates the nuclear localization through direct
binding to KPNB1 and is involved in Tat's transfer across cell
membranes (protein transduction). The same region is required for
the interaction with EP300, PCAF, EIF2AK2 and KDR.
{ECO:0000256|HAMAP-Rule:MF_04079}.
-!- DOMAIN: The Cys-rich region may bind 2 zinc ions. This region is
involved in binding to KAT5. {ECO:0000256|HAMAP-Rule:MF_04079}.
-!- DOMAIN: The cell attachment site mediates the interaction with
ITGAV/ITGB3 and ITGA5/ITGB1 integrins, leading to vascular cell
migration and invasion. This interaction also provides endothelial
cells with the adhesion signal they require to grow in response to
mitogens. {ECO:0000256|HAMAP-Rule:MF_04079}.
-!- DOMAIN: The transactivation domain mediates the interaction with
CCNT1, GCN5L2, and MDM2. {ECO:0000256|HAMAP-Rule:MF_04079}.
-!- PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates
the transactivation activity of Tat. EP300-mediated acetylation of
Lys-50 promotes dissociation of Tat from the TAR RNA through the
competitive binding to PCAF's bromodomain. In addition, the non-
acetylated Tat's N-terminus can also interact with PCAF. PCAF-
mediated acetylation of Lys-28 enhances Tat's binding to CCNT1.
Lys-50 is deacetylated by SIRT1. {ECO:0000256|HAMAP-
Rule:MF_04079}.
-!- PTM: Asymmetrical arginine methylation by host PRMT6 seems to
diminish the transactivation capacity of Tat and affects the
interaction with host CCNT1. {ECO:0000256|HAMAP-Rule:MF_04079}.
-!- PTM: Phosphorylated by EIF2AK2 on serine and threonine residues
adjacent to the basic region important for TAR RNA binding and
function. Phosphorylation of Tat by EIF2AK2 is dependent on the
prior activation of EIF2AK2 by dsRNA. {ECO:0000256|HAMAP-
Rule:MF_04079}.
-!- PTM: Polyubiquitination by host MDM2 does not target Tat to
degradation, but activates its transactivation function and
fosters interaction with CCNT1 and TAR RNA. {ECO:0000256|HAMAP-
Rule:MF_04079}.
-!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M
(for Major), O (for Outlier), and N (for New, or Non-M, Non-O).
The vast majority of strains found worldwide belong to the group
M. Group O seems to be endemic to and largely confined to Cameroon
and neighboring countries in West Central Africa, where these
viruses represent a small minority of HIV-1 strains. The group N
is represented by a limited number of isolates from Cameroonian
persons. The group M is further subdivided in 9 clades or subtypes
(A to D, F to H, J and K). {ECO:0000256|HAMAP-Rule:MF_04079}.
-!- SIMILARITY: Belongs to the lentiviruses Tat family.
{ECO:0000256|HAMAP-Rule:MF_04079, ECO:0000256|RuleBase:RU003311,
ECO:0000256|SAAS:SAAS00581731}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04079}.
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EMBL; KY112197; APU04154.1; -; Genomic_RNA.
EMBL; KY112198; APU04163.1; -; Genomic_RNA.
EMBL; KY112199; APU04172.1; -; Genomic_RNA.
EMBL; KY112200; APU04181.1; -; Genomic_RNA.
EMBL; KY112201; APU04190.1; -; Genomic_RNA.
EMBL; KY112202; APU04199.1; -; Genomic_RNA.
EMBL; KY112203; APU04208.1; -; Genomic_RNA.
EMBL; KY112204; APU04217.1; -; Genomic_RNA.
EMBL; KY112205; APU04226.1; -; Genomic_RNA.
EMBL; KY112206; APU04235.1; -; Genomic_RNA.
EMBL; KY112207; APU04244.1; -; Genomic_RNA.
EMBL; KY112208; APU04253.1; -; Genomic_RNA.
EMBL; KY112209; APU04262.1; -; Genomic_RNA.
EMBL; KY112210; APU04271.1; -; Genomic_RNA.
EMBL; KY112211; APU04280.1; -; Genomic_RNA.
EMBL; KY112212; APU04289.1; -; Genomic_RNA.
EMBL; KY112213; APU04298.1; -; Genomic_RNA.
EMBL; KY112214; APU04306.1; -; Genomic_RNA.
EMBL; KY112215; APU04315.1; -; Genomic_RNA.
EMBL; KY112216; APU04324.1; -; Genomic_RNA.
EMBL; KY112217; APU04333.1; -; Genomic_RNA.
EMBL; KY112269; APU04504.1; -; Genomic_RNA.
EMBL; KY112275; APU04558.1; -; Genomic_RNA.
