MERH_DROME
ID MERH_DROME Reviewed; 635 AA.
AC Q24564; Q24054; Q8SWY3;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Moesin/ezrin/radixin homolog 2;
DE AltName: Full=Ezrin-moesin-radixin 2;
DE AltName: Full=Merlin;
DE Short=dMerlin;
GN Name=Mer; Synonyms=EMR2; ORFNames=CG14228;
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|EMBL:AAM11326.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R {ECO:0000269|PubMed:8666669};
RC TISSUE=Embryo {ECO:0000269|PubMed:8666669};
RX PubMed=8666669; DOI=10.1083/jcb.133.4.843;
RA McCartney B.M., Fehon R.G.;
RT "Distinct cellular and subcellular patterns of expression imply distinct
RT functions for the Drosophila homologues of moesin and the neurofibromatosis
RT 2 tumor suppressor, merlin.";
RL J. Cell Biol. 133:843-852(1996).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
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 [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 218-307.
RC TISSUE=Embryo;
RA Winge P., Fleming J.T., Gobel V.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KIBRA; EX AND SAV.
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 [7]
RP INTERACTION WITH SCHIP1.
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: Regulator of 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 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. Mer acts synergistically along with Ex and Kibra to
CC regulate the Hippo signaling pathway. {ECO:0000269|PubMed:20159598,
CC ECO:0000269|PubMed:8666669}.
CC -!- SUBUNIT: Interacts with Moe and arm at the adherens junction
CC (PubMed:8666669). Forms a complex with Kibra and Ex (PubMed:20159598).
CC Interacts (via FERM domain) with Sav (via FBM motif) (PubMed:20159598).
CC Interacts with Schip1 (PubMed:26954546). {ECO:0000269|PubMed:20159598,
CC ECO:0000269|PubMed:26954546, ECO:0000269|PubMed:8666669}.
CC -!- INTERACTION:
CC Q24564; Q24564: Mer; NbExp=3; IntAct=EBI-180142, EBI-180142;
CC Q24564; Q9VA38: wts; NbExp=8; IntAct=EBI-180142, EBI-82717;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell membrane;
CC Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton.
CC Apical cell membrane. Note=Membrane-associated, adherens junctions and
CC endocytic compartments. Cytoplasmic, punctate.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the germline. Expressed
CC in the developing oocyte from stage 6 to the end of oogenesis and in
CC the apical ends of follical cells from stage 10. Ubiquitous expression
CC throughout embryogenesis with enhanced expression in mesoderm of early
CC embryos and midgut of late embryos. In embryonic CNS, expression is
CC seen in neuropil and developing brain and is enhanced in neuronal cell
CC bodies. In embryonic PNS, expression is seen within the cell body. In
CC third instar larvae, expression is uniform in the eye imaginal disk and
CC is enhanced at the morphogenetic furrow. In pupal eyes, expression is
CC seen in the cytoplasm of secondary and tertiary pigment cells, bristle
CC precursor cells and rhabdomeres. {ECO:0000269|PubMed:8666669}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically in embryos.
CC {ECO:0000269|PubMed:8666669}.
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DR EMBL; U49724; AAB08449.1; -; mRNA.
DR EMBL; AE014298; AAF49005.1; -; Genomic_DNA.
DR EMBL; AY094998; AAM11326.1; -; mRNA.
DR EMBL; U23799; AAA65060.1; -; mRNA.
DR RefSeq; NP_001285458.1; NM_001298529.1.
DR RefSeq; NP_523413.1; NM_078689.4.
DR PDB; 7EDR; X-ray; 2.53 A; A/B=8-314, C/D=510-635.
DR PDBsum; 7EDR; -.
DR AlphaFoldDB; Q24564; -.
DR SMR; Q24564; -.
DR BioGRID; 59275; 172.
DR DIP; DIP-17087N; -.
DR IntAct; Q24564; 9.
DR STRING; 7227.FBpp0074523; -.
DR TCDB; 8.A.25.1.3; the ezrin/radixin/moesin (ezrin) family.
DR iPTMnet; Q24564; -.
DR PaxDb; Q24564; -.
DR PRIDE; Q24564; -.
DR EnsemblMetazoa; FBtr0074754; FBpp0074523; FBgn0086384.
DR EnsemblMetazoa; FBtr0345992; FBpp0311877; FBgn0086384.
DR GeneID; 32979; -.
DR KEGG; dme:Dmel_CG14228; -.
DR CTD; 32979; -.
DR FlyBase; FBgn0086384; Mer.
DR VEuPathDB; VectorBase:FBgn0086384; -.
DR eggNOG; KOG3529; Eukaryota.
DR HOGENOM; CLU_003623_6_1_1; -.
DR InParanoid; Q24564; -.
DR OMA; KERVDYW; -.
DR OrthoDB; 627741at2759; -.
DR PhylomeDB; Q24564; -.
DR Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DME-5627123; RHO GTPases activate PAKs.
DR SignaLink; Q24564; -.
DR BioGRID-ORCS; 32979; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32979; -.
DR PRO; PR:Q24564; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0086384; Expressed in egg cell and 25 other tissues.
DR ExpressionAtlas; Q24564; baseline and differential.
DR Genevisible; Q24564; DM.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0106037; C:apicomedial cortex; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0098592; C:cytoplasmic side of apical plasma membrane; IDA:FlyBase.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0036375; C:Kibra-Ex-Mer complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:FlyBase.
