EXPA_DROME
ID EXPA_DROME Reviewed; 1427 AA.
AC Q07436; Q9VPQ0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Protein expanded;
GN Name=ex; ORFNames=CG4114;
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 DISRUPTION PHENOTYPE.
RC TISSUE=Imaginal disk;
RX PubMed=8269855; DOI=10.1242/dev.118.4.1291;
RA Boedigheimer M., Laughon A.;
RT "Expanded: a gene involved in the control of cell proliferation in imaginal
RT discs.";
RL Development 118:1291-1301(1993).
RN [2]
RP SEQUENCE REVISION.
RA Boedigheimer M.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1181, AND IDENTIFICATION BY
RP 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).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KIBRA; MER AND HPO.
RX PubMed=20159598; DOI=10.1016/j.devcel.2009.12.012;
RA Yu J., Zheng Y., Dong J., Klusza S., Deng W.-M., Pan D.;
RT "Kibra functions as a tumor suppressor protein that regulates Hippo
RT signaling in conjunction with Merlin and Expanded.";
RL Dev. Cell 18:288-299(2010).
RN [8]
RP FUNCTION, INTERACTION WITH ACK AND YKI, DEVELOPMENTAL STAGE,
RP PHOSPHORYLATION AT TYR-227; TYR-423; TYR-679; TYR-766 AND TYR-1103, AND
RP MUTAGENESIS OF TYR-227; TYR-423; TYR-679; TYR-766 AND TYR-1103.
RX PubMed=27462444; DOI=10.1038/celldisc.2015.47;
RA Hu L., Xu J., Yin M.X., Zhang L., Lu Y., Wu W., Xue Z., Ho M.S., Gao G.,
RA Zhao Y., Zhang L.;
RT "Ack promotes tissue growth via phosphorylation and suppression of the
RT Hippo pathway component Expanded.";
RL Cell Discov. 2:15047-15047(2016).
RN [9]
RP FUNCTION, INTERACTION WITH SCHIP1, AND DISRUPTION PHENOTYPE.
RX PubMed=26954546; DOI=10.1016/j.devcel.2016.02.004;
RA Chung H.L., Augustine G.J., Choi K.W.;
RT "Drosophila Schip1 links Expanded and Tao-1 to regulate hippo signaling.";
RL Dev. Cell 36:511-524(2016).
CC -!- FUNCTION: Activates the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a
CC signaling pathway that plays a pivotal role in organ size control and
CC tumor suppression by restricting proliferation and promoting apoptosis
CC (PubMed:8269855, PubMed:20159598, PubMed:27462444, PubMed:26954546).
CC The core of this pathway is composed of a kinase cascade wherein Hippo
CC (Hpo), in complex with its regulatory protein Salvador (Sav),
CC phosphorylates and activates Warts (Wts) in complex with its regulatory
CC protein Mats, which in turn phosphorylates and inactivates the Yorkie
CC (Yki) oncoprotein. Ex acts synergistically along with Mer and Kibra to
CC regulate the Hippo signaling pathway (PubMed:20159598). Involved in the
CC control of cell proliferation in imaginal disks (PubMed:8269855,
CC PubMed:27462444). May bind to certain proteins of signal transduction
CC pathways by interaction with their SH3 domains (PubMed:20159598).
CC Required for apical localization of Schip1 (PubMed:26954546).
CC {ECO:0000269|PubMed:20159598, ECO:0000269|PubMed:26954546,
CC ECO:0000269|PubMed:27462444, ECO:0000269|PubMed:8269855}.
CC -!- SUBUNIT: Forms a complex with Kibra and Mer (PubMed:20159598).
CC Interacts (via RXPPXY motif) with Kibra (via domain WW 1)
CC (PubMed:20159598). Interacts with Mer and Hpo (via SARAH domain)
CC (PubMed:20159598). Interacts with Schip1; the interaction results in
CC recruitment of Schip1 to the apical cell membrane (PubMed:26954546).
CC Interacts with ack and yki (PubMed:27462444).
CC {ECO:0000269|PubMed:20159598, ECO:0000269|PubMed:26954546,
CC ECO:0000269|PubMed:27462444}.
CC -!- INTERACTION:
CC Q07436; P10040: crb; NbExp=2; IntAct=EBI-192660, EBI-672928;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:20159598}. Note=Apical surface of disk cells.
CC -!- DEVELOPMENTAL STAGE: Detected in wing disks (at protein level).
CC {ECO:0000269|PubMed:27462444}.
CC -!- PTM: Phosphorylated by Ack at several tyrosines including Tyr-227, Tyr-
CC 423, Tyr-679, Tyr-766 and Tyr-1103. {ECO:0000269|PubMed:27462444}.
