MAST3_HUMAN
ID MAST3_HUMAN Reviewed; 1309 AA.
AC O60307; Q7LDZ8; Q9UPI0;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Microtubule-associated serine/threonine-protein kinase 3;
DE EC=2.7.11.1;
GN Name=MAST3; Synonyms=KIAA0561;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1309.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [3]
RP INTERACTION WITH PTEN.
RX PubMed=15951562; DOI=10.1074/jbc.m504761200;
RA Valiente M., Andres-Pons A., Gomar B., Torres J., Gil A., Tapparel C.,
RA Antonarakis S.E., Pulido R.;
RT "Binding of PTEN to specific PDZ domains contributes to PTEN protein
RT stability and phosphorylation by microtubule-associated serine/threonine
RT kinases.";
RL J. Biol. Chem. 280:28936-28943(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1223, AND IDENTIFICATION BY
RP 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-680 AND SER-1223,
RP AND 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774; SER-782; SER-792 AND
RP SER-793, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-85; SER-146; SER-754;
RP SER-782 AND SER-793, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP STRUCTURE BY NMR OF 181-281.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of putative domain of human KIAA0561 protein.";
RL Submitted (MAR-2005) to the PDB data bank.
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] SER-883.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with PTEN. {ECO:0000269|PubMed:15951562}.
CC -!- INTERACTION:
CC O60307; P60484: PTEN; NbExp=3; IntAct=EBI-311420, EBI-696162;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1, Met-171 or Met-172 is the
CC initiator. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC62830.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC005793; AAC62830.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC007192; AAD22670.1; -; Genomic_DNA.
DR EMBL; AC093054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB011133; BAA25487.1; -; mRNA.
DR CCDS; CCDS46014.1; -.
DR RefSeq; NP_055831.1; NM_015016.1.
DR PDB; 1V9V; NMR; -; A=181-281.
DR PDB; 3KHF; X-ray; 1.20 A; A/B=948-1040.
DR PDBsum; 1V9V; -.
DR PDBsum; 3KHF; -.
DR AlphaFoldDB; O60307; -.
DR BMRB; O60307; -.
DR SMR; O60307; -.
DR BioGRID; 116670; 117.
DR IntAct; O60307; 43.
DR STRING; 9606.ENSP00000262811; -.
DR BindingDB; O60307; -.
DR ChEMBL; CHEMBL2417352; -.
DR GuidetoPHARMACOLOGY; 1512; -.
DR GlyGen; O60307; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60307; -.
DR PhosphoSitePlus; O60307; -.
DR BioMuta; MAST3; -.
DR EPD; O60307; -.
DR jPOST; O60307; -.
DR MassIVE; O60307; -.
DR MaxQB; O60307; -.
DR PaxDb; O60307; -.
DR PeptideAtlas; O60307; -.
DR PRIDE; O60307; -.
DR ProteomicsDB; 49334; -.
DR Antibodypedia; 27914; 178 antibodies from 32 providers.
DR DNASU; 23031; -.
DR Ensembl; ENST00000262811.10; ENSP00000262811.4; ENSG00000099308.11.
DR GeneID; 23031; -.
DR KEGG; hsa:23031; -.
DR UCSC; uc002nhz.5; human.
DR CTD; 23031; -.
DR DisGeNET; 23031; -.
DR GeneCards; MAST3; -.
DR HGNC; HGNC:19036; MAST3.
DR HPA; ENSG00000099308; Tissue enhanced (brain).
DR MIM; 612258; gene.
DR neXtProt; NX_O60307; -.
DR OpenTargets; ENSG00000099308; -.
DR PharmGKB; PA134877725; -.
DR VEuPathDB; HostDB:ENSG00000099308; -.
DR eggNOG; KOG0606; Eukaryota.
DR GeneTree; ENSGT00940000157166; -.
DR HOGENOM; CLU_000288_9_0_1; -.
DR InParanoid; O60307; -.
DR OMA; INLDTMP; -.
DR OrthoDB; 323328at2759; -.
DR PhylomeDB; O60307; -.
DR TreeFam; TF313149; -.
DR PathwayCommons; O60307; -.
DR SignaLink; O60307; -.
DR SIGNOR; O60307; -.
DR BioGRID-ORCS; 23031; 27 hits in 1106 CRISPR screens.
DR ChiTaRS; MAST3; human.
DR EvolutionaryTrace; O60307; -.
DR GenomeRNAi; 23031; -.
DR Pharos; O60307; Tchem.
DR PRO; PR:O60307; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O60307; protein.
DR Bgee; ENSG00000099308; Expressed in frontal pole and 175 other tissues.
DR ExpressionAtlas; O60307; baseline and differential.
DR Genevisible; O60307; HS.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR CDD; cd05609; STKc_MAST; 1.
DR Gene3D; 1.20.1480.20; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR015022; MA_Ser/Thr_Kinase_dom.
DR InterPro; IPR037711; MAST.
