TSH_DROME
ID TSH_DROME Reviewed; 954 AA.
AC P22265; A8E6H0; Q6AWP7; Q7KRS3; Q9V9Q0;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Protein teashirt;
GN Name=tsh; ORFNames=CG1374;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=1846092; DOI=10.1016/0092-8674(91)90209-h;
RA Fasano L., Roeder L., Core N., Alexandre E., Vola C., Jacq B., Kerridge S.;
RT "The gene teashirt is required for the development of Drosophila embryonic
RT trunk segments and encodes a protein with widely spaced zinc finger
RT motifs.";
RL Cell 64:63-79(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Kapadia B.,
RA Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=1360402; DOI=10.1242/dev.115.4.1017;
RA Roeder L., Vola C., Kerridge S.;
RT "The role of the teashirt gene in trunk segmental identity in Drosophila.";
RL Development 115:1017-1033(1992).
RN [6]
RP FUNCTION.
RX PubMed=7925029; DOI=10.1242/dev.120.8.2287;
RA de Zulueta P., Alexandre E., Jacq B., Kerridge S.;
RT "Homeotic complex and teashirt genes co-operate to establish trunk
RT segmental identities in Drosophila.";
RL Development 120:2287-2296(1994).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=7607071; DOI=10.1242/dev.120.10.2799;
RA Mathies L.D., Kerridge S., Scott M.P.;
RT "Role of the teashirt gene in Drosophila midgut morphogenesis: secreted
RT proteins mediate the action of homeotic genes.";
RL Development 120:2799-2809(1994).
RN [8]
RP DNA-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8951796; DOI=10.1016/0925-4773(96)00594-1;
RA Alexandre E., Graba Y., Fasano L., Gallet A., Perrin L., De Zulueta P.,
RA Pradel J., Kerridge S., Jacq B.;
RT "The Drosophila teashirt homeotic protein is a DNA-binding protein and
RT modulo, a HOM-C regulated modifier of variegation, is a likely candidate
RT for being a direct target gene.";
RL Mech. Dev. 59:191-204(1996).
RN [9]
RP FUNCTION, INTERACTION WITH ARM, AND SUBCELLULAR LOCATION.
RX PubMed=9707400; DOI=10.1016/s0960-9822(07)00369-7;
RA Gallet A., Erkner A., Charroux B., Fasano L., Kerridge S.;
RT "Trunk-specific modulation of wingless signalling in Drosophila by teashirt
RT binding to armadillo.";
RL Curr. Biol. 8:893-902(1998).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10842058; DOI=10.1016/s0925-4773(00)00311-7;
RA Wu J., Cohen S.M.;
RT "Proximal distal axis formation in the Drosophila leg: distinct functions
RT of teashirt and homothorax in the proximal leg.";
RL Mech. Dev. 94:47-56(2000).
RN [11]
RP POSSIBLE FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11429289; DOI=10.1016/s0925-4773(01)00397-5;
RA Soanes K.H., MacKay J.O., Core N., Heslip T., Kerridge S., Bell J.B.;
RT "Identification of a regulatory allele of teashirt (tsh) in Drosophila
RT melanogaster that affects wing hinge development. An adult-specific tsh
RT enhancer in Drosophila.";
RL Mech. Dev. 105:145-151(2001).
RN [12]
RP FUNCTION.
RX PubMed=15110046; DOI=10.1016/j.mod.2004.02.005;
RA Singh A., Kango-Singh M., Choi K.W., Sun Y.H.;
RT "Dorso-ventral asymmetric functions of teashirt in Drosophila eye
RT development depend on spatial cues provided by early DV patterning genes.";
RL Mech. Dev. 121:365-370(2004).
RN [13]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15936749; DOI=10.1016/j.ydbio.2005.05.005;
RA Laugier E., Yang Z., Fasano L., Kerridge S., Vola C.;
RT "A critical role of teashirt for patterning the ventral epidermis is masked
RT by ectopic expression of tiptop, a paralog of teashirt in Drosophila.";
RL Dev. Biol. 283:446-458(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-750 AND SER-758, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Homeotic protein that acts downstream of Arm in the Wg
CC cascade during embryogenesis to determine segment identity throughout
CC the entire trunk. Acts cooperatively with other trunk homeotic proteins
CC to repress head homeotic genes and therefore repress head segmental
CC identity. Necessary, in combination with Scr, for the formation of the
CC prothoracic segment. Promotes eye development in the dorsal region of
CC the eye disk and suppresses eye development in the ventral region in
CC combination with Wg-signaling and several early dorso-ventral eye
CC patterning genes. Required for proper development of proximal leg
CC segments. Has differential functions along the dorso-ventral axs of the
CC antennal and leg disks. May play a role in wing hinge development.
