LYAR_MOUSE
ID LYAR_MOUSE Reviewed; 388 AA.
AC Q08288; Q9D9X2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Cell growth-regulating nucleolar protein;
DE AltName: Full=Ly1 antibody-reactive protein {ECO:0000303|PubMed:8491376};
DE AltName: Full=Protein expressed in male leptotene and zygotene spermatocytes 264;
DE Short=MLZ-264;
GN Name=Lyar;
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], AND SUBCELLULAR LOCATION.
RX PubMed=8491376; DOI=10.1101/gad.7.5.735;
RA Su L., Hershberger R.J., Weissman I.L.;
RT "LYAR, a novel nucleolar protein with zinc finger DNA-binding motifs, is
RT involved in cell growth regulation.";
RL Genes Dev. 7:735-748(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION, INTERACTION WITH NCL, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19489080; DOI=10.1002/stem.55;
RA Li H., Wang B., Yang A., Lu R., Wang W., Zhou Y., Shi G., Kwon S.W.,
RA Zhao Y., Jin Y.;
RT "Ly-1 antibody reactive clone is an important nucleolar protein for control
RT of self-renewal and differentiation in embryonic stem cells.";
RL Stem Cells 27:1244-1254(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, Spleen, and Testis;
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 [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20339383; DOI=10.1038/jhg.2010.26;
RA Kogo H., Kowa-Sugiyama H., Yamada K., Bolor H., Tsutsumi M., Ohye T.,
RA Inagaki H., Taniguchi M., Toda T., Kurahashi H.;
RT "Screening of genes involved in chromosome segregation during meiosis I:
RT toward the identification of genes responsible for infertility in humans.";
RL J. Hum. Genet. 55:293-299(2010).
RN [6]
RP INTERACTION WITH NCL, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=23212345; DOI=10.1007/s10059-013-2271-3;
RA Lee B., Jin S., Choi H., Kwon J.T., Kim J., Jeong J., Kwon Y.I., Cho C.;
RT "Expression and function of the testis-predominant protein LYAR in mice.";
RL Mol. Cells 35:54-60(2013).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24990247; DOI=10.1007/s11010-014-2128-x;
RA Yonezawa K., Sugihara Y., Oshima K., Matsuda T., Nadano D.;
RT "Lyar, a cell growth-regulating zinc finger protein, was identified to be
RT associated with cytoplasmic ribosomes in male germ and cancer cells.";
RL Mol. Cell. Biochem. 395:221-229(2014).
RN [8]
RP FUNCTION.
RX PubMed=25092918; DOI=10.1093/nar/gku718;
RA Ju J., Wang Y., Liu R., Zhang Y., Xu Z., Wang Y., Wu Y., Liu M.,
RA Cerruti L., Zou F., Ma C., Fang M., Tan R., Jane S.M., Zhao Q.;
RT "Human fetal globin gene expression is regulated by LYAR.";
RL Nucleic Acids Res. 42:9740-9752(2014).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25735755; DOI=10.1002/jcb.25089;
RA Guo F., Ding Y., Caberoy N.B., Alvarado G., Liu R., Shen C., Yu J.,
RA Zhou Y., Salero E., LeBlanc M.E., Wang W., Li W.;
RT "Lyar is a new ligand for retinal pigment epithelial phagocytosis.";
RL J. Cell. Biochem. 116:2177-2187(2015).
RN [10]
RP STRUCTURE BY NMR OF 1-66, AND ZINC-BINDING SITES.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the N-terminal zinc finger domain of cell growth
RT regulating nucleolar protein Lyar.";
RL Submitted (JAN-2006) to the PDB data bank.
CC -!- FUNCTION: Plays a role in the maintenance of the appropriate processing
CC of 47S/45S pre-rRNA to 32S/30S pre-rRNAs and their subsequent
CC processing to produce 18S and 28S rRNAs (By similarity). Also acts at
CC the level of transcription regulation. Along with PRMT5, binds
CC embryonic globin promoter (By similarity). Represses the expression of
CC embryonic globin Hbb-y gene (PubMed:25092918). In neuroblastoma cells,
CC may also repress the expression of oxidative stress genes, including
CC CHAC1, HMOX1, SLC7A11, ULBP1 and that encoding the small nucleolar RNA
CC SNORD41 (By similarity). Preferentially binds to a DNA motif containing
CC 5'-GGTTAT-3' (By similarity). Negatively regulates the antiviral innate
CC immune response by targeting IRF3 and impairing its DNA-binding
CC activity (By similarity). In addition, inhibits NF-kappa-B-mediated
CC expression of pro-inflammatory cytokines (By similarity). Stimulates
CC phagocytosis of photoreceptor outer segments by retinal pigment
CC epithelial cells (PubMed:25735755). Prevents NCL self-cleavage,
CC maintaining a normal steady-state level of NCL protein in
CC undifferentiated embryonic stem cells (ESCs), which in turn is
CC essential for ESC self-renewal (PubMed:19489080).
