2A5E_HUMAN
ID 2A5E_HUMAN Reviewed; 467 AA.
AC Q16537; A4FU37; B7ZAW5; B7ZKK8; B7ZKK9; J3KQN6; Q52LW4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform;
DE AltName: Full=PP2A B subunit isoform B'-epsilon;
DE AltName: Full=PP2A B subunit isoform B56-epsilon;
DE AltName: Full=PP2A B subunit isoform PR61-epsilon;
DE AltName: Full=PP2A B subunit isoform R5-epsilon;
GN Name=PPP2R5E;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 449-455.
RC TISSUE=Fetal retina;
RX PubMed=8694763; DOI=10.1042/bj3170187;
RA Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I.,
RA Merlevede W., Goris J., Hemmings B.A.;
RT "The variable subunit associated with protein phosphatase 2A0 defines a
RT novel multimember family of regulatory subunits.";
RL Biochem. J. 317:187-194(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=8703017; DOI=10.1074/jbc.271.36.22081;
RA McCright B., Rivers A.M., Audlin S., Virshup D.M.;
RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits
RT encodes differentiation-induced phosphoproteins that target PP2A to both
RT nucleus and cytoplasm.";
RL J. Biol. Chem. 271:22081-22089(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC 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 [6]
RP INTERACTION WITH SGO1.
RX PubMed=16541025; DOI=10.1038/nature04663;
RA Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T.,
RA Kawashima S.A., Watanabe Y.;
RT "Shugoshin collaborates with protein phosphatase 2A to protect cohesin.";
RL Nature 441:46-52(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-32 AND SER-34, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: The B regulatory subunit might modulate substrate selectivity
CC and catalytic activity, and also might direct the localization of the
CC catalytic enzyme to a particular subcellular compartment.
CC -!- SUBUNIT: Found in a complex with at least ARL2, PPP2CB; PPP2R1A,
CC PPP2R2A, PPP2R5E and TBCD (By similarity). PP2A consists of a common
CC heterodimeric core enzyme, composed of a 36 kDa catalytic subunit
CC (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit
CC A), that associates with a variety of regulatory subunits. Proteins
CC that associate with the core dimer include three families of regulatory
CC subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56
CC families), the 48 kDa variable regulatory subunit, viral proteins, and
CC cell signaling molecules. Interacts with SGO1. {ECO:0000250,
CC ECO:0000269|PubMed:16541025}.
CC -!- INTERACTION:
CC Q16537; O96017: CHEK2; NbExp=3; IntAct=EBI-968374, EBI-1180783;
CC Q16537; Q86YF9: DZIP1; NbExp=3; IntAct=EBI-968374, EBI-998108;
CC Q16537; P42858: HTT; NbExp=15; IntAct=EBI-968374, EBI-466029;
CC Q16537; Q9HC29: NOD2; NbExp=2; IntAct=EBI-968374, EBI-7445625;
CC Q16537; P30153: PPP2R1A; NbExp=7; IntAct=EBI-968374, EBI-302388;
CC Q16537; P30154: PPP2R1B; NbExp=3; IntAct=EBI-968374, EBI-357094;
CC Q16537; Q9H0H5: RACGAP1; NbExp=5; IntAct=EBI-968374, EBI-717233;
CC Q16537; Q8IUH5: ZDHHC17; NbExp=2; IntAct=EBI-968374, EBI-524753;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q16537-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16537-2; Sequence=VSP_054588;
CC Name=3;
CC IsoId=Q16537-3; Sequence=VSP_055163;
CC -!- PTM: Phosphorylated on serine residues.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
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DR EMBL; Z69029; CAA93153.1; -; mRNA.
DR EMBL; L76703; AAB69752.1; -; mRNA.
DR EMBL; AK316430; BAH14801.1; -; mRNA.
DR EMBL; AL118555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL132992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093766; AAH93766.1; -; mRNA.
DR EMBL; BC101479; AAI01480.1; -; mRNA.
DR EMBL; BC143231; AAI43232.1; -; mRNA.
DR EMBL; BC143234; AAI43235.1; -; mRNA.
DR CCDS; CCDS61467.1; -. [Q16537-3]
DR CCDS; CCDS61468.1; -. [Q16537-2]
DR CCDS; CCDS9758.1; -. [Q16537-1]
DR RefSeq; NP_001269108.1; NM_001282179.1. [Q16537-1]
DR RefSeq; NP_001269109.1; NM_001282180.1. [Q16537-2]
DR RefSeq; NP_001269110.1; NM_001282181.1. [Q16537-3]
DR RefSeq; NP_001269111.1; NM_001282182.1. [Q16537-3]
DR RefSeq; NP_006237.1; NM_006246.3. [Q16537-1]
DR AlphaFoldDB; Q16537; -.
DR SMR; Q16537; -.
DR BioGRID; 111521; 141.
DR ELM; Q16537; -.
DR IntAct; Q16537; 64.
DR MINT; Q16537; -.
DR STRING; 9606.ENSP00000337641; -.
DR iPTMnet; Q16537; -.
DR MetOSite; Q16537; -.
