ERM_DROME
ID ERM_DROME Reviewed; 611 AA.
AC Q9VQ56; Q95SM6;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Fez family zinc finger protein erm {ECO:0000305};
DE AltName: Full=Earmuff {ECO:0000312|FlyBase:FBgn0031375};
GN Name=erm {ECO:0000312|FlyBase:FBgn0031375};
GN Synonyms=dFezf {ECO:0000303|PubMed:29513217,
GN ECO:0000312|FlyBase:FBgn0031375}, dfezl {ECO:0000312|FlyBase:FBgn0031375};
GN ORFNames=CG31670 {ECO:0000312|FlyBase:FBgn0031375};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:AAL28247.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28247.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAL28247.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=18621688; DOI=10.1073/pnas.0803697105;
RA Pfeiffer B.D., Jenett A., Hammonds A.S., Ngo T.T., Misra S., Murphy C.,
RA Scully A., Carlson J.W., Wan K.H., Laverty T.R., Mungall C., Svirskas R.,
RA Kadonaga J.T., Doe C.Q., Eisen M.B., Celniker S.E., Rubin G.M.;
RT "Tools for neuroanatomy and neurogenetics in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9715-9720(2008).
RN [5] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-389.
RX PubMed=20152183; DOI=10.1016/j.devcel.2009.12.007;
RA Weng M., Golden K.L., Lee C.Y.;
RT "dFezf/Earmuff maintains the restricted developmental potential of
RT intermediate neural progenitors in Drosophila.";
RL Dev. Cell 18:126-135(2010).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DOMAIN.
RX PubMed=24550111; DOI=10.1242/dev.106534;
RA Janssens D.H., Komori H., Grbac D., Chen K., Koe C.T., Wang H., Lee C.Y.;
RT "Earmuff restricts progenitor cell potential by attenuating the competence
RT to respond to self-renewal factors.";
RL Development 141:1036-1046(2014).
RN [7] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH BRM-HDAC3-ERM, INTERACTION WITH
RP BRM; BAP60; SNR1 AND HDAC3, AND DISRUPTION PHENOTYPE.
RX PubMed=24618901; DOI=10.7554/elife.01906;
RA Koe C.T., Li S., Rossi F., Wong J.J., Wang Y., Zhang Z., Chen K., Aw S.S.,
RA Richardson H.E., Robson P., Sung W.K., Yu F., Gonzalez C., Wang H.;
RT "The Brm-HDAC3-Erm repressor complex suppresses dedifferentiation in
RT Drosophila type II neuroblast lineages.";
RL Elife 3:E01906-E01906(2014).
RN [8] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27151950; DOI=10.1242/dev.136184;
RA Li X., Xie Y., Zhu S.;
RT "Notch maintains Drosophila type II neuroblasts by suppressing expression
RT of the Fez transcription factor Earmuff.";
RL Development 143:2511-2521(2016).
RN [9] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=27510969; DOI=10.1242/dev.137281;
RA Xie Y., Li X., Deng X., Hou Y., O'Hara K., Urso A., Peng Y., Chen L.,
RA Zhu S.;
RT "The Ets protein Pointed prevents both premature differentiation and
RT dedifferentiation of Drosophila intermediate neural progenitors.";
RL Development 143:3109-3118(2016).
RN [10] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28245922; DOI=10.1016/j.devcel.2017.01.014;
RA Janssens D.H., Hamm D.C., Anhezini L., Xiao Q., Siller K.H., Siegrist S.E.,
RA Harrison M.M., Lee C.Y.;
RT "An Hdac1/Rpd3-poised circuit balances continual self-renewal and rapid
RT restriction of developmental potential during asymmetric stem cell
RT division.";
RL Dev. Cell 40:367-380(2017).
RN [11] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=28899667; DOI=10.1016/j.ydbio.2017.09.011;
RA Li X., Chen R., Zhu S.;
RT "bHLH-O proteins balance the self-renewal and differentiation of Drosophila
RT neural stem cells by regulating Earmuff expression.";
RL Dev. Biol. 431:239-251(2017).
RN [12]
RP FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP LEU-389.
RX PubMed=29513217; DOI=10.7554/elife.33962;
RA Peng J., Santiago I.J., Ahn C., Gur B., Tsui C.K., Su Z., Xu C.,
RA Karakhanyan A., Silies M., Pecot M.Y.;
RT "Fezf coordinates laminar-specific connectivity through cell-intrinsic and
RT cell-extrinsic mechanisms.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Zinc-finger transcriptional repressor (PubMed:24550111,
CC PubMed:24618901, PubMed:28245922). In larval brain, involved in the
CC maintenance of cell fate of intermediate neural progenitors (INPs) that
CC derive from type II neuroblasts (PubMed:20152183, PubMed:24618901,
CC PubMed:27151950, PubMed:27510969, PubMed:28245922, PubMed:28899667).
