CPE1A_XENLA
ID CPE1A_XENLA Reviewed; 568 AA.
AC Q91572; B7ZRW6; B7ZRZ4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 1-A;
DE Short=CPE-BP1-A;
DE Short=CPE-binding protein 1-A;
DE Short=CPEB-1-A;
DE AltName: Full=58 kDa CPE-binding protein;
GN Name=cpeb1-a; Synonyms=cpeb;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION, RNA-BINDING, AND
RP TISSUE SPECIFICITY.
RX PubMed=7954828; DOI=10.1016/0092-8674(94)90547-9;
RA Hake L.E., Richter J.D.;
RT "CPEB is a specificity factor that mediates cytoplasmic polyadenylation
RT during Xenopus oocyte maturation.";
RL Cell 79:617-627(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION.
RX PubMed=1653174; DOI=10.1101/gad.5.9.1697;
RA Paris J., Swenson K., Piwnica-Worms H., Richter J.D.;
RT "Maturation-specific polyadenylation: in vitro activation by p34cdc2 and
RT phosphorylation of a 58-kD CPE-binding protein.";
RL Genes Dev. 5:1697-1708(1991).
RN [4]
RP PHOSPHORYLATION, MUTAGENESIS OF CYS-529; CYS-539 AND HIS-547, AND
RP RNA-BINDING.
RX PubMed=9447964; DOI=10.1128/mcb.18.2.685;
RA Hake L.E., Mendez R., Richter J.D.;
RT "Specificity of RNA binding by CPEB: requirement for RNA recognition motifs
RT and a novel zinc finger.";
RL Mol. Cell. Biol. 18:685-693(1998).
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH TACC3 AND EIF4E, AND INTERACTION WITH
RP TACC3.
RX PubMed=10635326; DOI=10.1016/s1097-2765(00)80230-0;
RA Stebbins-Boaz B., Cao Q., de Moor C.H., Mendez R., Richter J.D.;
RT "Maskin is a CPEB-associated factor that transiently interacts with eIF-
RT 4E.";
RL Mol. Cell 4:1017-1027(1999).
RN [6]
RP INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=11081630; DOI=10.1016/s0092-8674(00)00135-5;
RA Groisman I., Huang Y.-S., Mendez R., Cao Q., Theurkauf W., Richter J.D.;
RT "CPEB, maskin, and cyclin B1 mRNA at the mitotic apparatus: implications
RT for local translational control of cell division.";
RL Cell 103:435-447(2000).
RN [7]
RP FUNCTION, INTERACTION WITH CPSF1, AND PHOSPHORYLATION.
RX PubMed=11106762; DOI=10.1016/s1097-2765(00)00121-0;
RA Mendez R., Murthy K.G., Ryan K., Manley J.L., Richter J.D.;
RT "Phosphorylation of CPEB by Eg2 mediates the recruitment of CPSF into an
RT active cytoplasmic polyadenylation complex.";
RL Mol. Cell 6:1253-1259(2000).
RN [8]
RP PROTEIN SEQUENCE OF 172-175, PHOSPHORYLATION AT SER-174, MUTAGENESIS OF
RP SER-174 AND 174-SER--SER-180, AND TISSUE SPECIFICITY.
RX PubMed=10749216; DOI=10.1038/35005126;
RA Mendez R., Hake L.E., Andresson T., Littlepage L.E., Ruderman J.V.,
RA Richter J.D.;
RT "Phosphorylation of CPE binding factor by Eg2 regulates translation of c-
RT mos mRNA.";
RL Nature 404:302-307(2000).
RN [9]
RP PROTEASOME MEDIATED DEGRADATION, AND TISSUE SPECIFICITY.
RX PubMed=11237472; DOI=10.1006/dbio.2001.0153;
RA Reverte C.G., Ahearn M.D., Hake L.E.;
RT "CPEB degradation during Xenopus oocyte maturation requires a PEST domain
RT and the 26S proteasome.";
RL Dev. Biol. 231:447-458(2001).
