CPEB4_MOUSE
ID CPEB4_MOUSE Reviewed; 729 AA.
AC Q7TN98; A6H6G0; Q69ZD7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 4;
DE Short=CPE-BP4;
DE Short=CPE-binding protein 4;
DE Short=mCPEB-4;
GN Name=Cpeb4; Synonyms=Kiaa1673;
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] (ISOFORMS 1; 2; 3 AND 4), ALTERNATIVE SPLICING,
RP INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=12871996; DOI=10.1073/pnas.1133424100;
RA Theis M., Si K., Kandel E.R.;
RT "Two previously undescribed members of the mouse CPEB family of genes and
RT their inducible expression in the principal cell layers of the
RT hippocampus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9602-9607(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17024188; DOI=10.1038/sj.emboj.7601322;
RA Huang Y.S., Kan M.C., Lin C.L., Richter J.D.;
RT "CPEB3 and CPEB4 in neurons: analysis of RNA-binding specificity and
RT translational control of AMPA receptor GluR2 mRNA.";
RL EMBO J. 25:4865-4876(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-99, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Spleen;
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 [7]
RP FUNCTION.
RX PubMed=22138752; DOI=10.1038/nm.2540;
RA Ortiz-Zapater E., Pineda D., Martinez-Bosch N., Fernandez-Miranda G.,
RA Iglesias M., Alameda F., Moreno M., Eliscovich C., Eyras E., Real F.X.,
RA Mendez R., Navarro P.;
RT "Key contribution of CPEB4-mediated translational control to cancer
RT progression.";
RL Nat. Med. 18:83-90(2011).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24386439; DOI=10.1371/journal.pone.0084978;
RA Tsai L.Y., Chang Y.W., Lin P.Y., Chou H.J., Liu T.J., Lee P.T., Huang W.H.,
RA Tsou Y.L., Huang Y.S.;
RT "CPEB4 knockout mice exhibit normal hippocampus-related synaptic plasticity
RT and memory.";
RL PLoS ONE 8:E84978-E84978(2013).
RN [9]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=27381259; DOI=10.1038/srep29395;
RA Shin J., Salameh J.S., Richter J.D.;
RT "Impaired neurodevelopment by the low complexity domain of CPEB4 reveals a
RT convergent pathway with neurodegeneration.";
RL Sci. Rep. 6:29395-29395(2016).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY ER STRESS,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=28092655; DOI=10.1038/ncb3461;
RA Maillo C., Martin J., Sebastian D., Hernandez-Alvarez M., Garcia-Rocha M.,
RA Reina O., Zorzano A., Fernandez M., Mendez R.;
RT "Circadian- and UPR-dependent control of CPEB4 mediates a translational
RT response to counteract hepatic steatosis under ER stress.";
RL Nat. Cell Biol. 19:94-105(2017).
CC -!- FUNCTION: Sequence-specific RNA-binding protein that binds to the
CC cytoplasmic polyadenylation element (CPE), an uridine-rich sequence
CC element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR
CC (PubMed:17024188). RNA binding results in a clear conformational change
CC analogous to the Venus fly trap mechanism (By similarity). Regulates
CC activation of unfolded protein response (UPR) in the process of
CC adaptation to ER stress in liver, by maintaining translation of CPE-
CC regulated mRNAs in conditions in which global protein synthesis is
CC inhibited (PubMed:28092655). Required for cell cycle progression,
CC specifically for cytokinesis and chromosomal segregation (By
CC similarity). Plays a role as an oncogene promoting tumor growth and
CC progression by positively regulating translation of t-plasminogen
CC activator/PLAT (PubMed:22138752). Stimulates proliferation of
CC melanocytes (By similarity). In contrast to CPEB1 and CPEB3, does not
CC play role in synaptic plasticity, learning and memory
CC (PubMed:24386439). {ECO:0000250|UniProtKB:Q17RY0,
CC ECO:0000269|PubMed:17024188, ECO:0000269|PubMed:22138752,
CC ECO:0000269|PubMed:24386439, ECO:0000269|PubMed:28092655}.
CC -!- SUBUNIT: Interacts with TOB1. {ECO:0000250|UniProtKB:Q17RY0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27381259}. Cell
CC projection, dendrite {ECO:0000269|PubMed:17024188,
CC ECO:0000269|PubMed:24386439}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:24386439}. Postsynaptic density
CC {ECO:0000269|PubMed:17024188}. Cell projection, axon
CC {ECO:0000269|PubMed:27381259}. Cell projection, growth cone
CC {ECO:0000269|PubMed:27381259}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:28092655}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:28092655}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=mCPEB-4a;
CC IsoId=Q7TN98-1; Sequence=Displayed;
CC Name=2; Synonyms=mCPEB-4b;
CC IsoId=Q7TN98-2; Sequence=VSP_022046;
CC Name=3; Synonyms=mCPEB-4c;
CC IsoId=Q7TN98-3; Sequence=VSP_022044;
CC Name=4; Synonyms=mCPEB-4d;
CC IsoId=Q7TN98-4; Sequence=VSP_022043;
CC Name=5;
CC IsoId=Q7TN98-5; Sequence=VSP_022045;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, including hippocampus,
CC amygdala, granule and Purkinje cells of the cerebellum (at protein
CC level) (PubMed:17024188, PubMed:24386439). Expressed in spinal cord (at
CC protein level) (PubMed:27381259). Expressed in kidney, lung and heart
CC (at protein level) (PubMed:12871996, PubMed:27381259, PubMed:24386439).
