EZRI_RAT
ID EZRI_RAT Reviewed; 586 AA.
AC P31977; Q5WQV4; Q66H97; Q8VHK3;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Ezrin;
DE AltName: Full=Cytovillin;
DE AltName: Full=Villin-2;
DE AltName: Full=p81;
GN Name=Ezr; Synonyms=Vil2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RA Harita Y., Koike H., Han G., Miyauchi N., Karasawa T., Suzuki K.,
RA Shimizu F., Kawachi H.;
RT "Rattus norvegicus ezrin.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-455.
RC STRAIN=Sprague-Dawley;
RA Gunn-Moore F.J., Tait S., Brophy P.J.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 427-586, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Wistar; TISSUE=Intestine;
RX PubMed=7640303; DOI=10.1016/0167-4781(95)00090-4;
RA Barila D., Murgia C., Nobili F., Perozzi G.;
RT "Transcriptional regulation of the ezrin gene during rat intestinal
RT development and epithelial differentiation.";
RL Biochim. Biophys. Acta 1263:133-140(1995).
RN [5]
RP PROTEIN SEQUENCE OF 28-35; 101-107; 263-273; 372-379; 428-435 AND 530-542,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP INTERACTION WITH PODXL AND SLC9A3R2, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11457882; DOI=10.1172/jci12539;
RA Takeda T., McQuistan T., Orlando R.A., Farquhar M.G.;
RT "Loss of glomerular foot processes is associated with uncoupling of
RT podocalyxin from the actin cytoskeleton.";
RL J. Clin. Invest. 108:289-301(2001).
RN [7]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15797715; DOI=10.1016/j.mcn.2004.11.014;
RA Groenholm M., Teesalu T., Tyynelaa J., Piltti K., Boehling T.,
RA Wartiovaara K., Vaheri A., Carpen O.;
RT "Characterization of the NF2 protein merlin and the ERM protein ezrin in
RT human, rat, and mouse central nervous system.";
RL Mol. Cell. Neurosci. 28:683-693(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Probably involved in connections of major cytoskeletal
CC structures to the plasma membrane. In epithelial cells, required for
CC the formation of microvilli and membrane ruffles on the apical pole.
CC Along with PLEKHG6, required for normal macropinocytosis (By
CC similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: A head-to-tail association, of the N-terminal and
CC C-terminal halves results in a closed conformation (inactive form)
CC which is incapable of actin or membrane-binding. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PODXL and SLC9A3R2. Found in a complex with
CC EZR, PODXL and SLC9A3R2 (PubMed:11457882). Interacts with PALS1.
CC Interacts with MCC, PLEKHG6, SCYL3/PACE1, SLC9A3R1 and TMEM8B.
CC Interacts (when phosphorylated) with FES/FPS. Interacts with dimeric
CC S100P, the interaction may be activating through unmasking of F-actin
CC binding sites. Identified in complexes that contain VIM, EZR, AHNAK,
CC BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin. Detected in a complex
CC composed of at least EZR, AHNAK, PPL and PRX. Interacts with PDPN (via
CC cytoplasmic domain); activates RHOA and promotes epithelial-mesenchymal
CC transition. Interacts with SPN/CD43 cytoplasmic tail, CD44 and ICAM2
CC (By similarity). {ECO:0000250|UniProtKB:P15311,
CC ECO:0000250|UniProtKB:P26040, ECO:0000250|UniProtKB:P31976,
CC ECO:0000250|UniProtKB:Q8HZQ5, ECO:0000269|PubMed:11457882}.
CC -!- INTERACTION:
CC P31977; Q63155: Dcc; NbExp=2; IntAct=EBI-917242, EBI-1798965;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P15311}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P15311}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P15311}. Cell projection
CC {ECO:0000250|UniProtKB:P15311}. Cell projection, microvillus membrane
CC {ECO:0000250|UniProtKB:P15311}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P15311}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P15311}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:P15311}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P15311}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P15311}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:P15311}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P15311}. Cell projection, microvillus
CC {ECO:0000250|UniProtKB:P26040}. Note=Localization to the apical
CC membrane of parietal cells depends on the interaction with PALS1.
CC Microvillar peripheral membrane protein (cytoplasmic side) (By
CC similarity). Localizes to cell extensions and peripheral processes of
CC astrocytes. Colocalizes with EZR and SLC9A3R2 at the apical cell
CC membrane of glomerular epithelium cells. {ECO:0000250|UniProtKB:P15311,
CC ECO:0000269|PubMed:11457882, ECO:0000269|PubMed:15797715}.
