TACC2_MOUSE
ID TACC2_MOUSE Reviewed; 1149 AA.
AC Q9JJG0; Q3TN02; Q811U0; Q8BQD4; Q99KQ6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Transforming acidic coiled-coil-containing protein 2;
GN Name=Tacc2; ORFNames=MNCb-3527;
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 [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=15207008; DOI=10.1186/1471-2148-4-16;
RA Still I.H., Vettaikkorumakankauv A.K., DiMatteo A., Liang P.;
RT "Structure-function evolution of the transforming acidic coiled coil genes
RT revealed by analysis of phylogenetically diverse organisms.";
RL BMC Evol. Biol. 4:16-16(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15226440; DOI=10.1128/mcb.24.14.6403-6409.2004;
RA Schuendeln M.M., Piekorz R.P., Wichmann C., Lee Y., McKinnon P.J., Boyd K.,
RA Takahashi Y., Ihle J.N.;
RT "The centrosomal, putative tumor suppressor protein TACC2 is dispensable
RT for normal development, and deficiency does not lead to cancer.";
RL Mol. Cell. Biol. 24:6403-6409(2004).
RN [6]
RP FUNCTION, INTERACTION WITH CCDC100, AND SUBCELLULAR LOCATION.
RX PubMed=17920017; DOI=10.1016/j.neuron.2007.08.026;
RA Xie Z., Moy L.Y., Sanada K., Zhou Y., Buchman J.J., Tsai L.-H.;
RT "Cep120 and TACCs control interkinetic nuclear migration and the neural
RT progenitor pool.";
RL Neuron 56:79-93(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510 AND SER-714, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354; SER-510; SER-514;
RP THR-516; SER-552; SER-585; SER-714 AND THR-755, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, 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).
CC -!- FUNCTION: Plays a role in the microtubule-dependent coupling of the
CC nucleus and the centrosome. Involved in the processes that regulate
CC centrosome-mediated interkinetic nuclear migration (INM) of neural
CC progenitors. May play a role in organizing centrosomal microtubules (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:15226440,
CC ECO:0000269|PubMed:17920017}.
CC -!- SUBUNIT: Interacts with microtubules. Interacts with YEATS4, GCN5L2 and
CC PCAF (By similarity). Interacts with CCDC100/CEP120. {ECO:0000250,
CC ECO:0000269|PubMed:17920017}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95359}. Nucleus
CC {ECO:0000250|UniProtKB:O95359}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:O95359}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9JJG0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JJG0-2; Sequence=VSP_022160, VSP_022161;
CC Name=3;
CC IsoId=Q9JJG0-3; Sequence=VSP_022160, VSP_022161, VSP_022162,
CC VSP_022164, VSP_022165;
CC Name=4;
CC IsoId=Q9JJG0-4; Sequence=VSP_022159, VSP_022162, VSP_022163,
CC VSP_022164, VSP_022165;
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney, lung, thymus and ovary.
CC Not detectable in normal tissues at protein level.
CC {ECO:0000269|PubMed:15226440}.
CC -!- PTM: Phosphorylated; which is required for localization in centrosome.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally, are fertile, and do not
CC present elevated tumorization rates. Cells deficient in TACC2 divide
CC normally and do not show any change in the frequency of apoptosis
CC induction. {ECO:0000269|PubMed:15226440}.
CC -!- SIMILARITY: Belongs to the TACC family. {ECO:0000305}.
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DR EMBL; AY177410; AAO18641.1; -; mRNA.
DR EMBL; AB041546; BAA95031.1; -; mRNA.
DR EMBL; AK050985; BAC34486.1; -; mRNA.
DR EMBL; AK165603; BAE38287.1; -; mRNA.
DR EMBL; BC004057; AAH04057.1; -; mRNA.
DR CCDS; CCDS85432.1; -. [Q9JJG0-3]
DR RefSeq; NP_001334566.1; NM_001347637.1. [Q9JJG0-3]
DR RefSeq; NP_067289.2; NM_021314.4.
DR RefSeq; NP_996738.2; NM_206856.3.
DR AlphaFoldDB; Q9JJG0; -.
DR SMR; Q9JJG0; -.
DR IntAct; Q9JJG0; 1.
DR STRING; 10090.ENSMUSP00000081561; -.
DR iPTMnet; Q9JJG0; -.
DR EPD; Q9JJG0; -.
DR jPOST; Q9JJG0; -.
DR MaxQB; Q9JJG0; -.
DR PaxDb; Q9JJG0; -.
DR PeptideAtlas; Q9JJG0; -.
DR PRIDE; Q9JJG0; -.
DR ProteomicsDB; 263057; -. [Q9JJG0-1]
DR ProteomicsDB; 263058; -. [Q9JJG0-2]
DR ProteomicsDB; 263059; -. [Q9JJG0-3]
DR ProteomicsDB; 263060; -. [Q9JJG0-4]
DR Antibodypedia; 46332; 272 antibodies from 20 providers.
DR DNASU; 57752; -.
DR Ensembl; ENSMUST00000207282; ENSMUSP00000146848; ENSMUSG00000030852. [Q9JJG0-3]
DR GeneID; 57752; -.
DR KEGG; mmu:57752; -.
DR UCSC; uc009kag.1; mouse. [Q9JJG0-3]
DR UCSC; uc009kan.1; mouse. [Q9JJG0-4]
DR CTD; 10579; -.
DR MGI; MGI:1928899; Tacc2.
DR VEuPathDB; HostDB:ENSMUSG00000030852; -.
