NHK1_DROME
ID NHK1_DROME Reviewed; 599 AA.
AC Q7KRY6; Q9U9Q0; Q9VBB2;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Nucleosomal histone kinase 1;
DE EC=2.7.11.1 {ECO:0000269|PubMed:15078818};
DE AltName: Full=Protein baellchen;
GN Name=ball; Synonyms=ballchen, nhk-1; ORFNames=CG6386;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP PROTEIN SEQUENCE OF 35-44 AND 186-195, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=15078818; DOI=10.1101/gad.1184604;
RA Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N., Takio K.,
RA Kaneko M., Takeshima Y., Muramatsu M., Ito T.;
RT "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in
RT the early Drosophila embryo.";
RL Genes Dev. 18:877-888(2004).
RN [5]
RP FUNCTION, MUTAGENESIS OF PRO-117, AND TISSUE SPECIFICITY.
RX PubMed=16230526; DOI=10.1101/gad.1348905;
RA Ivanovska I., Khandan T., Ito T., Orr-Weaver T.L.;
RT "A histone code in meiosis: the histone kinase, NHK-1, is required for
RT proper chromosomal architecture in Drosophila oocytes.";
RL Genes Dev. 19:2571-2582(2005).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RX PubMed=16301329; DOI=10.1083/jcb.200508127;
RA Cullen C.F., Brittle A.L., Ito T., Ohkura H.;
RT "The conserved kinase NHK-1 is essential for mitotic progression and
RT unifying acentrosomal meiotic spindles in Drosophila melanogaster.";
RL J. Cell Biol. 171:593-602(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376; SER-381; SER-382;
RP SER-388; SER-390; SER-483; SER-564; SER-586 AND THR-589, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [8]
RP FUNCTION, INTERACTION WITH UNC-89, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26251439; DOI=10.1242/jcs.170639;
RA Katzemich A., West R.J., Fukuzawa A., Sweeney S.T., Gautel M., Sparrow J.,
RA Bullard B.;
RT "Binding partners of the kinase domains in Drosophila obscurin and their
RT effect on the structure of the flight muscle.";
RL J. Cell Sci. 128:3386-3397(2015).
RN [9]
RP INTERACTION WITH L(2)GL.
RX PubMed=31735666; DOI=10.1016/j.devcel.2019.10.009;
RA Link N., Chung H., Jolly A., Withers M., Tepe B., Arenkiel B.R., Shah P.S.,
RA Krogan N.J., Aydin H., Geckinli B.B., Tos T., Isikay S., Tuysuz B.,
RA Mochida G.H., Thomas A.X., Clark R.D., Mirzaa G.M., Lupski J.R.,
RA Bellen H.J.;
RT "Mutations in ANKLE2, a ZIKA Virus Target, Disrupt an Asymmetric Cell
RT Division Pathway in Drosophila Neuroblasts to Cause Microcephaly.";
RL Dev. Cell 51:713-729.e6(2019).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in somatic mitosis
CC and female meiosis (PubMed:16230526). Required for spindle organization
CC in mitosis, and for the establishment or maintenance of meiosis-
CC specific chromosomal configurations, including the prophase I karyosome
CC and the metaphase I spindle (PubMed:15078818, PubMed:16301329).
CC Specifically phosphorylates nucleosomal H2A on 'Thr-119'
CC (PubMed:15078818). Required for the development and organization of
CC indirect flight muscle sarcomeres by regulating the formation of M line
CC and H zone and the correct assembly of thick and thin filaments in the
CC sarcomere (PubMed:26251439). {ECO:0000269|PubMed:15078818,
CC ECO:0000269|PubMed:16230526, ECO:0000269|PubMed:16301329,
CC ECO:0000269|PubMed:26251439}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:15078818};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15078818};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15078818};
CC -!- SUBUNIT: May interact with Unc-89 (via protein kinase domain 1)
CC (PubMed:26251439). Interacts with L(2)gl (PubMed:31735666).
CC {ECO:0000269|PubMed:26251439, ECO:0000269|PubMed:31735666}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15078818}. Nucleus
CC {ECO:0000269|PubMed:15078818}. Chromosome
CC {ECO:0000269|PubMed:15078818}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:26251439}. Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:26251439}. Note=Chromatin-associated during mitosis
CC (PubMed:15078818). In indirect flight muscle, colocalizes with sls
CC isoform A (kettin) to the sarcomere Z lines and appears to be weakly
CC distributed across the sarcomere (PubMed:26251439). More rarely,
CC localizes to M lines (PubMed:26251439). {ECO:0000269|PubMed:15078818,
CC ECO:0000269|PubMed:26251439}.
CC -!- TISSUE SPECIFICITY: Expressed in ovaries (at protein level)
CC (PubMed:16230526, PubMed:16301329). Expressed in indirect flight muscle
CC (IFM) (at protein level) (PubMed:26251439).
CC {ECO:0000269|PubMed:16230526, ECO:0000269|PubMed:16301329,
CC ECO:0000269|PubMed:26251439}.
CC -!- DEVELOPMENTAL STAGE: Present throughout development, with highest level
CC in early embryo (at protein level). {ECO:0000269|PubMed:15078818}.
CC -!- PTM: Phosphorylated during mitosis and female meiosis.