EMBL; KY112280; APU04603.1; -; Genomic_RNA.
EMBL; KY112281; APU04612.1; -; Genomic_RNA.
EMBL; KY112282; APU04621.1; -; Genomic_RNA.
EMBL; KY112283; APU04630.1; -; Genomic_RNA.
EMBL; KY112300; APU04782.1; -; Genomic_RNA.
EMBL; KY112303; APU04809.1; -; Genomic_RNA.
EMBL; KY112304; APU04818.1; -; Genomic_RNA.
EMBL; KY112315; APU04917.1; -; Genomic_RNA.
EMBL; KY112218; APU07262.1; -; Genomic_RNA.
EMBL; KY112220; APU07277.1; -; Genomic_RNA.
EMBL; KY112221; APU07285.1; -; Genomic_RNA.
EMBL; KY112222; APU07292.1; -; Genomic_RNA.
EMBL; KY112223; APU07300.1; -; Genomic_RNA.
EMBL; KY112224; APU07308.1; -; Genomic_RNA.
EMBL; KY112225; APU07316.1; -; Genomic_RNA.
EMBL; KY112226; APU07324.1; -; Genomic_RNA.
EMBL; KY112227; APU07332.1; -; Genomic_RNA.
EMBL; KY112228; APU07340.1; -; Genomic_RNA.
EMBL; KY112229; APU07348.1; -; Genomic_RNA.
EMBL; KY112230; APU07356.1; -; Genomic_RNA.
EMBL; KY112231; APU07363.1; -; Genomic_RNA.
EMBL; KY112232; APU07371.1; -; Genomic_RNA.
EMBL; KY112233; APU07379.1; -; Genomic_RNA.
EMBL; KY112234; APU07387.1; -; Genomic_RNA.
EMBL; KY112235; APU07395.1; -; Genomic_RNA.
EMBL; KY112236; APU07403.1; -; Genomic_RNA.
EMBL; KY112237; APU07410.1; -; Genomic_RNA.
EMBL; KY112238; APU07418.1; -; Genomic_RNA.
EMBL; KY112239; APU07426.1; -; Genomic_RNA.
EMBL; KY112240; APU07434.1; -; Genomic_RNA.
EMBL; KY112241; APU07442.1; -; Genomic_RNA.
EMBL; KY112242; APU07450.1; -; Genomic_RNA.
EMBL; KY112243; APU07458.1; -; Genomic_RNA.
EMBL; KY112244; APU07466.1; -; Genomic_RNA.
EMBL; KY112245; APU07473.1; -; Genomic_RNA.
EMBL; KY112246; APU07481.1; -; Genomic_RNA.
EMBL; KY112247; APU07489.1; -; Genomic_RNA.
EMBL; KY112248; APU07497.1; -; Genomic_RNA.
EMBL; KY112249; APU07505.1; -; Genomic_RNA.
EMBL; KY112250; APU07513.1; -; Genomic_RNA.
EMBL; KY112341; APU07671.1; -; Genomic_RNA.
EMBL; KY112344; APU07694.1; -; Genomic_RNA.
EMBL; KY112346; APU07710.1; -; Genomic_RNA.
EMBL; KY112347; APU07718.1; -; Genomic_RNA.
EMBL; KY112352; APU07758.1; -; Genomic_RNA.
EMBL; KY112354; APU07773.1; -; Genomic_RNA.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0042805; F:actinin binding; IEA:UniProtKB-UniRule.
GO; GO:0030332; F:cyclin binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0019904; F:protein domain specific binding; IEA:UniProtKB-UniRule.
GO; GO:0001070; F:RNA binding transcription regulator activity; IEA:UniProtKB-UniRule.
GO; GO:1990970; F:trans-activation response element binding; IEA:UniProtKB-UniRule.
GO; GO:0039525; P:modulation by virus of host chromatin organization; IEA:UniProtKB-UniRule.
GO; GO:0039586; P:modulation by virus of host PP1 activity; IEA:UniProtKB-UniRule.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IEA:UniProtKB-UniRule.
GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:UniProtKB-UniRule.
GO; GO:0050434; P:positive regulation of viral transcription; IEA:UniProtKB-UniRule.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-UniRule.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
Gene3D; 4.10.20.10; -; 1.
HAMAP; MF_04079; HIV_TAT; 1.
InterPro; IPR001831; IV_Tat.
InterPro; IPR036963; Tat_dom_sf.
Pfam; PF00539; Tat; 1.
PRINTS; PR00055; HIVTATDOMAIN.
