M3K19_HUMAN
ID M3K19_HUMAN Reviewed; 1328 AA.
AC Q56UN5; B2RP57; B7ZMH9; E2QRE3; Q56UN1; Q56UN2; Q56UN3; Q56UN4; Q8N4E9;
AC Q9H5T2;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 19;
DE EC=2.7.11.1;
DE AltName: Full=Regulated in COPD, protein kinase;
DE AltName: Full=SPS1/STE20-related protein kinase YSK4;
GN Name=MAP3K19; Synonyms=RCK, YSK4;
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] (ISOFORMS 1; 3; 4 AND 5).
RA Watanabe S., Kondo S., Tanabe E., Takao E., Bacon K.B., Encinas J.A.;
RT "Molecular cloning and characterization of RCK, a MAPK kinase kinase that
RT specifically phosphorylates MKK4.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 7).
RC TISSUE=Brain;
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 1075-1307 (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP VARIANT [LARGE SCALE ANALYSIS] MET-500.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
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 -!- 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;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q56UN5-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q56UN5-3; Sequence=VSP_017924;
CC Name=4;
CC IsoId=Q56UN5-4; Sequence=VSP_017925, VSP_017926;
CC Name=5;
CC IsoId=Q56UN5-5; Sequence=VSP_017925;
CC Name=7;
CC IsoId=Q56UN5-7; Sequence=VSP_055367;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT81412.1; Type=Miscellaneous discrepancy; Note=Non-canonical splice intron-exon junction.; Evidence={ECO:0000305};
CC Sequence=BAB15538.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AY574901; AAT81410.1; -; mRNA.
DR EMBL; AY574902; AAT81411.1; -; mRNA.
DR EMBL; AY574903; AAT81412.1; ALT_SEQ; mRNA.
DR EMBL; AY574904; AAT81413.1; -; mRNA.
DR EMBL; AY574905; AAT81414.1; -; mRNA.
DR EMBL; AK026727; BAB15538.1; ALT_INIT; mRNA.
DR EMBL; AC016725; AAY14999.1; -; Genomic_DNA.
DR EMBL; AC020602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034417; AAH34417.1; -; mRNA.
DR EMBL; BC137276; AAI37277.1; -; mRNA.
DR EMBL; BC137277; AAI37278.1; -; mRNA.
DR EMBL; BC144555; AAI44556.1; -; mRNA.
DR CCDS; CCDS2176.2; -. [Q56UN5-1]
DR CCDS; CCDS33293.1; -. [Q56UN5-5]
DR CCDS; CCDS63020.1; -. [Q56UN5-3]
DR CCDS; CCDS63021.1; -. [Q56UN5-7]
DR CCDS; CCDS63022.1; -. [Q56UN5-4]
DR RefSeq; NP_001018054.1; NM_001018044.2. [Q56UN5-3]
DR RefSeq; NP_001018056.1; NM_001018046.2. [Q56UN5-5]
DR RefSeq; NP_001018057.1; NM_001018047.2. [Q56UN5-4]
DR RefSeq; NP_001269812.1; NM_001282883.1. [Q56UN5-7]
DR RefSeq; NP_001308106.1; NM_001321177.1.
DR RefSeq; NP_079328.3; NM_025052.4. [Q56UN5-1]
DR RefSeq; XP_011510194.1; XM_011511892.1. [Q56UN5-1]
DR RefSeq; XP_016860492.1; XM_017005003.1. [Q56UN5-1]
DR AlphaFoldDB; Q56UN5; -.
DR SMR; Q56UN5; -.
DR BioGRID; 123124; 21.
DR IntAct; Q56UN5; 1.
DR MINT; Q56UN5; -.
DR STRING; 9606.ENSP00000365005; -.
DR BindingDB; Q56UN5; -.
DR ChEMBL; CHEMBL6191; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q56UN5; -.
DR GuidetoPHARMACOLOGY; 2076; -.
DR iPTMnet; Q56UN5; -.
