DACH1_HUMAN
ID DACH1_HUMAN Reviewed; 758 AA.
AC Q9UI36; A0A087WZP2; D0FY35; D0FY36; O75523; O75687; Q5VYY3; Q5VYY4; Q96SG3;
AC Q96SG4; Q9H524; Q9UMH4;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 4.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Dachshund homolog 1;
DE Short=Dach1;
GN Name=DACH1; Synonyms=DACH;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORMS 3; 4
RP AND 5), AND TISSUE SPECIFICITY.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-GLY-73 INS.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 108-758 (ISOFORM 2).
RC TISSUE=Retina;
RG The European IMAGE consortium;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 109-758 (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 186-758 (ISOFORM 2).
RC TISSUE=Uterus;
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 [8]
RP FUNCTION IN TGF-BETA SIGNALING, INTERACTION WITH HDAC3; SMAD3; SMAD4; NCOR1
RP AND SIN3A, AND SUBCELLULAR LOCATION.
RX PubMed=14525983; DOI=10.1074/jbc.m310021200;
RA Wu K., Yang Y., Wang C., Davoli M.A., D'Amico M., Li A., Cveklova K.,
RA Kozmik Z., Lisanti M.P., Russell R.G., Cvekl A., Pestell R.G.;
RT "DACH1 inhibits transforming growth factor-beta signaling through binding
RT Smad4.";
RL J. Biol. Chem. 278:51673-51684(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 184-282.
RX PubMed=12057194; DOI=10.1016/s0969-2126(02)00769-4;
RA Kim S.-S., Zhang R.-G., Braunstein S.E., Joachimiak A., Cvekl A.,
RA Hegde R.S.;
RT "Structure of the retinal determination protein dachshund reveals a DNA
RT binding motif.";
RL Structure 10:787-795(2002).
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 (By similarity). Inhibits
CC TGF-beta signaling through interaction with SMAD4 and NCOR1. Binds to
CC chromatin DNA via its DACHbox-N domain (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:14525983}.
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 (By similarity). Interacts with SMAD3 and SMAD4. {ECO:0000250,
CC ECO:0000269|PubMed:14525983}.
CC -!- INTERACTION:
CC Q9UI36; Q9UJ70: NAGK; NbExp=3; IntAct=EBI-347111, EBI-372578;
CC Q9UI36; O75376: NCOR1; NbExp=2; IntAct=EBI-347111, EBI-347233;
CC Q9UI36; Q13485: SMAD4; NbExp=3; IntAct=EBI-347111, EBI-347263;
CC Q9UI36-2; O43865: AHCYL1; NbExp=10; IntAct=EBI-10186082, EBI-2371423;
CC Q9UI36-2; P61328: FGF12; NbExp=3; IntAct=EBI-10186082, EBI-6657662;
CC Q9UI36-2; P61328-2: FGF12; NbExp=3; IntAct=EBI-10186082, EBI-10699759;
CC Q9UI36-2; Q9BU76: MMTAG2; NbExp=3; IntAct=EBI-10186082, EBI-742459;
CC Q9UI36-2; Q9UJ70: NAGK; NbExp=5; IntAct=EBI-10186082, EBI-372578;
CC Q9UI36-2; Q9UJ70-2: NAGK; NbExp=3; IntAct=EBI-10186082, EBI-11526455;
CC Q9UI36-2; Q13427: PPIG; NbExp=3; IntAct=EBI-10186082, EBI-396072;
CC Q9UI36-2; P31321: PRKAR1B; NbExp=3; IntAct=EBI-10186082, EBI-2805516;
CC Q9UI36-2; Q9UBS8: RNF14; NbExp=6; IntAct=EBI-10186082, EBI-2130308;
CC Q9UI36-2; Q05519-2: SRSF11; NbExp=3; IntAct=EBI-10186082, EBI-11975029;
CC Q9UI36-2; P26368: U2AF2; NbExp=3; IntAct=EBI-10186082, EBI-742339;
CC Q9UI36-2; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-10186082, EBI-597063;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14525983}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9UI36-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UI36-2; Sequence=VSP_009872;
CC Name=3;
CC IsoId=Q9UI36-3; Sequence=VSP_009872, VSP_009873;
CC Name=4;
CC IsoId=Q9UI36-4; Sequence=VSP_009486;
CC -!- TISSUE SPECIFICITY: Widely expressed. Isoform 2 is found in brain,
CC heart, kidney, liver, leukocytes and spleen. Isoform 3 is found in
CC liver and heart. Isoform 4 is found in spleen.
