ALPK3_HUMAN
ID ALPK3_HUMAN Reviewed; 1907 AA.
AC Q96L96; Q9P2L6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Alpha-protein kinase 3 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q96QP1};
DE AltName: Full=Muscle alpha-protein kinase {ECO:0000303|PubMed:10021370};
GN Name=ALPK3 {ECO:0000312|HGNC:HGNC:17574};
GN Synonyms=KIAA1330 {ECO:0000303|PubMed:10718198},
GN MAK {ECO:0000303|PubMed:10021370};
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], AND VARIANT LEU-1299.
RX PubMed=10021370; DOI=10.1016/s0960-9822(99)80006-2;
RA Ryazanov A.G., Pavur K.S., Dorovkov M.V.;
RT "Alpha-kinases: a new class of protein kinases with a novel catalytic
RT domain.";
RL Curr. Biol. 9:R43-R45(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 963-1907, AND VARIANT LEU-1299.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP INVOLVEMENT IN CMH27, AND VARIANT CMH27 1264-TRP--ARG-1907 DEL.
RX PubMed=27106955; DOI=10.1093/eurheartj/ehw160;
RA Phelan D.G., Anderson D.J., Howden S.E., Wong R.C., Hickey P.F., Pope K.,
RA Wilson G.R., Pebay A., Davis A.M., Petrou S., Elefanty A.G., Stanley E.G.,
RA James P.A., Macciocca I., Bahlo M., Cheung M.M., Amor D.J., Elliott D.A.,
RA Lockhart P.J.;
RT "ALPK3-deficient cardiomyocytes generated from patient-derived induced
RT pluripotent stem cells and mutant human embryonic stem cells display
RT abnormal calcium handling and establish that ALPK3 deficiency underlies
RT familial cardiomyopathy.";
RL Eur. Heart J. 37:2586-2590(2016).
RN [5]
RP INVOLVEMENT IN CMH27, AND VARIANTS CMH27 1261-ARG--ARG-1907 DEL AND
RP 1765-TRP--ARG-1907 DEL.
RX PubMed=26846950; DOI=10.1016/j.jacc.2015.10.093;
RA Almomani R., Verhagen J.M., Herkert J.C., Brosens E.,
RA van Spaendonck-Zwarts K.Y., Asimaki A., van der Zwaag P.A.,
RA Frohn-Mulder I.M., Bertoli-Avella A.M., Boven L.G., van Slegtenhorst M.A.,
RA van der Smagt J.J., van Ijcken W.F., Timmer B., van Stuijvenberg M.,
RA Verdijk R.M., Saffitz J.E., du Plessis F.A., Michels M., Hofstra R.M.,
RA Sinke R.J., van Tintelen J.P., Wessels M.W., Jongbloed J.D.,
RA van de Laar I.M.;
RT "Biallelic truncating mutations in ALPK3 cause severe pediatric
RT cardiomyopathy.";
RL J. Am. Coll. Cardiol. 67:515-525(2016).
RN [6]
RP INVOLVEMENT IN CMH27.
RX PubMed=28630369; DOI=10.1101/mcs.a001859;
RA Caglayan A.O., Sezer R.G., Kaymakcalan H., Ulgen E., Yavuz T.,
RA Baranoski J.F., Bozaykut A., Harmanci A.S., Yalcin Y., Youngblood M.W.,
RA Yasuno K., Bilguevar K., Gunel M.;
RT "ALPK3 gene mutation in a patient with congenital cardiomyopathy and
RT dysmorphic features.";
RL Cold Spring Harb. Mol. Case Stud. 3:0-0(2017).
RN [7]
RP VARIANTS [LARGE SCALE ANALYSIS] HIS-336; ILE-338; SER-414; GLU-433;
RP GLU-579; ARG-602; ASP-663; MET-761; LEU-836; ASP-929; LEU-1299; GLU-1364;
RP TRP-1412; ASP-1557 AND PRO-1622.
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).
RN [8]
RP INVOLVEMENT IN CMH27.