DR eggNOG; ENOG502QUT1; Eukaryota.
DR GeneTree; ENSGT00940000157052; -.
DR InParanoid; Q9JJG0; -.
DR OrthoDB; 669540at2759; -.
DR PhylomeDB; Q9JJG0; -.
DR BioGRID-ORCS; 57752; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Tacc2; mouse.
DR PRO; PR:Q9JJG0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JJG0; protein.
DR Bgee; ENSMUSG00000030852; Expressed in hindlimb stylopod muscle and 259 other tissues.
DR ExpressionAtlas; Q9JJG0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0030953; P:astral microtubule organization; IDA:MGI.
DR GO; GO:0008283; P:cell population proliferation; IBA:GO_Central.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0022027; P:interkinetic nuclear migration; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0007052; P:mitotic spindle organization; IEA:InterPro.
DR GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR GO; GO:0032886; P:regulation of microtubule-based process; IMP:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR InterPro; IPR039915; TACC.
DR InterPro; IPR007707; TACC_C.
DR PANTHER; PTHR13924; PTHR13924; 1.
DR Pfam; PF05010; TACC_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1149
FT /note="Transforming acidic coiled-coil-containing protein
FT 2"
FT /id="PRO_0000179989"
FT DOMAIN 508..596
FT /note="SPAZ"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 877..905
FT /evidence="ECO:0000255"
FT COILED 948..1148
FT /evidence="ECO:0000255"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..186
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95359"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95359"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95359"
FT MOD_RES 439
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95359"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 516
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95359"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95359"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95359"
FT MOD_RES 632
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95359"
FT MOD_RES 653
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95359"
FT MOD_RES 657
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95359"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95359"
FT MOD_RES 755
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95359"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95359"
FT VAR_SEQ 1..489
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022159"
FT VAR_SEQ 1..114
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.2"
FT /id="VSP_022160"
FT VAR_SEQ 115..137
FT /note="AAGPGVEVTPTGSPQHLAKNEPR -> MGGSQSLQPAPASDLNLEVSEAM
FT (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.2"
FT /id="VSP_022161"
FT VAR_SEQ 619..630
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_022162"
FT VAR_SEQ 717
FT /note="E -> EGKQLGGQPDPHLALENTVPRGQRARK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022163"
FT VAR_SEQ 835..911
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_022164"
FT VAR_SEQ 1000..1007
FT /note="PGTERKIL -> EDEQREKSI (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_022165"
FT CONFLICT 681
FT /note="Q -> K (in Ref. 3; BAC34486)"
FT /evidence="ECO:0000305"
FT CONFLICT 1129..1132
FT /note="NKEI -> DKQR (in Ref. 3; BAC34486)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1149 AA; 124130 MW; 9B4A46B38747898E CRC64;
MGNENSTSDH QRTSSVQSPR SLQPPGKSQS LQKQQGDLPG SCAGSIPGTD DVIQPAAPVD
PGHPPLAGIG SNQGEVCTSL QLSYTIVTVQ SASPSAARAS PAPLAPEHTA SAPSAAGPGV
EVTPTGSPQH LAKNEPRSSD SEEAFETPES TTPVKAPPAP PPPPPEVTPE PEVIDPPAPE
EPGCISEPPV VVPDGPRSSE SVEGSPFRPS HSSSAVFDED KPIASSGTYN LDFDSIELVD
NFQSLEPCSA DSKGQECKVS TRRKSTESVP PSKSTLSRSL SLQASDFDGA SCPGSPEAGT
LTTDACGTGS NSASSTLKRT KKTRPPSLKK KQATKKPTET PPVKETQQEP GEESPVPSEE
HLAPETKTES ATPEGAGCTL SDDTPLESPA VPTATCPLTL ESAEDVSPLV SGGGRVQNSP
PVGRKSVPLT TASEAVEVTL SDSGGQEDLP AKGLSVRLEF DYSEDKGSWE SQQENAPPTK
KIGKKPVAKM PLRRPKMKKT PEKLDNTPAS PPRSPTEPSD TPIAKGTYTF DIDKWDDPNF
NPFSSTSKMQ ESPKLSQQSY NFDPDACEES LDPFKASSKT PSSPSKSPAS FEIPASTTEA
DGDGLNKPAK KKKTPLKTMV EDVMSVCSLF DTFRVKKSPK RSPLSDPPSQ DPTPAATPEA
PSAISTVVHA TDEEKLAVTS QKWTCMTVDL DADKQDFPQP SDLSNFVNET KFNSPSEELD
YRNSYEIEYM EKLGSSLPQD DDTPKKQALY LMFDTPQESP VKSPPVRMSD SPTPCSGSSF
EDTEALVNAA TKLQHPVARG LPSSQEPLLQ VPEKPSQKEL EAMALGTPAE AIEITAPEGA
FASADTLLSR LAHPASLCGA LGYLEPDLAE KNPPVFAQKL QEELEFAVMR IEALKLARQI
ALASRSRQDT KREAAHPPDV SISKTALYSR IGSTEVEKPP GLLFQQPDLD SALQVARAEV
IAKEREVSEW RDKYEESRRE VVEMRKIVAE YEKTIAQMIP GTERKILSHQ TVQQLVLEKE
QALADLNSVE KSLADLFRRY EKMKEVLEGF RKNEEVLKKC AQEYLSRVKK EEQRYQALKV
HAEEKLDRAN AEIAQVRGKA QQEQAAYQAS LRKEQLRVDA LERTLEQKNK EIEELTKICD
ELIAKMGKS