3: Inferred from homology;
Acetylation {ECO:0000256|HAMAP-Rule:MF_04079};
Activator {ECO:0000256|HAMAP-Rule:MF_04079,
ECO:0000256|RuleBase:RU003311, ECO:0000256|SAAS:SAAS00111091};
Apoptosis {ECO:0000256|HAMAP-Rule:MF_04079};
Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04079};
Host nucleus {ECO:0000256|HAMAP-Rule:MF_04079,
ECO:0000256|RuleBase:RU003311, ECO:0000256|SAAS:SAAS00473431};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04079};
Inhibition of host innate immune response by virus {ECO:0000256|HAMAP-
Rule:MF_04079};
Inhibition of host interferon signaling pathway by virus
{ECO:0000256|HAMAP-Rule:MF_04079};
Isopeptide bond {ECO:0000256|HAMAP-Rule:MF_04079};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_04079};
Methylation {ECO:0000256|HAMAP-Rule:MF_04079};
Modulation of host chromatin by virus {ECO:0000256|HAMAP-
Rule:MF_04079};
Modulation of host PP1 activity by virus {ECO:0000256|HAMAP-
Rule:MF_04079}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04079};
RNA-binding {ECO:0000256|HAMAP-Rule:MF_04079,
ECO:0000256|RuleBase:RU003311, ECO:0000256|SAAS:SAAS00111359};
Secreted {ECO:0000256|HAMAP-Rule:MF_04079};
Transcription {ECO:0000256|HAMAP-Rule:MF_04079,
ECO:0000256|RuleBase:RU003311, ECO:0000256|SAAS:SAAS00111074};
Transcription regulation {ECO:0000256|HAMAP-Rule:MF_04079,
ECO:0000256|RuleBase:RU003311, ECO:0000256|SAAS:SAAS00111074};
Ubl conjugation {ECO:0000256|HAMAP-Rule:MF_04079};
Viral immunoevasion {ECO:0000256|HAMAP-Rule:MF_04079};
Zinc {ECO:0000256|HAMAP-Rule:MF_04079}.
REGION 1 48 Transactivation. {ECO:0000256|HAMAP-
Rule:MF_04079}.
REGION 1 24 Interaction with human CREBBP.
{ECO:0000256|HAMAP-Rule:MF_04079}.
REGION 22 37 Cysteine-rich. {ECO:0000256|HAMAP-
Rule:MF_04079}.
REGION 38 48 Core. {ECO:0000256|HAMAP-Rule:MF_04079}.
REGION 49 86 Interaction with the host capping enzyme
RNGTT. {ECO:0000256|HAMAP-Rule:MF_04079}.
MOTIF 49 57 Nuclear localization signal, RNA-binding
(TAR), and protein transduction.
{ECO:0000256|HAMAP-Rule:MF_04079}.
METAL 22 22 Zinc 1. {ECO:0000256|HAMAP-
Rule:MF_04079}.
METAL 25 25 Zinc 2. {ECO:0000256|HAMAP-
Rule:MF_04079}.
METAL 27 27 Zinc 2. {ECO:0000256|HAMAP-
Rule:MF_04079}.
METAL 30 30 Zinc 2. {ECO:0000256|HAMAP-
Rule:MF_04079}.
METAL 33 33 Zinc 1; via pros nitrogen.
{ECO:0000256|HAMAP-Rule:MF_04079}.
METAL 34 34 Zinc 1. {ECO:0000256|HAMAP-
Rule:MF_04079}.
METAL 37 37 Zinc 1. {ECO:0000256|HAMAP-
Rule:MF_04079}.
SITE 11 11 Essential for Tat translocation through
the endosomal membrane.
{ECO:0000256|HAMAP-Rule:MF_04079}.
MOD_RES 28 28 N6-acetyllysine; by host PCAF.
{ECO:0000256|HAMAP-Rule:MF_04079}.
MOD_RES 50 50 N6-acetyllysine; by host EP300 and
GCN5L2. {ECO:0000256|HAMAP-
Rule:MF_04079}.
MOD_RES 51 51 N6-acetyllysine; by host EP300 and
GCN5L2. {ECO:0000256|HAMAP-
Rule:MF_04079}.
MOD_RES 52 52 Asymmetric dimethylarginine; by host
PRMT6. {ECO:0000256|HAMAP-Rule:MF_04079}.
MOD_RES 53 53 Asymmetric dimethylarginine; by host
PRMT6. {ECO:0000256|HAMAP-Rule:MF_04079}.
CROSSLNK 71 71 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000256|HAMAP-Rule:MF_04079}.
SEQUENCE 99 AA; 11253 MW; 98446EA43666FF00 CRC64;
MEPVDPNLEP WNHPGSQPKT PCNRCFCKKC SYHCLVCFQT KGLGISYGRK KRRQRRTAPP
SSEDHQNPIS KQPLPQTRGN QTGSEESKKE VESKTETNP


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