CC {ECO:0000269|PubMed:11543628}.
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 -!- MISCELLANEOUS: [Isoform 2]: Major. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DACH/dachshund family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA06666.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF102546; AAF01351.1; -; mRNA.
DR EMBL; AF069509; AAC33466.1; -; mRNA.
DR EMBL; AF356492; AAL08487.1; -; mRNA.
DR EMBL; AL138698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL163542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMYH02028239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471093; EAW80509.1; -; Genomic_DNA.
DR EMBL; CH471093; EAW80510.1; -; Genomic_DNA.
DR EMBL; AL079278; CAB45153.1; -; mRNA.
DR EMBL; AJ005670; CAA06666.1; ALT_INIT; mRNA.
DR EMBL; BC021219; AAH21219.2; -; mRNA.
DR CCDS; CCDS41899.1; -. [Q9UI36-2]
DR RefSeq; NP_004383.4; NM_004392.6. [Q9UI36-4]
DR RefSeq; NP_542937.3; NM_080759.5. [Q9UI36-2]
DR RefSeq; NP_542938.3; NM_080760.5. [Q9UI36-3]
DR RefSeq; XP_011533241.1; XM_011534939.2.
DR PDB; 1L8R; X-ray; 1.65 A; A/B=184-282.
DR PDBsum; 1L8R; -.
DR AlphaFoldDB; Q9UI36; -.
DR SMR; Q9UI36; -.
DR BioGRID; 107972; 89.
DR IntAct; Q9UI36; 38.
DR MINT; Q9UI36; -.
DR STRING; 9606.ENSP00000482245; -.
DR GlyGen; Q9UI36; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UI36; -.
DR PhosphoSitePlus; Q9UI36; -.
DR BioMuta; DACH1; -.
DR DMDM; 519668677; -.
DR EPD; Q9UI36; -.
DR jPOST; Q9UI36; -.
DR MassIVE; Q9UI36; -.
DR MaxQB; Q9UI36; -.
DR PeptideAtlas; Q9UI36; -.
DR PRIDE; Q9UI36; -.
DR ProteomicsDB; 12719; -.
DR ProteomicsDB; 12720; -.
DR ProteomicsDB; 84464; -. [Q9UI36-1]
DR ProteomicsDB; 84465; -. [Q9UI36-2]
DR ProteomicsDB; 84466; -. [Q9UI36-3]
DR ProteomicsDB; 84467; -. [Q9UI36-4]
DR Antibodypedia; 72801; 315 antibodies from 37 providers.
DR DNASU; 1602; -.
DR Ensembl; ENST00000611519.4; ENSP00000482493.1; ENSG00000276644.5. [Q9UI36-3]
DR Ensembl; ENST00000613252.5; ENSP00000482245.1; ENSG00000276644.5. [Q9UI36-2]
DR Ensembl; ENST00000619232.1; ENSP00000482797.1; ENSG00000276644.5. [Q9UI36-1]
DR Ensembl; ENST00000620444.4; ENSP00000481551.1; ENSG00000276644.5. [Q9UI36-4]
DR GeneID; 1602; -.
DR KEGG; hsa:1602; -.
DR MANE-Select; ENST00000613252.5; ENSP00000482245.1; NM_080759.6; NP_542937.3. [Q9UI36-2]
DR UCSC; uc058xki.1; human. [Q9UI36-1]
DR CTD; 1602; -.
DR DisGeNET; 1602; -.
DR GeneCards; DACH1; -.
DR HGNC; HGNC:2663; DACH1.
DR HPA; ENSG00000276644; Low tissue specificity.
DR MalaCards; DACH1; -.
DR MIM; 603803; gene.
DR neXtProt; NX_Q9UI36; -.
DR OpenTargets; ENSG00000276644; -.
DR PharmGKB; PA27134; -.
DR VEuPathDB; HostDB:ENSG00000276644; -.
DR eggNOG; KOG3915; Eukaryota.
DR GeneTree; ENSGT00390000001134; -.
DR HOGENOM; CLU_027923_0_0_1; -.
DR InParanoid; Q9UI36; -.
DR OMA; VSHPLNH; -.
DR OrthoDB; 429758at2759; -.
DR PhylomeDB; Q9UI36; -.
DR TreeFam; TF316697; -.