CC -!- DISRUPTION PHENOTYPE: Hyperplasia of the imaginal disk resulting in
CC wing overgrowth (PubMed:8269855). This overgrowth is limited to
CC specific regions along the 2 wing axes (PubMed:8269855). Defects also
CC in eyes, head, thorax and limbs where duplication and bulging often
CC occur (PubMed:8269855). RNAi-mediated knockdown reduces the amount of
CC Schip1 in the apical region of the cell. {ECO:0000269|PubMed:26954546,
CC ECO:0000269|PubMed:8269855}.
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DR EMBL; L14768; AAB39774.1; -; mRNA.
DR EMBL; AE014134; AAF51495.1; -; Genomic_DNA.
DR EMBL; AY069068; AAL39213.1; -; mRNA.
DR PIR; T13720; T13720.
DR RefSeq; NP_001259823.1; NM_001272894.1.
DR RefSeq; NP_476840.2; NM_057492.4.
DR AlphaFoldDB; Q07436; -.
DR SMR; Q07436; -.
DR BioGRID; 59474; 44.
DR DIP; DIP-59337N; -.
DR IntAct; Q07436; 1.
DR STRING; 7227.FBpp0077719; -.
DR iPTMnet; Q07436; -.
DR PaxDb; Q07436; -.
DR DNASU; 33218; -.
DR EnsemblMetazoa; FBtr0078059; FBpp0077719; FBgn0004583.
DR EnsemblMetazoa; FBtr0329832; FBpp0302878; FBgn0004583.
DR GeneID; 33218; -.
DR KEGG; dme:Dmel_CG4114; -.
DR UCSC; CG4114-RA; d. melanogaster.
DR CTD; 110023; -.
DR FlyBase; FBgn0004583; ex.
DR VEuPathDB; VectorBase:FBgn0004583; -.
DR eggNOG; KOG4371; Eukaryota.
DR GeneTree; ENSGT00940000162787; -.
DR HOGENOM; CLU_003533_0_0_1; -.
DR InParanoid; Q07436; -.
DR OMA; IDGEYMF; -.
DR OrthoDB; 339620at2759; -.
DR PhylomeDB; Q07436; -.
DR Reactome; R-DME-451806; Phosphorylation-independent inhibition of YKI.
DR SignaLink; Q07436; -.
DR BioGRID-ORCS; 33218; 0 hits in 3 CRISPR screens.
DR ChiTaRS; ex; fly.
DR GenomeRNAi; 33218; -.
DR PRO; PR:Q07436; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0004583; Expressed in wing disc and 25 other tissues.
DR ExpressionAtlas; Q07436; baseline and differential.
DR Genevisible; Q07436; DM.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0098592; C:cytoplasmic side of apical plasma membrane; IDA:FlyBase.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0036375; C:Kibra-Ex-Mer complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0120219; C:subapical part of cell; IDA:FlyBase.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0001751; P:compound eye photoreceptor cell differentiation; IMP:FlyBase.
DR GO; GO:0032456; P:endocytic recycling; IGI:FlyBase.
DR GO; GO:0097009; P:energy homeostasis; IGI:FlyBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0045571; P:negative regulation of imaginal disc growth; IMP:FlyBase.
DR GO; GO:0046621; P:negative regulation of organ growth; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IDA:FlyBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0045595; P:regulation of cell differentiation; IGI:FlyBase.
DR GO; GO:0007096; P:regulation of exit from mitosis; IMP:FlyBase.
DR GO; GO:0040008; P:regulation of growth; IGI:FlyBase.
DR GO; GO:0009966; P:regulation of signal transduction; IGI:FlyBase.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13185; FERM_C_FRMD1_FRMD6; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR041781; FRMD6-FERM_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Membrane; Phosphoprotein;
KW Reference proteome; SH3-binding; Transcription; Transcription regulation.
FT CHAIN 1..1427
FT /note="Protein expanded"
FT /id="PRO_0000219443"
FT DOMAIN 26..399
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 176..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 842..847
FT /note="RXPPXY motif"
FT MOTIF 1008..1020
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 1149..1157
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 178..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..851
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1021
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1247
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 227
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:27462444"
FT MOD_RES 423
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:27462444"
FT MOD_RES 679
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:27462444"
FT MOD_RES 766
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:27462444"
FT MOD_RES 1103
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:27462444"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 227
FT /note="Y->A: Inhibits wing growth. Reduces phosphorylation
FT by Ack; when associated with A-423, A-679, A-766 and A-
FT 1103."
FT /evidence="ECO:0000269|PubMed:27462444"
FT MUTAGEN 423
FT /note="Y->A: Inhibits wing growth. Reduces phosphorylation
FT by Ack; when associated with A-227, A-679, A-766 and A-
FT 1103."
FT /evidence="ECO:0000269|PubMed:27462444"
FT MUTAGEN 679
FT /note="Y->A: Inhibits wing growth. Reduces phosphorylation
FT by Ack; when associated with A-227, A-423, A-766 and A-
FT 1103."