CC {ECO:0000250|UniProtKB:Q9NX58, ECO:0000269|PubMed:19489080,
CC ECO:0000269|PubMed:25092918, ECO:0000269|PubMed:25735755}.
CC -!- SUBUNIT: Interacts with PRMT5; this interaction is direct (By
CC similarity). Interacts with GNL2 and RPL23A (By similarity). Interacts
CC with nucleolin/NCL; this interaction is direct (PubMed:19489080,
CC PubMed:23212345). Interacts with phosphorylated IRF3; this interaction
CC impairs IRF3 DNA-binding activity (By similarity).
CC {ECO:0000250|UniProtKB:Q9NX58, ECO:0000269|PubMed:19489080,
CC ECO:0000269|PubMed:23212345}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19489080,
CC ECO:0000269|PubMed:23212345, ECO:0000269|PubMed:24990247,
CC ECO:0000269|PubMed:8491376}. Cytoplasm {ECO:0000269|PubMed:24990247}.
CC Cell projection, cilium, photoreceptor outer segment
CC {ECO:0000269|PubMed:25735755}. Note=Component of pre-ribosomal
CC particles, including pre-40S, pre-60S and pre-90S (By similarity).
CC Associated with cytoplasmic ribosomes, but not polysomes, as a
CC component of the 60S subunit (PubMed:24990247). In the retina,
CC predominantly expressed in photoreceptor outer segments
CC (PubMed:25735755). In the nucleolus, colocalizes with nucleolin/NCL,
CC therefore may reside in the dense fibrillar component (DFC)
CC (PubMed:19489080). {ECO:0000250|UniProtKB:Q9NX58,
CC ECO:0000269|PubMed:19489080, ECO:0000269|PubMed:24990247,
CC ECO:0000269|PubMed:25735755}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis, in germ cells,
CC and at a moderate level in spleen, liver and lung (at protein level)
CC (PubMed:19489080, PubMed:23212345, PubMed:24990247). Very high levels
CC in spermatogonia, spermatocytes and round spermatids, but not in
CC testicular sperm and mature sperm (at protein level) (PubMed:20339383,
CC PubMed:23212345, PubMed:24990247). Expressed in ovary
CC (PubMed:20339383). Expressed in the retina, including in photoreceptor
CC outer segments (at protein level) (PubMed:25735755). Expressed in
CC undifferentiated embryonic stem cells (PubMed:19489080,
CC PubMed:23212345). {ECO:0000269|PubMed:19489080,
CC ECO:0000269|PubMed:20339383, ECO:0000269|PubMed:23212345,
CC ECO:0000269|PubMed:24990247, ECO:0000269|PubMed:25735755}.
CC -!- DEVELOPMENTAL STAGE: Expressed in testis and ovary at 15.5 dpc
CC (PubMed:20339383). May be differentially expressed during
CC spermatogenesis. Detected first at P12, the early stage of
CC spermatogenesis. Levels considerably increase at P16, corresponding to
CC the development of pachytene spermatocytes (PubMed:23212345).
CC {ECO:0000269|PubMed:20339383, ECO:0000269|PubMed:23212345}.
CC -!- DOMAIN: The N-terminal zinc-finger domains are required for the
CC appropriate production of 28S rRNA and the formation of pre-60S
CC particles. {ECO:0000250|UniProtKB:Q9NX58}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mutant mice are fully
CC fertile and show intact spermatogenesis. {ECO:0000269|PubMed:23212345}.
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DR EMBL; S60885; AAB26644.1; -; mRNA.
DR EMBL; AK006373; BAB24554.1; -; mRNA.
DR CCDS; CCDS19253.1; -.
DR PIR; A40683; A40683.
DR RefSeq; NP_079557.2; NM_025281.3.
DR RefSeq; XP_006503822.1; XM_006503759.1.
DR RefSeq; XP_006503823.1; XM_006503760.1.
DR RefSeq; XP_006503824.1; XM_006503761.1.
DR RefSeq; XP_006503825.1; XM_006503762.1.
DR RefSeq; XP_006503826.1; XM_006503763.1.
DR RefSeq; XP_006503827.1; XM_006503764.1.
DR PDB; 1WJV; NMR; -; A=1-66.
DR PDBsum; 1WJV; -.
DR AlphaFoldDB; Q08288; -.
DR BMRB; Q08288; -.
