CDK19_HUMAN
ID CDK19_HUMAN Reviewed; 502 AA.
AC Q9BWU1; Q5JQZ7; Q5JR00; Q8TC78; Q9UPX2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Cyclin-dependent kinase 19;
DE EC=2.7.11.22;
DE AltName: Full=CDC2-related protein kinase 6;
DE AltName: Full=Cell division cycle 2-like protein kinase 6;
DE AltName: Full=Cell division protein kinase 19;
DE AltName: Full=Cyclin-dependent kinase 11;
DE AltName: Full=Death-preventing kinase;
GN Name=CDK19; Synonyms=CDC2L6, CDK11, KIAA1028;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Lan Y., Zhang H., Lin F., Smith C., Xu H.;
RT "Delayed onset of apoptosis in factor-dependent T cells expressing a novel
RT cyclin-C associated kinase.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-502 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP INVOLVEMENT IN DEE87, SUBCELLULAR LOCATION, VARIANTS DEE87 HIS-32 AND
RP ALA-196, AND CHARACTERIZATION OF VARIANTS DEE87 HIS-32 AND ALA-196.
RX PubMed=32330417; DOI=10.1016/j.ajhg.2020.04.001;
RG Undiagnosed Diseases Network;
RA Chung H.L., Mao X., Wang H., Park Y.J., Marcogliese P.C., Rosenfeld J.A.,
RA Burrage L.C., Liu P., Murdock D.R., Yamamoto S., Wangler M.F., Chao H.T.,
RA Long H., Feng L., Bacino C.A., Bellen H.J., Xiao B.;
RT "De novo variants in CDK19 are associated with a syndrome involving
RT intellectual disability and epileptic encephalopathy.";
RL Am. J. Hum. Genet. 106:717-725(2020).
RN [10]
RP VARIANT DEE87 HIS-32.
RX PubMed=33134521; DOI=10.1212/nxg.0000000000000527;
RA Sugawara Y., Mizuno T., Moriyama K., Ishiwata H., Kato M., Nakashima M.,
RA Mizuguchi T., Matsumoto N.;
RT "Cerebrospinal fluid abnormalities in developmental and epileptic
RT encephalopathy with a de novo CDK19 variant.";
RL Neurol. Genet. 6:e527-e527(2020).
RN [11]
RP VARIANTS DEE87 ALA-28; ARG-28; CYS-32; HIS-32; LEU-197; CYS-198 AND
RP TRP-200, AND CHARACTERIZATION OF VARIANTS DEE87 ARG-28 AND HIS-32.
RX PubMed=33495529; DOI=10.1038/s41436-020-01091-9;
RA Zarate Y.A., Uehara T., Abe K., Oginuma M., Harako S., Ishitani S.,
RA Lehesjoki A.E., Bierhals T., Kloth K., Ehmke N., Horn D., Holtgrewe M.,
RA Anderson K., Viskochil D., Edgar-Zarate C.L., Sacoto M.J.G., Schnur R.E.,
RA Morrow M.M., Sanchez-Valle A., Pappas J., Rabin R., Muona M.,
RA Anttonen A.K., Platzer K., Luppe J., Gburek-Augustat J., Kaname T.,
RA Okamoto N., Mizuno S., Kaido Y., Ohkuma Y., Hirose Y., Ishitani T.,
RA Kosaki K.;
RT "CDK19-related disorder results from both loss-of-function and gain-of-
RT function de novo missense variants.";
RL Genet. Med. 23:1050-1057(2021).
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=2.7.11.22;
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=2.7.11.22;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32330417}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:32330417}. Nucleus
CC {ECO:0000269|PubMed:32330417}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BWU1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BWU1-2; Sequence=VSP_015857;
CC -!- DISEASE: Developmental and epileptic encephalopathy 87 (DEE87)
CC [MIM:618916]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE87 inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:32330417, ECO:0000269|PubMed:33134521,
CC ECO:0000269|PubMed:33495529}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24247.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY028424; AAK27731.1; -; mRNA.