DR PathwayCommons; Q9UI36; -.
DR SignaLink; Q9UI36; -.
DR SIGNOR; Q9UI36; -.
DR BioGRID-ORCS; 1602; 17 hits in 1067 CRISPR screens.
DR ChiTaRS; DACH1; human.
DR EvolutionaryTrace; Q9UI36; -.
DR GeneWiki; DACH1; -.
DR GenomeRNAi; 1602; -.
DR Pharos; Q9UI36; Tbio.
DR PRO; PR:Q9UI36; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9UI36; protein.
DR Bgee; ENSG00000276644; Expressed in ventricular zone and 160 other tissues.
DR Genevisible; Q9UI36; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0046545; P:development of primary female sexual characteristics; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:BHF-UCL.
DR GO; GO:0060244; P:negative regulation of cell proliferation involved in contact inhibition; IEA:Ensembl.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IDA:CACAO.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:CACAO.
DR GO; GO:0033262; P:regulation of nuclear cell cycle DNA replication; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:Ensembl.
DR GO; GO:0001967; P:suckling behavior; IEA:Ensembl.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; IEA:Ensembl.
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 3D-structure; Activator; Alternative splicing; Coiled coil;
KW Developmental protein; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..758
FT /note="Dachshund homolog 1"
FT /id="PRO_0000095597"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..384
FT /note="Interaction with SIX6 and HDAC3"
FT /evidence="ECO:0000250"
FT REGION 189..275
FT /note="DACHbox-N"
FT REGION 280..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..696
FT /note="DACHbox-C"
FT REGION 627..706
FT /note="Interaction with SIN3A"
FT /evidence="ECO:0000250"
FT COILED 630..718
FT /evidence="ECO:0000255"
FT COMPBIAS 18..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB2"
FT VAR_SEQ 322..575
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_009486"
FT VAR_SEQ 376..427
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10502110,
FT ECO:0000303|PubMed:11543628, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9651501, ECO:0000303|Ref.5"
FT /id="VSP_009872"
FT VAR_SEQ 428..575
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_009873"
FT VARIANT 73
FT /note="T -> TGG"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_080662"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1L8R"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:1L8R"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:1L8R"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:1L8R"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:1L8R"
FT TURN 219..223
FT /evidence="ECO:0007829|PDB:1L8R"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:1L8R"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:1L8R"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:1L8R"
FT HELIX 269..280
FT /evidence="ECO:0007829|PDB:1L8R"
SQ SEQUENCE 758 AA; 78562 MW; DFB5054D7EC5FF11 CRC64;
MAVPAALIPP TQLVPPQPPI STSASSSGTT TSTSSATSSP APSIGPPASS GPTLFRPEPI
ASAAAAAATV TSTGGGGGGG GSGGGGGSSG NGGGGGGGGG GSNCNPNLAA ASNGSGGGGG
GISAGGGVAS STPINASTGS SSSSSSSSSS SSSSSSSSSS SSSCGPLPGK PVYSTPSPVE
NTPQNNECKM VDLRGAKVAS FTVEGCELIC LPQAFDLFLK HLVGGLHTVY TKLKRLEITP
VVCNVEQVRI LRGLGAIQPG VNRCKLISRK DFETLYNDCT NASSRPGRPP KRTQSVTSPE
NSHIMPHSVP GLMSPGIIPP TGLTAAAAAA AAATNAAIAE AMKVKKIKLE AMSNYHASNN
QHGADSENGD MNSSVGSSDG SWDKETLPSS PSQGPQASIT HPRMPGARSL PLSHPLNHLQ
QSHLLPNGLE LPFMMMPHPL IPVSLPPASV TMAMSQMNHL STIANMAAAA QVQSPPSRVE
TSVIKERVPD SPSPAPSLEE GRRPGSHPSS HRSSSVSSSP ARTESSSDRI PVHQNGLSMN
QMLMGLSPNV LPGPKEGDLA GHDMGHESKR MHIEKDETPL STPTARDSLD KLSLTGHGQP
LPPGFPSPFL FPDGLSSIET LLTNIQGLLK VAIDNARAQE KQVQLEKTEL KMDFLREREL
RETLEKQLAM EQKNRAIVQK RLKKEKKAKR KLQEALEFET KRREQAEQTL KQAASTDSLR
VLNDSLTPEI EADRSGGRTD AERTIQDGRL YLKTTVMY
