EPB41_MOUSE
ID EPB41_MOUSE Reviewed; 858 AA.
AC P48193; A2A843; Q5DTQ8; Q68FF1; Q6NVF5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Protein 4.1;
DE Short=P4.1;
DE AltName: Full=4.1R;
DE AltName: Full=Band 4.1;
DE AltName: Full=Erythrocyte membrane protein band 4.1 {ECO:0000312|MGI:MGI:95401};
GN Name=Epb41 {ECO:0000312|MGI:MGI:95401};
GN Synonyms=Epb4.1 {ECO:0000312|MGI:MGI:95401}, Kiaa4056;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RC STRAIN=BALB/cJ;
RX PubMed=8429050; DOI=10.1016/s0021-9258(18)53759-5;
RA Huang J.-P., Tang C.-J.C., Kou G.-H., Marchesi V.T., Benz E.J. Jr.,
RA Tang T.K.;
RT "Genomic structure of the locus encoding protein 4.1. Structural basis for
RT complex combinational patterns of tissue-specific alternative RNA
RT splicing.";
RL J. Biol. Chem. 268:3758-3766(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP PROTEIN SEQUENCE OF 709-713, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP CHARACTERIZATION OF CARBOXY-TERMINAL DOMAIN.
RX PubMed=11432737; DOI=10.1046/j.1432-1327.2001.02276.x;
RA Scott C., Phillips G.W., Baines A.J.;
RT "Properties of the C-terminal domain of 4.1 proteins.";
RL Eur. J. Biochem. 268:3709-3717(2001).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-223, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541 AND SER-543, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-541; SER-543;
RP SER-556; SER-658 AND SER-668, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH ATP2B1.
RX PubMed=23460639; DOI=10.1074/jbc.m112.436659;
RA Liu C., Weng H., Chen L., Yang S., Wang H., Debnath G., Guo X., Wu L.,
RA Mohandas N., An X.;
RT "Impaired intestinal calcium absorption in protein 4.1R-deficient mice due
RT to altered expression of plasma membrane calcium ATPase 1b (PMCA1b).";
RL J. Biol. Chem. 288:11407-11415(2013).
CC -!- FUNCTION: Protein 4.1 is a major structural element of the erythrocyte
CC membrane skeleton. It plays a key role in regulating membrane physical
CC properties of mechanical stability and deformability by stabilizing
CC spectrin-actin interaction. Recruits DLG1 to membranes. Required for
CC dynein-dynactin complex and NUMA1 recruitment at the mitotic cell
CC cortex during anaphase. {ECO:0000250|UniProtKB:P11171}.
CC -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower
CC affinity to band III protein. Associates with the nuclear mitotic
CC apparatus. Binds calmodulin, CENPJ and DLG1. Also found to associate
CC with contractile apparatus and tight junctions. Interacts with NUMA1;
CC this interaction is negatively regulated by CDK1 during metaphase and
CC promotes anaphase-specific localization of NUMA1 in symmetrically
CC dividing cells. Interacts with ATP2B1; regulates small intestinal
CC calcium absorption through regulation of membrane expression of ATP2B1
CC (PubMed:23460639). {ECO:0000250|UniProtKB:P11171,
CC ECO:0000269|PubMed:23460639}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11171}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P11171}. Cytoplasm, cell
CC cortex {ECO:0000250|UniProtKB:P11171}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=P48193-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48193-2; Sequence=VSP_012874;
CC -!- PTM: O-glycosylated; contains N-acetylglucosamine side chains in the C-
CC terminal domain. {ECO:0000250}.
CC -!- PTM: Phosphorylated at multiple sites by different protein kinases and
CC each phosphorylation event selectively modulates the protein's
CC functions.
CC -!- PTM: Phosphorylation on Tyr-654 reduces the ability of 4.1 to promote
CC the assembly of the spectrin/actin/4.1 ternary complex.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90280.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L00919; AAA37122.1; -; mRNA.
DR EMBL; L00919; AAA37123.1; -; mRNA.
DR EMBL; AK220462; BAD90280.1; ALT_INIT; mRNA.
DR EMBL; AL607088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL669981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC068138; AAH68138.1; -; mRNA.
DR EMBL; BC079875; AAH79875.1; -; mRNA.
DR CCDS; CCDS18717.1; -. [P48193-1]
DR CCDS; CCDS51317.1; -. [P48193-2]
DR PIR; A46613; A46613.
DR RefSeq; NP_001122078.1; NM_001128606.1. [P48193-2]
DR RefSeq; NP_001122079.1; NM_001128607.1.
DR RefSeq; NP_906273.3; NM_183428.3. [P48193-1]
DR AlphaFoldDB; P48193; -.
DR BMRB; P48193; -.
DR SMR; P48193; -.
DR BioGRID; 234673; 7.
DR STRING; 10090.ENSMUSP00000101595; -.
DR iPTMnet; P48193; -.
DR PhosphoSitePlus; P48193; -.
DR EPD; P48193; -.
DR jPOST; P48193; -.
DR MaxQB; P48193; -.
DR PaxDb; P48193; -.
DR PeptideAtlas; P48193; -.
DR PRIDE; P48193; -.
DR ProteomicsDB; 285570; -. [P48193-1]
DR ProteomicsDB; 285571; -. [P48193-2]
DR Antibodypedia; 30998; 361 antibodies from 30 providers.
DR DNASU; 269587; -.
