PKN3_HUMAN
ID PKN3_HUMAN Reviewed; 889 AA.
AC Q6P5Z2; Q9UM03;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Serine/threonine-protein kinase N3;
DE EC=2.7.11.13;
DE AltName: Full=Protein kinase PKN-beta;
DE AltName: Full=Protein-kinase C-related kinase 3;
GN Name=PKN3; Synonyms=PKNBETA;
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], AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-588,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=10441506; DOI=10.1006/bbrc.1999.1116;
RA Oishi K., Mukai H., Shibata H., Takahashi M., Ono Y.;
RT "Identification and characterization of PKNbeta, a novel isoform of protein
RT kinase PKN: expression and arachidonic acid dependency are different from
RT those of PKNalpha.";
RL Biochem. Biophys. Res. Commun. 261:808-814(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 FUNCTION IN MALIGNANT CELL GROWTH, PHOSPHORYLATION AT THR-718, AND
RP MUTAGENESIS OF LYS-588 AND THR-718.
RX PubMed=15282551; DOI=10.1038/sj.emboj.7600345;
RA Leenders F., Moepert K., Schmiedeknecht A., Santel A., Czauderna F.,
RA Aleku M., Penschuck S., Dames S., Sternberger M., Roehl T., Wellmann A.,
RA Arnold W., Giese K., Kaufmann J., Klippel A.;
RT "PKN3 is required for malignant prostate cell growth downstream of
RT activated PI 3-kinase.";
RL EMBO J. 23:3303-3313(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544; THR-722 AND THR-860, AND
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-548, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND THR-860, AND
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND SER-544, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-180.
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 -!- FUNCTION: Contributes to invasiveness in malignant prostate cancer.
CC {ECO:0000269|PubMed:15282551}.
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=2.7.11.13;
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=2.7.11.13;
CC -!- ACTIVITY REGULATION: Two specific sites, Thr-718 (activation loop of
CC the kinase domain) and Thr-860 (turn motif), need to be phosphorylated
CC for its full activation. {ECO:0000250}.
CC -!- INTERACTION:
CC Q6P5Z2; A1A4S6: ARHGAP10; NbExp=5; IntAct=EBI-1384335, EBI-1390944;
CC Q6P5Z2; Q9UNA1: ARHGAP26; NbExp=5; IntAct=EBI-1384335, EBI-1390913;
CC Q6P5Z2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1384335, EBI-618309;
CC Q6P5Z2; Q15323: KRT31; NbExp=3; IntAct=EBI-1384335, EBI-948001;
CC Q6P5Z2; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-1384335, EBI-11522433;
CC Q6P5Z2; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-1384335, EBI-302345;
CC Q6P5Z2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-1384335, EBI-1105213;
CC Q6P5Z2; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-1384335, EBI-2799833;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10441506}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:10441506}. Note=Nuclear and
CC perinuclear Golgi region.
CC -!- TISSUE SPECIFICITY: Expressed in prostate tumors and various cancer
CC cell lines. Not expressed in adult tissues.
CC {ECO:0000269|PubMed:10441506}.
CC -!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:15282551}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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DR EMBL; AB019692; BAA85625.1; -; mRNA.
DR EMBL; AL441992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC062558; AAH62558.1; -; mRNA.
DR CCDS; CCDS6908.1; -.
DR PIR; JC7083; JC7083.
DR RefSeq; NP_037487.2; NM_013355.4.
DR AlphaFoldDB; Q6P5Z2; -.
DR SMR; Q6P5Z2; -.
DR BioGRID; 118978; 135.
DR IntAct; Q6P5Z2; 110.
DR MINT; Q6P5Z2; -.
DR STRING; 9606.ENSP00000291906; -.
DR BindingDB; Q6P5Z2; -.
DR ChEMBL; CHEMBL3627581; -.
DR iPTMnet; Q6P5Z2; -.
DR PhosphoSitePlus; Q6P5Z2; -.
DR BioMuta; PKN3; -.
DR DMDM; 74749130; -.
DR EPD; Q6P5Z2; -.
DR jPOST; Q6P5Z2; -.
DR MassIVE; Q6P5Z2; -.
DR MaxQB; Q6P5Z2; -.
DR PaxDb; Q6P5Z2; -.
DR PeptideAtlas; Q6P5Z2; -.
DR PRIDE; Q6P5Z2; -.
DR ProteomicsDB; 67014; -.
DR Antibodypedia; 31249; 192 antibodies from 28 providers.
DR DNASU; 29941; -.
DR Ensembl; ENST00000291906.5; ENSP00000291906.4; ENSG00000160447.7.
DR GeneID; 29941; -.
DR KEGG; hsa:29941; -.
DR MANE-Select; ENST00000291906.5; ENSP00000291906.4; NM_013355.5; NP_037487.2.
DR UCSC; uc004bvw.4; human.
DR CTD; 29941; -.
DR DisGeNET; 29941; -.
DR GeneCards; PKN3; -.
DR HGNC; HGNC:17999; PKN3.
DR HPA; ENSG00000160447; Low tissue specificity.
DR MIM; 610714; gene.
DR neXtProt; NX_Q6P5Z2; -.
DR OpenTargets; ENSG00000160447; -.
