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   27-MAR-2024, entry version 140.
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}.
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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; 4.
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; 10090-ENSMUSP00000048238; -.
DR   PeptideAtlas; Q3TYD6; -.
DR   ProteomicsDB; 292108; -.
DR   Pumba; Q3TYD6; -.
DR   Antibodypedia; 2093; 276 antibodies from 33 providers.
DR   DNASU; 231876; -.
DR   Ensembl; ENSMUST00000041804.8; ENSMUSP00000048238.8; ENSMUSG00000038970.8.
DR   GeneID; 231876; -.
DR   KEGG; mmu:231876; -.
DR   UCSC; uc009alg.1; mouse.
DR   AGR; MGI:3036247; -.
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; SHKSVSC; -.
DR   OrthoDB; 2910608at2759; -.
DR   PhylomeDB; Q3TYD6; -.
DR   TreeFam; TF332280; -.
DR   BioGRID-ORCS; 231876; 1 hit in 80 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 219 other cell types or tissues.
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:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
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:0004672; F:protein kinase activity; IBA:GO_Central.
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: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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0001881; P:receptor recycling; ISO:MGI.
DR   GO; GO:0033572; P:transferrin transport; ISO:MGI.
DR   CDD; cd05086; PTKc_Aatyk2; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR24417; SERINE/THREONINE-PROTEIN KINASE LMTK1; 1.
DR   PANTHER; PTHR24417:SF8; SERINE_THREONINE-PROTEIN KINASE LMTK2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   Genevisible; Q3TYD6; MM.
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
//