RN [10]
RP FUNCTION, PHOSPHORYLATION AT SER-174, AND MUTAGENESIS OF SER-174.
RX PubMed=12086604; DOI=10.1016/s0092-8674(02)00733-x;
RA Groisman I., Jung M.-Y., Sarkissian M., Cao Q., Richter J.D.;
RT "Translational control of the embryonic cell cycle.";
RL Cell 109:473-483(2002).
RN [11]
RP FUNCTION, PHOSPHORYLATION AT SER-138; SER-210 AND SER-248, MUTAGENESIS OF
RP SER-138; SER-210 AND SER-248, PROTEASOME MEDIATED DEGRADATION, AND
RP UBIQUITINATION.
RX PubMed=11927567; DOI=10.1093/emboj/21.7.1833;
RA Mendez R., Barnard D., Richter J.D.;
RT "Differential mRNA translation and meiotic progression require Cdc2-
RT mediated CPEB destruction.";
RL EMBO J. 21:1833-1844(2002).
RN [12]
RP INTERACTION WITH XGEF.
RX PubMed=12648498; DOI=10.1016/s0012-1606(02)00089-1;
RA Reverte C.G., Yuan L., Keady B.T., Lacza C., Attfield K.R., Mahon G.M.,
RA Freeman B., Whitehead I.P., Hake L.E.;
RT "XGef is a CPEB-interacting protein involved in Xenopus oocyte
RT maturation.";
RL Dev. Biol. 255:383-398(2003).
RN [13]
RP IDENTIFICATION IN A CYTOPLASMIC POLYADENYLATION COMPLEX WITH SYMPK; PAPD4
RP AND CPSF1, AND INTERACTION WITH CPSF1; PAPD4 AND SYMPK.
RX PubMed=15550246; DOI=10.1016/j.cell.2004.10.029;
RA Barnard D.C., Ryan K., Manley J.L., Richter J.D.;
RT "Symplekin and xGLD-2 are required for CPEB-mediated cytoplasmic
RT polyadenylation.";
RL Cell 119:641-651(2004).
RN [14]
RP IDENTIFICATION IN A MRNP COMPLEX WITH XGEF AND MOS MRNA, INTERACTION WITH
RP XGEF, PHOSPHORYLATION, AND PHOSPHORYLATION AT SER-174.
RX PubMed=15635100; DOI=10.1091/mbc.e04-07-0585;
RA Martinez S.E., Yuan L., Lacza C., Ransom H., Mahon G.M., Whitehead I.P.,
RA Hake L.E.;
RT "XGef mediates early CPEB phosphorylation during Xenopus oocyte meiotic
RT maturation.";
RL Mol. Biol. Cell 16:1152-1164(2005).
RN [15]
RP INTERACTION WITH APLP1, PHOSPHORYLATION AT SER-174, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16314516; DOI=10.1128/mcb.25.24.10930-10939.2005;
RA Cao Q., Huang Y.-S., Kan M.-C., Richter J.D.;
RT "Amyloid precursor proteins anchor CPEB to membranes and promote
RT polyadenylation-induced translation.";
RL Mol. Cell. Biol. 25:10930-10939(2005).
RN [16]
RP IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX WITH LSM14B; DDX6; YBX2;
RP PAT1; EIF4ENIF1 AND EIF4E1B.
RX PubMed=17942399; DOI=10.1074/jbc.m704629200;
RA Minshall N., Reiter M.H., Weil D., Standart N.;
RT "CPEB interacts with an ovary-specific eIF4E and 4E-T in early Xenopus
RT oocytes.";
RL J. Biol. Chem. 282:37389-37401(2007).