DR PhosphoSitePlus; Q56UN5; -.
DR BioMuta; MAP3K19; -.
DR DMDM; 74755104; -.
DR jPOST; Q56UN5; -.
DR MassIVE; Q56UN5; -.
DR MaxQB; Q56UN5; -.
DR PaxDb; Q56UN5; -.
DR PeptideAtlas; Q56UN5; -.
DR PRIDE; Q56UN5; -.
DR ProteomicsDB; 62584; -. [Q56UN5-1]
DR ProteomicsDB; 62586; -. [Q56UN5-3]
DR ProteomicsDB; 62587; -. [Q56UN5-4]
DR ProteomicsDB; 62588; -. [Q56UN5-5]
DR ProteomicsDB; 7260; -.
DR Antibodypedia; 2102; 57 antibodies from 19 providers.
DR DNASU; 80122; -.
DR Ensembl; ENST00000358371.9; ENSP00000351140.4; ENSG00000176601.14. [Q56UN5-3]
DR Ensembl; ENST00000375844.7; ENSP00000365004.3; ENSG00000176601.14. [Q56UN5-5]
DR Ensembl; ENST00000375845.8; ENSP00000365005.3; ENSG00000176601.14. [Q56UN5-1]
DR Ensembl; ENST00000392915.7; ENSP00000376647.2; ENSG00000176601.14. [Q56UN5-1]
DR Ensembl; ENST00000392917.8; ENSP00000376649.3; ENSG00000176601.14. [Q56UN5-7]
DR Ensembl; ENST00000392918.7; ENSP00000376650.3; ENSG00000176601.14. [Q56UN5-4]
DR GeneID; 80122; -.
DR KEGG; hsa:80122; -.
DR MANE-Select; ENST00000392915.7; ENSP00000376647.2; NM_025052.5; NP_079328.3.
DR UCSC; uc002tue.2; human. [Q56UN5-1]
DR CTD; 80122; -.
DR DisGeNET; 80122; -.
DR GeneCards; MAP3K19; -.
DR HGNC; HGNC:26249; MAP3K19.
DR HPA; ENSG00000176601; Group enriched (brain, choroid plexus, fallopian tube, testis).
DR neXtProt; NX_Q56UN5; -.
DR OpenTargets; ENSG00000176601; -.
DR PharmGKB; PA142670554; -.
DR VEuPathDB; HostDB:ENSG00000176601; -.
DR eggNOG; KOG0198; Eukaryota.
DR GeneTree; ENSGT00940000160383; -.
DR HOGENOM; CLU_599846_0_0_1; -.
DR InParanoid; Q56UN5; -.
DR OMA; ISSSEXL; -.
DR OrthoDB; 55144at2759; -.
DR PhylomeDB; Q56UN5; -.
DR TreeFam; TF332735; -.
DR PathwayCommons; Q56UN5; -.
DR SignaLink; Q56UN5; -.
DR BioGRID-ORCS; 80122; 12 hits in 1081 CRISPR screens.
DR ChiTaRS; MAP3K19; human.
DR GenomeRNAi; 80122; -.
DR Pharos; Q56UN5; Tchem.
DR PRO; PR:Q56UN5; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q56UN5; protein.
DR Bgee; ENSG00000176601; Expressed in bronchial epithelial cell and 131 other tissues.
DR ExpressionAtlas; Q56UN5; baseline and differential.
