TAF5L_HUMAN
ID TAF5L_HUMAN Reviewed; 589 AA.
AC O75529; Q5TDI5; Q5TDI6; Q8IW31;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L {ECO:0000305};
DE Short=TAF5L {ECO:0000305};
DE AltName: Full=PCAF-associated factor 65 beta;
DE Short=PAF65-beta;
GN Name=TAF5L {ECO:0000312|HGNC:HGNC:17304}; Synonyms=PAF65B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 123-134 AND
RP 167-177, SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=9674425; DOI=10.1016/s0092-8674(00)81219-2;
RA Ogryzko V.V., Kotani T., Zhang X., Schiltz R.L., Howard T., Yang X.-J.,
RA Howard B.H., Qin J., Nakatani Y.;
RT "Histone-like TAFs within the PCAF histone acetylase complex.";
RL Cell 94:35-44(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 330-589 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11124703;
RX DOI=10.1002/1097-0061(200101)18:1<69::aid-yea647>3.0.co;2-h;
RA Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N.,
RA Zimbello R., Lanfranchi G., Valle G.;
RT "Characterization of 16 novel human genes showing high similarity to yeast
RT sequences.";
RL Yeast 18:69-80(2001).
RN [6]
RP REVIEW, AND PCAF COMPLEX COMPOSITION.
RX PubMed=9674419; DOI=10.1016/s0092-8674(00)81213-1;
RA Struhl K., Moqtaderi Z.;
RT "The TAFs in the HAT.";
RL Cell 94:1-4(1998).
RN [7]
RP IDENTIFICATION IN THE STAGA COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11564863; DOI=10.1128/mcb.21.20.6782-6795.2001;
RA Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M.,
RA Kundu T.K., Chait B.T., Roeder R.G.;
RT "Human STAGA complex is a chromatin-acetylating transcription coactivator
RT that interacts with pre-mRNA splicing and DNA damage-binding factors in
RT vivo.";
RL Mol. Cell. Biol. 21:6782-6795(2001).
RN [8]
RP IDENTIFICATION IN THE TFTC-HAT COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12601814; DOI=10.1002/pmic.200390030;
RA Cavusoglu N., Brand M., Tora L., van Dorsselaer A.;
RT "Novel subunits of the TATA binding protein free TAFII-containing
RT transcription complex identified by matrix-assisted laser
RT desorption/ionization-time of flight mass spectrometry following one-
RT dimensional gel electrophoresis.";
RL Proteomics 3:217-223(2003).
CC -!- FUNCTION: Functions as a component of the PCAF complex. The PCAF
CC complex is capable of efficiently acetylating histones in a nucleosomal
CC context. The PCAF complex could be considered as the human version of
CC the yeast SAGA complex (Probable). With TAF6L, acts as an epigenetic
CC regulator essential for somatic reprogramming. Regulates target genes
CC through H3K9ac deposition and MYC recruitment which trigger MYC
CC regulatory network to orchestrate gene expression programs to control
CC embryonic stem cell state (By similarity).
CC {ECO:0000250|UniProtKB:Q91WQ5, ECO:0000305|PubMed:9674419}.
CC -!- SUBUNIT: The PCAF complex is composed of a number of TBP-associated
CC factors (TAFS), such as TAF5, TAF5L, TAF6, TAF6L, TAF9, TAF10 and
CC TAF12, PCAF, and also PCAF-associated factors (PAFs), such as
CC TADA2L/ADA2, TADA3L/ADA3 and SPT3. Component of the STAGA transcription
CC coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L,
CC TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9.
CC {ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:12601814,
CC ECO:0000269|PubMed:9674425}.
CC -!- INTERACTION:
CC O75529; O43524: FOXO3; NbExp=2; IntAct=EBI-1785876, EBI-1644164;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863,
CC ECO:0000269|PubMed:9674425}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75529-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75529-2; Sequence=VSP_010156, VSP_010157;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the WD repeat TAF5 family. {ECO:0000305}.
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DR EMBL; AF069736; AAC39906.1; -; mRNA.
DR EMBL; AL121990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471098; EAW69902.1; -; Genomic_DNA.
DR EMBL; CH471098; EAW69903.1; -; Genomic_DNA.
DR EMBL; BC041094; AAH41094.1; -; mRNA.
DR EMBL; AJ009770; CAA08816.1; -; mRNA.
DR CCDS; CCDS1581.1; -. [O75529-1]
DR CCDS; CCDS31051.1; -. [O75529-2]
DR RefSeq; NP_001020418.1; NM_001025247.1. [O75529-2]
DR RefSeq; NP_055224.1; NM_014409.3. [O75529-1]
DR RefSeq; XP_005273156.1; XM_005273099.4. [O75529-1]
DR PDB; 7KTR; EM; 2.93 A; B=1-589.
DR PDB; 7KTS; EM; 19.09 A; B=1-589.
DR PDBsum; 7KTR; -.
DR PDBsum; 7KTS; -.
DR AlphaFoldDB; O75529; -.
DR SMR; O75529; -.
DR BioGRID; 117998; 91.
DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant.
DR ComplexPortal; CPX-903; TFTC histone acetylation complex.
DR ComplexPortal; CPX-989; PCAF histone acetylase complex.
DR CORUM; O75529; -.
DR DIP; DIP-28147N; -.
DR IntAct; O75529; 39.
DR MINT; O75529; -.
DR STRING; 9606.ENSP00000258281; -.
DR iPTMnet; O75529; -.
DR PhosphoSitePlus; O75529; -.
DR BioMuta; TAF5L; -.
DR EPD; O75529; -.
DR jPOST; O75529; -.