DR GO; GO:0016006; C:Nebenkern; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0120219; C:subapical part of cell; IDA:FlyBase.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0009798; P:axis specification; IMP:FlyBase.
DR GO; GO:0007267; P:cell-cell signaling; IEP:UniProtKB.
DR GO; GO:0001745; P:compound eye morphogenesis; IGI:FlyBase.
DR GO; GO:0001751; P:compound eye photoreceptor cell differentiation; IGI:FlyBase.
DR GO; GO:0032456; P:endocytic recycling; IGI:FlyBase.
DR GO; GO:0006897; P:endocytosis; IEP:UniProtKB.
DR GO; GO:0010669; P:epithelial structure maintenance; IMP:FlyBase.
DR GO; GO:0035329; P:hippo signaling; IMP:UniProtKB.
DR GO; GO:0007112; P:male meiosis cytokinesis; IMP:FlyBase.
DR GO; GO:0051307; P:meiotic chromosome separation; IMP:FlyBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0060253; P:negative regulation of glial cell proliferation; IMP:FlyBase.
DR GO; GO:0046621; P:negative regulation of organ growth; IMP:FlyBase.
DR GO; GO:0019094; P:pole plasm mRNA localization; IMP:FlyBase.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:FlyBase.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IGI:FlyBase.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IDA:FlyBase.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:FlyBase.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:FlyBase.
DR GO; GO:0045463; P:R8 cell development; IGI:FlyBase.
DR GO; GO:0045464; P:R8 cell fate specification; IMP:FlyBase.
DR GO; GO:0045595; P:regulation of cell differentiation; IGI:FlyBase.
DR GO; GO:0001558; P:regulation of cell growth; IEP:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0046669; P:regulation of compound eye retinal cell programmed cell death; IMP:FlyBase.
DR GO; GO:0014013; P:regulation of gliogenesis; IBA:GO_Central.
DR GO; GO:0035330; P:regulation of hippo signaling; IBA:GO_Central.
DR GO; GO:0009966; P:regulation of signal transduction; IGI:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13194; FERM_C_ERM; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 6.10.360.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR011174; ERM.
DR InterPro; IPR041789; ERM_FERM_C.
DR InterPro; IPR000798; Ez/rad/moesin-like.
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; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR008954; Moesin_tail_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23281; PTHR23281; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR PIRSF; PIRSF002305; ERM; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF48678; SSF48678; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
KW Endocytosis; Membrane; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..635
FT /note="Moesin/ezrin/radixin homolog 2"
FT /id="PRO_0000219426"
FT DOMAIN 12..305
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084,
FT ECO:0000305"
FT CONFLICT 166
FT /note="G -> R (in Ref. 4; AAM11326)"
FT /evidence="ECO:0000305"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:7EDR"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:7EDR"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:7EDR"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:7EDR"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:7EDR"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 106..121
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 129..144
FT /evidence="ECO:0007829|PDB:7EDR"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 175..188
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:7EDR"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:7EDR"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:7EDR"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:7EDR"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:7EDR"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:7EDR"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:7EDR"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:7EDR"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:7EDR"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 284..304
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:7EDR"
FT STRAND 528..532
FT /evidence="ECO:0007829|PDB:7EDR"
FT STRAND 535..539
FT /evidence="ECO:0007829|PDB:7EDR"
FT STRAND 546..551
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 552..572
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 574..587
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 588..590
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 593..595
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 598..608
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 613..621
FT /evidence="ECO:0007829|PDB:7EDR"
FT HELIX 625..633
FT /evidence="ECO:0007829|PDB:7EDR"
SQ SEQUENCE 635 AA; 74492 MW; 940D6B8A0D160A3F CRC64;
MSPFGSKKNR SLSVRVSTFD SELEFKLEPR ASGQDLFDLV CRTIGLRESW YFGLQYVDTR
SNVSWLKMEK RVRDQRVELH ASNNVYVFSF YAKFFPENVS EELIQEITQH LFFLQVKQSI
LSMDIYCRPE ASVLLASYAV HVQYGPYDYE TYKDGMLAGG ELLPKGVTDQ YQMTPEMWEE
RIKTWYMDHE PMTRDEVEME YLKIAQDLDM YGVNYFPITN KNKTKLWLGV TSVGLNIYDE
RDKLTPKTTF QWNEIRHVSF DDKKFTIRLV DAKVSNFIFY SQDLHINKMI LDLCKGNHDL
YMRRRKPDTM EIQQMKAQAK EEKQRRQIER KKFIREKKLR EKAEHERYEL EKSMEHLQNE
MRMANDALRR SEETKELYFE KSRVNEEQMQ LTECKANHFK TEMDRLRERQ MKIEREKHDL
EKKIRDADFY VHQLTVENDK REAETEKLRK ELICAKMAER EATARLLEFL NSGRKSSTDS
LLTASSVSHA ANTASSMAAI STPSLITSSS TNDLETAGGA ELTTHSSHYL VQGDNSSGIS
DDFEPKEFIL TDNEMEQITN EMERNHLDYL RNSKQVQSQL QTLRSEIAPH KIEENQSNLD
ILSEAQIKAG ENKYSTLKKL KSGSTKARVA FFEEL
