MAST1_MOUSE
ID MAST1_MOUSE Reviewed; 1570 AA.
AC Q9R1L5; Q7TQG9; Q80TN0;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Microtubule-associated serine/threonine-protein kinase 1;
DE EC=2.7.11.1;
DE AltName: Full=Syntrophin-associated serine/threonine-protein kinase;
GN Name=Mast1 {ECO:0000312|MGI:MGI:1861901};
GN Synonyms=Kiaa0973, Sast {ECO:0000312|MGI:MGI:1861901};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAD50548.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH SNTB2.
RC STRAIN=C57BL/10 {ECO:0000312|EMBL:AAD50548.1};
RX PubMed=10404183; DOI=10.1038/10165;
RA Lumeng C., Phelps S., Crawford G.E., Walden P.D., Barald K.,
RA Chamberlain J.S.;
RT "Interactions between beta 2-syntrophin and a family of microtubule-
RT associated serine/threonine kinases.";
RL Nat. Neurosci. 2:611-617(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH54524.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH54524.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH54524.1};
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 [3] {ECO:0000305, ECO:0000312|EMBL:BAC65693.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-1570.
RC TISSUE=Brain {ECO:0000312|EMBL:BAC65693.3};
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4] {ECO:0000305}
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-139; SER-167 AND
RP SER-895, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-279.
RX PubMed=30449657; DOI=10.1016/j.neuron.2018.10.044;
RA Tripathy R., Leca I., van Dijk T., Weiss J., van Bon B.W., Sergaki M.C.,
RA Gstrein T., Breuss M., Tian G., Bahi-Buisson N., Paciorkowski A.R.,
RA Pagnamenta A.T., Wenninger-Weinzierl A., Martinez-Reza M.F., Landler L.,
RA Lise S., Taylor J.C., Terrone G., Vitiello G., Del Giudice E.,
RA Brunetti-Pierri N., D'Amico A., Reymond A., Voisin N., Bernstein J.A.,
RA Farrelly E., Kini U., Leonard T.A., Valence S., Burglen L., Armstrong L.,
RA Hiatt S.M., Cooper G.M., Aldinger K.A., Dobyns W.B., Mirzaa G.,
RA Pierson T.M., Baas F., Chelly J., Cowan N.J., Keays D.A.;
RT "Mutations in MAST1 cause mega-corpus-callosum syndrome with cerebellar
RT hypoplasia and cortical malformations.";
RL Neuron 100:1354-1368(2018).
CC -!- FUNCTION: Microtubule-associated protein essential for correct brain
CC development (PubMed:30449657). Appears to link the dystrophin/utrophin
CC network with microtubule filaments via the syntrophins. Phosphorylation
CC of DMD or UTRN may modulate their affinities for associated proteins.
CC {ECO:0000269|PubMed:10404183, ECO:0000269|PubMed:30449657,
CC ECO:0000303|PubMed:10404183}.
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:Q9BXM7};
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:Q9BXM7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9BXM7};
CC -!- SUBUNIT: Interacts with the microtubules (PubMed:30449657). Part of a
CC low affinity complex that associates with, but is distinct from, the
CC postsynaptic density. Interacts with SNTB2.
CC {ECO:0000269|PubMed:10404183, ECO:0000269|PubMed:30449657}.
CC -!- INTERACTION:
CC Q9R1L5; P60484: PTEN; Xeno; NbExp=3; IntAct=EBI-491771, EBI-696162;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10404183};
CC Peripheral membrane protein {ECO:0000269|PubMed:10404183}; Cytoplasmic
CC side {ECO:0000269|PubMed:10404183}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10404183}. Cell projection, axon
CC {ECO:0000269|PubMed:30449657}. Cell projection, dendrite
CC {ECO:0000269|PubMed:30449657}. Note=Also localized in the soma of
CC neurons (PubMed:30449657). Observed as punctate clusters in the
CC processes of interneurons and along the cell body periphery.
CC Colocalizes with syntrophins at the cell membrane.
CC {ECO:0000269|PubMed:30449657}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain (PubMed:30449657). Expressed
CC in the developing cortical plate, the intermediate zone and corpus
CC callosal fibers that cross the midline (PubMed:30449657). Detected at
CC low levels in the testis, liver and spleen (PubMed:30449657). Expressed
CC in proximity to neuronal nuclei throughout the cortex and cerebellum,
CC and in the vascular endothelium. Also detected in ependymal cells, the
CC choroid plexus, and in developing spermatid acrosomes.