CC -!- FUNCTION: Sequence-specific RNA-binding protein that regulates mRNA
CC cytoplasmic polyadenylation and translation initiation during oocyte
CC maturation and early development. Binds to the cytoplasmic
CC polyadenylation element (CPE), an uridine-rich sequence element
CC (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. In the
CC absence of phosphorylation and in association with tacc3/maskin, also
CC acts as a repressor of translation of CPE-containing mRNA; a repression
CC that is relieved by phosphorylation or degradation. Requires zinc for
CC RNA binding. Involved in the cell cycle progression from S phase into M
CC phase. {ECO:0000269|PubMed:11106762, ECO:0000269|PubMed:11927567,
CC ECO:0000269|PubMed:12086604, ECO:0000269|PubMed:7954828}.
CC -!- SUBUNIT: Found in a complex with cpeb1, tacc3/maskin and eif4e;
CC dissolution of this complex results in the binding of eif4e to eif4g
CC and the translational activation of CPE-containing mRNAs. Found in a
CC complex with cpeb1, cpsf1, the cytoplasmic poly(A) polymerase
CC papd4/gld2 and sympk. Found in a mRNP complex with cpeb1, a guanine
CC exchange factor xgef and mos mRNA. Interacts with cpsf1, papd4/gld2,
CC tacc3/maskin, microtubules, sympk and xgef. Component of a
CC ribonucleoprotein (RNP) complex, at least composed of cpeb1,
CC lsm14b/rap55b, ddx6/Xp54, ybx2/frgy2, pat1/P100, eif4enif1/4E-T and
CC eif4e1b. Interaction with ybx2/frgy2 is RNA-dependent. May interact
CC with aplp1. Interaction with cpsf1 increases during meiotic maturation
CC and is not mediated through RNA. Interaction with xgef is necessary for
CC its early activating phosphorylation status.
CC {ECO:0000269|PubMed:10635326, ECO:0000269|PubMed:11081630,
CC ECO:0000269|PubMed:11106762, ECO:0000269|PubMed:12648498,
CC ECO:0000269|PubMed:15550246, ECO:0000269|PubMed:15635100,
CC ECO:0000269|PubMed:16314516, ECO:0000269|PubMed:17942399}.
CC -!- INTERACTION:
CC Q91572; Q91854: fbxw1; NbExp=2; IntAct=EBI-65730, EBI-7161238;
CC Q91572; Q9PTG8: tacc3; NbExp=3; IntAct=EBI-65730, EBI-65726;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole.
CC Membrane. Note=During mitosis localizes with tacc3/maskin and CPE-
CC containing mRNAs to both spindle poles. Membrane-associated.
CC Colocalizes with members of the polyadenylation and translation complex
CC factors (cpsf, aplp1, tacc3/maskin, aurka, etc.), including CPE-
CC containing RNAs.
CC -!- TISSUE SPECIFICITY: Expressed uniformly in growing oocytes (stage I to
CC IV) and distributed at the animal pole in fully-grown oocytes (stages V
CC and VI) (at protein level). During early oocyte maturation its
CC expression remains constant and then declines drastically during late
CC oocyte maturation between 4 hours and 6 hours after the germinal
CC vesicle breakdown (GVBD) (at protein level). Expressed during early
CC oogenesis until stage III, remains constant through stage V oocytes,
CC decreases slightly in stage VI oocytes, and then remains constant
CC throughout oocyte maturation. {ECO:0000269|PubMed:10749216,
CC ECO:0000269|PubMed:11237472, ECO:0000269|PubMed:7954828}.
CC -!- DEVELOPMENTAL STAGE: After fertilization, expressed at the animal pole
CC in embryo, blastomeres and blastula stage (at protein level).
CC {ECO:0000269|PubMed:11081630}.
CC -!- DOMAIN: The 2 RRM domains and the C-terminal region mediate interaction
CC with CPE-containing RNA.
