NUCL_MESAU
ID NUCL_MESAU Reviewed; 714 AA.
AC P08199;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Nucleolin;
DE AltName: Full=Protein C23;
GN Name=NCL;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-714, PROTEIN SEQUENCE OF 2-35, AND
RP METHYLATION AT ARG-656; ARG-660; ARG-666; ARG-670; ARG-674; ARG-680;
RP ARG-682; ARG-688; ARG-692 AND ARG-695.
RX PubMed=3470736; DOI=10.1073/pnas.84.6.1472;
RA Lapeyre B., Bourbon H., Amalric F.;
RT "Nucleolin, the major nucleolar protein of growing eukaryotic cells: an
RT unusual protein structure revealed by the nucleotide sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:1472-1476(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 180-239.
RX PubMed=2994013; DOI=10.1093/nar/13.16.5805;
RA Lapeyre B., Caizergues-Ferrer M., Bouche G., Amalric F.;
RT "Cloning of cDNA encoding a 100 kDa nucleolar protein (nucleoline) of
RT Chinese hamster ovary cells.";
RL Nucleic Acids Res. 13:5805-5816(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 523-714, PROTEIN SEQUENCE OF 631-672, AND
RP METHYLATION AT ARG-656; ARG-660; ARG-666; ARG-670 AND ARG-674.
RX PubMed=3755137; DOI=10.1016/s0021-9258(18)67634-3;
RA Lapeyre B., Amalric F., Ghaffari S.H., Rao S.V.V., Dumbar T.S.,
RA Olson M.O.J.;
RT "Protein and cDNA sequence of a glycine-rich, dimethylarginine-containing
RT region located near the carboxyl-terminal end of nucleolin (C23 and 100
RT kDa).";
RL J. Biol. Chem. 261:9167-9173(1986).
RN [4]
RP FUNCTION.
RX PubMed=3409881; DOI=10.1111/j.1432-1033.1988.tb14224.x;
RA Erard M.S., Belenguer P., Caizergues-Ferrer M., Pantaloni A., Amalric F.;
RT "A major nucleolar protein, nucleolin, induces chromatin decondensation by
RT binding to histone H1.";
RL Eur. J. Biochem. 175:525-530(1988).
RN [5]
RP STRUCTURE BY NMR OF 291-391; 376-473 AND 295-469.
RX PubMed=11023788; DOI=10.1006/jmbi.2000.4118;
RA Allain F.H.-T., Gilbert D.E., Bouvet P., Feigon J.;
RT "Solution structure of the two N-terminal RNA-binding domains of nucleolin
RT and NMR study of the interaction with its RNA target.";
RL J. Mol. Biol. 303:227-241(2000).
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 ECO:0000269|PubMed:3409881}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M15825; AAA36966.1; -; mRNA.
DR PIR; A27441; A27441.
DR PDB; 1FJ7; NMR; -; A=299-391.
DR PDB; 1FJC; NMR; -; A=387-469.
DR PDB; 1FJE; NMR; -; B=299-469.
DR PDB; 1RKJ; NMR; -; A=299-469.
DR PDBsum; 1FJ7; -.
DR PDBsum; 1FJC; -.
DR PDBsum; 1FJE; -.
DR PDBsum; 1RKJ; -.
DR AlphaFoldDB; P08199; -.
DR SMR; P08199; -.
DR iPTMnet; P08199; -.
DR PRIDE; P08199; -.
DR EvolutionaryTrace; P08199; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; ISS:UniProtKB.
