GENTAUR Molecular Products.

 I7FRF9_9HIV1            Unreviewed;       102 AA.
 I7FRF9;
 03-OCT-2012, integrated into UniProtKB/TrEMBL.
 03-OCT-2012, sequence version 1.
 28-MAR-2018, entry version 20.
 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:AFP25845.1};
 Human immunodeficiency virus 1.
 Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
 Lentivirus; Primate lentivirus group.
 NCBI_TaxID=11676 {ECO:0000313|EMBL:AFP25845.1};
 NCBI_TaxID=9606; Homo sapiens (Human).
 [1] {ECO:0000313|EMBL:AFP25845.1}
 NUCLEOTIDE SEQUENCE.
 STRAIN=703010256.e10 {ECO:0000313|EMBL:AFP25740.1},
 703010256.e11 {ECO:0000313|EMBL:AFP25748.1},
 703010256.e12 {ECO:0000313|EMBL:AFP25756.1},
 703010256.e13 {ECO:0000313|EMBL:AFP25762.1},
 703010256.e22 {ECO:0000313|EMBL:AFP25825.1},
 703010256.e23 {ECO:0000313|EMBL:AFP25831.1},
 703010256.e25 {ECO:0000313|EMBL:AFP25845.1},
 703010256.e27 {ECO:0000313|EMBL:AFP25859.1}, and
 703010256.e8 {ECO:0000313|EMBL:AFP25887.1};
 PubMed=22693444; DOI=10.1371/journal.ppat.1002686;
 Parrish N.F., Wilen C.B., Banks L.B., Iyer S.S., Pfaff J.M.,
 Salazar-Gonzalez J.F., Salazar M.G., Decker J.M., Parrish E.H.,
 Berg A., Hopper J., Hora B., Kumar A., Mahlokozera T., Yuan S.,
 Coleman C., Vermeulen M., Ding H., Ochsenbauer C., Tilton J.C.,
 Permar S.R., Kappes J.C., Betts M.R., Busch M.P., Gao F.,
 Montefiori D., Haynes B.F., Shaw G.M., Hahn B.H., Doms R.W.;
 "Transmitted/founder and chronic subtype C HIV-1 use CD4 and CCR5
 receptors with equal efficiency and are not inhibited by blocking the
 integrin alpha4beta7.";
 PLoS Pathog. 8:E1002686-E1002686(2012).
 [2] {ECO:0000313|EMBL:AGG96148.1}
 NUCLEOTIDE SEQUENCE.
 STRAIN=C.703010256.w24.172dps.e1 {ECO:0000313|EMBL:AGG96148.1},
 C.703010256.w24.172dps.e12 {ECO:0000313|EMBL:AGG96154.1},
 C.703010256.w24.172dps.e5 {ECO:0000313|EMBL:AGG96182.1},
 C.703010256.w60.426dps.e1 {ECO:0000313|EMBL:AGG96216.1},
 C.703010256.w60.426dps.e12 {ECO:0000313|EMBL:AGG96236.1},
 C.703010256.w60.426dps.e13 {ECO:0000313|EMBL:AGG96243.1},
 C.703010256.w60.426dps.e18 {ECO:0000313|EMBL:AGG96263.1},
 C.703010256.w60.426dps.e2 {ECO:0000313|EMBL:AGG96270.1},
 C.703010256.w60.426dps.e3 {ECO:0000313|EMBL:AGG96276.1},
 C.703010256.w60.426dps.e4 {ECO:0000313|EMBL:AGG96283.1},
 C.703010256.w60.426dps.e8 {ECO:0000313|EMBL:AGG96303.1},
 C.703010256.w60.426dps.e9 {ECO:0000313|EMBL:AGG96310.1},
 C.703010256.w96.684dps.e10 {ECO:0000313|EMBL:AGG96324.1},
 C.703010256.w96.684dps.e11 {ECO:0000313|EMBL:AGG96331.1},
 C.703010256.w96.684dps.e12 {ECO:0000313|EMBL:AGG96338.1},
 C.703010256.w96.684dps.e13 {ECO:0000313|EMBL:AGG96344.1},
 C.703010256.w96.684dps.e22 {ECO:0000313|EMBL:AGG96407.1},
 C.703010256.w96.684dps.e23 {ECO:0000313|EMBL:AGG96413.1},
 C.703010256.w96.684dps.e25 {ECO:0000313|EMBL:AGG96427.1},
 C.703010256.w96.684dps.e27 {ECO:0000313|EMBL:AGG96441.1}, and
 C.703010256.w96.684dps.e8 {ECO:0000313|EMBL:AGG96469.1};
 PubMed=23221345; DOI=10.1172/JCI65330;
 CHAVI Core B;
 Liu M.K., Hawkins N., Ritchie A.J., Ganusov V.V., Whale V.,
 Brackenridge S., Li H., Pavlicek J.W., Cai F., Rose-Abrahams M.,
 Treurnicht F., Hraber P., Riou C., Gray C., Ferrari G., Tanner R.,
 Ping L.H., Anderson J.A., Swanstrom R., B C.C., Cohen M., Karim S.S.,
 Haynes B., Borrow P., Perelson A.S., Shaw G.M., Hahn B.H.,
 Williamson C., Korber B.T., Gao F., Self S., McMichael A.,
 Goonetilleke N.;
 "Vertical T cell immunodominance and epitope entropy determine HIV-1
 escape.";
 J. Clin. Invest. 123:380-393(2013).
 -!- 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}.