CC {ECO:0000269|PubMed:10404183, ECO:0000269|PubMed:30449657}.
CC -!- DEVELOPMENTAL STAGE: Expression in the brain begins at 12.5 dpc, peaks
CC at 16.5 dpc, and decreases postnatally. {ECO:0000269|PubMed:30449657}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice do not show morphological defects.
CC {ECO:0000269|PubMed:30449657}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD50548.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC65693.3; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence={ECO:0000305};
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DR EMBL; AF077818; AAD50548.1; ALT_FRAME; mRNA.
DR EMBL; BC054524; AAH54524.1; -; mRNA.
DR EMBL; AK122411; BAC65693.3; ALT_SEQ; Transcribed_RNA.
DR CCDS; CCDS40415.1; -.
DR RefSeq; NP_064329.2; NM_019945.2.
DR AlphaFoldDB; Q9R1L5; -.
DR SMR; Q9R1L5; -.
DR BioGRID; 208038; 7.
DR IntAct; Q9R1L5; 3.
DR MINT; Q9R1L5; -.
DR STRING; 10090.ENSMUSP00000105363; -.
DR iPTMnet; Q9R1L5; -.
DR PhosphoSitePlus; Q9R1L5; -.
DR SwissPalm; Q9R1L5; -.
DR MaxQB; Q9R1L5; -.
DR PaxDb; Q9R1L5; -.
DR PeptideAtlas; Q9R1L5; -.
DR PRIDE; Q9R1L5; -.
DR ProteomicsDB; 292091; -.
DR Antibodypedia; 26218; 102 antibodies from 24 providers.
DR DNASU; 56527; -.
DR Ensembl; ENSMUST00000109741; ENSMUSP00000105363; ENSMUSG00000053693.
DR GeneID; 56527; -.
DR KEGG; mmu:56527; -.
DR UCSC; uc009mof.1; mouse.
DR CTD; 22983; -.
DR MGI; MGI:1861901; Mast1.
DR VEuPathDB; HostDB:ENSMUSG00000053693; -.
DR eggNOG; KOG0605; Eukaryota.
DR eggNOG; KOG0606; Eukaryota.
DR GeneTree; ENSGT00940000157700; -.
DR HOGENOM; CLU_000288_9_0_1; -.
DR InParanoid; Q9R1L5; -.
DR OMA; GMREKSW; -.
DR OrthoDB; 323328at2759; -.
DR PhylomeDB; Q9R1L5; -.
DR TreeFam; TF313149; -.
DR BRENDA; 2.7.11.1; 3474.
DR BioGRID-ORCS; 56527; 6 hits in 76 CRISPR screens.
DR ChiTaRS; Mast1; mouse.
DR PRO; PR:Q9R1L5; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9R1L5; protein.
DR Bgee; ENSMUSG00000053693; Expressed in motor neuron and 159 other tissues.
DR ExpressionAtlas; Q9R1L5; baseline and differential.
DR Genevisible; Q9R1L5; MM.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
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; IPR028777; MAST1.
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 PANTHER; PTHR24356:SF150; PTHR24356:SF150; 1.
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 ATP-binding; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1570
FT /note="Microtubule-associated serine/threonine-protein
FT kinase 1"
FT /id="PRO_0000086310"
FT DOMAIN 375..648
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 650..721
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 968..1056
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 23..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1096
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 498
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM7,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 381..389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM7,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM7,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810W7"
FT MOD_RES 351
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q810W7"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810W7"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 954
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810W7"
FT MOD_RES 1414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810W7"
FT MUTAGEN 279
FT /note="Missing: Mutant heterozygous mice have a thicker
FT corpus callosum, hypoplastic cortex and cerebellum,
FT increased neuronal apoptosis, and decreased protein
FT levels."