DR InterPro; IPR023142; MAST_pre-PK_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF08926; DUF1908; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF140482; SSF140482; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Magnesium; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1309
FT /note="Microtubule-associated serine/threonine-protein
FT kinase 3"
FT /id="PRO_0000086314"
FT DOMAIN 367..640
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 641..712
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 950..1038
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..825
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1068
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1213
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 490
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 373..381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 396
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U214"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U214"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 793
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195"
FT MOD_RES 1273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U214"
FT VARIANT 203
FT /note="R -> Q (in dbSNP:rs35945810)"
FT /id="VAR_051646"
FT VARIANT 861
FT /note="G -> S (in dbSNP:rs8108738)"
FT /id="VAR_051647"
FT VARIANT 883
FT /note="G -> S (in dbSNP:rs369960905)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040786"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:1V9V"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:1V9V"
FT HELIX 209..230
FT /evidence="ECO:0007829|PDB:1V9V"
FT HELIX 236..255
FT /evidence="ECO:0007829|PDB:1V9V"
FT HELIX 259..276
FT /evidence="ECO:0007829|PDB:1V9V"
FT STRAND 951..954
FT /evidence="ECO:0007829|PDB:3KHF"
FT STRAND 962..975
FT /evidence="ECO:0007829|PDB:3KHF"
FT STRAND 977..986
FT /evidence="ECO:0007829|PDB:3KHF"
FT HELIX 991..995
FT /evidence="ECO:0007829|PDB:3KHF"
FT STRAND 1002..1006
FT /evidence="ECO:0007829|PDB:3KHF"
FT HELIX 1016..1025
FT /evidence="ECO:0007829|PDB:3KHF"
FT STRAND 1028..1035
FT /evidence="ECO:0007829|PDB:3KHF"
SQ SEQUENCE 1309 AA; 143137 MW; 87E82F2D032ED122 CRC64;
MDESSLLRRR GLQKELSLPR RGRGCRSGNR KSLVVGTPSP TLSRPLSPLS VPTAGSSPLD
SPRNFSAASA LNFPFARRAD GRRWSLASLP SSGYGTNTPS STLSSSSSSR ERLHQLPFQP
TPDELHFLSK HFRSSENVLD EEGGRSPRLR PRSRSLSPGR ATGTFDNEIV MMNHVYRERF
PKATAQMEGR LQEFLTAYAP GARLALADGV LGFIHHQIVE LARDCLAKSG ENLVTSRYFL
EMQEKLERLL QDAHERSDSE EVSFIVQLVR KLLIIISRPA RLLECLEFDP EEFYHLLEAA
EGHAREGQGI KTDLPQYIIG QLGLAKDPLE EMVPLSHLEE EQPPAPESPE SRALVGQSRR
KPCESDFETI KLISNGAYGA VYLVRHRDTR QRFAIKKINK QNLILRNQIQ QVFVERDILT
FAENPFVVSM FCSFETRRHL CMVMEYVEGG DCATLLKNMG PLPVDMARLY FAETVLALEY
LHNYGIVHRD LKPDNLLITS LGHIKLTDFG LSKIGLMSMA TNLYEGHIEK DAREFIDKQV
CGTPEYIAPE VIFRQGYGKP VDWWAMGVVL YEFLVGCVPF FGDTPEELFG QVVSDEIMWP
EGDEALPADA QDLITRLLRQ SPLDRLGTGG THEVKQHPFF LALDWAGLLR HKAEFVPQLE
AEDDTSYFDT RSERYRHLGS EDDETNDEES STEIPQFSSC SHRFSKVYSS SEFLAVQPTP
TFAERSFSED REEGWERSEV DYGRRLSADI RLRSWTSSGS SCQSSSSQPE RGPSPSLLNT
ISLDTMPKFA FSSEDEGVGP GPAGPKRPVF ILGEPDPPPA ATPVMPKPSS LSADTAALSH
ARLRSNSIGA RHSTPRPLDA GRGRRLGGPR DPAPEKSRAS SSGGSGGGSG GRVPKSASVS
ALSLIITADD GSGGPLMSPL SPRSLSSNPS SRDSSPSRDP SPVCGSLRPP IVIHSSGKKY
GFSLRAIRVY MGDSDVYTVH HVVWSVEDGS PAQEAGLRAG DLITHINGES VLGLVHMDVV
ELLLKSGNKI SLRTTALENT SIKVGPARKN VAKGRMARRS KRSRRRETQD RRKSLFKKIS
KQTSVLHTSR SFSSGLHHSL SSSESLPGSP THSLSPSPTT PCRSPAPDVP ADTTASPPSA
SPSSSSPASP AAAGHTRPSS LHGLAAKLGP PRPKTGRRKS TSSIPPSPLA CPPISAPPPR
SPSPLPGHPP APARSPRLRR GQSADKLGTG ERLDGEAGRR TRGPEAELVV MRRLHLSERR
DSFKKQEAVQ EVSFDEPQEE ATGLPTSVPQ IAVEGEEAVP VALGPTGRD
