LMTK2_MOUSE
ID LMTK2_MOUSE Reviewed; 1471 AA.
AC Q3TYD6; A6BLY9; Q6PDK6; Q6ZPY9; Q8CA34;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Serine/threonine-protein kinase LMTK2;
DE EC=2.7.11.1;
DE AltName: Full=Brain-enriched kinase;
DE AltName: Full=Lemur tyrosine kinase 2;
GN Name=Lmtk2; Synonyms=Brek, Kiaa1079;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17651901; DOI=10.1016/j.neuroscience.2007.05.048;
RA Tomomura M., Morita N., Yoshikawa F., Konishi A., Akiyama H., Furuichi T.,
RA Kamiguchi H.;
RT "Structural and functional analysis of the apoptosis-associated tyrosine
RT kinase (AATYK) family.";
RL Neuroscience 148:510-521(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-632 AND 1263-1471.
RC STRAIN=C57BL/6J; TISSUE=Spinal cord, and Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 410-1471.
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1253-1471.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP TISSUE SPECIFICITY, PHOSPHORYLATION, CHARACTERIZATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15005709; DOI=10.1111/j.1356-9597.2004.00714.x;
RA Kawa S., Fujimoto J., Tezuka T., Nakazawa T., Yamamoto T.;
RT "Involvement of BREK, a serine/threonine kinase enriched in brain, in NGF
RT signalling.";
RL Genes Cells 9:219-232(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781 AND THR-783, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-784; SER-797; SER-1274;
RP SER-1276; SER-1277; SER-1279; SER-1464 AND SER-1465, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
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).
CC -!- FUNCTION: Phosphorylates PPP1C, phosphorylase b and CFTR.
CC {ECO:0000250}.
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 -!- SUBUNIT: Interacts with PPP1C and inhibitor-2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain, especially in the
CC olfactory bulb, olfactory tubercle, hippocampus, striatum, cerebellum
CC and cerebral cortex. Weakly expressed in skeletal muscle and not
CC expressed in liver. {ECO:0000269|PubMed:15005709}.
CC -!- DEVELOPMENTAL STAGE: Expression observed during all tested stages from
CC 18 dpc to postnatal week 6, but it was especially high during the early
CC postnatal stage (postnatal weeks 0-2). {ECO:0000269|PubMed:15005709}.
CC -!- PTM: Autophosphorylated. Phosphorylated (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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; AB288872; BAF64833.1; -; mRNA.
DR EMBL; AK039738; BAC30433.1; -; mRNA.
DR EMBL; AK158724; BAE34627.1; -; mRNA.
DR EMBL; AK129279; BAC98089.2; -; mRNA.
DR EMBL; BC058653; AAH58653.1; -; mRNA.
DR CCDS; CCDS39376.1; -.
DR RefSeq; NP_001074578.1; NM_001081109.1.
DR AlphaFoldDB; Q3TYD6; -.
DR SMR; Q3TYD6; -.
DR BioGRID; 231189; 1.
DR IntAct; Q3TYD6; 1.
DR STRING; 10090.ENSMUSP00000048238; -.
DR iPTMnet; Q3TYD6; -.
DR PhosphoSitePlus; Q3TYD6; -.
DR SwissPalm; Q3TYD6; -.
DR EPD; Q3TYD6; -.
DR MaxQB; Q3TYD6; -.
DR PaxDb; Q3TYD6; -.
DR PeptideAtlas; Q3TYD6; -.
DR PRIDE; Q3TYD6; -.
DR ProteomicsDB; 292108; -.
DR Antibodypedia; 2093; 246 antibodies from 33 providers.
DR DNASU; 231876; -.
DR Ensembl; ENSMUST00000041804; ENSMUSP00000048238; ENSMUSG00000038970.
DR GeneID; 231876; -.
DR KEGG; mmu:231876; -.
DR UCSC; uc009alg.1; mouse.
DR CTD; 22853; -.
DR MGI; MGI:3036247; Lmtk2.
DR VEuPathDB; HostDB:ENSMUSG00000038970; -.
DR eggNOG; ENOG502QSD2; Eukaryota.
DR GeneTree; ENSGT00940000158475; -.
DR HOGENOM; CLU_004618_0_0_1; -.
DR InParanoid; Q3TYD6; -.
DR OMA; EQSWPHV; -.
DR OrthoDB; 53680at2759; -.
DR PhylomeDB; Q3TYD6; -.
DR TreeFam; TF332280; -.
DR BioGRID-ORCS; 231876; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Lmtk2; mouse.