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 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3470736"
FT CHAIN 2..714
FT /note="Nucleolin"
FT /id="PRO_0000081692"
FT REPEAT 57..64
FT /note="1"
FT REPEAT 74..81
FT /note="2"
FT REPEAT 82..89
FT /note="3"
FT REPEAT 90..97
FT /note="4"
FT REPEAT 98..103
FT /note="5; truncated"
FT REPEAT 104..111
FT /note="6"
FT REPEAT 119..126
FT /note="7"
FT REPEAT 127..134
FT /note="8"
FT DOMAIN 308..384
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 394..467
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 486..560
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 572..647
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..134
FT /note="8 X 8 AA tandem repeats of X-T-P-X-K-K-X-X"
FT REGION 642..714
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..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..169
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..215
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..272
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..300
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:0000250|UniProtKB:P19338"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 68
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 83
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 98
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 101
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 105
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 219
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 319
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 349
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 368
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 378
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 399
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 428
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 445
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 468
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 477
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 513
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 521
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 572
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 577
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 646
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT MOD_RES 656
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:3470736,
FT ECO:0000269|PubMed:3755137"
FT MOD_RES 660
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:3470736,
FT ECO:0000269|PubMed:3755137"
FT MOD_RES 666
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:3470736,
FT ECO:0000269|PubMed:3755137"
FT MOD_RES 670
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:3470736,
FT ECO:0000269|PubMed:3755137"
FT MOD_RES 674
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:3470736,
FT ECO:0000269|PubMed:3755137"
FT MOD_RES 680
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:3470736"
FT MOD_RES 682
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:3470736"
FT MOD_RES 688
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:3470736"
FT MOD_RES 692
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:3470736"
FT MOD_RES 695
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:3470736"
FT MOD_RES 695
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09405"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 325
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 325
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 371
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 378
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 513
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 577
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 589
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 589
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CROSSLNK 624
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P19338"
FT CONFLICT 543
FT /note="C -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="M -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:1FJE"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:1FJ7"
FT HELIX 321..335
FT /evidence="ECO:0007829|PDB:1FJ7"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:1FJ7"
FT TURN 346..349
FT /evidence="ECO:0007829|PDB:1FJ7"
FT STRAND 350..357
FT /evidence="ECO:0007829|PDB:1FJ7"
FT HELIX 358..366
FT /evidence="ECO:0007829|PDB:1FJ7"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:1FJ7"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:1FJE"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:1FJ7"
FT TURN 384..387
FT /evidence="ECO:0007829|PDB:1FJC"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:1FJC"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:1FJC"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:1FJC"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:1FJC"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:1FJC"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:1FJC"
FT STRAND 428..439
FT /evidence="ECO:0007829|PDB:1FJC"
FT HELIX 440..449
FT /evidence="ECO:0007829|PDB:1FJC"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:1FJC"
FT STRAND 458..464
FT /evidence="ECO:0007829|PDB:1FJC"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:1FJC"
SQ SEQUENCE 714 AA; 77128 MW; 3363EA8A165E3A73 CRC64;
MVKLAKAGKT HGEAKKMAPP PKEVEEDSED EEMSEEEDDS SGEEVVIPQK KGKKATATPA
KKVVVSQTKK VAVPTPAKKA AVTPGKKAAA TPAKKAVTPA KAVATPGKKG ATQAKALVAT
PGKKGAVTPA KGAKNGKNAK KEDSDEDEDD DDDEDDSDED EEDEEEDEFE PPVVKGKQGK
VAAAAPASED EDEEEDEEEE EEDEEEEDDS EEEEAMEITP AKGKKAPAKV VPVKAKNVAE
EDDDDEEEDE DEEEDEEEEE DEEEEEEEEE EEPVKPAPGK RKKEMTKQKE VPEAKKQKVE
GSESTTPFNL FIGNLNPNKS VAELKVAISE PFAKNDLAVV DVRTGTNRKF GYVDFESAED
LEKALELTGL KVFGNEIKLE KPKGRDSKKV RAARTLLAKN LSFNITEDEL KEVFEDALEI
RLVSQDGKSK GIAYIEFKSE ADAEKNLEEK QGAEIDGRSV SLYYTGEKGQ RQERTGKNST
WSGESKTLVL SNLSYSATEE TLQEVFEKAT FIKVPQNQQG KSKGYAFIEF ASFEDAKEAL
NSCNKMEIEG RTIRLELQGP RGSPNARSQP SKTLFVKGLS EDTTEETLKE SFEGSVRARI
VTDRETGSSK GFGFVDFNSE EDAKAAKEAM EDGEIDGNKV TLDWAKPKGE GGFGGRGGGR
GGFGGRGGGR GGGRGGFGGR GRGGFGGRGG FRGGRGGGGG GGDFKPQGKK TKFE