DR MassIVE; O75529; -.
DR MaxQB; O75529; -.
DR PaxDb; O75529; -.
DR PeptideAtlas; O75529; -.
DR PRIDE; O75529; -.
DR ProteomicsDB; 50066; -. [O75529-1]
DR ProteomicsDB; 50067; -. [O75529-2]
DR Antibodypedia; 20789; 224 antibodies from 30 providers.
DR DNASU; 27097; -.
DR Ensembl; ENST00000258281.6; ENSP00000258281.2; ENSG00000135801.10. [O75529-1]
DR Ensembl; ENST00000366675.3; ENSP00000355635.3; ENSG00000135801.10. [O75529-2]
DR GeneID; 27097; -.
DR KEGG; hsa:27097; -.
DR MANE-Select; ENST00000258281.7; ENSP00000258281.2; NM_014409.4; NP_055224.1.
DR UCSC; uc001htq.5; human. [O75529-1]
DR CTD; 27097; -.
DR DisGeNET; 27097; -.
DR GeneCards; TAF5L; -.
DR HGNC; HGNC:17304; TAF5L.
DR HPA; ENSG00000135801; Low tissue specificity.
DR neXtProt; NX_O75529; -.
DR OpenTargets; ENSG00000135801; -.
DR PharmGKB; PA38223; -.
DR VEuPathDB; HostDB:ENSG00000135801; -.
DR eggNOG; KOG0263; Eukaryota.
DR GeneTree; ENSGT00940000153342; -.
DR HOGENOM; CLU_005884_3_0_1; -.
DR InParanoid; O75529; -.
DR OMA; RPHQADV; -.
DR OrthoDB; 620721at2759; -.
DR PhylomeDB; O75529; -.
DR TreeFam; TF300669; -.
DR PathwayCommons; O75529; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; O75529; -.
DR BioGRID-ORCS; 27097; 164 hits in 1098 CRISPR screens.
DR ChiTaRS; TAF5L; human.
DR GeneWiki; TAF5L; -.
DR GenomeRNAi; 27097; -.
DR Pharos; O75529; Tbio.
DR PRO; PR:O75529; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75529; protein.
DR Bgee; ENSG00000135801; Expressed in buccal mucosa cell and 168 other tissues.
DR ExpressionAtlas; O75529; baseline and differential.
DR Genevisible; O75529; HS.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000124; C:SAGA complex; IDA:UniProtKB.
DR GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:1904672; P:regulation of somatic stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR CDD; cd08044; TAF5_NTD2; 1.
DR Gene3D; 1.25.40.500; -; 1.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037783; Taf5.
DR InterPro; IPR037826; TAF5L.
DR InterPro; IPR007582; TFIID_NTD2.
DR InterPro; IPR037264; TFIID_NTD2_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19879; PTHR19879; 1.
DR PANTHER; PTHR19879:SF6; PTHR19879:SF6; 1.
DR Pfam; PF04494; TFIID_NTD2; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF160897; SSF160897; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW WD repeat.
FT CHAIN 1..589
FT /note="TAF5-like RNA polymerase II p300/CBP-associated
FT factor-associated factor 65 kDa subunit 5L"
FT /id="PRO_0000051261"
FT REPEAT 266..305
FT /note="WD 1"
FT REPEAT 340..379
FT /note="WD 2"
FT REPEAT 382..421
FT /note="WD 3"
FT REPEAT 424..463
FT /note="WD 4"
FT REPEAT 466..505
FT /note="WD 5"
FT REPEAT 508..547
FT /note="WD 6"
FT REGION 211..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 325
FT /note="D -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010156"
FT VAR_SEQ 326..589
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010157"
FT HELIX 6..19
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 39..50
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 69..83
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 292..300
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 326..330
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 354..361
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 371..374
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 396..403
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 415..422
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 429..434
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 438..445
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 450..454
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 471..476
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 480..487
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 492..496
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 497..500
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 501..506
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 513..518
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 524..529
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 533..538
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 553..559
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 565..569
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 573..582
FT /evidence="ECO:0007829|PDB:7KTR"
SQ SEQUENCE 589 AA; 66155 MW; BBF0A1CDD17EE22E CRC64;
MKRVRTEQIQ MAVSCYLKRR QYVDSDGPLK QGLRLSQTAE EMAANLTVQS ESGCANIVSA
APCQAEPQQY EVQFGRLRNF LTDSDSQHSH EVMPLLYPLF VYLHLNLVQN SPKSTVESFY
SRFHGMFLQN ASQKDVIEQL QTTQTIQDIL SNFKLRAFLD NKYVVRLQED SYNYLIRYLQ
SDNNTALCKV LTLHIHLDVQ PAKRTDYQLY ASGSSSRSEN NGLEPPDMPS PILQNEAALE
VLQESIKRVK DGPPSLTTIC FYAFYNTEQL LNTAEISPDS KLLAAGFDNS CIKLWSLRSK
KLKSEPHQVD VSRIHLACDI LEEEDDEDDN AGTEMKILRG HCGPVYSTRF LADSSGLLSC
SEDMSIRYWD LGSFTNTVLY QGHAYPVWDL DISPYSLYFA SGSHDRTARL WSFDRTYPLR
IYAGHLADVD CVKFHPNSNY LATGSTDKTV RLWSAQQGNS VRLFTGHRGP VLSLAFSPNG
KYLASAGEDQ RLKLWDLASG TLYKELRGHT DNITSLTFSP DSGLIASASM DNSVRVWDIR
NTYCSAPADG SSSELVGVYT GQMSNVLSVQ FMACNLLLVT GITQENQEH