CC Expressed in liver (at protein level) (PubMed:28092655,
CC PubMed:12871996, PubMed:27381259, PubMed:24386439). Expressed in spleen
CC and testis (at protein level) (PubMed:24386439, PubMed:12871996).
CC Weakly expressed in ovary and in granular cells of dentate gyrus and
CC the pyramidal cells of CA3 and CA1 of the hippocampus
CC (PubMed:12871996). {ECO:0000269|PubMed:12871996,
CC ECO:0000269|PubMed:17024188, ECO:0000269|PubMed:24386439,
CC ECO:0000269|PubMed:27381259, ECO:0000269|PubMed:28092655}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in developing brain, spinal cord
CC and attached dorsal root ganglia (DRG) (at protein level). At embryonic
CC day 18.5 expressed in gray matter of spinal cord, diencephalons,
CC hippocampus and parts of midbrain and hindbrain. At postnatal day 20
CC expression persists in spinal cord and brain. Expressed in embryonic
CC heart. {ECO:0000269|PubMed:27381259}.
CC -!- INDUCTION: Up-regulated in granular cells of the dentate gyrus of CA1
CC and CA3 after kainate-induced seizures (PubMed:12871996). Up-regulated
CC by high-fat-diet and aging-induced endoplasmic reticulum stress
CC (PubMed:28092655). Expression level fluctuation follows the circadian
CC clock amplitude (PubMed:28092655). {ECO:0000269|PubMed:12871996,
CC ECO:0000269|PubMed:28092655}.
CC -!- DOMAIN: The 2 RRM domains and the C-terminal region mediate interaction
CC with CPE-containing RNA. The interdomain linker (564-579) acts as a
CC hinge to fix the relative orientation of the 2 RRMs. The ZZ domain
CC (509-566) coordinates 2 Zn ions and is probably implicated in mediating
CC interactions with other proteins in addition to increasing the affinity
CC of the RRMs for the CPEs. Unlike in CPEB1, a continuous polar interface
CC is formed between the 2 RRMs. {ECO:0000250|UniProtKB:Q17RY0,
CC ECO:0000250|UniProtKB:Q9BZB8}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype at young age or under
CC unchallenged conditions (PubMed:24386439, PubMed:28092655). At 80 weeks
CC or under high fat diet feeding conditions, mutant mice develop
CC hepatosteatosis with excessive liver weight and accumulation of
CC cytosolic lipid droplets sometimes accompanied by fibrosis
CC (PubMed:28092655). {ECO:0000269|PubMed:24386439,
CC ECO:0000269|PubMed:28092655}.
CC -!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
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DR EMBL; AY313775; AAQ20844.1; -; mRNA.
DR EMBL; AK173229; BAD32507.1; -; mRNA.
DR EMBL; BC115430; AAI15431.1; -; mRNA.
DR EMBL; BC115431; AAI15432.1; -; mRNA.
DR EMBL; BC145863; AAI45864.1; -; mRNA.
DR EMBL; BC145865; AAI45866.1; -; mRNA.
DR CCDS; CCDS24514.1; -. [Q7TN98-1]
DR RefSeq; NP_001277607.1; NM_001290678.1. [Q7TN98-5]
DR RefSeq; NP_080528.2; NM_026252.4. [Q7TN98-1]
DR AlphaFoldDB; Q7TN98; -.
DR BMRB; Q7TN98; -.
DR SMR; Q7TN98; -.
DR BioGRID; 212288; 13.
DR STRING; 10090.ENSMUSP00000020543; -.
DR iPTMnet; Q7TN98; -.
DR PhosphoSitePlus; Q7TN98; -.
DR EPD; Q7TN98; -.
DR jPOST; Q7TN98; -.
DR MaxQB; Q7TN98; -.
DR PaxDb; Q7TN98; -.
DR PRIDE; Q7TN98; -.
DR ProteomicsDB; 285285; -. [Q7TN98-1]
DR ProteomicsDB; 285286; -. [Q7TN98-2]
DR ProteomicsDB; 285287; -. [Q7TN98-3]
DR ProteomicsDB; 285288; -. [Q7TN98-4]
DR ProteomicsDB; 285289; -. [Q7TN98-5]
DR Antibodypedia; 28980; 160 antibodies from 24 providers.
