NUCL_RAT
ID NUCL_RAT Reviewed; 713 AA.
AC P13383;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Nucleolin;
DE AltName: Full=Protein C23;
GN Name=Ncl; Synonyms=Nuc;
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 [GENOMIC DNA].
RX PubMed=2347493; DOI=10.1016/0378-1119(90)90031-l;
RA Bourbon H.-M., Amalric F.;
RT "Nucleolin gene organization in rodents: highly conserved sequences within
RT three of the 13 introns.";
RL Gene 88:187-196(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RX PubMed=2906027; DOI=10.1016/0378-1119(88)90600-2;
RA Bourbon H.-M., Prudhomme M., Amalric F.;
RT "Sequence and structure of the nucleolin promoter in rodents:
RT characterization of a strikingly conserved CpG island.";
RL Gene 68:73-84(1988).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-157, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-40; SER-41; SER-145;
RP SER-157; SER-187; SER-213; SER-305; SER-405; SER-566; SER-583 AND SER-622,
RP AND IDENTIFICATION BY 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: Nucleolin is the major nucleolar protein of growing
CC eukaryotic cells. It is found associated with intranucleolar chromatin
CC and pre-ribosomal particles. It induces chromatin decondensation by
CC binding to histone H1. It is thought to play a role in pre-rRNA
CC transcription and ribosome assembly. May play a role in the process of
CC transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-
CC 3' repeats more tightly than the telomeric single-stranded DNA 5'-
CC TTAGGG-3' repeats (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Component of the SWAP complex that
CC consists of NPM1, NCL/nucleolin, PARP1 and SWAP70. Component of a
CC complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb
CC complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and
CC NCL/nucleolin. Interacts with AICDA. Interacts with APTX. Interacts
CC with C1QBP. Interacts with ERBB4. Interacts (via C-terminus) with FMR1
CC isoform 6 (via N-terminus). Interacts with GZF1; this interaction is
CC important for nucleolar localization of GZF1. Interacts with NSUN2.
CC Interacts with NVL. Interacts (via N-terminus domain) with SETX.
CC Interacts (via RRM1 and C-terminal RRM4/Arg/Gly-rich domains) with
CC TERT; the interaction is important for nucleolar localization of TERT.
CC Interacts with WDR46. Interacts with ZFP36. Interacts with LRRC34.
CC Interacts with RRP1B. Interacts with HNRNPU; this interaction occurs
CC during mitosis. Interacts with RIOK1; RIOK1 recruits NCL to PRMT5 for
CC symmetrically methylation (By similarity). Interacts with ZBTB7B (By
CC similarity). Interacts with MDK; this interaction promotes NCL
CC clustering and lateral movements of this complex into lipid rafts
CC leading to MDK internalization (By similarity). Interacts with HDGF (By
CC similarity). Interacts with ALKBH2. {ECO:0000250|UniProtKB:P09405,
CC ECO:0000250|UniProtKB:P19338}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm {ECO:0000250}.
CC Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs. {ECO:0000250}.
CC -!- PTM: Some glutamate residues are glycylated by TTLL8. This modification
CC occurs exclusively on glutamate residues and results in a glycine chain
CC on the gamma-carboxyl group (By similarity). {ECO:0000250}.
CC -!- PTM: Symmetrically methylated by PRMT5 (By similarity).
CC {ECO:0000250|UniProtKB:P19338}.
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DR EMBL; M55022; AAA41732.1; -; Genomic_DNA.
DR EMBL; M55015; AAA41732.1; JOINED; Genomic_DNA.
DR EMBL; M55017; AAA41732.1; JOINED; Genomic_DNA.
DR EMBL; M55020; AAA41732.1; JOINED; Genomic_DNA.
DR EMBL; M22090; AAA41733.1; -; Genomic_DNA.
DR PIR; JH0148; JH0148.
DR AlphaFoldDB; P13383; -.
DR SMR; P13383; -.
DR IntAct; P13383; 6.
DR MINT; P13383; -.
DR STRING; 10116.ENSRNOP00000024712; -.
DR iPTMnet; P13383; -.
DR PhosphoSitePlus; P13383; -.
DR jPOST; P13383; -.
DR PaxDb; P13383; -.
DR PRIDE; P13383; -.
DR UCSC; RGD:3153; rat.
DR RGD; 3153; Ncl.
DR eggNOG; KOG0123; Eukaryota.