DR PRO; PR:Q3TYD6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q3TYD6; protein.
DR Bgee; ENSMUSG00000038970; Expressed in caudate-putamen and 218 other tissues.
DR Genevisible; Q3TYD6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070853; F:myosin VI binding; ISO:MGI.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0007411; P:axon guidance; ISO:MGI.
DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISO:MGI.
DR GO; GO:0032456; P:endocytic recycling; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0001881; P:receptor recycling; ISO:MGI.
DR GO; GO:0033572; P:transferrin transport; ISO:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1471
FT /note="Serine/threonine-protein kinase LMTK2"
FT /id="PRO_0000259459"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..41
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..1471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 136..406
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 510..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1248..1292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1452..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1264
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 142..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 783
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1076
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWU2"
FT MOD_RES 1274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWU2"
FT MOD_RES 1464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 421
FT /note="F -> L (in Ref. 2; BAE34627)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1471 AA; 160508 MW; 13C0C905F585D23F CRC64;
MPGPPASPPP PMLLLLLLLT VGCARAAPLP QTGAGEVPVV EVPSLFVILS VCSLLILIVL
IANCVSCCKD PEIDFKEFED NFDDEIDFTP PAEDTPSIQS PAEVFTLSVP NISLPAPSQF
QASVEGLKSQ VARHSLNYIQ EIGSGWFGKV LLGETYTGTS VARVIVKELK VSASPKEQDT
FLKSGEPYYI LQHPNVLQCV GQCVEAIPYL LVFEFCDLGD LKAYLHNEQE HVRGDSQTML
LQRMACEIAA GLAAMHKLHF LHSDLALRNC YLTSDLNVKV GDYGIGFSRY KEDYIETDDK
KVFPLRWTAP ELVTSFQDRL LTADQTKYSN IWSLGVTLWE LFNNAAQPYA NLSDLDVLNQ
VIRERDMKLP KPQLEQPYSD RWYEVLQFCW LPPDKRPAAE DVHRLLTYLR MQSQRDSEVD
FEQQWTALKP DTNSRDASSS AAFPILDHFA RDRLGREMEE VLTVTETSQG LSFEYVWEAA
KHDHFDEQGR GHPDEALSYS SMFFPVEVFE NSLSDPGPGK QDDSGQEVPV RAPGVVPVFD
AHNLSVGSDY YIQLEEKSSS NLGLDPPALL TTEVDKLERA GAEEPRTEED FFQSSAHPKE
ASSTEDSRAT SIPGSPFNLF SDLDKADDLP SHQKIFDLME LNGVQADFKP AILSSSLDDP
KDTCQSDKEK PHKLLDQGPL CLSESLLHQD HFDPLSVQEL SENFLFLQEK NLLKGSLTTK
EQVSDLQTEL KNAGFTSALL ESPQRGSESS ELEFLENTLD FPLSQGDTRG QNEGAGVRRH
SGTSPQASPA LLTEEGSPTA PTDPILKPEE TKSFRDVRVP EDSICLELGP DPVTVGVEIP
ATDAKTLDGG NRPPDVTCQS KEALSLTNRH PILVNDITAQ GSVESCLPES RQDLQNEPFS
EDPLSVSSLE KHSEAAETLN QLNSKAAPED AALASALSSD STSQDSLLED SLSTPIPTSE
QSVETPDSLD SVDVREALLE SLGSHTPRKL LPPDKPADSG YETENLESPE WTLHPAPEGT
ADSDAAAAGD SGHSSLPPNP VIVISDAGDG HRGAEGPPQS FTLGPQSSYR DSAYFSDNDS
EPDKKPEEVP GTSANALVLV KGQSPPESVV PEESSDVREG CLEAPQDKPD QSRVSTLQNS
CHSELQETLQ PTPADASRES CPVNDEASSP LSLLNSEPSS CDDLDTQEDR PCTLASTGTN
TNELLAYMSS TLDKSLPSHL ESSKLKEPDI EGKYLGKLCV SGMLDLSEDG MDADEEDENS
DDSDEDLRAF NLHSLSSESE DDTEHPVPII VSNDDGRHLR SLLKPSAAEA IEQLPEDWKK
EKKAVTFFDD VTVYLFDQET PTKELGHCGG EAHGPGPSSP AASSSSPYLG RCMNSESSTD
EEGGGFEWDD DFSPDPFMSK TTSLLGSKPS LQTSKYFSPP PPARSAEQSW PHVSPCSRFS
ISPANIASFS LTHLTDSDIE QGGSSEDGDK D