FT /evidence="ECO:0000269|PubMed:27462444"
FT MUTAGEN 766
FT /note="Y->A: Inhibits wing growth. Reduces phosphorylation
FT by Ack; when associated with A-227, A-423, A-679, and A-
FT 1103."
FT /evidence="ECO:0000269|PubMed:27462444"
FT MUTAGEN 1103
FT /note="Y->A: Inhibits wing growth. Reduces phosphorylation
FT by Ack; when associated with A-227, A-423, A-679 and A-
FT 766."
FT /evidence="ECO:0000269|PubMed:27462444"
FT CONFLICT 160..161
FT /note="EQ -> DE (in Ref. 1; AAB39774)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="S -> L (in Ref. 1; AAB39774)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="F -> S (in Ref. 1; AAB39774)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="I -> T (in Ref. 1; AAB39774)"
FT /evidence="ECO:0000305"
FT CONFLICT 671
FT /note="A -> D (in Ref. 1; AAB39774)"
FT /evidence="ECO:0000305"
FT CONFLICT 693
FT /note="Q -> S (in Ref. 1; AAB39774)"
FT /evidence="ECO:0000305"
FT CONFLICT 1293..1294
FT /note="SM -> FN (in Ref. 1; AAB39774)"
FT /evidence="ECO:0000305"
FT CONFLICT 1422
FT /note="Q -> QQQ (in Ref. 1; AAB39774)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1427 AA; 153644 MW; 3CC1AD0B4D900EB2 CRC64;
MRAFCTVSAP LEVCASSAEQ LSPGSRFLAL RLLGQQQPKT LYFLVDAKSR VREVYTQTCL
HFATQGMLDT ELFGLAVLID GEYMFADPES KLSKYGPKSW RSSHTHGLDA NGRPLLELHF
RVQFYIESPF MLKDETSRHN YYLQLRHNIL QRDLPREQAE QALVFLAGLA LQADLGDAPP
GTSNSKDDSG EETSASPSNG GRGLSATTTL PKISKRANER MLRLSTYVAS TSKRETIPLP
PSLPPNGADY YRIEDYLPSG LHTPWARSAM RACHREHLGM ATAEAELLYI QQACSLHETI
NAHTYRMRLA KSEQGSGSAW FVVYAKGIKI LGGESTNSSS NPETTTFLWP NITKLSFERK
KFEIRSGESR ITLYAASDEK NKLLLTLCKD THQWSMKLAA RLKEVSKREE EEAAESQRLH
ASYACSRSLL LPYKSKNEQR ISVISSTSSN TTSGIVSDRV HSEDELEIMI NTPPAPLAAP
STESLALAHL LDRPSVSRQT SSVGQMSLKD LEEQLAALSV RPQDASSNGA TIVTNSSVQR
NSMGTTANDS STATDSPSSQ HNIGSQCSST CSTVVVTSPV NGAGASSSGA PIPVHSTSSS
LELGFSHTAQ NSALSETSPD DFLSTSAREE TESVSGASGV YTLAHGAPPT ETSGVYTMHS
SELTGQSSEI AESEKSSHYG MFQPQKLEET HVQHSDSVDG KKKEDFRPRS DSNVSTGSSF
RGDGSDPTDN KHSLLSAEEL TNLIVGRGTY PSRKTVSSSL HSDCDYVTLP LGDQGEEEVD
QPPAPPPPYS ARHEKTGLCG PPIAKPIPKP IAVVAPKPDS PPCSPPVPPA PIPAPPPAIR
RRDPPPYSIS SKPRPTSLIS VSSSAHPAPS AAGSMSSLKS EEVTARFITT RPQISILKAH
TSLIPDGAKP SYAAPHHCSS VASSNGSVCS HQLSQQSLHN SNYAGGSQAS LHHHHVPSHH
RHSGSAAIGI VPYGLHKSTA SLHHQQSCVL LPVIKPRQFL APPPPSLPRQ PPPPPPPNHP
HLASHLYERE MARKQLELYQ QQLYSDVDYV IYPIQDPAVS QQEYLDAKQG SLLAAMAQAA
PPPPHHPYLA MQVSPAIYRS TPYLPLTLST HSRYASTQNL SDTYVQLPGP GYSPLYSPSM
ASLCSSYEPP PPPPLHPAAL AAAAAAGAGS SSSSMFARSR SDDNILNSLD LLPKGKRLPP
PPPPPYVNRR LKKPPMPAPS EKPPPIPSKP IPSRMSPIPP RKPPTLNPHH ANSPLTKTSS
GAQWAGERPR PDLGLGLGLN RGNNSILAQL QASMVAQSHA QAQAQALDIA LLREKSKHLD
LPLISALCND RSLLKQTKVV INPKTGQEMP TSSAQPSGAT TNGVANSSAG AGTLSKARKG
STVSHRHPQD KLPPLPVQQL AEANNYVIDP AVMMKQQQQQ QQHNKTS
