TRA1_DROME
ID TRA1_DROME Reviewed; 3790 AA.
AC Q8I8U7; A0A140SQB4; A8DY44; Q2EZ47; Q8T3L7; Q9V9E9;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 4.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Transcription-associated protein 1;
DE AltName: Full=dTRA1;
GN Name=Nipped-A; Synonyms=Tra1; ORFNames=CG2905;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INTERACTION WITH SPT3; GCN5; ADA3 AND ADA2B.
RX PubMed=12697829; DOI=10.1128/mcb.23.9.3305-3319.2003;
RA Kusch T., Guelman S., Abmayr S.M., Workman J.L.;
RT "Two Drosophila Ada2 homologues function in different multiprotein
RT complexes.";
RL Mol. Cell. Biol. 23:3305-3319(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16508010; DOI=10.1128/mcb.26.6.2347-2359.2006;
RA Gause M., Eissenberg J.C., Macrae A.F., Dorsett M., Misulovin Z.,
RA Dorsett D.;
RT "Nipped-A, the Tra1/TRRAP subunit of the Drosophila SAGA and Tip60
RT complexes, has multiple roles in Notch signaling during wing development.";
RL Mol. Cell. Biol. 26:2347-2359(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 357-593 (ISOFORM F).
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP IDENTIFICATION IN THE TIP60 COMPLEX, AND FUNCTION.
RX PubMed=15528408; DOI=10.1126/science.1103455;
RA Kusch T., Florens L., Macdonald W.H., Swanson S.K., Glaser R.L.,
RA Yates J.R. III, Abmayr S.M., Washburn M.P., Workman J.L.;
RT "Acetylation by Tip60 is required for selective histone variant exchange at
RT DNA lesions.";
RL Science 306:2084-2087(2004).
CC -!- FUNCTION: Part of the Tip60 chromatin-remodeling complex which is
CC involved in DNA repair (PubMed:15528408). Upon induction of DNA double-
CC strand breaks, this complex acetylates phosphorylated H2AV in
CC nucleosomes and exchanges it with unmodified H2AV (PubMed:15528408).
CC During wing development, required for activity of Notch and its
CC coactivator mam (PubMed:16508010). Function in promoting mam function
CC is likely to involve both the Tip60 and SAGA complexes
CC (PubMed:16508010). {ECO:0000269|PubMed:15528408,
CC ECO:0000269|PubMed:16508010}.
CC -!- SUBUNIT: Component of the Tip60 chromatin-remodeling complex which
CC contains the catalytic subunit Tip60 and the subunits Domino, Tra1,
CC Brd8, E(Pc), DMAP1, Pontin, Reptin, Ing3, Act87E, BAP55, Mrg15, MrgBP,
CC Gas41 and YL-1 (PubMed:15528408). Probable component of some SAGA
CC complex (PubMed:12697829). Interacts with Spt3, Gcn5, Ada3 and Ada2b
CC (PubMed:12697829). {ECO:0000269|PubMed:12697829,
CC ECO:0000269|PubMed:15528408}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16508010}. Cytoplasm
CC {ECO:0000269|PubMed:16508010}. Chromosome
CC {ECO:0000269|PubMed:16508010}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=E {ECO:0000312|FlyBase:FBgn0053554};
CC IsoId=Q8I8U7-1; Sequence=Displayed;
CC Name=F {ECO:0000312|FlyBase:FBgn0053554};
CC IsoId=Q8I8U7-2; Sequence=VSP_059312;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12697829}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:12697829}.
CC -!- MISCELLANEOUS: Although strongly related to the PI3/PI4-kinase family,
CC it lacks the typical motifs that constitute the catalytic site of
CC PI3/PI4-kinase proteins, suggesting that it probably lacks such
CC activity.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. TRA1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM11122.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN52145.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Insertion of several transposable element sequences.; Evidence={ECO:0000305};
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DR EMBL; AY142217; AAN52145.1; ALT_SEQ; mRNA.
DR EMBL; AE013599; ABI31023.2; -; Genomic_DNA.
DR EMBL; AE013599; ABV53702.2; -; Genomic_DNA.