DR DNASU; 67579; -.
DR Ensembl; ENSMUST00000020543; ENSMUSP00000020543; ENSMUSG00000020300. [Q7TN98-1]
DR GeneID; 67579; -.
DR KEGG; mmu:67579; -.
DR UCSC; uc007iir.2; mouse. [Q7TN98-2]
DR UCSC; uc007iis.2; mouse. [Q7TN98-5]
DR UCSC; uc007iit.2; mouse. [Q7TN98-1]
DR CTD; 80315; -.
DR MGI; MGI:1914829; Cpeb4.
DR VEuPathDB; HostDB:ENSMUSG00000020300; -.
DR eggNOG; KOG0129; Eukaryota.
DR GeneTree; ENSGT00940000154998; -.
DR InParanoid; Q7TN98; -.
DR OMA; AENDTMK; -.
DR PhylomeDB; Q7TN98; -.
DR TreeFam; TF317658; -.
DR BioGRID-ORCS; 67579; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cpeb4; mouse.
DR PRO; PR:Q7TN98; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q7TN98; protein.
DR Bgee; ENSMUSG00000020300; Expressed in ciliary body and 246 other tissues.
DR ExpressionAtlas; Q7TN98; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0008135; F:translation factor activity, RNA binding; IBA:GO_Central.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
DR GO; GO:0036294; P:cellular response to decreased oxygen levels; ISS:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0002931; P:response to ischemia; IDA:UniProtKB.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 4.10.640.40; -; 1.
DR InterPro; IPR032296; CEBP_ZZ.
DR InterPro; IPR038446; CEBP_ZZ_sf.
DR InterPro; IPR034819; CPEB.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR12566; PTHR12566; 1.
DR Pfam; PF16366; CEBP_ZZ; 1.
DR Pfam; PF16367; RRM_7; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasm; Endoplasmic reticulum;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Synapse; Zinc.
FT CHAIN 1..729
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 4"
FT /id="PRO_0000269265"
FT DOMAIN 472..563
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 580..662
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 20..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..543
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q17RY0"
FT COMPBIAS 33..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 667
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 675
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 684
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 689
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 694
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 697
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 702
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 710
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT SITE 473
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q17RY0"
FT SITE 561
FT /note="Important for the positionning of RRM1 relative to
FT RRM2"
FT /evidence="ECO:0000250|UniProtKB:Q17RY0"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q17RY0"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q17RY0"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q17RY0"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q17RY0"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q17RY0"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q17RY0"
FT VAR_SEQ 402..427
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12871996"
FT /id="VSP_022043"
FT VAR_SEQ 402..419
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12871996"
FT /id="VSP_022044"
FT VAR_SEQ 404..428
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_022045"
FT VAR_SEQ 420..427
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12871996"
FT /id="VSP_022046"
SQ SEQUENCE 729 AA; 80122 MW; 7CB042EDE4B7C0CA CRC64;
MGDYGFGVLV QSNTGNKSAF PVRFHPHLQP PHHHQNATPN PAAFINNNTA ANGSSAGSAW
LFPAPATHNI QDEILGSEKA KSQQQEQQDP LEKQQLSPSP GQEAGILPET EKAKAEENPG
DSSSENSNGK EKLRIESPVL TGFDYQEATG LGTSTQPLTS SASSLTGFSN WSAAIAPSSS
TIINEDASFF HQGGVPGASA NNGALLFQNF PHHVSPGFGG SFSPQIGPLS QHHPHHPHFQ
HHHSQHQQQR RSPASPHPPP FTHRSAAFNQ LPHLANNLNK PPSPWSSYQS PSPTPSSSWS
PGGGGYGGWG ASQGRDHRRG LNGGITPLNS ISPLKKNFAS NHIQLQKYAR PSSAFAPKSW
MEDSLNRADN IFPFPERPRT FDMHSLESSL IDIMRAENDS IKGRLNYSYP GSDSSLLINA
RTYGRRRGQS SLFPMEDGFL DDGRGDQPLH SGLGSPHCFT HQNGERVERY SRKVFVGGLP
PDIDEDEITA SFRRFGPLIV DWPHKAESKS YFPPKGYAFL LFQDESSVQA LIDACIEEDG
KLYLCVSSPT IKDKPVQIRP WNLSDSDFVM DGSQPLDPRK TIFVGGVPRP LRAVELAMIM
DRLYGGVCYA GIDTDPELKY PKGAGRVAFS NQQSYIAAIS ARFVQLQHGE IDKRVEVKPY
VLDDQLCDEC QGARCGGKFA PFFCANVTCL QYYCEYCWAA IHSRAGREFH KPLVKEGGDR
PRHISFRWN