DR Genevisible; Q56UN5; HS.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; 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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1328
FT /note="Mitogen-activated protein kinase kinase kinase 19"
FT /id="PRO_0000232640"
FT DOMAIN 1061..1324
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1186
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1067..1075
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1089
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 79..191
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_017924"
FT VAR_SEQ 207..1074
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055367"
FT VAR_SEQ 207..1024
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_017925"
FT VAR_SEQ 1064..1111
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_017926"
FT VARIANT 438
FT /note="T -> I (in dbSNP:rs16831235)"
FT /id="VAR_051687"
FT VARIANT 500
FT /note="I -> M (in a breast pleomorphic lobular carcinoma
FT sample; somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041334"
FT VARIANT 676
FT /note="E -> Q (in dbSNP:rs1112542)"
FT /id="VAR_051688"
FT VARIANT 812
FT /note="E -> G (in dbSNP:rs3905317)"
FT /id="VAR_051689"
FT CONFLICT 1073..1074
FT /note="GT -> RE (in Ref. 3; AAH34417)"
FT /evidence="ECO:0000305"
FT CONFLICT 1235
FT /note="A -> V (in Ref. 4; BAB15538)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1328 AA; 150537 MW; 10E225EDB1EF4FA3 CRC64;
MSSMPKPERH AESLLDICHD TNSSPTDLMT VTKNQNIILQ SISRSEEFDQ DGDCSHSTLV
NEEEDPSGGR QDWQPRTEGV EITVTFPRDV SPPQEMSQED LKEKNLINSS LQEWAQAHAV
SHPNEIETVE LRKKKLTMRP LVLQKEESSR ELCNVNLGFL LPRSCLELNI SKSVTREDAP
HFLKEQQRKS EEFSTSHMKY SGRSIKFLLP PLSLLPTRSG VLTIPQNHKF PKEKERNIPS
LTSFVPKLSV SVRQSDELSP SNEPPGALVK SLMDPTLRSS DGFIWSRNMC SFPKTNHHRQ
CLEKEENWKS KEIEECNKIE ITHFEKGQSL VSFENLKEGN IPAVREEDID CHGSKTRKPE
EENSQYLSSR KNESSVAKNY EQDPEIVCTI PSKFQETQHS EITPSQDEEM RNNKAASKRV
SLHKNEAMEP NNILEECTVL KSLSSVVFDD PIDKLPEGCS SMETNIKISI AERAKPEMSR
MVPLIHITFP VDGSPKEPVI AKPSLQTRKG TIHNNHSVNI PVHQENDKHK MNSHRSKLDS
KTKTSKKTPQ NFVISTEGPI KPTMHKTSIK TQIFPALGLV DPRPWQLPRF QKKMPQIAKK
QSTHRTQKPK KQSFPCICKN PGTQKSCVPL SVQPTEPRLN YLDLKYSDMF KEINSTANGP
GIYEMFGTPV YCHVRETERD ENTYYREICS APSGRRITNK CRSSHSERKS NIRTRLSQKK
THMKCPKTSF GIKQEHKVLI SKEKSSKAVH SNLHDIENGD GISEPDWQIK SSGNEFLSSK
DEIHPMNLAQ TPEQSMKQNE FPPVSDLSIV EEVSMEESTG DRDISNNQIL TTSLRDLQEL
EELHHQIPFI PSEDSWAVPS EKNSNKYVQQ EKQNTASLSK VNASRILTND LEFDSVSDHS
KTLTNFSFQA KQESASSQTY QYWVHYLDHD SLANKSITYQ MFGKTLSGTN SISQEIMDSV
NNEELTDELL GCLAAELLAL DEKDNNSCQK MANETDPENL NLVLRWRGST PKEMGRETTK
VKIQRHSSGL RIYDREEKFL ISNEKKIFSE NSLKSEEPIL WTKGEILGKG AYGTVYCGLT
SQGQLIAVKQ VALDTSNKLA AEKEYRKLQE EVDLLKALKH VNIVAYLGTC LQENTVSIFM
EFVPGGSISS IINRFGPLPE MVFCKYTKQI LQGVAYLHEN CVVHRDIKGN NVMLMPTGII
KLIDFGCARR LAWAGLNGTH SDMLKSMHGT PYWMAPEVIN ESGYGRKSDI WSIGCTVFEM
ATGKPPLASM DRMAAMFYIG AHRGLMPPLP DHFSENAADF VRMCLTRDQH ERPSALQLLK
HSFLERSH
