MAML1_MOUSE
ID MAML1_MOUSE Reviewed; 1020 AA.
AC Q6T264; Q505D8; Q5SUC2; Q6PDK3; Q6ZQG5; Q8BIU5; Q8R3T0;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Mastermind-like protein 1;
DE Short=Mam-1;
GN Name=Maml1 {ECO:0000312|EMBL:AAS07633.1, ECO:0000312|MGI:MGI:1890504};
GN Synonyms=Kiaa0200 {ECO:0000312|EMBL:BAC97898.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAS07633.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH NOTCH1; NOTCH2; NOTCH3 AND NOTCH4.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAS07633.1};
RX PubMed=15019995; DOI=10.1016/j.gene.2003.12.007;
RA Wu L., Kobayashi K., Sun T., Gao P., Liu J., Nakamura M., Weisberg E.,
RA Mukhopadhyay N.K., Griffin J.D.;
RT "Cloning and functional characterization of the murine mastermind-like 1
RT (Maml1) gene.";
RL Gene 328:153-165(2004).
RN [2] {ECO:0000312|EMBL:BAC97898.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail {ECO:0000312|EMBL:BAC97898.1};
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH24668.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 130-1020.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH58658.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH24668.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH58658.1}, and
RC Mammary gland {ECO:0000312|EMBL:AAH24668.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-1020.
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 [6]
RP FUNCTION.
RX PubMed=15187027; DOI=10.1182/blood-2004-02-0514;
RA Maillard I., Weng A.P., Carpenter A.C., Rodriguez C.G., Sai H., Xu L.,
RA Allman D., Aster J.C., Pear W.S.;
RT "Mastermind critically regulates Notch-mediated lymphoid cell fate
RT decisions.";
RL Blood 104:1696-1702(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-1019, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-321, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Spleen;
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 [9]
RP INTERACTION WITH NOTCH1 AND MAML1.
RX PubMed=25038227; DOI=10.1158/0008-5472.can-14-1547;
RA Weaver K.L., Alves-Guerra M.C., Jin K., Wang Z., Han X., Ranganathan P.,
RA Zhu X., DaSilva T., Liu W., Ratti F., Demarest R.M., Tzimas C., Rice M.,
RA Vasquez-Del Carpio R., Dahmane N., Robbins D.J., Capobianco A.J.;
RT "NACK is an integral component of the Notch transcriptional activation
RT complex and is critical for development and tumorigenesis.";
RL Cancer Res. 74:4741-4751(2014).
CC -!- FUNCTION: Acts as a transcriptional coactivator for NOTCH proteins. Has
CC been shown to amplify NOTCH-induced transcription of HES1. Enhances
CC phosphorylation and proteolytic turnover of the NOTCH intracellular
CC domain in the nucleus through interaction with CDK8. Binds to
CC CREBBP/CBP which promotes nucleosome acetylation at NOTCH enhancers and
CC activates transcription. Induces phosphorylation and localization of
CC CREBBP to nuclear foci. Plays a role in hematopoietic development by
CC regulating NOTCH-mediated lymphoid cell fate decisions.
CC {ECO:0000269|PubMed:15019995, ECO:0000269|PubMed:15187027}.
CC -!- SUBUNIT: Interacts (via N-terminus) with NOTCH1, NOTCH2, NOTCH3 and
CC NOTCH4 (via ankyrin repeat region). Interacts (via N-terminus) with p53
CC (via DNA-binding region). Forms a DNA-binding complex with Notch
CC proteins and RBPSUH/RBP-J kappa/CBF1. Also binds CREBBP/CBP and CDK8.
CC Forms a complex with PRAG1, NOTCH1 and MAML1, in a MAML1-dependent
CC manner (PubMed:25038227). {ECO:0000269|PubMed:15019995,
CC ECO:0000269|PubMed:25038227}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15019995}.
CC Note=Nuclear, in a punctate manner.