CC Restricts INP developmental potential and dedifferentiation by
CC interacting with HDAC3 and the chromatin remodeling Brahma-associated
CC protein (BAP) complex (PubMed:24618901, PubMed:24550111,
CC PubMed:27151950, PubMed:28899667, PubMed:28245922). Restricts INP
CC proliferation by regulating neuroblast specific factors such as
CC prospero, pnt and grh, and by antagonizing the function of self-renewal
CC factors, such as klu, dpn and E(spl)mgamma-HLH (PubMed:20152183,
CC PubMed:24550111, PubMed:28899667). In the optic lobe, essential for
CC coordinating the innervation/ targeting of the L3 and R8 axons to the
CC M3 layer of the medulla (PubMed:29513217). Early in medulla
CC development, functions in parallel to CadN and Sema1a pathways to
CC promote targeting of the L3 growth cones to the proximal domain of the
CC outer medulla possibly by controlling the expression of various cell
CC surface genes such as dpr1 and dpr17 which function in L3 growth cone
CC targeting (PubMed:29513217). Then once L3 growth cones segregate into
CC the developing M3 layer, it activates the expression of netrins NetA
CC and NetB which act locally to promote the attachment of R8 growth cones
CC within the M3 layer (PubMed:29513217). {ECO:0000269|PubMed:20152183,
CC ECO:0000269|PubMed:24550111, ECO:0000269|PubMed:24618901,
CC ECO:0000269|PubMed:27151950, ECO:0000269|PubMed:27510969,
CC ECO:0000269|PubMed:28245922, ECO:0000269|PubMed:28899667,
CC ECO:0000269|PubMed:29513217}.
CC -!- SUBUNIT: Found in a probable chromatin remodeling Brahma-associated
CC proteins (BAP) complex composed of at least brm, Bap60, Snr1 and erm.
CC Within the complex, interacts (via N-terminus) with Bap60 and HDAC3.
CC {ECO:0000269|PubMed:24618901}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24550111,
CC ECO:0000269|PubMed:27151950, ECO:0000269|PubMed:27510969,
CC ECO:0000269|PubMed:28245922, ECO:0000269|PubMed:28899667}.
CC -!- DEVELOPMENTAL STAGE: Expressed in immature intermediate neural
CC progenitors (INP) and type II neuroblasts in larval brains (at protein
CC level) (PubMed:24550111, PubMed:27151950, PubMed:27510969,
CC PubMed:28245922). Expressed in lamina L3 neurons from early pupal to
CC adult stages, but is absent in late third instar larvae when lamina
CC neurons begin to differentiate (at protein level) (PubMed:29513217).
CC Expressed in the developing embryonic brain from stage 4
CC (PubMed:18621688). {ECO:0000269|PubMed:18621688,
CC ECO:0000269|PubMed:24550111, ECO:0000269|PubMed:27151950,
CC ECO:0000269|PubMed:27510969, ECO:0000269|PubMed:28245922,
CC ECO:0000269|PubMed:29513217}.
CC -!- DOMAIN: The second, third and fourth zinc finger domains are necessary
CC for repressing gene transcription. {ECO:0000269|PubMed:24550111,
CC ECO:0000269|PubMed:28899667}.
CC -!- DISRUPTION PHENOTYPE: Results in abnormal expansion of type II
CC neuroblasts and in ectopic expression of pnt and grh (PubMed:28245922,
CC PubMed:20152183). Simultaneous RNAi-mediated knockdown of N partially
CC restores normal neuroblast numbers and prevents loss of pnt expression
CC (PubMed:27151950). Simultaneous RNAi-mediated knockdown of erm with
CC either HDAC3 or members of the Brm-associated protein (BAP) chromatin-
CC remodeling complex brm and Snr1 further increases the number of type II
CC neuroblasts compared with the single knockdown (PubMed:24618901).
CC Simultaneous RNAi-mediated knockdown of both erm and the ETS protein
CC pnt restores normal neuroblast numbers (PubMed:28899667). RNAi-mediated
CC knockdown in lamina neurons and their precursor cells, results in
CC defective targeting of R8 neurons, with 45% of them terminating in
CC medulla layers other than the correct M3 layer (PubMed:29513217). RNAi-
CC mediated knockdown in L3 neurons, reduces expression of NetB in L3
CC neurons, L3 somas and the developing M3 layer (PubMed:29513217).