DR SMR; Q08288; -.
DR BioGRID; 201254; 5.
DR IntAct; Q08288; 2.
DR MINT; Q08288; -.
DR STRING; 10090.ENSMUSP00000084791; -.
DR DrugBank; DB09130; Copper.
DR iPTMnet; Q08288; -.
DR PhosphoSitePlus; Q08288; -.
DR EPD; Q08288; -.
DR MaxQB; Q08288; -.
DR PaxDb; Q08288; -.
DR PeptideAtlas; Q08288; -.
DR PRIDE; Q08288; -.
DR ProteomicsDB; 287278; -.
DR Antibodypedia; 22562; 234 antibodies from 29 providers.
DR DNASU; 17089; -.
DR Ensembl; ENSMUST00000087514; ENSMUSP00000084791; ENSMUSG00000067367.
DR Ensembl; ENSMUST00000114106; ENSMUSP00000109741; ENSMUSG00000067367.
DR GeneID; 17089; -.
DR KEGG; mmu:17089; -.
DR UCSC; uc008xgh.2; mouse.
DR CTD; 55646; -.
DR MGI; MGI:107470; Lyar.
DR VEuPathDB; HostDB:ENSMUSG00000067367; -.
DR eggNOG; KOG2186; Eukaryota.
DR GeneTree; ENSGT00390000003477; -.
DR HOGENOM; CLU_057137_0_1_1; -.
DR InParanoid; Q08288; -.
DR OMA; QKIHEVM; -.
DR OrthoDB; 1567501at2759; -.
DR PhylomeDB; Q08288; -.
DR TreeFam; TF314925; -.
DR BioGRID-ORCS; 17089; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Lyar; mouse.
DR EvolutionaryTrace; Q08288; -.
DR PRO; PR:Q08288; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q08288; protein.
DR Bgee; ENSMUSG00000067367; Expressed in otic placode and 268 other tissues.
DR ExpressionAtlas; Q08288; baseline and differential.
DR Genevisible; Q08288; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; ISO:MGI.
DR GO; GO:0048821; P:erythrocyte development; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045824; P:negative regulation of innate immune response; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:UniProtKB.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
DR InterPro; IPR039999; LYAR.
DR InterPro; IPR014898; Znf_C2H2_LYAR.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR13100; PTHR13100; 2.
DR Pfam; PF08790; zf-LYAR; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS51804; ZF_C2HC_LYAR; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Coiled coil; Cytoplasm; DNA-binding;
KW Immunity; Innate immunity; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..388
FT /note="Cell growth-regulating nucleolar protein"
FT /id="PRO_0000084529"
FT ZN_FING 1..26
FT /note="C2HC LYAR-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT ZN_FING 28..52
FT /note="C2HC LYAR-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT REGION 140..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 174..216
FT /evidence="ECO:0000255"
FT COMPBIAS 140..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NX58"
FT CROSSLNK 204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NX58"
FT CONFLICT 21
FT /note="H -> Q (in Ref. 1; AAB26644)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="R -> I (in Ref. 1; AAB26644)"
FT /evidence="ECO:0000305"
FT CONFLICT 234..238
FT /note="EAAEA -> DGADG (in Ref. 1; AAB26644)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="A -> R (in Ref. 1; AAB26644)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="N -> K (in Ref. 2; BAB24554)"
FT /evidence="ECO:0000305"
FT CONFLICT 356..359
FT /note="HHTS -> TSHH (in Ref. 1; AAB26644)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1WJV"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1WJV"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:1WJV"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1WJV"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:1WJV"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1WJV"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1WJV"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:1WJV"
SQ SEQUENCE 388 AA; 43736 MW; D39A0CDC2257BE8C CRC64;
MVFFTCNACG ESVKKIQVEK HVSNCRNCEC LSCIDCGKDF WGDDYKSHVK CISEGQKYGG
KGYEAKTHKG DAKQQAWIQK INELIKKPNV SPKVRELLQQ ISAFDNVPRK KAKFQNWMKN
SLKVHSDSVL EQVWDIFSEA SSSEQDQQQP PSHTAKPHAE MPITKVPSAK TNGTTEEQTE
AKKNKRERKE ERQKNRKKEK KELKLENHQE NLRGQKPKKR KKNQEAGHEA AGEEAAEASG
PPEKKKAQGG QASEEGADRN GGPGEDAAEG QTKTAAGKRK RPKHSGAESG YKKKKMKLPE
QPEEGEAKDH EAPSKGKFNW KGTIKAVLKQ APDNEISVKK LKKKVIAQYH AVMNDHHTSE
EELLAIFNRK ISRNPTFKVL KDRVKLLK
