ID   MGAP_HUMAN              Reviewed;        3026 AA.
AC   Q8IWI9; Q9H8R3; Q9H9N7; Q9UG69; Q9Y4E9;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   05-OCT-2010, entry version 61.
DE   RecName: Full=MAX gene-associated protein;
DE   AltName: Full=MAX dimerization protein 5;
GN   Name=MGA; Synonyms=KIAA0518, MAD5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 183-1134 (ISOFORM 1).
RC   TISSUE=Ovary, and Teratocarcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
RA   Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA   Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA   Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA   Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA   Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA   Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA   Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human
RT   chromosome 15.";
RL   Nature 440:671-675(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1139 (ISOFORM 1).
RC   TISSUE=Duodenum;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2377-3026 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=98290545; PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA   Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA   Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. IX.
RT   The complete sequences of 100 new cDNA clones from brain which can
RT   code for large proteins in vitro.";
RL   DNA Res. 5:31-39(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2778-3026 (ISOFORM 1).
RC   TISSUE=Uterus;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX   PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA   Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA   Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT   "Physical association and coordinate function of the H3 K4
RT   methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL   Cell 121:873-885(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1973, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924; SER-1208 AND
RP   SER-1457, AND MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; SER-449; SER-607;
RP   SER-924 AND SER-2882, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645; SER-2496; SER-2502
RP   AND SER-2871, AND MASS SPECTROMETRY.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
CC   -!- FUNCTION: Functions as a dual-specificity transcription factor,
CC       regulating the expression of both MAX-network and T-box family
CC       target genes. Functions as a repressor or an activator. Binds to
CC       5'-AATTTCACACCTAGGTGTGAAATT-3' core sequence and seems to regulate
CC       MYC-MAX target genes. Suppresses transcriptional activation by MYC
CC       and inhibits MYC-dependent cell transformation. Function activated
CC       by heterodimerization with MAX. This heterodimerization serves the
CC       dual function of both generating an E-box-binding heterodimer and
CC       simultaneously blocking interaction of a corepressor (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with MAX. Requires dimerization with MAX for E-
CC       box binding (By similarity). Component of some MLL1/MLL complex,
CC       at least composed of the core components MLL, ASH2L, HCFC1/HCF1,
CC       WDR5 and RBBP5, as well as the facultative components C17orf49,
CC       CHD8, E2F6, HSP70, IN80C, KIAA1267, LAS1L, MAX, MCRS1, MGA,
CC       MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
CC       SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8IWI9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IWI9-2; Sequence=VSP_034534, VSP_034535;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: Transcription repression is enhanced or dependent on the
CC       presence of the T-box DNA-binding domain (By similarity).
CC   -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain.
CC   -!- SIMILARITY: Contains 1 T-box DNA-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB14186.1; Type=Erroneous initiation;
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DR   EMBL; AK022696; BAB14186.1; ALT_INIT; mRNA.
DR   EMBL; AK023360; BAB14543.1; -; mRNA.
DR   EMBL; AC016134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC073657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC038449; AAH38449.1; -; mRNA.
DR   EMBL; AB011090; BAA25444.1; -; mRNA.
DR   EMBL; AL050181; CAB43310.1; -; mRNA.
DR   IPI; IPI00741005; -.
DR   IPI; IPI00943971; -.
DR   PIR; T00081; T00081.
DR   RefSeq; NP_001074010.2; -.
DR   UniGene; Hs.187569; -.
DR   HSSP; O15119; 1H6F.
DR   ProteinModelPortal; Q8IWI9; -.
DR   SMR; Q8IWI9; 75-260, 2386-2458.
DR   IntAct; Q8IWI9; 2.
DR   MINT; MINT-1183008; -.
DR   STRING; Q8IWI9; -.
DR   PRIDE; Q8IWI9; -.
DR   Ensembl; ENST00000389936; ENSP00000374586; ENSG00000174197.
DR   GeneID; 23269; -.
DR   KEGG; hsa:23269; -.
DR   UCSC; uc001zoh.1; human.
