NOLC1_RAT
ID NOLC1_RAT Reviewed; 704 AA.
AC P41777; F1LPS3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Nucleolar and coiled-body phosphoprotein 1 {ECO:0000305};
DE AltName: Full=140 kDa nucleolar phosphoprotein {ECO:0000303|PubMed:1623516};
DE Short=Nopp140 {ECO:0000303|PubMed:1623516};
DE AltName: Full=Nucleolar 130 kDa protein;
DE AltName: Full=Nucleolar phosphoprotein p130;
GN Name=Nolc1 {ECO:0000312|RGD:621578};
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 [MRNA], PROTEIN SEQUENCE OF 292-309 AND 563-601,
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RC TISSUE=Liver;
RX PubMed=1623516; DOI=10.1016/0092-8674(92)90539-o;
RA Meier U.T., Blobel G.;
RT "Nopp140 shuttles on tracks between nucleolus and cytoplasm.";
RL Cell 70:127-138(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP INTERACTION WITH NOP58, AND FIBRILLARIN.
RX PubMed=10679015; DOI=10.1091/mbc.11.2.567;
RA Yang Y., Isaac C., Wang C., Dragon F., Pogacic V., Meier U.T.;
RT "Conserved composition of mammalian box H/ACA and box C/D small nucleolar
RT ribonucleoprotein particles and their interaction with the common factor
RT Nopp140.";
RL Mol. Biol. Cell 11:567-577(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567 AND SER-703, AND
RP 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: Nucleolar protein that acts as a regulator of RNA polymerase
CC I by connecting RNA polymerase I with enzymes responsible for ribosomal
CC processing and modification. Required for neural crest specification:
CC following monoubiquitination by the BCR(KBTBD8) complex, associates
CC with TCOF1 and acts as a platform to connect RNA polymerase I with
CC enzymes responsible for ribosomal processing and modification, leading
CC to remodel the translational program of differentiating cells in favor
CC of neural crest specification. Involved in nucleologenesis, possibly by
CC playing a role in the maintenance of the fundamental structure of the
CC fibrillar center and dense fibrillar component in the nucleolus. It has
CC intrinsic GTPase and ATPase activities. {ECO:0000250|UniProtKB:Q14978}.
CC -!- SUBUNIT: Interacts with RNA polymerase I 194 kDa subunit (RPA194) and
CC with casein kinase-II (By similarity). Interacts with DKC1/NAP57, NOP58
CC and fibrillarin (PubMed:10679015). {ECO:0000250|UniProtKB:Q14978,
CC ECO:0000269|PubMed:10679015}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1623516}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:1623516}. Note=Shuttles on curvilinear
CC tracks between nucleolus and cytoplasm. These tracks extend from the
CC dense fibrillar component of the nucleolus across the nucleoplasm to a
CC limited number of nuclear pore complexes. {ECO:0000269|PubMed:1623516}.
CC -!- PTM: Undergoes rapid and massive phosphorylation/dephosphorylation
CC cycles on CK2 and PKC sites. NOLC1 is one of the mostly phosphorylated
CC proteins in the cell. {ECO:0000269|PubMed:1623516}.
CC -!- PTM: Ubiquitinated. Monoubiquitination by the BCR(KBTBD8) complex
CC promotes the formation of a NOLC1-TCOF1 complex that acts as a platform
CC to connect RNA polymerase I with enzymes responsible for ribosomal
CC processing and modification, leading to remodel the translational
CC program of differentiating cells in favor of neural crest
CC specification. {ECO:0000250|UniProtKB:Q14978}.
CC -!- PTM: Pyrophosphorylated by 5-diphosphoinositol pentakisphosphate (5-
CC IP7). Serine pyrophosphorylation is achieved by Mg(2+)-dependent, but
CC enzyme independent transfer of a beta-phosphate from a inositol
CC pyrophosphate to a pre-phosphorylated serine residue.
CC {ECO:0000250|UniProtKB:E9Q5C9}.
CC -!- SIMILARITY: Belongs to the NOLC1 family. {ECO:0000305}.
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DR EMBL; M94287; AAA41718.1; -; mRNA.
DR EMBL; M94288; AAA41719.1; -; mRNA.
DR EMBL; AC119478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B42680; B42680.
DR RefSeq; NP_074060.1; NM_022869.1.
DR AlphaFoldDB; P41777; -.
DR SMR; P41777; -.
DR BioGRID; 249215; 2.
DR IntAct; P41777; 2.
DR STRING; 10116.ENSRNOP00000025788; -.
DR iPTMnet; P41777; -.
DR PhosphoSitePlus; P41777; -.
DR jPOST; P41777; -.
DR PaxDb; P41777; -.
DR PRIDE; P41777; -.
DR GeneID; 64896; -.
DR KEGG; rno:64896; -.
DR CTD; 9221; -.
DR RGD; 621578; Nolc1.
DR VEuPathDB; HostDB:ENSRNOG00000018704; -.
DR eggNOG; KOG2992; Eukaryota.
DR InParanoid; P41777; -.
DR OMA; RESGCQG; -.