CC -!- TISSUE SPECIFICITY: Glomerular epithelium cell (podocyte). Expressed in
CC cerebrum, cerebellum and hippocampus (at protein level). Expressed in
CC the small intestine, lung, kidney and ovaries.
CC {ECO:0000269|PubMed:11457882, ECO:0000269|PubMed:15797715,
CC ECO:0000269|PubMed:7640303}.
CC -!- DEVELOPMENTAL STAGE: Levels increase in the fetal gut epithelium
CC between day 15 and day 20 of gestation and during the first week after
CC birth. {ECO:0000269|PubMed:7640303}.
CC -!- DOMAIN: Has three main structural domains: an N-terminal FERM domain, a
CC central alpha-helical domain and a C-terminal actin-binding domain.
CC {ECO:0000250|UniProtKB:P15311}.
CC -!- DOMAIN: The FERM domain is organized in a clover-shaped structure that
CC comprises three subdomains identified as F1 (residues 2-82), F2
CC (residues 96-198), and F3 (residues 204-296). In the active form, the
CC subdomain F3 adopts two mutually exclusive conformational isomers where
CC a row of four phenylalanine side chains (Phe250, Phe255, Phe267 and
CC Phe269) must point in the same direction. In the autoinhibited form,
CC the F3 subdomain interacts with the C-terminal domain (residues 516-
CC 586) and stabilizes the structure, selecting only one possible
CC arrangement of phenylalanine side chains. The FERM domain mediates
CC binding to membrane lipids and signaling molecules.
CC {ECO:0000250|UniProtKB:P15311}.
CC -!- DOMAIN: The central alpha-helical domain is composed of two alpha
CC helices (residues 326-406 and 417-466) connected by a linker. It
CC protrudes from the FERM domain forming a coiled coil structure where
CC the linker can have either a loop or a helix conformation. The monomer
CC is predicted to form an intra-molecular helix-loop-helix coiled coil
CC structure. Whereas the dimer adopts an elongated dumbbell-shaped
CC configuration where continuous alpha helices from each protomer are
CC organized in a antiparallel coiled coil structure that connect FERM:C-
CC terminal domain swapped complex at each end. The dimer is predicted to
CC link actin filaments parallel to the plasma membrane.
CC {ECO:0000250|UniProtKB:P15311}.
CC -!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
CC cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
CC transnitrosylase complex. {ECO:0000250|UniProtKB:P15311}.
CC -!- PTM: Phosphorylated by tyrosine-protein kinases. Phosphorylation by
CC ROCK2 suppresses the head-to-tail association of the N-terminal and C-
CC terminal halves resulting in an opened conformation which is capable of
CC actin and membrane-binding (By similarity). {ECO:0000250}.
CC -!- PTM: S-nitrosylation is induced by interferon-gamma and oxidatively-
CC modified low-densitity lipoprotein (LDL(ox)) possibly implicating the
CC iNOS-S100A8/9 transnitrosylase complex. {ECO:0000250|UniProtKB:P15311}.
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DR EMBL; AY428869; AAR91694.1; -; mRNA.
DR EMBL; BC081958; AAH81958.1; -; mRNA.
DR EMBL; AF450298; AAL47844.1; -; mRNA.
DR EMBL; X67788; CAA48004.1; -; mRNA.
DR PIR; S58759; S58759.
DR RefSeq; NP_062230.1; NM_019357.1.
DR AlphaFoldDB; P31977; -.
DR BMRB; P31977; -.
DR SMR; P31977; -.
DR BioGRID; 248535; 2.
DR CORUM; P31977; -.
DR IntAct; P31977; 3.
DR STRING; 10116.ENSRNOP00000046593; -.
DR iPTMnet; P31977; -.
DR PhosphoSitePlus; P31977; -.
DR World-2DPAGE; 0004:P31977; -.
DR jPOST; P31977; -.
DR PaxDb; P31977; -.
DR PRIDE; P31977; -.
DR Ensembl; ENSRNOT00000046746; ENSRNOP00000046593; ENSRNOG00000018524.
DR GeneID; 54319; -.
DR KEGG; rno:54319; -.
DR CTD; 7430; -.
DR RGD; 621161; Ezr.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT00960000186596; -.
DR HOGENOM; CLU_003623_6_2_1; -.
DR InParanoid; P31977; -.
DR OMA; HSGMLRE; -.
DR OrthoDB; 627741at2759; -.
DR PhylomeDB; P31977; -.
DR TreeFam; TF313935; -.
DR Reactome; R-RNO-373752; Netrin-1 signaling.
DR Reactome; R-RNO-437239; Recycling pathway of L1.
DR PRO; PR:P31977; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018524; Expressed in stomach and 19 other tissues.
DR ExpressionAtlas; P31977; baseline and differential.