DR   CTD; 23269; -.
DR   GeneCards; GC15P041952; -.
DR   H-InvDB; HIX0012158; -.
DR   HGNC; HGNC:14010; MGA.
DR   PharmGKB; PA134976336; -.
DR   HOVERGEN; HBG108131; -.
DR   InParanoid; Q8IWI9; -.
DR   ArrayExpress; Q8IWI9; -.
DR   Bgee; Q8IWI9; -.
DR   CleanEx; HS_MGA; -.
DR   Genevestigator; Q8IWI9; -.
DR   GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR   GO; GO:0003700; F:transcription factor activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR011598; HLH_DNA-bd.
DR   InterPro; IPR001092; HLH_DNA-bd_dom.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR001699; TF_T-box.
DR   InterPro; IPR018186; TF_T-box_CS.
DR   Gene3D; G3DSA:4.10.280.10; HLH_DNA_bd; 1.
DR   Gene3D; G3DSA:2.60.40.820; TF_T-box; 1.
DR   PANTHER; PTHR11267; TF_T-box; 1.
DR   Pfam; PF00010; HLH; 1.
DR   Pfam; PF00907; T-box; 1.
DR   PRINTS; PR00937; TBOX.
DR   SMART; SM00353; HLH; 1.
DR   SMART; SM00425; TBOX; 1.
DR   SUPFAM; SSF47459; HLH_basic; 1.
DR   SUPFAM; SSF49417; P53_like_DNA_bnd; 1.
DR   PROSITE; PS50888; HLH; 1.
DR   PROSITE; PS01283; TBOX_1; FALSE_NEG.
DR   PROSITE; PS01264; TBOX_2; 1.
DR   PROSITE; PS50252; TBOX_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Complete proteome; DNA-binding;
KW   Nucleus; Phosphoprotein; Polymorphism; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   3026       MAX gene-associated protein.
FT                                /FTId=PRO_0000342692.
FT   DOMAIN     2384   2436       Helix-loop-helix motif.
FT   DNA_BIND     84    260       T-box.
FT   DNA_BIND   1876   2383       Basic motif.
FT   COILED     1111   1147       Potential.
FT   COILED     2778   2802       Potential.
FT   COMPBIAS    967    981       Gln-rich.
FT   COMPBIAS   1255   1263       Poly-Ser.
FT   COMPBIAS   1594   1714       Thr-rich.
FT   MOD_RES     448    448       Phosphoserine.
FT   MOD_RES     449    449       Phosphoserine.
FT   MOD_RES     607    607       Phosphoserine.
FT   MOD_RES     645    645       Phosphoserine.
FT   MOD_RES     924    924       Phosphoserine.
FT   MOD_RES    1208   1208       Phosphoserine.
FT   MOD_RES    1457   1457       Phosphoserine.
FT   MOD_RES    1973   1973       Phosphoserine.
FT   MOD_RES    2496   2496       Phosphoserine.
FT   MOD_RES    2502   2502       Phosphoserine.
FT   MOD_RES    2871   2871       Phosphoserine.
FT   MOD_RES    2882   2882       Phosphoserine.
FT   VAR_SEQ       1   1790       Missing (in isoform 2).
FT                                /FTId=VSP_034534.
FT   VAR_SEQ    2488   3026       Missing (in isoform 2).
FT                                /FTId=VSP_034535.
FT   VARIANT     338    338       T -> A (in dbSNP:rs3803348).
FT                                /FTId=VAR_044341.
FT   VARIANT     716    716       S -> T (in dbSNP:rs2178004).
FT                                /FTId=VAR_044342.
FT   VARIANT    1270   1270       C -> R (in dbSNP:rs17677811).
FT                                /FTId=VAR_044343.
FT   VARIANT    1523   1523       P -> A (in dbSNP:rs17677991).
FT                                /FTId=VAR_057268.
FT   VARIANT    1572   1572       P -> A (in dbSNP:rs17677991).
FT                                /FTId=VAR_044344.
FT   CONFLICT    266    266       K -> N (in Ref. 1; BAB14186).