CC {ECO:0000269|PubMed:16301329, ECO:0000269|PubMed:18327897}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in muscles causes 91
CC percent lethality at the early pupal stage and the few surviving
CC animals cannot fly. Severe defects in the indirect flight muscle
CC structure characterized by narrower and wavy myofibrils and abnormal
CC positioning of sarcomere Z line, M line and H line. Although the
CC spacing between Z line and M lines stays regular, in less affected
CC myobrils Z lines and M lines appear fragmented, Z lines are diffused at
CC the edges and sarcomere length is shorter. In the more affected
CC myofibrils, rudimentary Z lines are shifted into the region of thick
CC and thin filament overlap and are by-passed by abnormally long
CC filaments and H zones fail to localize to the middle of the sarcomere.
CC Localization of unc-89/obscurin to M lines and localization of kettin
CC (sls isoform A) to Z line is not affected.
CC {ECO:0000269|PubMed:26251439}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. VRK subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD46857.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF56630.2; -; Genomic_DNA.
DR EMBL; AF160917; AAD46857.2; ALT_INIT; mRNA.
DR RefSeq; NP_651508.1; NM_143251.1.
DR RefSeq; NP_733171.1; NM_170292.2.
DR AlphaFoldDB; Q7KRY6; -.
DR SMR; Q7KRY6; -.
DR BioGRID; 68119; 16.
DR IntAct; Q7KRY6; 3.
DR STRING; 7227.FBpp0084465; -.
DR iPTMnet; Q7KRY6; -.
DR PaxDb; Q7KRY6; -.
DR PRIDE; Q7KRY6; -.
DR EnsemblMetazoa; FBtr0085095; FBpp0084465; FBgn0027889.
DR EnsemblMetazoa; FBtr0085096; FBpp0084466; FBgn0027889.
DR GeneID; 43228; -.
DR KEGG; dme:Dmel_CG6386; -.
DR CTD; 43228; -.
DR FlyBase; FBgn0027889; ball.
DR VEuPathDB; VectorBase:FBgn0027889; -.
DR eggNOG; KOG1164; Eukaryota.
DR GeneTree; ENSGT00940000168643; -.
DR HOGENOM; CLU_019279_4_2_1; -.
DR InParanoid; Q7KRY6; -.
DR OMA; PDYDKCR; -.
DR OrthoDB; 866200at2759; -.
DR PhylomeDB; Q7KRY6; -.
DR Reactome; R-DME-202670; ERKs are inactivated.
DR Reactome; R-DME-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-DME-9013405; RHOD GTPase cycle.
DR BioGRID-ORCS; 43228; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43228; -.
DR PRO; PR:Q7KRY6; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0027889; Expressed in cleaving embryo and 26 other tissues.
DR ExpressionAtlas; Q7KRY6; baseline and differential.
DR Genevisible; Q7KRY6; DM.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031430; C:M band; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030017; C:sarcomere; IDA:FlyBase.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035184; F:histone threonine kinase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:FlyBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IMP:FlyBase.
DR GO; GO:0036099; P:female germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:UniProtKB.
DR GO; GO:0060361; P:flight; IMP:UniProtKB.
DR GO; GO:0016572; P:histone phosphorylation; IDA:FlyBase.
DR GO; GO:0036098; P:male germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0030717; P:oocyte karyosome formation; IMP:FlyBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007130; P:synaptonemal complex assembly; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Chromatin regulator; Chromosome;
KW Cytoplasm; Direct protein sequencing; Kinase; Magnesium; Meiosis;
KW Metal-binding; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..599
FT /note="Nucleosomal histone kinase 1"
FT /id="PRO_0000086441"
FT DOMAIN 47..328
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 340..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 53..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 589
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 117
FT /note="P->L: In Z3-0437; induces female and male sterility
FT and abolishes T-119 phosphorylation of H2A in the oocyte."
FT /evidence="ECO:0000269|PubMed:16230526"
SQ SEQUENCE 599 AA; 65994 MW; B32EE3004477EBDB CRC64;
MPRVAKPKAA APAKKVVSAK KAKSKLYKMP EKVKEGTVFT DLAKGQWRIG PSIGVGGFGE
IYAACKVGEK NYDAVVKCEP HGNGPLFVEM HFYLRNAKLE DIKQFMQKHG LKSLGMPYIL
ANGSVEVNGE KHRFIVMPRY GSDLTKFLEQ NGKRLPEGTV YRLAIQMLDV YQYMHSNGYV
HADLKAANIL LGLEKGGAAQ AYLVDFGLAS HFVTGDFKPD PKKMHNGTIE YTSRDAHLGV
PTRRADLEIL GYNLIEWLGA ELPWVTQKLL AVPPKVQKAK EAFMDNIGES LKTLFPKGVP
PPIGDFMKYV SKLTHNQEPD YDKCRSWFSS ALKQLKIPNN GDLDFKMKPQ TSSNNNLSPP
GTSKAATARK AKKIDSPVLN SSLDEKISAS EDDEEEEEKS HRKKTAKKVT PSARNAKVSP
LKRVADSSPP SQKRVKTEPK STPRERATPK ASPKPRSTPK ASPKPQTPTA ARLRTPNAKI
NFSPSISLRG RPGGKTVIND DLTPQPRSKK TYEFNFELDV SMDANVIVNV KRKKKADQDK
ATAVDSRTPS SRSALASSSK EEASPVTRVN LRKVNGHGDS STPGRSPRTP AVTVRKYQG