DR EMBL; AY094769; AAM11122.1; ALT_INIT; mRNA.
DR EMBL; DQ352451; ABD22987.1; -; mRNA.
DR RefSeq; NP_001097192.2; NM_001103722.3. [Q8I8U7-1]
DR RefSeq; NP_001303335.1; NM_001316406.1. [Q8I8U7-2]
DR SMR; Q8I8U7; -.
DR BioGRID; 61398; 31.
DR IntAct; Q8I8U7; 20.
DR MINT; Q8I8U7; -.
DR STRING; 7227.FBpp0085431; -.
DR PaxDb; Q8I8U7; -.
DR PRIDE; Q8I8U7; -.
DR EnsemblMetazoa; FBtr0303293; FBpp0292385; FBgn0053554. [Q8I8U7-1]
DR EnsemblMetazoa; FBtr0347556; FBpp0312589; FBgn0053554. [Q8I8U7-2]
DR GeneID; 35483; -.
DR KEGG; dme:Dmel_CG33554; -.
DR UCSC; CG33554-RA; d. melanogaster.
DR UCSC; CG33554-RD; d. melanogaster.
DR CTD; 35483; -.
DR FlyBase; FBgn0053554; Nipped-A.
DR VEuPathDB; VectorBase:FBgn0053554; -.
DR eggNOG; KOG0889; Eukaryota.
DR GeneTree; ENSGT00390000017961; -.
DR InParanoid; Q8I8U7; -.
DR OMA; NPIFAMD; -.
DR PhylomeDB; Q8I8U7; -.
DR SignaLink; Q8I8U7; -.
DR BioGRID-ORCS; 35483; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Nipped-A; fly.
DR GenomeRNAi; 35483; -.
DR PRO; PR:Q8I8U7; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0053554; Expressed in eye disc (Drosophila) and 30 other tissues.
DR ExpressionAtlas; Q8I8U7; baseline and differential.
DR Genevisible; Q8I8U7; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
DR GO; GO:0000124; C:SAGA complex; IDA:FlyBase.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
DR GO; GO:0043486; P:histone exchange; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0035222; P:wing disc pattern formation; IGI:FlyBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
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; 2.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
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 Activator; Alternative splicing; Chromatin regulator; Chromosome;
KW Cytoplasm; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..3790
FT /note="Transcription-associated protein 1"
FT /id="PRO_0000088853"
FT REPEAT 98..136
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 335..381
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 740..778
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 1185..1223
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 1332..1370
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 1826..1864
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT DOMAIN 2610..3173
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 3429..3753