RX PubMed=30046096; DOI=10.1038/s10038-018-0492-1;
RA Jaouadi H., Kraoua L., Chaker L., Atkinson A., Delague V., Levy N.,
RA Benkhalifa R., Mrad R., Abdelhak S., Zaffran S.;
RT "Novel ALPK3 mutation in a Tunisian patient with pediatric cardiomyopathy
RT and facio-thoraco-skeletal features.";
RL J. Hum. Genet. 63:1077-1082(2018).
CC -!- FUNCTION: Involved in cardiomyocyte differentiation.
CC {ECO:0000305|PubMed:26846950, ECO:0000305|PubMed:27106955,
CC ECO:0000305|PubMed:28630369, ECO:0000305|PubMed:30046096}.
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:0000250|UniProtKB:Q96QP1};
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:0000250|UniProtKB:Q96QP1};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q924C5}.
CC -!- DISEASE: Cardiomyopathy, familial hypertrophic 27 (CMH27) [MIM:618052]:
CC A form of hypertrophic cardiomyopathy, a heart disorder characterized
CC by ventricular hypertrophy, which is usually asymmetric and often
CC involves the interventricular septum. The symptoms include dyspnea,
CC syncope, collapse, palpitations, and chest pain. They can be readily
CC provoked by exercise. The disorder has inter- and intrafamilial
CC variability ranging from benign to malignant forms with high risk of
CC cardiac failure and sudden cardiac death. CMH27 is a severe, early-
CC onset form with features of hypertrophic and dilated cardiomyopathy.
CC {ECO:0000269|PubMed:26846950, ECO:0000269|PubMed:27106955,
CC ECO:0000269|PubMed:28630369, ECO:0000269|PubMed:30046096}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. ALPK subfamily. {ECO:0000305}.
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DR EMBL; AY044449; AAK95951.1; -; mRNA.
DR EMBL; AB037751; BAA92568.1; -; mRNA.
DR EMBL; AC012291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_065829.3; NM_020778.4.
DR AlphaFoldDB; Q96L96; -.
DR SMR; Q96L96; -.
DR BioGRID; 121597; 6.
DR IntAct; Q96L96; 8.
DR STRING; 9606.ENSP00000258888; -.
DR iPTMnet; Q96L96; -.
DR PhosphoSitePlus; Q96L96; -.
DR BioMuta; ALPK3; -.
DR DMDM; 296434393; -.
DR EPD; Q96L96; -.
DR jPOST; Q96L96; -.
DR MassIVE; Q96L96; -.
DR PaxDb; Q96L96; -.
DR PeptideAtlas; Q96L96; -.
DR PRIDE; Q96L96; -.
DR ProteomicsDB; 77171; -.
DR Antibodypedia; 15507; 57 antibodies from 20 providers.
DR DNASU; 57538; -.
DR Ensembl; ENST00000258888.6; ENSP00000258888.6; ENSG00000136383.7.
DR GeneID; 57538; -.
DR KEGG; hsa:57538; -.
DR UCSC; uc002ble.3; human.
DR CTD; 57538; -.
DR DisGeNET; 57538; -.
DR GeneCards; ALPK3; -.
DR HGNC; HGNC:17574; ALPK3.
DR HPA; ENSG00000136383; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR MalaCards; ALPK3; -.
DR MIM; 617608; gene.
DR MIM; 618052; phenotype.
DR neXtProt; NX_Q96L96; -.
DR PharmGKB; PA134921552; -.
DR VEuPathDB; HostDB:ENSG00000136383; -.
DR eggNOG; ENOG502QPP5; Eukaryota.
DR HOGENOM; CLU_003270_1_0_1; -.
DR InParanoid; Q96L96; -.
DR OrthoDB; 32441at2759; -.
DR PhylomeDB; Q96L96; -.
DR TreeFam; TF332629; -.
DR PathwayCommons; Q96L96; -.
DR SignaLink; Q96L96; -.
DR BioGRID-ORCS; 57538; 13 hits in 1077 CRISPR screens.
DR ChiTaRS; ALPK3; human.
DR GenomeRNAi; 57538; -.
DR Pharos; Q96L96; Tdark.
DR PRO; PR:Q96L96; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q96L96; protein.
