DACH1_MOUSE
ID DACH1_MOUSE Reviewed; 751 AA.
AC Q9QYB2; B2RUG1; O88716; Q8BPQ0; Q8C8D7; Q9QY47; Q9R218; Q9Z0Y5;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Dachshund homolog 1;
DE Short=Dach1;
GN Name=Dach1; Synonyms=Dach;
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), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=10502110; DOI=10.1007/s004270050286;
RA Kozmik Z., Pfeffer P., Kralova J., Paces J., Paces V., Kalousova A.,
RA Cvekl A.;
RT "Molecular cloning and expression of the human and mouse homologues of the
RT Drosophila dachshund gene.";
RL Dev. Genes Evol. 209:537-545(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND DEVELOPMENTAL STAGE.
RC TISSUE=Limb bud;
RX PubMed=9915577;
RX DOI=10.1002/(sici)1097-0177(199901)214:1<66::aid-dvdy7>3.0.co;2-7;
RA Caubit X., Thangarajah R., Theil T., Wirth J., Nothwang H.-G., Ruether U.,
RA Krauss S.;
RT "Mouse Dac, a novel nuclear factor with homology to Drosophila dachshund
RT shows a dynamic expression in the neural crest, the eye, the neocortex, and
RT the limb bud.";
RL Dev. Dyn. 214:66-80(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10502109; DOI=10.1007/s004270050285;
RA Davis R.J., Shen W., Heanue T.A., Mardon G.;
RT "Mouse Dach, a homologue of Drosophila dachshund, is expressed in the
RT developing retina, brain and limbs.";
RL Dev. Genes Evol. 209:526-536(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
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 113-751 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Eye;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 180-751 (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RX PubMed=9651501; DOI=10.1016/s0925-4773(98)00071-9;
RA Hammond K.L., Hanson I.M., Brown A.G., Lettice L.A., Hill R.E.;
RT "Mammalian and Drosophila dachshund genes are related to the Ski proto-
RT oncogene and are expressed in eye and limb.";
RL Mech. Dev. 74:121-131(1998).
RN [7]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=12215533; DOI=10.1128/mcb.22.19.6759-6766.2002;
RA Ikeda K., Watanabe Y., Ohto H., Kawakami K.;
RT "Molecular interaction and synergistic activation of a promoter by Six,
RT Eya, and Dach proteins mediated through CREB binding protein.";
RL Mol. Cell. Biol. 22:6759-6766(2002).
RN [8]
RP FUNCTION, AND INTERACTION WITH SIX6; NCOR1; HDAC3 AND SIN3A.
RX PubMed=12130660; DOI=10.1126/science.1073263;
RA Li X., Perissi V., Liu F., Rose D.W., Rosenfeld M.G.;
RT "Tissue-specific regulation of retinal and pituitary precursor cell
RT proliferation.";
RL Science 297:1180-1183(2002).
RN [9]
RP FUNCTION, AND INTERACTION WITH SIX1 AND EYA3.
RX PubMed=14628042; DOI=10.1038/nature02083;
RA Li X., Oghi K.A., Zhang J., Krones A., Bush K.T., Glass C.K., Nigam S.K.,
RA Aggarwal A.K., Maas R., Rose D.W., Rosenfeld M.G.;
RT "Eya protein phosphatase activity regulates Six1-Dach-Eya transcriptional
RT effects in mammalian organogenesis.";
RL Nature 426:247-254(2003).
RN [10]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11543628; DOI=10.1006/geno.2001.6618;
RA Ayres J.A., Shum L., Akarsu A.N., Dashner R., Takahashi K., Ikura T.,
RA Slavkin H.C., Nuckolls G.H.;
RT "Dach: genomic characterization, evaluation as a candidate for postaxial
RT polydactyly type A2, and developmental expression pattern of the mouse
RT homolog.";
RL Genomics 77:18-26(2001).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
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: Transcription factor that is involved in regulation of
CC organogenesis. Seems to be a regulator of SIX1, SIX6 and probably SIX5.
CC Corepression of precursor cell proliferation in myoblasts by SIX1 is
CC switched to coactivation through recruitment of EYA3 to the SIX1-DACH1
CC complex. Transcriptional activation seems also to involve association
CC of CREBBP. Seems to act as a corepressor of SIX6 in regulating
CC proliferation by directly repressing cyclin-dependent kinase
CC inhibitors, including the p27Kip1 promoter. Inhibits TGF-beta signaling
CC through interaction with SMAD4 and NCOR1 (By similarity). Binds to
CC chromatin DNA via its DACHbox-N domain. {ECO:0000250,
CC ECO:0000269|PubMed:12130660, ECO:0000269|PubMed:12215533,
CC ECO:0000269|PubMed:14628042}.
