LMTK1_MOUSE
ID LMTK1_MOUSE Reviewed; 1365 AA.
AC Q80YE4; A6BLY8; O35211; Q3U2U5; Q3UHR8; Q66JN3; Q80YE3; Q8CB63; Q8CHE2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Serine/threonine-protein kinase LMTK1;
DE EC=2.7.11.1;
DE AltName: Full=Apoptosis-associated tyrosine kinase;
DE Short=AATYK;
DE AltName: Full=Brain apoptosis-associated tyrosine kinase;
DE AltName: Full=Lemur tyrosine kinase 1;
GN Name=Aatk; Synonyms=Aatyk, Kiaa0641, Lmr1, Lmtk1;
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] (ISOFORM 2), INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=9444961; DOI=10.1038/sj.onc.1201575;
RA Gaozza E., Baker S.J., Vora R.K., Reddy E.P.;
RT "AATYK: a novel tyrosine kinase induced during growth arrest and apoptosis
RT of myeloid cells.";
RL Oncogene 15:3127-3135(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), INDUCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/SvJ; TISSUE=Brain;
RX PubMed=11314039; DOI=10.1038/sj.onc.1204209;
RA Baker S.J., Sumerson R., Reddy C.D., Berrebi A.S., Flynn D.C., Reddy E.P.;
RT "Characterization of an alternatively spliced AATYK mRNA: expression
RT pattern of AATYK in the brain and neuronal cells.";
RL Oncogene 20:1015-1021(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING (ISOFORM 2),
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP PHOSPHORYLATION, AND MUTAGENESIS OF ASP-254.
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [5]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [8]
RP TISSUE SPECIFICITY, PHOSPHORYLATION, AND MUTAGENESIS OF ASP-254.
RX PubMed=11314040; DOI=10.1038/sj.onc.1204210;
RA Tomomura M., Fernandez-Gonzales A., Yano R., Yuzaki M.;
RT "Characterization of the apoptosis-associated tyrosine kinase (AATYK)
RT expressed in the CNS.";
RL Oncogene 20:1022-1032(2001).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1035; THR-1156; SER-1159;
RP SER-1162; SER-1175 AND SER-1178, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: May be involved in neuronal differentiation. {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 CDK5. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17651901}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:17651901}. Cytoplasm
CC {ECO:0000269|PubMed:17651901}. Cytoplasm, perinuclear region
CC {ECO:0000250}. Cell projection, dendrite {ECO:0000269|PubMed:17651901}.
CC Cell projection, axon {ECO:0000269|PubMed:17651901}. Cell projection,
CC growth cone {ECO:0000269|PubMed:17651901}. Note=Predominantly
CC perinuclear. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Membrane. Note=Peripheral membrane
CC protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Membrane; Single-pass type I
CC membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q80YE4-1; Sequence=Displayed;
CC Name=2; Synonyms=AATYK1A;
CC IsoId=Q80YE4-2; Sequence=VSP_020230;
CC Name=3; Synonyms=AATYK1B;
CC IsoId=Q80YE4-3; Sequence=VSP_020231;
CC Name=4;
CC IsoId=Q80YE4-4; Sequence=VSP_020229, VSP_020232;
CC -!- TISSUE SPECIFICITY: Expressed in brain, and, to a lower extent, in
CC kidney, heart, lung and skeletal muscle. In the brain, expressed in the
CC olfactory bulb, cerebellum, striatum, hippocampal formation, thalamus,
CC hypothalamus, and pontine nuclei (at protein level).
CC {ECO:0000269|PubMed:11314039, ECO:0000269|PubMed:11314040,
CC ECO:0000269|PubMed:17651901, ECO:0000269|PubMed:9444961}.
CC -!- DEVELOPMENTAL STAGE: Isoform 2 is predominantly expressed in adult
CC stage. Isoform 3 is up-regulated during postnatal development.
CC {ECO:0000269|PubMed:17651901}.