DR OrthoDB; 1610147at2759; -.
DR PhylomeDB; P41777; -.
DR TreeFam; TF341730; -.
DR PRO; PR:P41777; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018704; Expressed in ovary and 20 other tissues.
DR GO; GO:0031428; C:box C/D RNP complex; IDA:RGD.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; IDA:RGD.
DR GO; GO:0015030; C:Cajal body; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034512; F:box C/D RNA binding; IDA:RGD.
DR GO; GO:0062064; F:box C/D snoRNP complex binding; IDA:UniProtKB.
DR GO; GO:0034513; F:box H/ACA snoRNA binding; IDA:RGD.
DR GO; GO:0062065; F:box H/ACA snoRNP complex binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0008139; F:nuclear localization sequence binding; IDA:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
DR GO; GO:0001093; F:TFIIB-class transcription factor binding; IDA:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0033979; P:box H/ACA RNA metabolic process; IGI:RGD.
DR GO; GO:0014032; P:neural crest cell development; ISS:UniProtKB.
DR GO; GO:0014029; P:neural crest formation; ISS:UniProtKB.
DR GO; GO:0007000; P:nucleolus organization; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0042306; P:regulation of protein import into nucleus; IDA:RGD.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEP:RGD.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR007718; Srp40_C.
DR InterPro; IPR003993; Treacle_dom.
DR Pfam; PF05022; SRP40_C; 1.
DR Pfam; PF03546; Treacle; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing;
KW GTP-binding; Isopeptide bond; Methylation; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..704
FT /note="Nucleolar and coiled-body phosphoprotein 1"
FT /id="PRO_0000096943"
FT DOMAIN 10..42
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REPEAT 84..95
FT /note="Acidic serine cluster 1"
FT REPEAT 127..138
FT /note="Acidic serine cluster 2"
FT REPEAT 170..181
FT /note="Acidic serine cluster 3"
FT REPEAT 231..242
FT /note="Acidic serine cluster 4"
FT REPEAT 274..285
FT /note="Acidic serine cluster 5"
FT REPEAT 335..346
FT /note="Acidic serine cluster 6"
FT REPEAT 373..384
FT /note="Acidic serine cluster 7"
FT REPEAT 434..445
FT /note="Acidic serine cluster 8"
FT REPEAT 479..490
FT /note="Acidic serine cluster 9"
FT REPEAT 524..535
FT /note="Acidic serine cluster 10"
FT REPEAT 559..570
FT /note="Acidic serine cluster 11"
FT REGION 65..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..570
FT /note="11 X 12 AA approximate repeats of an acidic serine
FT cluster"
FT COMPBIAS 221..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 88
FT /note="Diphosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q5C9"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q5C9"
FT MOD_RES 91
FT /note="Diphosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q5C9"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 424
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 596
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:E9Q5C9"
FT MOD_RES 612
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 615
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 668
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 688
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 67
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 189
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 200
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 352
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 399
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 405
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 410
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 416
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 449
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 461
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 510
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 584
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 609
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 618
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 652
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 668
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 700
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT VARIANT 150
FT /note="Missing (in Nopp140b)"
FT CONFLICT 141
FT /note="E -> K (in Ref. 1; AAA41718/AAA41719)"
SQ SEQUENCE 704 AA; 73564 MW; 0A911BF1C15E9DBC CRC64;
MADTGLRRVV PSDLYPLVLG FLRDNQLSEV ASKFAKATGA TQQDANASSL LDIYSFWLKS
TKAPKVKLQS NGPVAKKAKK ETSSSDSSED SSEEEDKAQV PTQKAAAPAK RASLPQHAGK
AAAKASESSS SEESSEEEEE EDKKKKPVQQ KAVKPQAKAV RPPPKKAESS ESESDSSSED
EAPQTQKPKA AATAAKAPTK AQTKAPAKPG PPAKAQPKAA NGKAGSSSSS SSSSSSDDSE
EEKKAAAPLK KTAPKKQVVA KAPVKVTAAP TQKSSSSEDS SSEEEEEQKK PMKKKAGPYS
SVPPPSVSLS KKSVGAQSPK KAAAQTQPAD SSADSSEESD SSSEEEKKTP AKTVVSKTPA
KPAPVKKKAE SSSDSSDSDS SEDEAPAKPV SATKSPLSKP AVTPKPPAAK AVATPKQPAG
SGQKPQSRKA DSSSSEEESS SSEEEATKKS VTTPKARVTA KAAPSLPAKQ APRAGGDSSS
DSESSSSEEE KKTPPKPPAK KKAAGAAVPK PTPVKKAAAE SSSSSSSSED SSEEEKKKPK
SKATPKPQAG KANGVPASQN GKAGKESEEE EEDTEQNKKA AGTKPGSGKK RKHNETADEA
ATPQSKKVKL QTPNTFPKRK KGEKRASSPF RRVREEEIEV DSRVADNSFD AKRGAAGDWG
ERANQVLKFT KGKSFRHEKT KKKRGSYRGG SISVQVNSVK FDSE