CC -!- PTM: Ser-174 phosphorylation by aurka in immature oocytes is essential
CC to trigger CPE-containing mRNA cytoplasmic polyadenylation and
CC translation activation and the subsequent signaling events that result
CC in meiotic progression. Ser-174 phosphorylation recruits the cleavage
CC and polyadenylation specificity factor (cpsf1) into an active
CC cytoplasmic polyadenylation complex. Ser-174 phosphorylation increases
CC its affinity for cpsf1 and papd4/gld2. Heavily phosphorylated by CDK1
CC on serines late during oocyte maturation. Ser-210 phosphorylation is
CC sufficient to target cpeb1 for degradation. Ser-174 phosphorylation
CC oscillates with the cell cycle (phosphorylated at M phase, but not at S
CC phase) and is necessary for S phase to M phase progression.
CC Phosphorylation at Ser-174 may be promoted by aplp1.
CC {ECO:0000269|PubMed:10749216, ECO:0000269|PubMed:11927567,
CC ECO:0000269|PubMed:12086604, ECO:0000269|PubMed:15635100,
CC ECO:0000269|PubMed:16314516}.
CC -!- PTM: Ubiquitinated. Requires a PEST box and the proteasome pathway for
CC destruction during oocyte maturation. Ser-210 phosphorylation triggers
CC its destruction, an event important to allow the transition from
CC metaphase I to metaphase II and cytokinesis in the early embryo.
CC {ECO:0000269|PubMed:11927567}.
CC -!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
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DR EMBL; U14169; AAA80483.1; -; mRNA.
DR EMBL; BC170313; AAI70313.1; -; mRNA.
DR EMBL; BC170341; AAI70341.1; -; mRNA.
DR PIR; A55377; A55377.
DR RefSeq; NP_001084072.1; NM_001090603.1.
DR AlphaFoldDB; Q91572; -.
DR SMR; Q91572; -.
DR BioGRID; 100614; 6.
DR DIP; DIP-30935N; -.
DR IntAct; Q91572; 7.
DR MINT; Q91572; -.
DR iPTMnet; Q91572; -.
DR PRIDE; Q91572; -.
DR GeneID; 399289; -.
DR KEGG; xla:399289; -.
DR CTD; 399289; -.
DR Xenbase; XB-GENE-946172; cpeb1.L.
DR OrthoDB; 1075356at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 399289; Expressed in egg cell and 17 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IPI:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; ISS:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; ISS:UniProtKB.
DR CDD; cd12723; RRM1_CPEB1; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 4.10.640.40; -; 1.
DR InterPro; IPR032292; CEBP1_N.
DR InterPro; IPR032296; CEBP_ZZ.
DR InterPro; IPR038446; CEBP_ZZ_sf.
DR InterPro; IPR034819; CPEB.
DR InterPro; IPR034977; CPEB1_RRM1.
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; PF16368; CEBP1_N; 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 Activator; Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane;
KW Metal-binding; mRNA processing; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Ribonucleoprotein; RNA-binding; Translation regulation;
KW Ubl conjugation; Zinc.
FT CHAIN 1..568
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 1-A"
FT /id="PRO_0000269257"
FT DOMAIN 313..410
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 432..513
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 172..175
FT /note="Necessary for interaction with microtubules and
FT localization at the mitotic apparatus"
FT REGION 173..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..208
FT /note="Necessary for degradation by the proteasome"
FT REGION 182..191
FT /note="Necessary for interaction with microtubules and
FT localization at the mitotic apparatus"
FT BINDING 517
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 529
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 534
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 542
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 138
FT /note="Phosphoserine; by cdk1"
FT /evidence="ECO:0000269|PubMed:11927567"
FT MOD_RES 174
FT /note="Phosphoserine; by aurka"
FT /evidence="ECO:0000269|PubMed:10749216,
FT ECO:0000269|PubMed:12086604, ECO:0000269|PubMed:15635100,
FT ECO:0000269|PubMed:16314516"
FT MOD_RES 210
FT /note="Phosphoserine; by cdk1"
FT /evidence="ECO:0000269|PubMed:11927567"
FT MOD_RES 248
FT /note="Phosphoserine; by cdk1"
FT /evidence="ECO:0000269|PubMed:11927567"
FT MUTAGEN 138
FT /note="S->A: Abolishes degradation by the proteasome; when
FT associated with A-210 and A-248."
