TRRAP_MOUSE
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 25-MAY-2022, entry version 145.
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}.
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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 iPTMnet; Q80YV3; -.
DR PhosphoSitePlus; Q80YV3; -.
DR EPD; Q80YV3; -.
DR jPOST; Q80YV3; -.
DR MaxQB; Q80YV3; -.
DR PaxDb; Q80YV3; -.
DR PeptideAtlas; Q80YV3; -.
DR PRIDE; Q80YV3; -.
DR ProteomicsDB; 300029; -.
DR MGI; MGI:2153272; Trrap.
DR eggNOG; KOG0889; Eukaryota.
DR InParanoid; Q80YV3; -.
DR PhylomeDB; Q80YV3; -.
DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
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:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0016578; P:histone deubiquitination; ISO:MGI.
DR GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; ISO:MGI.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISO:MGI.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
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; IPR033317; TRA1/TRRAP.
DR PANTHER; PTHR11139:SF1; PTHR11139:SF1; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 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
