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 27-MAR-2024, entry version 184. 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}; 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; 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 GlyGen; Q9R1L5; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q9R1L5; -. DR PhosphoSitePlus; Q9R1L5; -. DR SwissPalm; Q9R1L5; -. DR MaxQB; Q9R1L5; -. DR PaxDb; 10090-ENSMUSP00000105363; -. DR PeptideAtlas; Q9R1L5; -. DR ProteomicsDB; 292091; -. DR Antibodypedia; 26218; 112 antibodies from 24 providers. DR DNASU; 56527; -. DR Ensembl; ENSMUST00000109741.9; ENSMUSP00000105363.3; ENSMUSG00000053693.17. DR GeneID; 56527; -. DR KEGG; mmu:56527; -. DR UCSC; uc009mof.1; mouse. DR AGR; MGI:1861901; -. 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; SFGMREK; -. DR OrthoDB; 2915765at2759; -. DR PhylomeDB; Q9R1L5; -. DR TreeFam; TF313149; -. DR BRENDA; 2.7.11.1; 3474. DR BioGRID-ORCS; 56527; 6 hits in 81 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 160 other cell types or tissues. DR ExpressionAtlas; Q9R1L5; baseline and differential. 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:0006468; P:protein phosphorylation; ISS:UniProtKB. DR CDD; cd00992; PDZ_signaling; 1. DR CDD; cd05609; STKc_MAST; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 1.20.1480.20; MAST3 pre-PK domain-like; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR037711; MAST. DR InterPro; IPR015022; MAST_pre-PK_dom. 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; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 1; 1. DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 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; MAST3 pre-PK domain-like; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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. DR Genevisible; Q9R1L5; MM. 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 //