DR Bgee; ENSG00000136383; Expressed in gastrocnemius and 131 other tissues.
DR Genevisible; Q96L96; HS.
DR GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0055013; P:cardiac muscle cell development; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; ISS:HGNC-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR004166; MHCK_EF2_kinase.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00811; Alpha_kinase; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Cardiomyopathy; Developmental protein; Disease variant; Disulfide bond;
KW Immunoglobulin domain; Kinase; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1907
FT /note="Alpha-protein kinase 3"
FT /id="PRO_0000260031"
FT DOMAIN 279..370
FT /note="Ig-like 1"
FT DOMAIN 1476..1564
FT /note="Ig-like 2"
FT DOMAIN 1592..1827
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00501"
FT REGION 65..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1375..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1830..1907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1846..1900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q924C5"
FT MOD_RES 1424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q924C5"
FT DISULFID 1498..1548
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 336
FT /note="R -> H (in dbSNP:rs34407151)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041524"
FT VARIANT 338
FT /note="T -> I (in dbSNP:rs56015306)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041525"
FT VARIANT 414
FT /note="T -> S (in dbSNP:rs3803403)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_028989"
FT VARIANT 433
FT /note="Q -> E (in a lung large cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041526"
FT VARIANT 579
FT /note="G -> E (in dbSNP:rs3803405)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_028990"
FT VARIANT 602
FT /note="Q -> R (in dbSNP:rs55702300)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041527"
FT VARIANT 663
FT /note="G -> D (in dbSNP:rs34409363)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041528"
FT VARIANT 761
FT /note="T -> M (in dbSNP:rs16974569)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_028991"
FT VARIANT 836
FT /note="R -> L (in dbSNP:rs34906636)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041529"
FT VARIANT 929
FT /note="E -> D (in dbSNP:rs56191073)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041530"
FT VARIANT 1013
FT /note="E -> K (in dbSNP:rs35633849)"
FT /id="VAR_057743"
FT VARIANT 1137
FT /note="A -> G (in dbSNP:rs34173528)"
FT /id="VAR_057744"
FT VARIANT 1261..1907
FT /note="Missing (in CMH27)"
FT /evidence="ECO:0000269|PubMed:26846950"
FT /id="VAR_079142"
FT VARIANT 1264..1907
FT /note="Missing (in CMH27)"
FT /evidence="ECO:0000269|PubMed:27106955"
FT /id="VAR_079143"
FT VARIANT 1299
FT /note="P -> L (in dbSNP:rs306197)"
FT /evidence="ECO:0000269|PubMed:10021370,
FT ECO:0000269|PubMed:10718198, ECO:0000269|PubMed:17344846"