CC Possible involvement in chromatin structure for modulation of
CC transcription. Binds DNA and can act as both a transcriptional
CC repressor and activator. Positively regulates its own expression as
CC well as that of Dll. Negatively regulates the expression of mod.
CC Required for Wg-mediated transcriptional repression of Ubx in the
CC midgut. Also represses transcription of lab in the midgut and is
CC necessary for the proper formation of anterior and central midgut
CC structures. Tiptop (tio) and teashirt (tsh) have, on the whole, common
CC activities. Tio and tsh repress each other's expression and tsh has a
CC crucial role for trunk patterning that is in part masked by ectopic
CC expression of tiptop. Both genes share a common activity required for
CC the activation of Ser and svb and the maintenance of en and wg.
CC {ECO:0000269|PubMed:10842058, ECO:0000269|PubMed:1360402,
CC ECO:0000269|PubMed:15110046, ECO:0000269|PubMed:15936749,
CC ECO:0000269|PubMed:1846092, ECO:0000269|PubMed:7607071,
CC ECO:0000269|PubMed:7925029, ECO:0000269|PubMed:9707400}.
CC -!- SUBUNIT: Binds arm.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Initially localized in
CC the cytoplasm soon after the blastoderm stage, and becomes nuclear by
CC stage 9.
CC -!- TISSUE SPECIFICITY: Shows a dynamic expression pattern during
CC embryogenesis. Expressed in the embryonic trunk region (PS 3-13) with
CC expression strongest in the thoracic segments. Expressed in a small
CC group of cells corresponding to the anal tuft from stage 14. Strongly
CC expressed in the embryonic ventral nerve cord. Also expressed in the
CC proximal domain of the leg imaginal disk and in the region of the wing
CC disk that will give rise to the proximal wing hinge. Expressed at high
CC levels in the anterior and central embryonic midgut mesoderm and in the
CC embryonic midgut endoderm. Expressed at a low level in more posterior
CC visceral mesoderm of the gut. From stage 12 onwards, tsh and tio are
CC colocalized in some cells of the CNS, trunk epidermis, hindgut and
CC Malpighian tubules. {ECO:0000269|PubMed:10842058,
CC ECO:0000269|PubMed:11429289, ECO:0000269|PubMed:1360402,
CC ECO:0000269|PubMed:15936749, ECO:0000269|PubMed:7607071,
CC ECO:0000269|PubMed:8951796}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic, larval and adult
CC development. Not maternally expressed.
CC -!- MISCELLANEOUS: The tsh tio gene pair seems to have arisen from a recent
CC duplication event: tsh has the dominant role compared to tio.
CC -!- SIMILARITY: Belongs to the teashirt C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28983.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAT94430.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M57496; AAA28983.1; ALT_FRAME; mRNA.
DR EMBL; AE014134; AAF57236.2; -; Genomic_DNA.
DR EMBL; BT015201; AAT94430.1; ALT_FRAME; mRNA.
DR EMBL; BT030762; ABV82144.1; -; mRNA.
DR PIR; A38437; A38437.
DR RefSeq; NP_523615.2; NM_078891.3.
DR AlphaFoldDB; P22265; -.
DR BioGRID; 61373; 30.
DR IntAct; P22265; 5.
DR STRING; 7227.FBpp0085261; -.
DR iPTMnet; P22265; -.
DR PaxDb; P22265; -.
DR DNASU; 35430; -.
DR EnsemblMetazoa; FBtr0085906; FBpp0085261; FBgn0003866.
DR GeneID; 35430; -.
DR KEGG; dme:Dmel_CG1374; -.
DR CTD; 35430; -.
DR FlyBase; FBgn0003866; tsh.
DR VEuPathDB; VectorBase:FBgn0003866; -.
DR eggNOG; ENOG502QV71; Eukaryota.
DR GeneTree; ENSGT00950000183051; -.
DR HOGENOM; CLU_302525_0_0_1; -.
DR InParanoid; P22265; -.
DR OMA; ANIFRAG; -.
DR OrthoDB; 967773at2759; -.
DR PhylomeDB; P22265; -.
DR Reactome; R-DME-390193; Transcriptional activation by YKI.