CC -!- TISSUE SPECIFICITY: At E9.5, strongly expressed in the telencephalon,
CC first branchial arch, forelimb buds and somites. By 10.5 dpc,
CC continuously expressed in brain and spinal cord. Also expressed in
CC first and second branchial arches and limb buds. By 11.5 dpc,
CC expression in CNS is weak but increases in mesodermal tissues. At 14.5
CC dpc, detected in epithelial cells in trachea, esophagus and proximal
CC and distal tubules of the developing lungs.
CC {ECO:0000269|PubMed:15019995}.
CC -!- DOMAIN: The C-terminal region is required for transcriptional
CC activation. {ECO:0000269|PubMed:15019995}.
CC -!- SIMILARITY: Belongs to the mastermind family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH94599.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC39618.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC97898.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY442299; AAS07633.1; -; mRNA.
DR EMBL; AK129088; BAC97898.1; ALT_INIT; mRNA.
DR EMBL; AL646002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024668; AAH24668.1; -; mRNA.
DR EMBL; BC058658; AAH58658.1; -; mRNA.
DR EMBL; BC094599; AAH94599.2; ALT_INIT; mRNA.
DR EMBL; AK086146; BAC39618.1; ALT_INIT; mRNA.
DR CCDS; CCDS24632.2; -.
DR RefSeq; NP_780543.2; NM_175334.3.
DR AlphaFoldDB; Q6T264; -.
DR SMR; Q6T264; -.
DR BioGRID; 222170; 5.
DR CORUM; Q6T264; -.
DR IntAct; Q6T264; 6.
DR MINT; Q6T264; -.
DR STRING; 10090.ENSMUSP00000059210; -.
DR iPTMnet; Q6T264; -.
DR PhosphoSitePlus; Q6T264; -.
DR EPD; Q6T264; -.
DR jPOST; Q6T264; -.
DR MaxQB; Q6T264; -.
DR PaxDb; Q6T264; -.
DR PRIDE; Q6T264; -.
DR ProteomicsDB; 292014; -.
DR Antibodypedia; 29514; 243 antibodies from 35 providers.
DR DNASU; 103806; -.
DR Ensembl; ENSMUST00000059458; ENSMUSP00000059210; ENSMUSG00000050567.
DR GeneID; 103806; -.
DR KEGG; mmu:103806; -.
DR UCSC; uc007isd.2; mouse.
DR CTD; 9794; -.
DR MGI; MGI:1890504; Maml1.
DR VEuPathDB; HostDB:ENSMUSG00000050567; -.
DR eggNOG; ENOG502QSU1; Eukaryota.
DR GeneTree; ENSGT00950000183201; -.
DR HOGENOM; CLU_008569_1_0_1; -.
DR InParanoid; Q6T264; -.
DR OMA; KEMSSAH; -.
DR OrthoDB; 177202at2759; -.
DR PhylomeDB; Q6T264; -.
DR TreeFam; TF332922; -.
DR Reactome; R-MMU-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-MMU-350054; Notch-HLH transcription pathway.
DR Reactome; R-MMU-8941856; RUNX3 regulates NOTCH signaling.
DR BioGRID-ORCS; 103806; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Maml1; mouse.
DR PRO; PR:Q6T264; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6T264; protein.
DR Bgee; ENSMUSG00000050567; Expressed in left lung lobe and 229 other tissues.
DR ExpressionAtlas; Q6T264; baseline and differential.
DR Genevisible; Q6T264; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0002193; C:MAML1-RBP-Jkappa- ICN1 complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0042605; F:peptide antigen binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0060928; P:atrioventricular node cell development; IMP:BHF-UCL.
DR GO; GO:0045445; P:myoblast differentiation; IEP:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:UniProtKB.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IMP:UniProtKB.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; IGI:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; IGI:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR Gene3D; 6.10.250.970; -; 1.
DR InterPro; IPR046369; MAML1-3.
DR InterPro; IPR046370; MAML_N_sf.
DR InterPro; IPR019082; Mastermind-like_N.
DR PANTHER; PTHR15692; PTHR15692; 1.