DR InParanoid; P13383; -.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P13383; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0001533; C:cornified envelope; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0001651; C:dense fibrillar component; IDA:RGD.
DR GO; GO:0001650; C:fibrillar center; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0044547; F:DNA topoisomerase binding; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:1990631; F:ErbB-4 class receptor binding; IPI:RGD.
DR GO; GO:0042393; F:histone binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0043236; F:laminin binding; IDA:RGD.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; IDA:RGD.
DR GO; GO:0042134; F:rRNA primary transcript binding; IDA:RGD.
DR GO; GO:0035368; F:selenocysteine insertion sequence binding; IDA:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IDA:RGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:RGD.
DR GO; GO:0042162; F:telomeric DNA binding; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISO:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:RGD.
DR GO; GO:0006897; P:endocytosis; IMP:RGD.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0017148; P:negative regulation of translation; ISO:RGD.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:RGD.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISO:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:RGD.
DR GO; GO:2000232; P:regulation of rRNA processing; IDA:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR CDD; cd12403; RRM1_NCL; 1.
DR CDD; cd12405; RRM3_NCL; 1.
DR CDD; cd12406; RRM4_NCL; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR034230; Nucleolin_RRM1.
DR InterPro; IPR034234; Nucleolin_RRM3.
DR InterPro; IPR034235; Nucleolin_RRM4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF54928; SSF54928; 4.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; DNA-binding; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT CHAIN 1..713
FT /note="Nucleolin"
FT /id="PRO_0000081694"
FT REPEAT 58..65
FT /note="1"
FT REPEAT 75..82
FT /note="2"
FT REPEAT 83..90
FT /note="3"
FT REPEAT 91..98
FT /note="4"
FT REPEAT 99..104
FT /note="5; truncated"
FT REPEAT 105..112
FT /note="6"
FT REPEAT 120..127
FT /note="7"
FT REPEAT 128..135
FT /note="8"
FT DOMAIN 311..387
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 397..470
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 489..563
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 575..650
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..135
FT /note="8 X 8 AA tandem repeats of X-T-P-X-K-K-X-X"
FT REGION 645..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..43
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..168
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..217
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..275
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 76
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 96
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 99
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 121
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 221
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 322
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 352
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 371
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 381
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 402
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 409
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 448
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 471
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 480
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 516
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 524
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 575
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 580
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 649
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 659
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 663
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 669
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 673
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 676
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 682
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 684
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 690
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 694
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 697
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08199"
FT MOD_RES 697
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT CROSSLNK 301
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 301
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 328
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 328
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 374
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 516
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 580
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 592
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 592
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 627
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P19338"
SQ SEQUENCE 713 AA; 77147 MW; 9652B27BFD12C8EC CRC64;
MVKLAKAGKT HGESKKMAPP PKEVEEDSED EEMSEDEDDS SGEEEVVIPQ KKGKKATTTP
AKKVVVSQTK KAAVPTPAKK AAVTPGKKAA ATPAKKAVTP AKVVPTPGKK GAAQAKALVP
TPGKKGAVTP AKGAKNGKNA KKEDSDEDED EEDEDDSDED EDEEDEFEPP VVKGVKPAKA
APAAPASEDE DEEDDDDEDD DDDDEEEEEE DDSEEEVMEI TPAKGKKTPA KVVPVKAKSV
AEEEEDDEDD EDEEEDEDEE DEEDDEDEDE EEEEEPVKAA PGKRKKEMTK QKEAPEAKKQ
KIEGSEPTTP FNLFIGNLNP NKSVAELKVA ISELFAKNDL AAVDVRTGTN RKFGYVDFES
AEDLEKALEL TGLKVFGNEI KLEKPKGRDS KKVRAARTLL AKNLSFNITE DELKEVFEDA
VEIRLVSQDG RSKGIAYIEF KSEADAEKNL EEKQGAEIDG RSVSLYYTGE KGQRQERTGK
NSTWSGESKT LVLSNLSYSA TEETLQEVFE KATFIKVPQN PHGKSKGYAF IEFASFEDAK
EALNSCNKME IEGRTIRLEL QGPRGSPNAR SQPSKTLFVK GLSEDTTEET LKESFEGSVR
ARIVTDRETG SSKGFGFVDF NSEEDAKAAK EAMEDGEIDG NKVTLDWAKP KGEGGFGGRG
GGRGGFGGRG GGRGGRGGFG GRGRGGFGGR GGFRGGRGGG GDFKPQGKKT KFE