DR SignaLink; P22265; -.
DR BioGRID-ORCS; 35430; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35430; -.
DR PRO; PR:P22265; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0003866; Expressed in wing disc and 40 other tissues.
DR Genevisible; P22265; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
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:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0007450; P:dorsal/ventral pattern formation, imaginal disc; IMP:UniProtKB.
DR GO; GO:0048730; P:epidermis morphogenesis; IMP:FlyBase.
DR GO; GO:0035214; P:eye-antennal disc development; IMP:UniProtKB.
DR GO; GO:0008258; P:head involution; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0007479; P:leg disc proximal/distal pattern formation; IMP:UniProtKB.
DR GO; GO:0061330; P:Malpighian tubule stellate cell differentiation; IMP:FlyBase.
DR GO; GO:0007494; P:midgut development; IMP:UniProtKB.
DR GO; GO:0045705; P:negative regulation of salivary gland boundary specification; TAS:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:2000497; P:positive regulation of cell proliferation involved in compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0007380; P:specification of segmental identity, head; IMP:FlyBase.
DR GO; GO:0007384; P:specification of segmental identity, thorax; IMP:FlyBase.
DR GO; GO:0035292; P:specification of segmental identity, trunk; IMP:UniProtKB.
DR GO; GO:0007473; P:wing disc proximal/distal pattern formation; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IMP:UniProtKB.
DR InterPro; IPR027008; Teashirt_fam.
DR InterPro; IPR026807; Tio/Tsh.
DR InterPro; IPR041661; ZN622/Rei1/Reh1_Znf-C2H2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12487; PTHR12487; 1.
DR PANTHER; PTHR12487:SF7; PTHR12487:SF7; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR Pfam; PF12756; zf-C2H2_2; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Developmental protein; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Wnt signaling pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..954
FT /note="Protein teashirt"
FT /id="PRO_0000047061"
FT ZN_FING 354..378
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 466..490
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 533..557
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 20..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..410
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 668..673
FT /note="SAKAAG -> QQRLR (in Ref. 1; AAA28983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 954 AA; 100651 MW; 33FB3677DC8C4B33 CRC64;
MLHEALMLEI YRQALNAGAL PTARPRSTES ANSSERCPSH DSNSSEHGGG AGSGGVGHRL
DAAALSTGVM PGEGPTTLHS SFPAVPQSLP SQPPSMEAYL HMVAAAAQQY GFPLAAAAAA
GAGPRLPLPL ANEAAAPFKL PPQASPTASS NNSEALDFRT NLYGRAESAE PPASEGEEEE
FDDGANNPLD LSVGTRKRGH ESEPQLGHIQ VKKMFKSDSP PANSVASPSA SQLLPGVNPY
LAAVAAANIF RAGQFPDWNS KNDLVVDPLE KMSDIVKGGA SGMGTKEKMH SSKATTPQAA
SQPPKSPVQP TPNQNSESGG GSGGGAAGSG AVTKARHNIW QSHWQNKGVA SSVFRCVWCK
QSFPTLEALT THMKDSKHCG VNVPPFGNLP SNNPQPQHHH PTPPPPPQNH NLRKHSSGSA
SNHSPSANVK NAFQYRGDPP TPLPRKLVRG QNVWLGKGVE QAMQILKCMR CGESFRSLGE
MTKHMQETQH YTNILSQEQS ISIKSGNANA NSDAKESHNS LSSEESRTLS AVLTCKVCDK
AFNSLGDLSN HMAKNNHYAE PLLQSAGARK RPAPKKREKS LPVRKLLEMK GGSGTTQEDH
SNEKTSVQGK PGLGPGGGDK NDAALFAERM RQYITGVKAP EEIAKVAAAQ LLAKNKSPEL
VEQKNGGSAK AAGASSVLSA IEQMFTTSFD TPPRHASLPA SSPSNSSTKN TSPVASSILK
RLGIDETVDY NKPLIDTNDP YYQHYRYTSS ERSGSECSAE ARPRLDAPTP EKQQQGGGHD
EESSKPAIKQ EREAESKPVK MEIKSEFVDE PNEAEETSKM EAAVVNGSAT NNNNNIVERS
SPKTPSSAAS PQTRLLPPRS PAESQRSVTP KSPASSHKSY DGSSEGTKKF PSDSLNALSS
MFDSLGSSGA GANSRAKLAA AAAAGGSESP ENLTAGGNSL AALRQFCVKK EKTA