CC {ECO:0000269|PubMed:20152183, ECO:0000269|PubMed:24618901,
CC ECO:0000269|PubMed:27151950, ECO:0000269|PubMed:28245922,
CC ECO:0000269|PubMed:28899667, ECO:0000269|PubMed:29513217}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AE014134; AAF51325.2; -; Genomic_DNA.
DR EMBL; AY060699; AAL28247.1; -; mRNA.
DR RefSeq; NP_608631.1; NM_134787.3.
DR AlphaFoldDB; Q9VQ56; -.
DR SMR; Q9VQ56; -.
DR IntAct; Q9VQ56; 3.
DR STRING; 7227.FBpp0077539; -.
DR DNASU; 326152; -.
DR EnsemblMetazoa; FBtr0077870; FBpp0077539; FBgn0031375.
DR GeneID; 326152; -.
DR KEGG; dme:Dmel_CG31670; -.
DR UCSC; CG31670-RA; d. melanogaster.
DR CTD; 326152; -.
DR FlyBase; FBgn0031375; erm.
DR VEuPathDB; VectorBase:FBgn0031375; -.
DR GeneTree; ENSGT00940000170086; -.
DR HOGENOM; CLU_021813_1_0_1; -.
DR InParanoid; Q9VQ56; -.
DR BioGRID-ORCS; 326152; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Moe; fly.
DR GenomeRNAi; 326152; -.
DR PRO; PR:Q9VQ56; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031375; Expressed in anlage in statu nascendi and 26 other tissues.
DR ExpressionAtlas; Q9VQ56; baseline and differential.
DR GO; GO:0044295; C:axonal growth cone; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0007412; P:axon target recognition; IMP:UniProtKB.
DR GO; GO:0060385; P:axonogenesis involved in innervation; IMP:UniProtKB.
DR GO; GO:0043697; P:cell dedifferentiation; IGI:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1902843; P:positive regulation of netrin-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IGI:FlyBase.
DR GO; GO:1902692; P:regulation of neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:FlyBase.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Developmental protein; Metal-binding; Neurogenesis; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..611
FT /note="Fez family zinc finger protein erm"
FT /evidence="ECO:0000305"
FT /id="PRO_0000443091"
FT ZN_FING 318..340
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 346..368
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 374..396
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 402..424
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 430..452
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 458..481
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 389
FT /note="L->H: In Fez-1; Reduced protein stability resulting
FT is abnormal expansion of Type II neuroblast lineage due to
FT dedifferentiation of intermediate neuronal progenitors
FT (INPs). In lamina L3 neurons, growth cones display defects
FT in morphology and incorrect targeting to the proximal
FT domain of the outer medulla. Reduced expression of cell
FT surface proteins dpr17 and dpr1 as well as the netrins NetA
FT and NetB in L3 neurons. No effect on L3 dendrite branching
FT and M3 layer innervation of Tm9 neurons."
FT /evidence="ECO:0000269|PubMed:20152183,
FT ECO:0000269|PubMed:29513217"
SQ SEQUENCE 611 AA; 66441 MW; 2C9744B031DA9A95 CRC64;
MVYFSPRGMQ PCSPAGEIAM MPPSKSPVME SAASEQNPAQ QSQQQDEQSA KRACPLKFSI
AKIMEPDHRP SQVPPPQPAP VSFATNDDDE DEDPEIDADS ERSCSPIEVI SLDQSPSTVN
YDSAFKKYVP GPCSGATSSV ASPPSTAAVQ QFVSSRHQEL LSQYPLLYYA PNQLMCAAAA
AQYAALTAQQ QSLASAAHLS SFTASLNASL HHSQSLRRNL GHPLAAAAAV AAVAQSQAVP
NLQHTLEKSP VAQRTAQSSG LQANLKRKRS PQDQGEVTPP PASTATSATG ARSRSPSPQG
SIEDSSPGSA SGGKPKTFSC LECGKVFNAH YNLTRHMPVH TGARPFVCKV CGKGFRQAST
LCRHKIIHTS EKPHKCQTCG KAFNRSSTLN THSRIHAGYK PFVCEYCGKG FHQKGNYKNH
KLTHSGEKAY KCNICNKAFH QVYNLTFHMH THNDKKPYTC RVCAKGFCRN FDLKKHMRKL
HEIGGDLDDL DMPPTYDRRR EYTRREPLAS GYGQASGQLT PDSSSGSMSP PINVTTPPLS
SGETSNPAWP RSAVSQYPPG GFHHQLGVAP PHDYPSGSAF LQLQPQQPHP QSQQHHQQQQ
RLSETFIAKV F