DR PhosphoSitePlus; Q16537; -.
DR BioMuta; PPP2R5E; -.
DR DMDM; 7387498; -.
DR EPD; Q16537; -.
DR jPOST; Q16537; -.
DR MassIVE; Q16537; -.
DR MaxQB; Q16537; -.
DR PaxDb; Q16537; -.
DR PeptideAtlas; Q16537; -.
DR PRIDE; Q16537; -.
DR ProteomicsDB; 60898; -.
DR ProteomicsDB; 7180; -.
DR Antibodypedia; 50; 157 antibodies from 34 providers.
DR DNASU; 5529; -.
DR Ensembl; ENST00000337537.8; ENSP00000337641.3; ENSG00000154001.14. [Q16537-1]
DR Ensembl; ENST00000422769.6; ENSP00000404632.2; ENSG00000154001.14. [Q16537-3]
DR Ensembl; ENST00000555899.1; ENSP00000452396.1; ENSG00000154001.14. [Q16537-2]
DR GeneID; 5529; -.
DR KEGG; hsa:5529; -.
DR MANE-Select; ENST00000337537.8; ENSP00000337641.3; NM_006246.5; NP_006237.1.
DR UCSC; uc001xgd.3; human. [Q16537-1]
DR CTD; 5529; -.
DR DisGeNET; 5529; -.
DR GeneCards; PPP2R5E; -.
DR HGNC; HGNC:9313; PPP2R5E.
DR HPA; ENSG00000154001; Low tissue specificity.
DR MIM; 601647; gene.
DR neXtProt; NX_Q16537; -.
DR OpenTargets; ENSG00000154001; -.
DR PharmGKB; PA33677; -.
DR VEuPathDB; HostDB:ENSG00000154001; -.
DR eggNOG; KOG2085; Eukaryota.
DR GeneTree; ENSGT01030000234620; -.
DR HOGENOM; CLU_012437_4_0_1; -.
DR InParanoid; Q16537; -.
DR OMA; GADNNCK; -.
DR OrthoDB; 890437at2759; -.
DR PhylomeDB; Q16537; -.
DR TreeFam; TF105556; -.
DR PathwayCommons; Q16537; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
DR Reactome; R-HSA-432142; Platelet sensitization by LDL.
DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-HSA-5339716; Signaling by GSK3beta mutants.
DR Reactome; R-HSA-5358747; CTNNB1 S33 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358749; CTNNB1 S37 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358751; CTNNB1 S45 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358752; CTNNB1 T41 mutants aren't phosphorylated.
DR Reactome; R-HSA-5467337; APC truncation mutants have impaired AXIN binding.
DR Reactome; R-HSA-5467340; AXIN missense mutants destabilize the destruction complex.
DR Reactome; R-HSA-5467348; Truncations of AMER1 destabilize the destruction complex.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-5673000; RAF activation.
DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q16537; -.
DR BioGRID-ORCS; 5529; 32 hits in 1075 CRISPR screens.
DR ChiTaRS; PPP2R5E; human.
DR GeneWiki; PPP2R5E; -.
DR GenomeRNAi; 5529; -.
DR Pharos; Q16537; Tbio.
DR PRO; PR:Q16537; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q16537; protein.
DR Bgee; ENSG00000154001; Expressed in pancreatic ductal cell and 204 other tissues.
DR Genevisible; Q16537; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; TAS:ProtInc.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002554; PP2A_B56.
DR PANTHER; PTHR10257; PTHR10257; 1.
DR Pfam; PF01603; B56; 1.
DR PIRSF; PIRSF028043; PP2A_B56; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..467
FT /note="Serine/threonine-protein phosphatase 2A 56 kDa
FT regulatory subunit epsilon isoform"
FT /id="PRO_0000071454"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..76
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055163"
FT VAR_SEQ 430..435
FT /note="KSDRQR -> N (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054588"
FT CONFLICT 194
FT /note="R -> W (in Ref. 3; BAH14801)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 54699 MW; DD9CE11433F499CF CRC64;
MSSAPTTPPS VDKVDGFSRK SVRKARQKRS QSSSQFRSQG KPIELTPLPL LKDVPSSEQP
ELFLKKLQQC CVIFDFMDTL SDLKMKEYKR STLNELVDYI TISRGCLTEQ TYPEVVRMVS
CNIFRTLPPS DSNEFDPEED EPTLEASWPH LQLVYEFFIR FLESQEFQPS IAKKYIDQKF
VLQLLELFDS EDPRERDYLK TVLHRIYGKF LGLRAFIRKQ INNIFLRFVY ETEHFNGVAE
LLEILGSIIN GFALPLKAEH KQFLVKVLIP LHTVRSLSLF HAQLAYCIVQ FLEKDPSLTE
PVIRGLMKFW PKTCSQKEVM FLGELEEILD VIEPSQFVKI QEPLFKQIAK CVSSPHFQVA
ERALYYWNNE YIMSLIEENS NVILPIMFSS LYRISKEHWN PAIVALVYNV LKAFMEMNST
MFDELTATYK SDRQREKKKE KEREELWKKL EDLELKRGLR RDGIIPT