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 3758..3790
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 3435..3441
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 3616..3624
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 3636..3661
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT VAR_SEQ 1999..2048
FT /note="VGSHTKPDDILRSIDKSYCDTVLNFLIRLACQVNDPQAPILSPGESLSRR
FT -> K (in isoform F)"
FT /id="VSP_059312"
FT CONFLICT 468
FT /note="A -> T (in Ref. 5; AAM11122)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3790 AA; 435330 MW; 366CF25BBC7C5435 CRC64;
MSVIENVPVN TFRNYLNILN DSSSKDELKL KATQELSEHF EMIMQSPAYP SFLDNSLKIF
MRILQDGEPQ FIQENTMQHI RKLILEMIHR LPITESLRQH VKTIITMMLK ILKTDNEENV
LVCLRIIIEL HKHFRPSFNS EIQLFLGFVK EIYTNLPNHL TSIFETSNDV WVTDLKDLNL
EVLLSESYSV RTIHVEKALD SNSQQQIYNL LPRGILSLKV LQELPIIVVL MYQIYKNAVH
QEVSEFIPLI LTTINLQPTV TRRNSPQKEI YVEFMGAQIK TLSFLAYIVR IFQEVVIASS
LSVTSGMLNL MKNCPKEAAH LRKELLIAAR HIFATDLRQK FIPSIEQLFD EDLLIGKGVT
LDSIRPLAYS TLADLAHHVR QSLNIDVLIK AVNLFSKNVH DESLAVGIQT MSCKLLLNLV
DCLRHHSETE PQRSKALLSK LLKVFVKKFE TIAKIQLPLI IQKCKGHAFS GALVNSSGNA
SLSHINAPDL KDDISNIQVS ASGSQWIYSV NVAEFRSLVK TLVGGVKTIT WGFFNSKFQL
TDTKLANHEK IFGPEIVCSY IDLVYYAMEA LDIYTINVNP NQQRTSGLIS RSKEEKEVLE
HFSGIFLMMH SQNFQEIFST TINFLVERIY KNQSLQVIAN SFLANPTTSP LFATVLVEYL
LNKMEEMGSN LERSNLYLRL FKLVFGSVSL FPVENEQMLR PHLHKIVNRS MELALISEEP
YNYFLLLRAL FRSIGGGSHD LLYQEFLPLL PNLLEGLNRL QSGFHKQHMR DLFVELCLTV
PVRLSSLLPY LPMLMDPLVS ALNGSPTLIS QGLRTLELCV DNLQPDFLYD HIQPVRAALM
QALWKTLRNQ DNAALVAFRV LGKFGGGNRK MMVEPQALSY IINDKPTISI VTYFQEYETP
IDFPVDEAIK SAFRALGSNS TDQFYRRQSW EVIRCFLAAF ISLDDEKHML LKLFTHVDFV
ENKIMNWSTF QHKAGNETVR ETHQTALIGM LVASATKDLR DSVCPVMAAV VRHYTMVAIA
QQAGPFPQKG YQATHGIDPM ILIDALASCM GHEEKELCKP GIACMGIILD TATNIMGNKD
RACKLPIIQY LAEKMVSLCY DRPWYSKVGG CQAIQFLCKH MSLRALFQNL FNFLKAFMFV
LMDLEGDVSN GAIEITKSYM KSMLEICLTP INECYKNIDL KDLQAKATYE VIHELVRHIT
SPNTIVREES MVLLKHIGTI QSKTVSEVMD PHKDVLADII PPKKHLLRHQ PANAQIGLMD
GNTFCTTLEP RLFTIDLTNT YHKLFFHELL TLSEAEDATL AKLDCYKNVP NLIPLRTSAL
RALAACHYIS DIGYKEKIIN IIFKVMESDK SELQTTAFHC MKHFITGVTL EKEKVQSAMR
PLLLKLGDHR NLSIPAIKRL SYFTQIFPQM FNEKLSEQIL QHCSKIMEIF VSEYKSTSPN
VNFFASSKGG EYEQKIVILI EMFFYISASV KYIEKLCQLV LKTEKNLMIE ASSPYREALI
KFLQRFPTET VDLFLTESLM IDPQWNRLFI YLLKHETGVS FRAVIKSSRY NNLIHYLNTH
TEFPEALKYE IQHQAVLIIF TLMESDDQWI PTRQDIVDAL KNCWQNYLST LSSEDVLCDL
