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 27-MAR-2024, entry version 184. 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}; 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; 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; 87. DR ComplexPortal; CPX-3263; CKM complex variant 2. DR CORUM; Q9BWU1; -. DR DIP; DIP-29013N; -. DR IntAct; Q9BWU1; 51. 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 CPTAC; non-CPTAC-6017; -. DR EPD; Q9BWU1; -. DR jPOST; Q9BWU1; -. DR MassIVE; Q9BWU1; -. DR MaxQB; Q9BWU1; -. DR PaxDb; 9606-ENSP00000357907; -. DR PeptideAtlas; Q9BWU1; -. DR ProteomicsDB; 79317; -. [Q9BWU1-1] DR ProteomicsDB; 79318; -. [Q9BWU1-2] DR Pumba; Q9BWU1; -. DR Antibodypedia; 2087; 226 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 AGR; HGNC:19338; -. DR CTD; 23097; -. DR DisGeNET; 23097; -. DR GeneCards; CDK19; -. DR HGNC; HGNC:19338; CDK19. DR HPA; ENSG00000155111; Low tissue specificity. 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; 46620at2759; -. 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 1168 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 200 other cell types or tissues. DR ExpressionAtlas; Q9BWU1; baseline and differential. DR GO; GO:1990508; C:CKM complex; ISS:ComplexPortal. DR GO; GO:0005829; C:cytosol; IDA:HPA. 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; IEA:UniProtKB-EC. 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:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl. DR CDD; cd07867; STKc_CDC2L6; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1. DR PANTHER; PTHR24056:SF572; CYCLIN-DEPENDENT KINASE 19; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q9BWU1; HS. 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; dbSNP:rs1783518890)" 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; dbSNP:rs1783517622)" 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 dbSNP:rs1779473650)" FT /evidence="ECO:0000269|PubMed:32330417" FT /id="VAR_084396" FT VARIANT 197 FT /note="F -> L (in DEE87; dbSNP:rs1779473436)" FT /evidence="ECO:0000269|PubMed:33495529" FT /id="VAR_084397" FT VARIANT 198 FT /note="W -> C (in DEE87; dbSNP:rs1779473213)" FT /evidence="ECO:0000269|PubMed:33495529" FT /id="VAR_084398" FT VARIANT 200 FT /note="R -> W (in DEE87; dbSNP:rs1779472995)" 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 //