DR Ensembl; ENSMUST00000030739; ENSMUSP00000030739; ENSMUSG00000028906. [P48193-1]
DR Ensembl; ENSMUST00000054917; ENSMUSP00000060375; ENSMUSG00000028906. [P48193-2]
DR Ensembl; ENSMUST00000084253; ENSMUSP00000081274; ENSMUSG00000028906. [P48193-2]
DR Ensembl; ENSMUST00000105972; ENSMUSP00000101592; ENSMUSG00000028906. [P48193-1]
DR Ensembl; ENSMUST00000105981; ENSMUSP00000101601; ENSMUSG00000028906. [P48193-1]
DR GeneID; 269587; -.
DR KEGG; mmu:269587; -.
DR UCSC; uc008val.3; mouse. [P48193-2]
DR UCSC; uc008vam.3; mouse. [P48193-1]
DR CTD; 2035; -.
DR MGI; MGI:95401; Epb41.
DR VEuPathDB; HostDB:ENSMUSG00000028906; -.
DR eggNOG; KOG3527; Eukaryota.
DR GeneTree; ENSGT00940000157833; -.
DR InParanoid; P48193; -.
DR OMA; EHHTFFX; -.
DR OrthoDB; 262540at2759; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 269587; 2 hits in 39 CRISPR screens.
DR ChiTaRS; Epb41; mouse.
DR PRO; PR:P48193; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P48193; protein.
DR Bgee; ENSMUSG00000028906; Expressed in blood and 244 other tissues.
DR ExpressionAtlas; P48193; baseline and differential.
DR Genevisible; P48193; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISS:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0030507; F:spectrin binding; ISS:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:MGI.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0032092; P:positive regulation of protein binding; IGI:MGI.
DR GO; GO:1904778; P:positive regulation of protein localization to cell cortex; ISS:UniProtKB.
DR GO; GO:0051924; P:regulation of calcium ion transport; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:MGI.
DR GO; GO:1904478; P:regulation of intestinal absorption; IMP:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR008379; Band_4.1_C.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR021187; Band_41_protein_chordates.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FERM-adjacent.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR007477; SAB_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23280:SF12; PTHR23280:SF12; 2.
DR Pfam; PF05902; 4_1_CTD; 1.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF04382; SAB; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF47031; SSF47031; 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 Actin-binding; Alternative splicing; Calmodulin-binding; Cell cycle;
KW Cell division; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Glycoprotein; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..858
FT /note="Protein 4.1"
FT /id="PRO_0000219391"
FT DOMAIN 211..492
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..608
FT /note="Hydrophilic"
FT REGION 518..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..707
FT /note="Spectrin--actin-binding"
FT REGION 710..858
FT /note="C-terminal (CTD)"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 223
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 654
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 730
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 853
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT VAR_SEQ 610..663
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_012874"
FT CONFLICT 1..3
FT /note="MTT -> EPLKGREPRRARTRPGPARPGPCQVPVLCSP (in Ref. 4;
FT AAH68138)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="A -> V (in Ref. 1; AAA37123)"
FT /evidence="ECO:0000305"
FT CONFLICT 232..233
FT /note="KG -> NL (in Ref. 1; AAA37122)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="Y -> S (in Ref. 1; AAA37122)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="A -> R (in Ref. 1; AAA37122)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 858 AA; 95911 MW; 7CF1CD52D790D1FD CRC64;
MTTEKSLAAE AENSQHQQQK EEGEGATNSG QQETQLEEAS QAAAAEGSDQ GEQKLKASNG
DTPTHEDLTK NKERTSESRG LSRLLSSFLK RPKSQVSEEE GREVESEKEK GEGGQKEIEL
GNSLDEDIIL KAPIAAPEPE LKTDPSLDLH SLSSIETQPA QEEHREDPDS ETKEGEGIEE
CSGTEVKEDP ESRAEREPEA SQKPVRRHRN MHCKVSLLDD TVYECVVEKH AKGQDLLKRV
CEHLNLLEED YFGLALWDSA TSKTWLDSAK EIKKQVRGVP WNFTFNVKFY PPDPAQLTED
ITRYYLCLQL RQDIVAGRLP CSFATLALLG SYTIQSELGD YDPELHGMDY VSDFKLAPNQ
TKELEEKVME LHKSYRSMTP AQADLEFLEN AKKLSMYGVD LHKAKDLEGV DIILGVCSSG
LLVYKDKLRI NRFPWPKVLK ISYKRSSFFI KIRPGEQEHY ESTIGFKLPS YRAAKKLWKV
CVEHHTFFRL TSTDTIPKSK FLALGSKFRY SGRTQAQTRQ ASALIDRPAP HFERTASKRA
SRSLDGAAAA ESTDRSPRPT SAPAIAQSQV TEGPGAPIKK TPKEAVKVEE KRGEEPAEPA
EPEPTEAWKV EKTHTEVTVP TSNGDQTQKL AGKGEDLIRM RKKKRERLDG ENIYIRHSNL
MLEDLDKSQE EIKKHHASIS ELKKNFMESV PEPRPSEWDK RLSTHSPFRT LNINGQVPTG
DGPPLVKTQT VTISDTANAV KSEIPTKDVP IVHTETKTIT YEAAQTEDSN GDLDPGVLLT
AQTITSETTS STTTTQITKT VKGGISETRI EKRIVITGDA DIDHDQVLVQ AIKEAKEQHP
DMSVTKVVVH QETEISEE