CC -!- INDUCTION: Up-regulated during the apoptotic death of myeloid cells
CC induced by cytokine withdrawal, such as IL3, and during G-CSF-induced
CC terminal differentiation of myeloblasts to granulocytes.
CC {ECO:0000269|PubMed:11314039, ECO:0000269|PubMed:9444961}.
CC -!- PTM: Autophosphorylated. Phosphorylated by CDK5 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41437.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF011908; AAB71837.1; -; mRNA.
DR EMBL; AY236858; AAO92350.1; -; mRNA.
DR EMBL; AY236859; AAO92351.1; -; mRNA.
DR EMBL; AB288871; BAF64832.1; -; mRNA.
DR EMBL; AB093253; BAC41437.2; ALT_INIT; mRNA.
DR EMBL; AK036705; BAC29541.1; -; mRNA.
DR EMBL; AK147239; BAE27789.1; -; mRNA.
DR EMBL; AK155100; BAE33045.1; -; mRNA.
DR EMBL; BC080846; AAH80846.1; -; mRNA.
DR CCDS; CCDS25725.1; -. [Q80YE4-2]
DR CCDS; CCDS56826.1; -. [Q80YE4-3]
DR PIR; T03748; T03748.
DR RefSeq; NP_001185714.1; NM_001198785.1.
DR RefSeq; NP_001185716.1; NM_001198787.1.
DR RefSeq; NP_031403.2; NM_007377.4.
DR AlphaFoldDB; Q80YE4; -.
DR SMR; Q80YE4; -.
DR IntAct; Q80YE4; 1.
DR STRING; 10090.ENSMUSP00000099309; -.
DR iPTMnet; Q80YE4; -.
DR PhosphoSitePlus; Q80YE4; -.
DR SwissPalm; Q80YE4; -.
DR MaxQB; Q80YE4; -.
DR PaxDb; Q80YE4; -.
DR PeptideAtlas; Q80YE4; -.
DR PRIDE; Q80YE4; -.
DR ProteomicsDB; 292104; -. [Q80YE4-1]
DR ProteomicsDB; 292105; -. [Q80YE4-2]
DR ProteomicsDB; 292106; -. [Q80YE4-3]
DR ProteomicsDB; 292107; -. [Q80YE4-4]
DR DNASU; 11302; -.
DR GeneID; 11302; -.
DR KEGG; mmu:11302; -.
DR UCSC; uc007mrn.3; mouse. [Q80YE4-4]
DR CTD; 9625; -.
DR MGI; MGI:1197518; Aatk.
DR eggNOG; ENOG502RCHK; Eukaryota.
DR InParanoid; Q80YE4; -.
DR OrthoDB; 53680at2759; -.
DR BioGRID-ORCS; 11302; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q80YE4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80YE4; protein.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; IDA:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IDA:MGI.
DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR CDD; cd05087; PTKc_Aatyk1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR042817; LMTK1_c.
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 Alternative splicing; ATP-binding; Cell projection; Cytoplasm; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1365
FT /note="Serine/threonine-protein kinase LMTK1"
FT /id="PRO_0000248301"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 126..396
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 550..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1237..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1164
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 254
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 132..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZMQ8"
FT MOD_RES 1035
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1156
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZMQ8"
FT VAR_SEQ 1..168
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020229"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12465718,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9444961"
FT /id="VSP_020230"
FT VAR_SEQ 1
FT /note="M -> MLIALLALAM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11314039,
FT ECO:0000303|PubMed:17651901"
FT /id="VSP_020231"
FT VAR_SEQ 1354..1365
FT /note="PAAGAGGRYTEA -> MSVVGAEVEQRDTTNGDL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020232"
FT MUTAGEN 254
FT /note="D->V: Significant decrease in autophosphorylation."
