ID   TRRAP_MOUSE             Reviewed;        2565 AA.
AC   Q80YV3; Q8C0Z5; Q8K104;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 2.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Transformation/transcription domain-associated protein;
DE   AltName: Full=Tra1 homolog;
GN   Name=Trrap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2211-2565.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   FUNCTION.
RX   PubMed=11544477; DOI=10.1038/ng725;
RA   Herceg Z., Hulla W., Gell D., Cuenin C., Lleonart M., Jackson S.,
RA   Wang Z.-Q.;
RT   "Disruption of Trrap causes early embryonic lethality and defects in cell
RT   cycle progression.";
RL   Nat. Genet. 29:206-211(2001).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=31231791; DOI=10.1111/cge.13590;
RA   Xia W., Hu J., Ma J., Huang J., Wang X., Jiang N., Zhang J., Ma Z., Ma D.;
RT   "Novel TRRAP mutation causes autosomal dominant non-syndromic hearing
RT   loss.";
RL   Clin. Genet. 96:300-308(2019).
CC   -!- FUNCTION: Adapter protein, which is found in various multiprotein
CC       chromatin complexes with histone acetyltransferase activity (HAT),
CC       which gives a specific tag for epigenetic transcription activation.
CC       Component of the NuA4 histone acetyltransferase complex which is
CC       responsible for acetylation of nucleosomal histones H4 and H2A. Plays a
CC       central role in MYC transcription activation, and also participates in
CC       cell transformation by MYC. Required for p53/TP53-, E2F1- and E2F4-
CC       mediated transcription activation. Probably acts by linking
CC       transcription factors such as E1A, MYC or E2F1 to HAT complexes such as
CC       STAGA thereby allowing transcription activation. Probably not required
CC       in the steps following histone acetylation in processes of
CC       transcription activation. May be required for the mitotic checkpoint
CC       and normal cell cycle progression. Component of a SWR1-like complex
CC       that specifically mediates the removal of histone H2A.Z/H2AZ1 from the
CC       nucleosome. May play a role in the formation and maintenance of the
CC       auditory system (By similarity). {ECO:0000250|UniProtKB:A0A0R4ITC5,
CC       ECO:0000269|PubMed:11544477}.
CC   -!- SUBUNIT: Interacts with MYC, E2F1 and E2F4 transcription factors.
CC       Interacts directly with p53/TP53. Interacts with GCN5L2. Component of
CC       various HAT complexes. Component of the PCAF complex, at least composed
CC       of TADA2L/ADA2, SUPT3H, TADA3L/ADA3, TAF5L/PAF65-beta, TAF6L/PAF65-
CC       alpha, TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and TRRAP. Component
CC       of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TADA3L,
CC       SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100, GCN5L2/GCN5,
CC       TAF10 and TRRAP. Component of the NuA4 histone acetyltransferase
CC       complex which contains the catalytic subunit KAT5/TIP60 and the
CC       subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1,
CC       RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15,
CC       MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. Component of
CC       the STAGA complex, at least composed of SUPT3H, GCN5L2, SUPT7L, TAF5L,
CC       TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. The STAGA core
CC       complex is associated with a subcomplex required for histone
CC       deubiquitination composed of ATXN7L3, ENY2 and USP22. Component of the
CC       BAF53 complex, at least composed of BAF53A, RUVBL1, SMARCA4/BRG1, and
CC       TRRAP, which preferentially acetylates histone H4 (and H2A) within
CC       nucleosomes. Interacts with NPAT (By similarity). Interaction with
CC       TELO2 and TTI1. Component of a SWR1-like complex (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q80YV3; Q8R4I1: Atxn7; NbExp=3; IntAct=EBI-2942477, EBI-7990748;
CC       Q80YV3; Q9JHD2: Kat2a; NbExp=4; IntAct=EBI-2942477, EBI-2943116;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in the cochlea.
CC       {ECO:0000269|PubMed:31231791}.
CC   -!- DOMAIN: The PI3K/PI4K domain is required for the recruitment of HAT
CC       complexes, and the MYC-dependent transactivation. Although it is
CC       strongly related to the PI3/PI4-kinase family, it lacks the typical
CC       motifs that constitute the catalytic site of PI3/PI4-kinase proteins,
CC       and lacks such activity (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. TRA1 subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC029023; AAH29023.1; -; mRNA.
DR   EMBL; BC050105; AAH50105.1; -; mRNA.
DR   EMBL; AK029388; BAC26431.1; -; mRNA.
DR   AlphaFoldDB; Q80YV3; -.
DR   SMR; Q80YV3; -.
DR   ComplexPortal; CPX-1024; PCAF histone acetylase complex.
DR   ComplexPortal; CPX-6803; SAGA complex, KAT2B variant.
DR   ComplexPortal; CPX-916; TFTC histone acetylation complex.
DR   ComplexPortal; CPX-920; SAGA complex, KAT2A variant.