FT /evidence="ECO:0000269|PubMed:30449657"
FT CONFLICT 158
FT /note="R -> P (in Ref. 1; AAD50548)"
FT /evidence="ECO:0000305"
FT CONFLICT 197..198
FT /note="LR -> P (in Ref. 1; AAD50548)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="S -> T (in Ref. 1; AAD50548)"
FT /evidence="ECO:0000305"
FT CONFLICT 672
FT /note="D -> E (in Ref. 1; AAD50548)"
FT /evidence="ECO:0000305"
FT CONFLICT 1190
FT /note="H -> L (in Ref. 1; AAD50548)"
FT /evidence="ECO:0000305"
FT CONFLICT 1219..1250
FT /note="SPPPLPGHTVGSSHTTQSFPAKLHSSPPVVRP -> ARRRCQATRWAAHIHA
FT ELPCQTTYIATCVRR (in Ref. 1; AAD50548)"
FT /evidence="ECO:0000305"
FT CONFLICT 1454
FT /note="L -> V (in Ref. 1; AAD50548)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1570 AA; 170997 MW; A8F9C868CF241486 CRC64;
MSDSLWTALS NFSMPSFPGG SMFRRTKSCR TSNRKSLILT STSPTLPRPH SPLPGHLGSS
PLDSPRNFSP NTPAHFSFAS SRRADGRRWS LASLPSSGYG TNTPSSTVSS SCSSQERLHQ
LPYQPTVDEL HFLSKHFGST ESITDEDGGR RSPAVRPRSR SLSPGRSPSS YDNEIVMMNH
VYKERFPKAT AQMEEKLRDF ARAYEPDSVL PLADGVLSFI HHQIIELARD CLTKSRDGLI
TTVYFYELQE NLEKLLQDAY ERSESLEVAF VTQLVKKLLI IISRPARLLE CLEFNPEEFY
HLLEAAEGHA KEGHLVKTDI PRYIIRQLGL TRDPFPDVVR LEEQDSGGSN TPEQDDTSEG
RSSTSKAKKP PGESDFDTIK LISNGAYGAV YLVRHRDTRQ RFAMKKINKQ NLILRNQIQQ
AFVERDILTF AENPFVVGMF CSFETRRHLC MVMEYVEGGD CATLLKNIGA LPVEMARMYF
AETVLALEYL HNYGIVHRDL KPDNLLITSM GHIKLTDFGL SKMGLMSLTT NLYEGHIEKD
AREFLDKQVC GTPEYIAPEV ILRQGYGKPV DWWAMGIILY EFLVGCVPFF GDTPEELFGQ
VISDDILWPE GDEALPTDAQ LLISSLLQTN PLVRLGAGGA FEVKQHSFFR DLDWTGLLRQ
KAEFIPHLES EDDTSYFDTR SDRYHHVNSY DEDDTTEEEP VEIRQFSSCS PRFSKVYSSM
EQLSQHEPKT PVSASGASKR DPSAKGPEEK VAGKREGLGG LTLREKTWRG GSPEIKRFSA
SEASFLEGEA SPPLGARRRF SALLEPSRFT APQEDEDEAR LRRPPRPSSD PPSSLDTRVP
KEAVQGEGTS TPGEPEATER SHPGDLGPPS KDGDPSGPRA TNDLVLRRAR HQQLSGDLAV
EKRPSRTGGK VIKSASATAL SVMIPAVDPH GGSPLASPMS PRSLSSNPSS RDSSPSRDYS
PAVSGLRSPI TIQRSGKKYG FTLRAIRVYM GDSDVYSVHH IVWHVEEGGP AQEAGLCAGD
LITHVNGEPV HGMVHPEVVE LILKSGNKVA VTTTPFENTS IRIGPARRSS YKAKMARRNK
RPSAKDGQES KKRSSLFRKI TKQSNLLHTS RSLSSLNRSL SSSDSLPGSP THGLPARSPT
HSYRSTPDSA YLGASSQSSS PASSTPNSPA SSASHHIRPS TLHGLSPKLH RQYRSARCKS
AGNIPLSPLA HTPSPTQASP PPLPGHTVGS SHTTQSFPAK LHSSPPVVRP RPKSAEPPRS
PLLKRVQSAE KLGASLGADK KGALRKHSLE VGHPDFRKDF HGELALHSLA ESDGETPPIE
GPGATRQVAV RRLGRQESPL SLGADPLLPD GVQRPMASSK EDSAGGTEAC TPPRATTPGS
RTLERDSGCT RHQSVQTEDG PGGVARALAK AALSPVQEHE TGRRSSSGEA GTPPVPIVVE
PARPGVKTQA PQPLGTDSKG LKEPVAQMPL MPDAPRGRER WVLEEVEERT TLSGLRSKPA
SPKLSPDPQT PTLVPTKNVP RSAAPSVPPA SLMVPGTKPE AGLNSRCPAE AVTPAGLTKT
GAPSPASLGP