FT /evidence="ECO:0000269|PubMed:11314040,
FT ECO:0000269|PubMed:17651901"
FT CONFLICT 270
FT /note="V -> D (in Ref. 6; BAC29541)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="R -> G (in Ref. 6; BAC29541/BAE27789/BAE33045 and 7;
FT AAH80846)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="T -> K (in Ref. 6; BAE33045)"
FT /evidence="ECO:0000305"
FT CONFLICT 988
FT /note="G -> S (in Ref. 6; BAE27789)"
FT /evidence="ECO:0000305"
FT CONFLICT 1317
FT /note="A -> S (in Ref. 6; BAC29541)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1365 AA; 144607 MW; 051A53505EDAF502 CRC64;
MSSSFFNPSF AFSSHFDPDG APLSELSWSS SLAVVAVSFS GIFTVVILML ACLCCKKGGI
GFKEFENAEG DEYVADFSEQ GSPAAAAQTG PDVYVLPLTE VSLPMAKQPG RSVQLLKSTD
LGRHSLLYLK EIGHGWFGKV FLGEVHSGVS GTQVVVKELK VSASVQEQMQ FLEEAQPYRA
LQHSNLLQCL AQCAEVTPYL LVMEFCPLGD LKGYLRSCRV TESMAPDPLT LQRMACEVAC
GVLHLHRHNY VHSDLALRNC LLTADLTVKV GDYGLSHCKY REDYLVTADQ LWVPLRWIAP
ELVDEVHGNL LVVDQTKSSN VWSLGVTIWE LFELGAQPYP QHSDRQVLAY AVREQQLKLP
KPQLQLALSD RWYEVMQFCW LQPEQRPTAE EVHLLLSYLC AKGTTELEEE FERRWRSLRP
GGSTGLGSGS AAPAAATAAS AELTAASSFP LLERFTSDGF HVDSDDVLTV TETSHGLNFE
YKWEAGCGAE EYPPSGAASS PGSAARLQEL CAPDSSPPGV VPVLSAHSPS VGSEYFIRLE
GAVPAAGHDP DCAGCAPSPQ AVTDQDNNSE ESTVASLAME PLLGHAPPTE GLWGPCDHHS
HRRQGSPCPS RSPSPGTPML PAEDIDWGVA TFCPPFFDDP LGASPSGSPG AQPSPSDEEP
EEGKVGLAAQ CGHWSSNMSA NNNSASRDPE SWDPGYVSSF TDSYRDDCSS LEQTPRASPE
VGHLLSQEDP RDFLPGLVAV SPGQEPSRPF NLLPLCPAKG LAPAACLITS PWTEGAVGGA
ENPIVEPKLA QEAEGSAEPQ LPLPSVPSPS CEGASLPSEE ASAPDILPAS PTPAAGSWVT
VPEPAPTLES SGSSLGQEAP SSEDEDTTEA TSGVFTDLSS DGPHTEKSGI VPALRSLQKQ
VGTPDSLDSL DIPSSASDGG CEVLSPSAAG PPGGQPRAVD SGYDTENYES PEFVLKEAHE
SSEPEAFGEP ASEGESPGPD PLLSVSLGGL SKKSPYRDSA YFSDLDAESE PTFGPEKHSG
IQDSQKEQDL RSPPSPGHQS VQAFPRSAVS SEVLSPPQQS EEPLPEVPRP EPLGAQGPVG
VQPVPGPSHS KCFPLTSVPL ISEGSGTEPQ GPSGQLSGRA QQGQMGNPST PRSPLCLALP
GHPGALEGRP EEDEDTEDSE ESDEELRCYS VQEPSEDSEE EPPAVPVVVA ESQSARNLRS
LLKMPSLLSE AFCDDLERKK KAVSFFDDVT VYLFDQESPT RETGEPFPST KESLPTFLEG
GPSSPSATGL PLRAGHSPDS SAPEPGSRFE WDGDFPLVPG KAALVTELDP ADPVLAAPPT
PAAPFSRFTV SPTPASRFSI THISDSDAQS VGGPAAGAGG RYTEA