CC -!- SUBUNIT: Interacts with SIX1, SIX6 and EYA3. Interacts with NCOR1 and
CC HDAC3 through its N-terminus. Interacts with SIN3A through its C-
CC terminus. Interacts with SMAD3 and SMAD4 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9QYB2; Q60974: Ncor1; NbExp=2; IntAct=EBI-348961, EBI-349004;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QYB2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QYB2-2; Sequence=VSP_009489;
CC -!- TISSUE SPECIFICITY: Expressed at higher levels in adult kidney and
CC lung, and at lower levels in brain and testis. Expressed in embryonal
CC kidneys, eyes, cochleae and limb buds. {ECO:0000269|PubMed:10502110,
CC ECO:0000269|PubMed:11543628}.
CC -!- DEVELOPMENTAL STAGE: Highest expression was found at 11.5 dpc, and
CC expression rapidly declines at later stages of the development. Between
CC 8.0 and 13.5 dpc is found in neural crest cells during their pre-
CC migratory, migratory, and, in some cases post-migratory phase
CC throughout the body axis. Also found in lateral mesenchyme of trunk and
CC head. At 10 and 12 dpc found in mesonephric tubules. At 16 dpc found in
CC epithalial cells of metanephric 'comma' and 'S'-shaped bodies, in
CC mesenchymal cells of the medulla and the cortex. Colocalized to the
CC nucleus of glomerular podocytes and epithelial cells lining many of the
CC convoluted tubes. At 10.5 dpc found in both the anterior and posterior
CC of the limb bud. At 11.5 dpc expression becomes increasingly
CC peripheral, extending around the entire handplate in the mesenchymal
CC cells underlying the apical ectodermal ridge. At 12.5 dpc expression is
CC entirely peripheral an by 13.5 dpc is localized to the mesenchyme at
CC the distal tips of the digits. At 10 dpc found in cells of the optic
CC cup and in some cells surrounding the eye. At 12 dpc found in
CC developing lens fibers, the ectoderm overlaying the developing eye and
CC less intensely in the retina. At 12 dpc found in cells of the
CC dorsomedial and dorsolateral epithelium of the otic vesicle. At later
CC stages expressed in only a few specialized cell types of the cochlear
CC duct, including the inner and outer hair cells, stria vascularis, and
CC the mesenchymal cells directly underlying the organ of Corti. From 10.5
CC to 12.5 dpc expressed in the telencephalon including the olfactory
CC bulbs, throughout the length of the neural tube and within the dorsal
CC root ganglia, in cranial ganglia in the trigeminal ganglion and the
CC glossopharyngeal-vagal ganglion complex. At 10.5 and 11.5 dpc expressed
CC in punctate pattern on the ventral side of the embryo between the fore
CC and hind limbs, the rib primordia; this expression disappears by 12.5
CC dpc. At 11.5 and 12.5 dpc found in genital eminence.
CC {ECO:0000269|PubMed:10502110, ECO:0000269|PubMed:11543628,
CC ECO:0000269|PubMed:9651501, ECO:0000269|PubMed:9915577}.
CC -!- DOMAIN: The DACHbox-N/DD1 domain forms a structure containing a DNA
CC binding motif similar to that of the forkhead/winged helix domain.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DACH/dachshund family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA06665.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF102547; AAF04742.1; -; mRNA.
DR EMBL; AF090436; AAD16097.1; -; mRNA.
DR EMBL; AF090437; AAD16098.1; -; mRNA.
DR EMBL; AF129510; AAF22955.1; -; mRNA.
DR EMBL; BC141130; AAI41131.1; -; mRNA.
DR EMBL; AK053594; BAC35441.1; -; mRNA.
DR EMBL; AK047409; BAC33046.1; -; mRNA.
DR EMBL; AJ005669; CAA06665.1; ALT_INIT; mRNA.
DR CCDS; CCDS36993.1; -. [Q9QYB2-2]
DR CCDS; CCDS36994.1; -. [Q9QYB2-1]
DR RefSeq; NP_001033699.1; NM_001038610.2. [Q9QYB2-2]
DR RefSeq; NP_031852.1; NM_007826.3. [Q9QYB2-1]
DR AlphaFoldDB; Q9QYB2; -.
DR SMR; Q9QYB2; -.
DR BioGRID; 199044; 8.
DR CORUM; Q9QYB2; -.
DR IntAct; Q9QYB2; 5.
DR STRING; 10090.ENSMUSP00000071464; -.
DR iPTMnet; Q9QYB2; -.
DR PhosphoSitePlus; Q9QYB2; -.
DR MaxQB; Q9QYB2; -.
DR PaxDb; Q9QYB2; -.
DR PRIDE; Q9QYB2; -.
DR ProteomicsDB; 279309; -. [Q9QYB2-1]
DR ProteomicsDB; 279310; -. [Q9QYB2-2]
DR Antibodypedia; 72801; 315 antibodies from 37 providers.