DR   ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR   DIP; DIP-29177N; -.
DR   IntAct; Q80YV3; 26.
DR   MINT; Q80YV3; -.
DR   STRING; 10090.ENSMUSP00000098035; -.
DR   GlyGen; Q80YV3; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q80YV3; -.
DR   PhosphoSitePlus; Q80YV3; -.
DR   EPD; Q80YV3; -.
DR   jPOST; Q80YV3; -.
DR   MaxQB; Q80YV3; -.
DR   PaxDb; 10090-ENSMUSP00000098035; -.
DR   PeptideAtlas; Q80YV3; -.
DR   ProteomicsDB; 300029; -.
DR   Pumba; Q80YV3; -.
DR   AGR; MGI:2153272; -.
DR   MGI; MGI:2153272; Trrap.
DR   eggNOG; KOG0889; Eukaryota.
DR   InParanoid; Q80YV3; -.
DR   PhylomeDB; Q80YV3; -.
DR   ChiTaRS; Trrap; mouse.
DR   PRO; PR:Q80YV3; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q80YV3; Protein.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0000123; C:histone acetyltransferase complex; TAS:MGI.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0000786; C:nucleosome; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0000124; C:SAGA complex; IDA:MGI.
DR   GO; GO:0000812; C:Swr1 complex; ISS:UniProtKB.
DR   GO; GO:0033276; C:transcription factor TFTC complex; ISO:MGI.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR   GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal.
DR   GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO:MGI.
DR   GO; GO:0042981; P:regulation of apoptotic process; NAS:ComplexPortal.
DR   GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR   GO; GO:0006282; P:regulation of DNA repair; NAS:ComplexPortal.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI.
DR   GO; GO:2000779; P:regulation of double-strand break repair; NAS:ComplexPortal.
DR   GO; GO:0043484; P:regulation of RNA splicing; NAS:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR   CDD; cd05163; PIKK_TRRAP; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR003151; PIK-rel_kinase_FAT.
DR   InterPro; IPR014009; PIK_FAT.
DR   InterPro; IPR046805; Tra1_ring.
DR   PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR   PANTHER; PTHR11139:SF1; TRANSFORMATION_TRANSCRIPTION DOMAIN-ASSOCIATED PROTEIN; 1.
DR   Pfam; PF02259; FAT; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF20206; Tra1_ring; 1.
DR   SMART; SM01343; FATC; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Chromatin regulator; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..2565
FT                   /note="Transformation/transcription domain-associated
FT                   protein"
FT                   /id="PRO_0000088852"
FT   DOMAIN          1391..1963
FT                   /note="FAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT   DOMAIN          2206..2529
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   DOMAIN          2533..2565
FT                   /note="FATC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT                   ECO:0000255|PROSITE-ProRule:PRU00535"
FT   REGION          710..1087
FT                   /note="Interaction with TP53"
FT                   /evidence="ECO:0000250"
FT   REGION          1242..1277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1973..1995
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2212..2218
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          2393..2401
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          2413..2438
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   MOTIF           745..760
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1975..1994