WHLIGKILLH YFSNNTNDIE LLFQLLRALC FRFIPDVYFL RDFLQHTVAQ SFTVNWKRNA
FFYFVENFNN SFLSEELKAK IITAVIIPCF AVSFDKGEGN KLIGAPPTPY QEDEKNIVSV
FINKVFDPDK QYDDAVRIAL LQLACLLVER ASQHIHDGDA NNKRQGNKLR RLMTFAWPCL
LSKSSVDPTA RYHGHLLLSH IIARLAIHKK IVLQVFHSLL KGHALEARSI VKQALDVLTP
AMPLRMEDGN TMLTHWTKKI IVEEGHAMQQ LFHILQLIIR HYKVYFPVRH QLVQHLINYM
QRLGFPPTAS IEHKKLAVDL AEVIIKWELH RIKDDRETKT DGTEEELIQE SSVKRSGIDL
VETRKKSFDI IRETTVQGVG SHTKPDDILR SIDKSYCDTV LNFLIRLACQ VNDPQAPILS
PGESLSRRCV MLLKMAMRPE IWPQPFDIKL NWLDKVLATV ETPHHNLNNI CTGIDFLTFL
TTILSPDQLV SIIRPVQRGL SLCIIHQNTR IVRLMHMFLT RIMAIFPPDT QHKHEDLDLL
YTAVSKMIAE NLTSYEKSPQ PNASSLFGTL MILKACTTNN ASYIDRILVQ FIRVLNHLTR
DHINTIGGNT VISQSPDSNA LPLELLVLSL ELIKNRIFVM SVEIRKLFIG TILVSLIEKS
TEVKIIKCII KMLDEWIKTK EPNVMTQVPS IREKSALLVK LMQNVEKKFT DEIELNIQFL
EIINFIYRDE ILKQTELTNK LEGAFLNGLR FQNPNVRSKF FEILDSSMRR RLHDRLLYII
CSQAWDTIGS HYWIKQCIEL LILTANTMMQ IQCSNEQFKI PSITSVIPVN SSETQENSFV
SFLSSHSESF DIIQTVDDKD DVYDIDLNAD RKEDCQQILP NRRVTLVELV YKQAEFLEAN
RNIRTDQMLV ATSQLCHIDT QLAQSVWLSM FPRIWSIFTE DQRCNITKEL IPFLSSGTNV
NQKDCHPSTL NTFVESLTKC APPIYIPPNL LAYLGKSHNL WHRAILVLED MAVNQSMQSK
DIDGGENQFS DLDVQQSNNI FDSLSKMYSS MHEEDLWAGL WLKFAHYPET NIAVSYEQMG
FFEEAQGAYD LAMTKFKQDL SNGVVNTYVN SELLLWENHW MRCAKELNQW DILLDYAQTN
KDKNMFLILE SSWRVPDWNL MKIALAKTEQ CYLKHYGFKI NLYKGYLSIL HQEERQTGNI
ERYVEIASSL CIREWRRLPN IVSHIHLPYL QASQQIMELH EASQIHQGLA QSRNNSLHDM
KAIVKTWRNR LPIISDDLSH WSDIFTWRQH HYQIITQHLE QQSDQGSTML GVHASAQAII
SFGKIARKHN LTGVCQETLS RIYTIPSVPI VDCFQKIRQQ VKCYLQMPST SGKNEINEAL
EVIESTNLKY FTGEMNAEFY ALKGLLLAQI GRSEEAGKSF SVAAQLHDGL TKAWAMWGDY
MEQIFLKERK ITLAVDALIC YLQASRNQIE SKTRKYIAKV LWFLSYDNNT KILISTLEKH
VAGIPPSYWL PWIPQLLCCL EQFEGDVILN LLSQIGRLYP QAVYFPIRTL YLTLKIEQRE
KHKTAEQAVK SSCSNIDGTT LSFGRGASHG NIPSINPIKA TPPMWRCSKV MQLQREVHPT
ILSSLEGIVD QMVWFRESWT EEVLRQLRQG LIKCYAIAFE KRDTVQHSTI TPHTLHFVKK
LGSTFGIGIE NVPGSVTSSI SNSAASESLA RRAQVTFQDP VFQKMKEQFT NDFDFSKPGA
MKLHNLISKL KTWIKVLETK VKKLPTSFLI EDKCRFLSNF SQKTAEVELP GELLIPLSSH
YYVRIARFMP RVEIVQKNNT AARRLYIRGT NGKIYPYLVV LDSGLGDARR EERVLQLKRM
LNYYLEKQKE TSRRFLNITV PRVVPISPQM RLAEDNPNSI SLLKIFKKCC QSMQVDYDMP
IVKYYDRLSE VQARGTPTTH TLLREIFSEI QWTMVPKTLL KHWALKTFLA ATDFWHFRKM
LTLQLALAFL CEHALNLTRL NADMMYLHQD SGLMNISYFK FDVNDDKCQL NQHRPVPFRL
TPNVGEFITH FGITGPLSAA IVATARCFIQ PNYKLSSILQ TILRDEIIAL QKKGFRECKL
IEGSEDRYSD GNCMEHSVNI VNSAVDIIMT RFNKISYFDS IENKKISVLV QSATNIDNLC
RMDPAWHPWL