FT   CONFLICT    742    742       S -> R (in Ref. 1; BAB14186).
FT   CONFLICT   1138   1138       R -> K (in Ref. 3; AAH38449).
FT   CONFLICT   2191   2191       Missing (in Ref. 1; BAB14543).
FT   CONFLICT   2326   2326       A -> T (in Ref. 1; BAB14543).
SQ   SEQUENCE   3026 AA;  331822 MW;  8697BA2C6BADEA0A CRC64;
     MEEKQQIILA NQDGGTVAGA APTFFVILKQ PGNGKTDQGI LVTNQDACAL ASSVSSPVKS
     KGKICLPADC TVGGITVTLD NNSMWNEFYH RSTEMILTKQ GRRMFPYCRY WITGLDSNLK
     YILVMDISPV DNHRYKWNGR WWEPSGKAEP HVLGRVFIHP ESPSTGHYWM HQPVSFYKLK
     LTNNTLDQEG HIILHSMHRY LPRLHLVPAE KAVEVIQLNG PGVHTFTFPQ TEFFAVTAYQ
     NIQITQLKID YNPFAKGFRD DGLNNKPQRD GKQKNSSDQE GNNISSSSGH RVRLTEGQGS
     EIQPGDLDPL SRGHETSGKG LEKTSLNIKR DFLGFMDTDS ALSEVPQLKQ EISECLIASS
     FEDDSRVASP LDQNGSFNVV IKEEPLDDYD YELGECPEGV TVKQEETDEE TDVYSNSDDD
     PILEKQLKRH NKVDNPEADH LSSKWLPSSP SGVAKAKMFK LDTGKMPVVY LEPCAVTRST
     VKISELPDNM LSTSRKDKSS MLAELEYLPT YIENSNETAF CLGKESENGL RKHSPDLRVV
     QKYPLLKEPQ WKYPDISDSI STERILDDSK DSVGDSLSGK EDLGRKRTTM LKIATAAKVV
     NANQNASPNV PGKRGRPRKL KLCKAGRPPK NTGKSLISTK NTPVSPGSTF PDVKPDLEDV
     DGVLFVSFES KEALDIHAVD GTTEESSSLQ ASTTNDSGYR ARISQLEKEL IEDLKSLRHK
     QVIHPGLQEV GLKLNSVDPT MSIDLKYLGV QLPLAPATSF PFWNLTGTNP ASPDAGFPFV
     SRTGKTNDFT KIKGWRGKFH SASASRNEGG NSESSLKNRS AFCSDKLDEY LENEGKLMET
     SMGFSSNAPT SPVVYQLPTK STSYVRTLDS VLKKQSTISP STSYSLKPHS VPPVSRKAKS
     QNRQATFSGR TKSSYKSILP YPVSPKQKYS HVILGDKVTK NSSGIISENQ ANNFVVPTLD
     ENIFPKQISL RQAQQQQQQQ QGSRPPGLSK SQVKLMDLED CALWEGKPRT YITEERADVS
     LTTLLTAQAS LKTKPIHTII RKRAPPCNND FCRLGCVCSS LALEKRQPAH CRRPDCMFGC
     TCLKRKVVLV KGGSKTKHFQ RKAAHRDPVF YDTLGEEARE EEEGIREEEE QLKEKKKRKK
     LEYTICETEP EQPVRHYPLW VKVEGEVDPE PVYIPTPSVI EPMKPLLLPQ PEVLSPTVKG
     KLLTGIKSPR SYTPKPNPVI REEDKDPVYL YFESMMTCAR VRVYERKKED QRQPSSSSSP
     SPSFQQQTSC HSSPENHNNA KEPDSEQQPL KQLTCDLEDD SDKLQEKSWK SSCNEGESSS
     TSYMHQRSPG GPTKLIEIIS DCNWEEDRNK ILSILSQHIN SNMPQSLKVG SFIIELASQR