FT /id="VAR_028992"
FT VARIANT 1364
FT /note="G -> E (in a metastatic melanoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041531"
FT VARIANT 1412
FT /note="R -> W (in dbSNP:rs55752937)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041532"
FT VARIANT 1557
FT /note="A -> D (in dbSNP:rs34775428)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041533"
FT VARIANT 1622
FT /note="L -> P (in dbSNP:rs187316)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_028993"
FT VARIANT 1765..1907
FT /note="Missing (in CMH27)"
FT /evidence="ECO:0000269|PubMed:26846950"
FT /id="VAR_079144"
FT VARIANT 1873
FT /note="A -> V (in dbSNP:rs36002219)"
FT /id="VAR_057745"
FT CONFLICT 210
FT /note="S -> T (in Ref. 1; AAK95951)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1907 AA; 201272 MW; 3896A1EC187BF5C7 CRC64;
MEVAWLVYVL GQQPLARQGE GQSRLVPGRG LVLWLPGLPR SSPSWPAVDL APLAPARPRG
PLICHTGHEQ AGREPGPGSS TKGPVLHDQD TRCAFLPRPP GPLQTRRYCR HQGRQGSGLG
AGPGAGTWAP APPGVSKPRC PGRARPGEGQ QQVTTARPPA INRGARQPRA GAAAAGRGPG
AGAWRTGEAA ASAGPAVGEG GAMGSRRAPS RGWGAGGRSG AGGDGEDDGP VWIPSPASRS
YLLSVRPETS LSSNRLSHPS SGRSTFCSII AQLTEETQPL FETTLKSRSV SEDSDVRFTC
IVTGYPEPEV TWYKDDTELD RYCGLPKYEI THQGNRHTLQ LYRCREEDAA IYQASAQNSK
GIVSCSGVLE VGTMTEYKIH QRWFAKLKRK AAAKLREIEQ SWKHEKAVPG EVDTLRKLSP
DRFQRKRRLS GAQAPGPSVP TREPEGGTLA AWQEGETETA QHSGLGLINS FASGEVTTNG
EAAPENGEDG EHGLLTYICD AMELGPQRAL KEESGAKKKK KDEESKQGLR KPELEKAAQS
RRSSENCIPS SDEPDSCGTQ GPVGVEQVQT QPRGRAARGP GSSGTDSTRK PASAVGTPDK
AQKAPGPGPG QEVYFSLKDM YLENTQAVRP LGEEGPQTLS VRAPGESPKG KAPLRARSEG
VPGAPGQPTH SLTPQPTRPF NRKRFAPPKP KGEATTDSKP ISSLSQAPEC GAQSLGKAPP
QASVQVPTPP ARRRHGTRDS TLQGQAGHRT PGEVLECQTT TAPTMSASSS SDVASIGVST
SGSQGIIEPM DMETQEDGRT SANQRTGSKK NVQADGKIQV DGRTRGDGTQ TAQRTRADRK
TQVDAGTQES KRPQSDRSAQ KGMMTQGRAE TQLETTQAGE KIQEDRKAQA DKGTQEDRRM
QGEKGMQGEK GTQSEGSAPT AMEGQSEQEV ATSLGPPSRT PKLPPTAGPR APLNIECFVQ
TPEGSCFPKK PGCLPRSEEA VVTASRNHEQ TVLGPLSGNL MLPAQPPHEG SVEQVGGERC
RGPQSSGPVE AKQEDSPFQC PKEERPGGVP CMDQGGCPLA GLSQEVPTMP SLPGTGLTAS
PKAGPCSTPT SQHGSTATFL PSEDQVLMSS APTLHLGLGT PTQSHPPETM ATSSEGACAQ
VPDVEGRTPG PRSCDPGLID SLKNYLLLLL KLSSTETSGA GGESQVGAAT GGLVPSATLT
PTVEVAGLSP RTSRRILERV ENNHLVQSAQ TLLLSPCTSR RLTGLLDREV QAGRQALAAA
RGSWGPGPSS LTVPAIVVDE EDPGLASEGA SEGEGEVSPE GPGLLGASQE SSMAGRLGEA
GGQAAPGQGP SAESIAQEPS QEEKFPGEAL TGLPAATPEE LALGARRKRF LPKVRAAGDG
EATTPEERES PTVSPRGPRK SLVPGSPGTP GRERRSPTQG RKASMLEVPR AEEELAAGDL
GPSPKAGGLD TEVALDEGKQ ETLAKPRKAK DLLKAPQVIR KIRVEQFPDA SGSLKLWCQF
FNILSDSVLT WAKDQRPVGE VGRSAGDEGP AALAIVQASP VDCGVYRCTI HNEHGSASTD
FCLSPEVLSG FISREEGEVG EEIEMTPMVF AKGLADSGCW GDKLFGRLVS EELRGGGYGC
GLRKASQAKV IYGLEPIFES GRTCIIKVSS LLVFGPSSET SLVGRNYDVT IQGCKIQNMS
REYCKIFAAE ARAAPGFGEV PEIIPLYLIY RPANNIPYAT LEEDLGKPLE SYCSREWGCA
EAPTASGSSE AMQKCQTFQH WLYQWTNGSF LVTDLAGVDW KMTDVQIATK LRGYQGLKES
CFPALLDRFA SSHQCNAYCE LLGLTPLKGP EAAHPQAKAK GSKSPSAGRK GSQLSPQPQK
KGLPSPQGTR KSAPSSKATP QASEPVTTQL LGQPPTQEEG SKAQGMR