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4A5"
FT   MOD_RES         749
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4A5"
FT   MOD_RES         775
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4A5"
FT   MOD_RES         1766
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4A5"
FT   CROSSLNK        1242
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4A5"
SQ   SEQUENCE   2565 AA;  291557 MW;  702138B3F2642B21 CRC64;
     MTRKFVKRSI FLHLLRHQPA NAQIGLMEGN TFCTTLQPRL FTMDLNVVEH KVFYTELLNL
     CEAEDSALTK LPCYKSLPSL VPLRIAALNA LAACNYLPQS REKIIAALFK ALNSTNSELQ
     EAGEACMRKF LEGATIEVDQ IHTHMRPLLM MLGDYRSLTL NVVNRLTSVT RLFPNSFNDK
     FCDQMMQHLR KWMEVVVITH KGGQRSDGNE MKICSAIINL FHLIPAAPQT LVKPPLEVVM
     ETERAMLIEA GSPFREPLIK FLTRHPSQTV ELFMMGATLN DPQWSRMFMS FLKHKDARPL
     RDVLAANPNR FITLLLPGGA QTAVRPGSSS TSNMRLDLQF QAIKIISIIV KNDDAWLASQ
     HSLVSQLRRV WVSETFQERH RKENMAATNW KEPKLLAFCL LNYCKRNYGD IELLFQLLRA
     FTGRFLCNMT FLKEYMEEEI PKNYSIAQKR ALFFRFVEFN DPNFGDELKA KVLQHILNPA
     FLYSFEKGEG EQLLGPPNPE GDNPESITSV FITKVLDPEK QADMLDSLRI YLLQYATLLV
     EHAPHHIHDN NKNRNSKLRR LMTFAWPCLL SKACVDPACR YSGHLLLAHI IAKFAIHKKI
     VLQVFHSLLK AHAMEARAIV RQAMAILTPA VPARMEDGHQ MLTHWTRKII VEEGHTVPQL
     VHILHPIVQH FKVYYPVRHH LVQHMVSAMQ RLGFTPSVTI EQRRLAVDLS EVVIKWELQR
     IKDQQPDSDM DPNSSGEGVN SVSIKRGLSV DSAQEVKRFR AATGAISAVF GRSQSLPGAD
     SLLAKPIDKQ HTDTVVNFLI RVACQVNDNT NTAGSPGEVL SRRCVNLLKT ALRPDMWCKS
     ELKLQWFDKL LMTVEQPNQV NYGNICTGLE VLNFLLTVLQ SPAILSSFKP LQRGIAACMT
     CGNTKVLRAV HSLLSRLMSI FPTEPSTSSV ASKYEELECL YAAVGKVIYE GLTNYEKATS
     ANPSQLFGTL MIHKSACCNN PSYIDRLISV FMRSLQKMVR EHLNPQTASG STEATAAGTS
     ELVMLSLDLV KTRLAVMSME MRKNFIQTIL TSLIEKSPDA KILRAVVKIV EEWVKNNSPM
     AANQTPTLRE KSILLVKMMT YIEKRFPEDL ELNAQFLDLV NYVYRDEALS GSELTAKLEP
     AFLSGLRCAQ PLIRAKFFEV FDNSMKRRVY ERLLYVTCSQ NWEAMGSHFW IKQCIELLLA
     VCEKSTAIGT SCQGAMLPSI TNVINLADSH DRAAFAMVTH VKQEPREREN SESKEEDVEI
     DIELAPGDQT STPKTKELSE KDIGNQLHML TNRHDKFLDT LREVKTGALL SAFVQLCHIS
     TTLAEKTWVQ LFPRLWKILS DRQQHALAGE ISPFLCSGSH QVQRDCQPSA LNCFVEAMSQ
     CVPPIPMRPC VLKYLGKTHN LWFRSTLMLE HQAFEKGLSL PIKPKQTTEF YEQESITPPQ
     QEILDSLAEL YSLLQEEDMW AGLWQKRCKF SETATAIAYE QHGFFEQAQE SYEKAMDKAK
     KEHERSNASP AIFPEYQLWE DHWIRCSKEL NQWEALTEFG QSKGHINPYL VLECAWRVSN
     WTAMKEALVQ VEVSCPKEMA WKVNMYRGYL AICHPEEQQL SFIERLVEMA SSLAIREWRR
     LPHVVSHVHT PLLQAAQQII ELQEAAQINA GLQPTNLGRN NSLHDMKTVV KTWRNRLPIV
     SDDLSHWSSV FMWRQHHYQA IVTAYENSSH HDPSSNNAML GVHASASAII QYGKIARKQG
     LVNVALDILS RIHTIPTVPI VDCFQKIRQQ VKCYLQLAGV MGKNECMQGL EVIESTNLKY
     FTKEMTAEFY ALKGMFLAQI NKSEEANKAF SAAVQMHDVL VKAWAMWGDY LESIFVKERQ
     LHLGVSAITC YLHACRHQNE SKSRKYLAKV LWLLSFDDDK NTLADAVDKY CIGVPPIQWL
     AWIPQLLTCL VGSEGKLLLN LISQVGRVYP QAVYFPIRTL YLTLKIEQRE RYKSDSGQQQ
     PSSAGNQSHS ASDPGPIRAT APMWRCSRIM HMQRELHPTL LSSLEGIVDQ MVWFRENWHE
     EVLRQLQQGL AKCYSVAFEK SGAVSDAKIT PHTLNFVKKL VSTFGVGLEN VSNVSTMFSS
     AASESLARRA QATAQDPVFQ KLKGQFTTDF DFSVPGSMKL HNLISKLKKW IKILEAKTKQ
     LPKFFLIEEK CRFLSNFSAQ TAEVEIPGEF LMPKPTHYYI KIARFMPRVE IVQKHNTAAR
     RLHIRGHNGK IYPYLVMNDA CLTESRREER VLQLLRLLNP CLEKRKETTK RHLFFTVPRV
     VAVSPQMRLV EDNPSSLSLV EIYKQRCAKK GIEHDNPISR YYDRLATVQA RGTQASHQVL
     RDILKEVQSN MVPRSMLKEW ALHTFPNATD YWTFRKMFTI QLALIGFAEF VLHLNRLNPE
     MLQIAQDTGK LNVAYFRFDI NDATGDLDAN RPVPFRLTPN ISEFLTTIGV SGPLTASMIA
     VARCFAQPNF KVDGVLKTVL RDEIIAWHKK TQEDTSSPLS AAGQPENMDS QQLVSLVQKA
     VTAIMTRLHN LAQFDGGESK VNTLVAAANS LDNLCRMDPA WHPWL
//