DR PharmGKB; PA134919098; -.
DR VEuPathDB; HostDB:ENSG00000160447; -.
DR eggNOG; KOG0694; Eukaryota.
DR GeneTree; ENSGT00940000161818; -.
DR HOGENOM; CLU_000288_132_1_1; -.
DR InParanoid; Q6P5Z2; -.
DR OMA; NMNVAAW; -.
DR OrthoDB; 520651at2759; -.
DR PhylomeDB; Q6P5Z2; -.
DR TreeFam; TF102005; -.
DR PathwayCommons; Q6P5Z2; -.
DR Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR SignaLink; Q6P5Z2; -.
DR SIGNOR; Q6P5Z2; -.
DR BioGRID-ORCS; 29941; 20 hits in 1112 CRISPR screens.
DR ChiTaRS; PKN3; human.
DR GeneWiki; PKN3_(gene); -.
DR GenomeRNAi; 29941; -.
DR Pharos; Q6P5Z2; Tchem.
DR PRO; PR:Q6P5Z2; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q6P5Z2; protein.
DR Bgee; ENSG00000160447; Expressed in apex of heart and 109 other tissues.
DR ExpressionAtlas; Q6P5Z2; baseline and differential.
DR Genevisible; Q6P5Z2; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
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:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
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:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0010631; P:epithelial cell migration; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd11622; HR1_PKN_1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR037313; PKN_HR1_1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF02185; HR1; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00742; Hr1; 3.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46585; SSF46585; 3.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51860; REM_1; 3.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..889
FT /note="Serine/threonine-protein kinase N3"
FT /id="PRO_0000055725"
FT DOMAIN 5..80
FT /note="REM-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 93..163
FT /note="REM-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 165..245
FT /note="REM-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 559..818
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 819..889
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 468..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..518
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 684
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 565..573
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 588
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 718
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15282551"
FT MOD_RES 722
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 860
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT VARIANT 180
FT /note="A -> E (in dbSNP:rs56251280)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042346"
FT VARIANT 404
FT /note="V -> L (in dbSNP:rs12932)"
FT /id="VAR_050565"
FT MUTAGEN 588
FT /note="K->E: Abolishes autophosphorylation and catalytic
FT activity."
FT /evidence="ECO:0000269|PubMed:10441506,
FT ECO:0000269|PubMed:15282551"
FT MUTAGEN 588
FT /note="K->R: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:10441506,
FT ECO:0000269|PubMed:15282551"
FT MUTAGEN 718
FT /note="T->A: Abolishes phosphorylation."
FT /evidence="ECO:0000269|PubMed:15282551"
FT CONFLICT 444
FT /note="A -> R (in Ref. 1; BAA85625)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="A -> V (in Ref. 1; BAA85625)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="C -> R (in Ref. 1; BAA85625)"
FT /evidence="ECO:0000305"
FT CONFLICT 738
FT /note="R -> Q (in Ref. 1; BAA85625)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="G -> A (in Ref. 1; BAA85625)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 889 AA; 99421 MW; F3891DA1420DF54E CRC64;
MEEGAPRQPG PSQWPPEDEK EVIRRAIQKE LKIKEGVENL RRVATDRRHL GHVQQLLRSS
NRRLEQLHGE LRELHARILL PGPGPGPAEP VASGPRPWAE QLRARHLEAL RRQLHVELKV
KQGAENMTHT CASGTPKERK LLAAAQQMLR DSQLKVALLR MKISSLEASG SPEPGPELLA
EELQHRLHVE AAVAEGAKNV VKLLSSRRTQ DRKALAEAQA QLQESSQKLD LLRLALEQLL
EQLPPAHPLR SRVTRELRAA VPGYPQPSGT PVKPTALTGT LQVRLLGCEQ LLTAVPGRSP
AAALASSPSE GWLRTKAKHQ RGRGELASEV LAVLKVDNRV VGQTGWGQVA EQSWDQTFVI
PLERARELEI GVHWRDWRQL CGVAFLRLED FLDNACHQLS LSLVPQGLLF AQVTFCDPVI
ERRPRLQRQE RIFSKRRGQD FLRASQMNLG MAAWGRLVMN LLPPCSSPST ISPPKGCPRT
PTTLREASDP ATPSNFLPKK TPLGEEMTPP PKPPRLYLPQ EPTSEETPRT KRPHMEPRTR
RGPSPPASPT RKPPRLQDFR CLAVLGRGHF GKVLLVQFKG TGKYYAIKAL KKQEVLSRDE
IESLYCEKRI LEAVGCTGHP FLLSLLACFQ TSSHACFVTE FVPGGDLMMQ IHEDVFPEPQ
ARFYVACVVL GLQFLHEKKI IYRDLKLDNL LLDAQGFLKI ADFGLCKEGI GFGDRTSTFC
GTPEFLAPEV LTQEAYTRAV DWWGLGVLLY EMLVGECPFP GDTEEEVFDC IVNMDAPYPG
FLSVQGLEFI QKLLQKCPEK RLGAGEQDAE EIKVQPFFRT TNWQALLART IQPPFVPTLC
GPADLRYFEG EFTGLPPALT PPAPHSLLTA RQQAAFRDFD FVSERFLEP