     KSRGEKNPPV YSSRVKISMP SCQDQDDMAE KSGSETPDGP LSPGKMEDIS PVQTDALDSV
     RERLHGGKGL PFYAGLSPAG KLVAYKRKPS SSTSGLIQVA SNAKVAASRK PRTLLPSTSN
     SKMASSSGTA TNRPGKNLKA FVPAKRPIAA RPSPGGVFTQ FVMSKVGALQ QKIPGVSTPQ
     TLAGTQKFSI RPSPVMVVTP VVSSEPVQVC SPVTAAVTTT TPQVFLENTT AVTPMTAISD
     VETKETTYSS GATTTGVVEV SETNTSTSVT STQSTATVNL TKTTGITTPV ASVAFPKSLV
     ASPSTITLPV ASTASTSLVV VTAAASSSMV TTPTSSLGSV PIILSGINGS PPVSQRPENA
     AQIPVATPQV SPNTVKRAGP RLLHPNGQIV QLLPLHQLRG SNTQPNLQPV MFRNPGSVMG
     IRLPAPSKPS ETPPSSTSSS AFSVMNPVIQ AVGSSSAVNV ITQAPSLLSS GASFVSQAGT
     LTLRISPPEP QSFASKTGSE TKITYSSGGQ PVGTASLIPL QSGSFALLQL PGQKPVPSSI
     LQHVASLQMK RESQNPDQKD ETNSIKREQE TKKVLQSEGE AVDPEANVIK QNSGAATSEE
     TLNDSLEDRG DHLDEECLPE EGCATVKPSE HSCITGSHTD QDYKDVNEEY GARNRKSSKE
     KVAVLEVRTI SEKASNKTVQ NLSKVQHQKL GDVKVEQQKG FDNPEENSSE FPVTFKEESK
     FELSGSKVME QQSNLQPEAK EKECGDSLEK DRERWRKHLK GPLTRKCVGA SQECKKEADE
     QLIKETKTCQ ENSDVFQQEQ GISDLLGKSG ITEDARVLKT ECDSWSRISN PSAFSIVPRR
     AAKSSRGNGH FQGHLLLPGE QIQPKQEKKG GRSSADFTVL DLEEDDEDDN EKTDDSIDEI
     VDVVSDYQSE EVDDVEKNNC VEYIEDDEEH VDIETVEELS EEINVAHLKT TAAHTQSFKQ
     PSCTHISADE KAAERSRKAP PIPLKLKPDY WSDKLQKEAE AFAYYRRTHT ANERRRRGEM
     RDLFEKLKIT LGLLHSSKVS KSLILTRAFS EIQGLTDQAD KLIGQKNLLT RKRNILIRKV
     SSLSGKTEEV VLKKLEYIYA KQQALEAQKR KKKMGSDEFD ISPRISKQQE GSSASSVDLG
     QMFINNRRGK PLILSRKKDQ ATENTSPLNT PHTSANLVMT PQGQLLTLKG PLFSGPVVAV
     SPDLLESDLK PQVAGSAVAL PENDDLFMMP RIVNVTSLAT EGGLVDMGGS KYPHEVPDSK
     PSDHLKDTVR NEDNSLEDKG RISSRGNRDG RVTLGPTQVF LANKDSGYPQ IVDVSNMQKA
     QEFLPKKISG DMRGIQYKWK ESESRGERVK SKDSSFHKLK MKDLKDSSIE MELRKVTSAI
     EEAALDSSEL LTNMEDEDDT DETLTSLLNE IAFLNQQLND DSVGLAELPS SMDTEFPGDA
     RRAFISKVPP GSRATFQVEH LGTGLKELPD VQGESDSISP LLLHLEDDDF SENEKQLAEP
     ASEPDVLKIV IDSEIKDSLL SNKKAIDGGK NTSGLPAEPE SVSSPPTLHM KTGLENSNST
     DTLWRPMPKL APLGLKVANP SSDADGQSLK VMPCLAPIAA KVGSVGHKMN LTGNDQEGRE
     SKVMPTLAPV VAKLGNSGAS PSSAGK
//