 -!- FUNCTION: Nuclear transcriptional activator of viral gene
     expression, that is essential for viral transcription from the LTR
     promoter and replication. Acts as a sequence-specific molecular
     adapter, directing components of the cellular transcription
     machinery to the viral RNA to promote processive transcription
     elongation by the RNA polymerase II (RNA pol II) complex, thereby
     increasing the level of full-length transcripts. In the absence of
     Tat, the RNA Pol II generates short or non-processive transcripts
     that terminate at approximately 60 bp from the initiation site.
     Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb
     complex (CDK9 and CCNT1), which promotes RNA chain elongation.
     This binding increases Tat's affinity for a hairpin structure at
     the 5'-end of all nascent viral mRNAs referred to as the
     transactivation responsive RNA element (TAR RNA) and allows Tat/P-
     TEFb complex to bind cooperatively to TAR RNA. The CDK9 component
     of P-TEFb and other Tat-activated kinases hyperphosphorylate the
     C-terminus of RNA Pol II that becomes stabilized and much more
     processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5,
     and HTATIP2 are also important for Tat's function. Besides its
     effect on RNA Pol II processivity, Tat induces chromatin
     remodeling of proviral genes by recruiting the histone
     acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin.
     This also contributes to the increase in proviral transcription
     rate, especially when the provirus integrates in transcriptionally
     silent region of the host genome. To ensure maximal activation of
     the LTR, Tat mediates nuclear translocation of NF-kappa-B by
     interacting with host RELA. Through its interaction with host TBP,
     Tat may also modulate transcription initiation. Tat can reactivate
     a latently infected cell by penetrating in it and transactivating
     its LTR promoter. In the cytoplasm, Tat is thought to act as a
     translational activator of HIV-1 mRNAs. {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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 Distributed under the Creative Commons Attribution-NoDerivs License
 -----------------------------------------------------------------------
 EMBL; JQ779075; AFP25740.1; -; Genomic_RNA.
 EMBL; JQ779076; AFP25748.1; -; Genomic_RNA.
 EMBL; JQ779077; AFP25756.1; -; Genomic_RNA.
 EMBL; JQ779078; AFP25762.1; -; Genomic_RNA.
 EMBL; JQ779087; AFP25825.1; -; Genomic_RNA.
 EMBL; JQ779088; AFP25831.1; -; Genomic_RNA.
 EMBL; JQ779090; AFP25845.1; -; Genomic_RNA.
 EMBL; JQ779092; AFP25859.1; -; Genomic_RNA.
 EMBL; JQ779096; AFP25887.1; -; Genomic_RNA.
 EMBL; JX972789; AGG96148.1; -; Genomic_RNA.
 EMBL; JX972790; AGG96154.1; -; Genomic_RNA.
 EMBL; JX972794; AGG96182.1; -; Genomic_RNA.
 EMBL; JX972799; AGG96216.1; -; Genomic_RNA.
 EMBL; JX972802; AGG96236.1; -; Genomic_RNA.
 EMBL; JX972803; AGG96243.1; -; Genomic_RNA.
 EMBL; JX972806; AGG96263.1; -; Genomic_RNA.
 EMBL; JX972807; AGG96270.1; -; Genomic_RNA.
 EMBL; JX972808; AGG96276.1; -; Genomic_RNA.
 EMBL; JX972809; AGG96283.1; -; Genomic_RNA.
 EMBL; JX972812; AGG96303.1; -; Genomic_RNA.
 EMBL; JX972813; AGG96310.1; -; Genomic_RNA.
 EMBL; JX972815; AGG96324.1; -; Genomic_RNA.
 EMBL; JX972816; AGG96331.1; -; Genomic_RNA.
 EMBL; JX972817; AGG96338.1; -; Genomic_RNA.
 EMBL; JX972818; AGG96344.1; -; Genomic_RNA.
 EMBL; JX972827; AGG96407.1; -; Genomic_RNA.
 EMBL; JX972828; AGG96413.1; -; Genomic_RNA.
 EMBL; JX972830; AGG96427.1; -; Genomic_RNA.
 EMBL; JX972832; AGG96441.1; -; Genomic_RNA.
 EMBL; JX972836; AGG96469.1; -; 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   102 AA;  11646 MW;  2BB4001B777F2251 CRC64;
 MEPIDPKLEP WNHPGSQPKT ACNKCYCKKC SYHCLVCFQT KGLGISYGRK KRRQRRSAPP
 SSEDHQNPLP KQPLSQTRGN PTGSEESKKK VESQTETDPF DW

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