DR Pfam; PF09596; MamL-1; 1.
DR SMART; SM01275; MamL-1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Notch signaling pathway; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1020
FT /note="Mastermind-like protein 1"
FT /id="PRO_0000129494"
FT REGION 1..97
FT /note="Required for interaction with NOTCH proteins"
FT /evidence="ECO:0000269|PubMed:15019995"
FT REGION 67..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92585"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92585"
FT MOD_RES 827
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92585"
FT MOD_RES 1019
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CONFLICT 574
FT /note="M -> T (in Ref. 4; AAH58658)"
FT /evidence="ECO:0000305"
FT CONFLICT 643..646
FT /note="Missing (in Ref. 1; AAS07633 and 2; BAC97898)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="P -> S (in Ref. 1; AAS07633)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="A -> P (in Ref. 5; BAC39618)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="A -> T (in Ref. 1; AAS07633)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="Q -> H (in Ref. 5; BAC39618)"
FT /evidence="ECO:0000305"
FT CONFLICT 822
FT /note="P -> L (in Ref. 1; AAS07633)"
FT /evidence="ECO:0000305"
FT CONFLICT 861
FT /note="S -> C (in Ref. 1; AAS07633)"
FT /evidence="ECO:0000305"
FT CONFLICT 1003
FT /note="N -> K (in Ref. 5; BAC39618)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1020 AA; 107726 MW; 637132736ECD3A78 CRC64;
MVLPTCPMAE FALPRHSAVM ERLRRRIELC RRHHSTCEAR YEAVSPERLE LERQHTFALH
QRCIQAKAKR AGKHRQPPAA ATAPVAAPAP ASAPAAARLD AADGPEHGRP VAHLHDTVKR
SLDSAASPQN GDQPNGYGDL FPGHKKTRRE APLGVSVSAN GLPPASPLGQ PDKPSGGDTL
QTAGKHSLGL DPINKKCLAD SGIHLNGGSN SSEPFPLSLS KELKQEPVDD LPCMIAGAGG
SVAQSNLMPD LNLNEQEWKE LIEELNRSVP DEDMKDLFTE DFEEKKDPEP PGSATQTPLA
QDINIKTEFS PAAFEQEQLG SPQVRAGSAG QTFLGASSAP VGTDSPSLGS SQTLFHTTSQ
PGVDNSSPNL MPASAQAQSA QRALTSVVLP SQGPGGASEL SSAHQLQQIA AKQKREQMLQ
NPQQAAPAPG PGQLATWQQA GPSHSPLDVP YPMEKPASPS GYKQDFTNSK LLMMPGVNKS
SPRPGGPYLQ PSHSNLLSHQ SPSNLNQNPV NNQGSVLDYG NTKPLSHYKA DCGQGGPGSG
QNKPALMAYL PQQLPHLSNE QNSLFLMKPK SGNMPFRSLV PPGQEQNPSS VPVAAPAASV
GTQPTVSVAS THNSSPYLSS QQQAAVMKQH QLLLDQQKQR EQQQQQLQQQ QFLQRQHLLA
EQEKQQFQRH LTRPPPQYQD PTQSTFPQQV GQFTGPSAAV PGMNNLGPSN SSCPRVFPQP
GTLMSMGPGH APVSSLPSSS GQQDRGVAQF TGSQSLPQNS LYGMASGLAQ IVAQPPPQAT
STHAHIPRQT NVGQNASTSA AYGQNSLGSA SLSQQHSKGT LPPGLTKPQV PRVSAAMGSQ
NASWQHQGMP NLSSQTSGNS SVNPFTAAPS FHIQQAHLKL AGQQFSQAMP SRPMAPLSSA
GAAGPMLPPV SAQQRNSAPA SAPPQAAPQQ GLPGLSPSGP ELGAFGQSPT SQMSGRPGLH
CAQAYPVRTM GQELPFAYSG QPGSSGLSSV AGHTDLIDSL LKNRTSEEWI NELDDLLGSQ