FT /evidence="ECO:0000269|PubMed:11927567"
FT MUTAGEN 174..180
FT /note="SRSILDS->ARSILDA: Abolishes phosphorylation and CPE-
FT containing mRNA cytoplasmic polyadenylation and oocyte
FT maturation."
FT /evidence="ECO:0000269|PubMed:10749216"
FT MUTAGEN 174..180
FT /note="SRSILDS->DRSILD: Does not abolish interaction with
FT cpsf2 and CPE-containing mRNA cytoplasmic polyadenylation
FT and oocyte maturation."
FT /evidence="ECO:0000269|PubMed:10749216"
FT MUTAGEN 174
FT /note="S->A: Abolishes phosphorylation and CPE-containing
FT mRNA cytoplasmic polyadenylation and oocyte maturation.
FT Diminishes the interaction with cpsf2 and papd4/gld2."
FT /evidence="ECO:0000269|PubMed:10749216,
FT ECO:0000269|PubMed:12086604"
FT MUTAGEN 174
FT /note="S->D: Stimulates premature CPE-dependent
FT polyadenylation and translation in primary oocytes. Does
FT not diminishes the interaction with cpsf and papd4/gld2."
FT /evidence="ECO:0000269|PubMed:10749216,
FT ECO:0000269|PubMed:12086604"
FT MUTAGEN 210
FT /note="S->A: Abolishes degradation by the proteasome; when
FT associated with A-138 and A-248."
FT /evidence="ECO:0000269|PubMed:11927567"
FT MUTAGEN 248
FT /note="S->A: Abolishes degradation by the proteasome; when
FT associated with A-138 and A-210."
FT /evidence="ECO:0000269|PubMed:11927567"
FT MUTAGEN 529
FT /note="C->A: Abolishes RNA-binding."
FT /evidence="ECO:0000269|PubMed:9447964"
FT MUTAGEN 539
FT /note="C->A: Abolishes RNA-binding."
FT /evidence="ECO:0000269|PubMed:9447964"
FT MUTAGEN 547
FT /note="H->A: Abolishes RNA-binding."
FT /evidence="ECO:0000269|PubMed:9447964"
FT CONFLICT 19
FT /note="P -> S (in Ref. 2; AAI70313)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="P -> H (in Ref. 1; AAA80483)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="R -> A (in Ref. 1; AAA80483)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 568 AA; 62605 MW; EF812949F5B4DE54 CRC64;
MAFPLKDDLG RAKDCWGCPS DTPALSTCSN ADIFRRINAM LDNSLDFTGV CTTPNTKGKC
EHLQDYQDTE GPAASRMLFS TSHEPLPRGL PDTNDLCLGL QSLSLTGWDR PWSTQDSEAG
GHSSTPTAAQ SVFSMLNSPM GKPSPLGFLT FDPIGSDLME KYPTPLLRSS RLDSRSILDS
RSSSPSDSDT SGFSSGSDHL SDLISSLRIS PPLPFLPLGG GVSRDPLKLG IGSRLDQDHA
ALAAATVSPL GITKGWPSTS VWPSWDLLDS AEDPFSIERE ARLHRQAAAV NEATCTWSGQ
LPPRNYKNPV YSCKVFLGGV PWDITETGLI NTFRVFGALS VEWPGKDGKH PRCPPKGNMP
KGYVYLVFES EKSVRALLQA CSQDLLSQDG LSEHYFKMSS RRMRCKEVQV IPWVLADSNF
VRSPSQRLDP SKTVFVGALH GMLNAEALAS IMNDLFGGVV YAGIDTDKHK YPIGSGRVTF
NNQRSYLKAV SAAFVEIKTA KFTKKVQIDP YLEDSVCQVC NAQPGPFFCR DQVCFKYFCR
SCWHWQHSME ILRHHRPLMR NQKSRDSS