DR EMBL; Z84480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL603914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024247; AAH24247.1; ALT_INIT; mRNA.
DR EMBL; BC037289; AAH37289.1; -; mRNA.
DR EMBL; AB028951; BAA82980.2; -; mRNA.
DR CCDS; CCDS5085.1; -. [Q9BWU1-1]
DR CCDS; CCDS75503.1; -. [Q9BWU1-2]
DR RefSeq; NP_001287889.1; NM_001300960.1.
DR RefSeq; NP_001287892.1; NM_001300963.1. [Q9BWU1-2]
DR RefSeq; NP_001287893.1; NM_001300964.1. [Q9BWU1-2]
DR RefSeq; NP_055891.1; NM_015076.4. [Q9BWU1-1]
DR AlphaFoldDB; Q9BWU1; -.
DR SMR; Q9BWU1; -.
DR BioGRID; 116725; 80.
DR ComplexPortal; CPX-3263; CKM complex variant 2.
DR CORUM; Q9BWU1; -.
DR DIP; DIP-29013N; -.
DR IntAct; Q9BWU1; 52.
DR MINT; Q9BWU1; -.
DR STRING; 9606.ENSP00000357907; -.
DR BindingDB; Q9BWU1; -.
DR ChEMBL; CHEMBL6002; -.
DR DrugCentral; Q9BWU1; -.
DR GuidetoPHARMACOLOGY; 1972; -.
DR iPTMnet; Q9BWU1; -.
DR PhosphoSitePlus; Q9BWU1; -.
DR BioMuta; CDK19; -.
DR DMDM; 60391917; -.
DR EPD; Q9BWU1; -.
DR jPOST; Q9BWU1; -.
DR MassIVE; Q9BWU1; -.
DR MaxQB; Q9BWU1; -.
DR PaxDb; Q9BWU1; -.
DR PeptideAtlas; Q9BWU1; -.
DR PRIDE; Q9BWU1; -.
DR ProteomicsDB; 79317; -. [Q9BWU1-1]
DR ProteomicsDB; 79318; -. [Q9BWU1-2]
DR Antibodypedia; 2087; 207 antibodies from 31 providers.
DR DNASU; 23097; -.
DR Ensembl; ENST00000323817.7; ENSP00000317665.3; ENSG00000155111.15. [Q9BWU1-2]
DR Ensembl; ENST00000368911.8; ENSP00000357907.3; ENSG00000155111.15. [Q9BWU1-1]
DR GeneID; 23097; -.
DR KEGG; hsa:23097; -.
DR MANE-Select; ENST00000368911.8; ENSP00000357907.3; NM_015076.5; NP_055891.1.
DR UCSC; uc003puh.2; human. [Q9BWU1-1]
DR CTD; 23097; -.
DR DisGeNET; 23097; -.
DR GeneCards; CDK19; -.
DR HGNC; HGNC:19338; CDK19.
DR HPA; ENSG00000155111; Tissue enhanced (brain).
DR MalaCards; CDK19; -.
DR MIM; 614720; gene.
DR MIM; 618916; phenotype.
DR neXtProt; NX_Q9BWU1; -.
DR OpenTargets; ENSG00000155111; -.
DR Orphanet; 442835; Non-specific early-onset epileptic encephalopathy.
DR PharmGKB; PA165617767; -.
DR VEuPathDB; HostDB:ENSG00000155111; -.
DR eggNOG; KOG0666; Eukaryota.
DR GeneTree; ENSGT00940000158213; -.
DR HOGENOM; CLU_000288_181_6_1; -.
DR InParanoid; Q9BWU1; -.
DR OMA; SAQYHSS; -.
DR OrthoDB; 642369at2759; -.
DR PhylomeDB; Q9BWU1; -.
DR TreeFam; TF101025; -.