DR Genevisible; P31977; RN.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0097449; C:astrocyte projection; IDA:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0051286; C:cell tip; IDA:RGD.
DR GO; GO:0036064; C:ciliary basal body; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0098592; C:cytoplasmic side of apical plasma membrane; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0030175; C:filopodium; IDA:RGD.
DR GO; GO:0001772; C:immunological synapse; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0044393; C:microspike; IDA:RGD.
DR GO; GO:0005902; C:microvillus; ISO:RGD.
DR GO; GO:0031528; C:microvillus membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0044853; C:plasma membrane raft; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097454; C:Schwann cell microvillus; IDA:RGD.
DR GO; GO:0030315; C:T-tubule; IDA:RGD.
DR GO; GO:0001931; C:uropod; ISO:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0051018; F:protein kinase A binding; ISO:RGD.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:RGD.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0044548; F:S100 protein binding; ISO:RGD.
DR GO; GO:0005198; F:structural molecule activity; TAS:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0030953; P:astral microtubule organization; ISO:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:RGD.
DR GO; GO:0043622; P:cortical microtubule organization; ISO:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; IEP:RGD.
DR GO; GO:0051660; P:establishment of centrosome localization; ISO:RGD.
DR GO; GO:0061028; P:establishment of endothelial barrier; ISO:RGD.
DR GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; ISO:RGD.
DR GO; GO:0046847; P:filopodium assembly; IMP:RGD.
DR GO; GO:0001951; P:intestinal D-glucose absorption; ISO:RGD.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:0022614; P:membrane to membrane docking; ISO:RGD.
DR GO; GO:0030033; P:microvillus assembly; ISO:RGD.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; ISO:RGD.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; ISO:RGD.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISO:RGD.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; ISO:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:RGD.
DR GO; GO:0010737; P:protein kinase A signaling; ISO:RGD.
DR GO; GO:0072697; P:protein localization to cell cortex; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0031503; P:protein-containing complex localization; ISO:RGD.
DR GO; GO:0031623; P:receptor internalization; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR GO; GO:0032532; P:regulation of microvillus length; ISO:RGD.
DR GO; GO:1902115; P:regulation of organelle assembly; ISO:RGD.
DR GO; GO:0003376; P:sphingosine-1-phosphate receptor signaling pathway; ISO:RGD.
DR GO; GO:1902896; P:terminal web assembly; ISO:RGD.
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; IPR019747; FERM_CS.
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; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cell projection; Cell shape; Coiled coil;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane;
KW Phosphoprotein; Reference proteome; S-nitrosylation.
FT CHAIN 1..586
FT /note="Ezrin"
FT /id="PRO_0000219411"
FT DOMAIN 2..295
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 244..586
FT /note="Interaction with SCYL3"
FT /evidence="ECO:0000250"
FT REGION 306..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 302..462
FT /evidence="ECO:0000255"
FT MOTIF 115..120
FT /note="[IL]-x-C-x-x-[DE] motif"
FT /evidence="ECO:0000250|UniProtKB:P15311"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P15311"
FT MOD_RES 146
FT /note="Phosphotyrosine; by PDGFR"
FT /evidence="ECO:0000250|UniProtKB:P15311"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15311"
FT MOD_RES 478
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15311"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 567
FT /note="Phosphothreonine; by ROCK2 and PKC/PRKCI"
FT /evidence="ECO:0000250|UniProtKB:P15311"
FT CONFLICT 455
FT /note="D -> E (in Ref. 3; AAL47844)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="L -> P (in Ref. 4; CAA48004)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="L -> Q (in Ref. 1; AAR91694)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 69391 MW; 3A5287052E74CCC9 CRC64;
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV DNKGFPTWLK
LDKKVSAQEV RKENPVQFKF RAKFYPEDVA DELIQDITQK LFFLQVKEGI LSDEIYCPPE
TAVLLGSYAV QAKFGDYNKE MHKSGYLSSE RLIPQRVMDQ HKLSRDQWED RIQVWHAEHR
GMLKDSAMLE YLKIAQDLEM YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF
PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI
EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM LREKEELMLR LQDFEQKTKR
AEKELSEQIE KALQLEEERR RAQEEAERLE ADRMAALRAK EELERQAQDQ IKSQEQLAAE
LAEYTAKIAL LEEARRRKED EVEEWQHRAK EAQDDLVKTK EELHLVMTAP PPPPPPVYEP
VNYHVQEGLQ DEGAEPMGYS AELSSEGILD DRNEEKRITE AEKNERVQRQ LLTLSNELSQ
ARDENKRTHN DIIHNENMRQ GRDKYKTLRQ IRQGNTKQRI DEFEAM