DR DNASU; 13134; -.
DR Ensembl; ENSMUST00000069334; ENSMUSP00000064970; ENSMUSG00000055639. [Q9QYB2-2]
DR Ensembl; ENSMUST00000071533; ENSMUSP00000071464; ENSMUSG00000055639. [Q9QYB2-1]
DR GeneID; 13134; -.
DR KEGG; mmu:13134; -.
DR UCSC; uc007uur.2; mouse. [Q9QYB2-1]
DR UCSC; uc007uus.2; mouse. [Q9QYB2-2]
DR CTD; 1602; -.
DR MGI; MGI:1277991; Dach1.
DR VEuPathDB; HostDB:ENSMUSG00000055639; -.
DR eggNOG; KOG3915; Eukaryota.
DR GeneTree; ENSGT00390000001134; -.
DR HOGENOM; CLU_027923_0_0_1; -.
DR InParanoid; Q9QYB2; -.
DR OMA; VSHPLNH; -.
DR PhylomeDB; Q9QYB2; -.
DR TreeFam; TF316697; -.
DR BioGRID-ORCS; 13134; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Dach1; mouse.
DR PRO; PR:Q9QYB2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9QYB2; protein.
DR Bgee; ENSMUSG00000055639; Expressed in ureter smooth muscle and 291 other tissues.
DR Genevisible; Q9QYB2; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0046545; P:development of primary female sexual characteristics; IGI:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0060244; P:negative regulation of cell proliferation involved in contact inhibition; IGI:MGI.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:MGI.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0033262; P:regulation of nuclear cell cycle DNA replication; IMP:CACAO.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IMP:MGI.
DR GO; GO:0001967; P:suckling behavior; IMP:MGI.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; IMP:MGI.
DR Gene3D; 3.10.260.20; -; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR003380; SKI/SNO/DAC.
DR InterPro; IPR037000; Ski_DNA-bd_sf.
DR Pfam; PF02437; Ski_Sno; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Developmental protein;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..751
FT /note="Dachshund homolog 1"
FT /id="PRO_0000095598"
FT REGION 1..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..377
FT /note="Interaction with SIX6 and HDAC3"
FT /evidence="ECO:0000269|PubMed:12130660"
FT REGION 182..268
FT /note="DACHbox-N"
FT REGION 273..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..689
FT /note="DACHbox-C"
FT REGION 620..699
FT /note="Interaction with SIN3A"
FT /evidence="ECO:0000269|PubMed:12130660"
FT COILED 623..711
FT /evidence="ECO:0000255"
FT COMPBIAS 18..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 370..421
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10502109,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9915577"
FT /id="VSP_009489"
FT CONFLICT 62
FT /note="S -> Y (in Ref. 2; AAD16097/AAD16098)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="K -> E (in Ref. 5; BAC33046)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="A -> T (in Ref. 2; CAA06665)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 751 AA; 77972 MW; 0679337DBA742EC9 CRC64;
MAVPAALIPP TQLVPPQPPI STSASSSGTT TSTSSATSSP APSIGPPASS GPTLFRPEPI
ASSASSSAAA TVTSPGGGGG GSGGGGGSGG NGGGGGSNCN PSLAAGSSGG GVSAGGGGAS
STPITASTGS SSSSSSSSSS SSSSSSSSSS SSSSSSCGPL PGKPVYSTPS PVENTPQNNE
CKMVDLRGAK VASFTVEGCE LICLPQAFDL FLKHLVGGLH TVYTKLKRLE ITPVVCNVEQ
VRILRGLGAI QPGVNRCKLI SRKDFETLYN DCTNASSRPG RPPKRTQSVT SPENSHIMPH
SVPGLMSPGI IPPTGLTAAA AAAAAATNAA IAEAMKVKKI KLEAMSNYHA SNNQHGADSE
NGDMNSSVGS SGGSWDKETL HSPPSQGSQA PVAHARMPAA FSLPVSHPLN HLQHSHLPPN
GLELPFMMMP HPLIPVSLPP ASVTMAMSQM NHLSTIANMA AAAQVQSPPS RVETSVIKER
VPDSPSPAPS LEEGRRPGSH PSSHRSSSVS SSPARTESSS DRIPVHQNGL SMNQMLMGLS
PNVLPGPKEG DLAGHDMGHE SKRIHIEKDE TPLSTPTARD SIDKLSLTGH GQPLPPGFPS
PFLFPDGLSS IETLLTNIQG LLKVAIDNAR AQEKQVQLEK TELKMDFLRE RELRETLEKQ
LAMEQKNRAI VQKRLKKEKK AKRKLQEALE FETKRREQAE QTLKQAASAD SLRVLNDSLT
PEIEADRSGG RADAERTIQD GRLYLKTTVM Y