DR PathwayCommons; Q9BWU1; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; Q9BWU1; -.
DR SIGNOR; Q9BWU1; -.
DR BioGRID-ORCS; 23097; 9 hits in 1090 CRISPR screens.
DR ChiTaRS; CDK19; human.
DR GenomeRNAi; 23097; -.
DR Pharos; Q9BWU1; Tchem.
DR PRO; PR:Q9BWU1; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9BWU1; protein.
DR Bgee; ENSG00000155111; Expressed in endothelial cell and 198 other tissues.
DR ExpressionAtlas; Q9BWU1; baseline and differential.
DR Genevisible; Q9BWU1; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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 Acetylation; Alternative splicing; ATP-binding; Cytoplasm; Disease variant;
KW Epilepsy; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..502
FT /note="Cyclin-dependent kinase 19"
FT /id="PRO_0000085713"
FT DOMAIN 21..335
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 359..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015857"
FT VARIANT 28
FT /note="G -> A (in DEE87)"
FT /evidence="ECO:0000269|PubMed:33495529"
FT /id="VAR_084392"
FT VARIANT 28
FT /note="G -> R (in DEE87; decreased protein kinase
FT activity)"
FT /evidence="ECO:0000269|PubMed:33495529"
FT /id="VAR_084393"
FT VARIANT 32
FT /note="Y -> C (in DEE87)"
FT /evidence="ECO:0000269|PubMed:33495529"
FT /id="VAR_084394"
FT VARIANT 32
FT /note="Y -> H (in DEE87; fails to rescue neurologic
FT phenotypes in a Drosophila model system; increased protein
FT kinase activity; dbSNP:rs1236246272)"
FT /evidence="ECO:0000269|PubMed:32330417,
FT ECO:0000269|PubMed:33134521, ECO:0000269|PubMed:33495529"
FT /id="VAR_084395"
FT VARIANT 196
FT /note="T -> A (in DEE87; fails to rescue neurologic
FT phenotypes in a Drosophila model system)"
FT /evidence="ECO:0000269|PubMed:32330417"
FT /id="VAR_084396"
FT VARIANT 197
FT /note="F -> L (in DEE87)"
FT /evidence="ECO:0000269|PubMed:33495529"
FT /id="VAR_084397"
FT VARIANT 198
FT /note="W -> C (in DEE87)"
FT /evidence="ECO:0000269|PubMed:33495529"
FT /id="VAR_084398"
FT VARIANT 200
FT /note="R -> W (in DEE87)"
FT /evidence="ECO:0000269|PubMed:33495529"
FT /id="VAR_084399"
SQ SEQUENCE 502 AA; 56802 MW; D9EED1BBB582EABA CRC64;
MDYDFKAKLA AERERVEDLF EYEGCKVGRG TYGHVYKARR KDGKDEKEYA LKQIEGTGIS
MSACREIALL RELKHPNVIA LQKVFLSHSD RKVWLLFDYA EHDLWHIIKF HRASKANKKP
MQLPRSMVKS LLYQILDGIH YLHANWVLHR DLKPANILVM GEGPERGRVK IADMGFARLF
NSPLKPLADL DPVVVTFWYR APELLLGARH YTKAIDIWAI GCIFAELLTS EPIFHCRQED
IKTSNPFHHD QLDRIFSVMG FPADKDWEDI RKMPEYPTLQ KDFRRTTYAN SSLIKYMEKH
KVKPDSKVFL LLQKLLTMDP TKRITSEQAL QDPYFQEDPL PTLDVFAGCQ IPYPKREFLN
EDDPEEKGDK NQQQQQNQHQ QPTAPPQQAA APPQAPPPQQ NSTQTNGTAG GAGAGVGGTG
AGLQHSQDSS LNQVPPNKKP RLGPSGANSG GPVMPSDYQH SSSRLNYQSS VQGSSQSQST
LGYSSSSQQS SQYHPSHQAH RY
