TESK1_MOUSE
ID TESK1_MOUSE Reviewed; 627 AA.
AC O70146; O70147; Q499W7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Dual specificity testis-specific protein kinase 1;
DE EC=2.7.12.1;
DE AltName: Full=Testicular protein kinase 1;
GN Name=Tesk1;
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=9469938; DOI=10.1016/s0378-1119(97)00591-x;
RA Toshima J., Nakagawara K., Mori M., Noda T., Mizuno K.;
RT "Structural organization and chromosomal localization of the mouse tesk1
RT (testis-specific protein kinase 1) gene.";
RL Gene 206:237-245(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 INTERACTION WITH SPRY2, AND TISSUE SPECIFICITY.
RX PubMed=17974561; DOI=10.1074/jbc.m705457200;
RA Chandramouli S., Yu C.Y., Yusoff P., Lao D.H., Leong H.F., Mizuno K.,
RA Guy G.R.;
RT "Tesk1 interacts with Spry2 to abrogate its inhibition of ERK
RT phosphorylation downstream of receptor tyrosine kinase signaling.";
RL J. Biol. Chem. 283:1679-1691(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-338, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [8]
RP FUNCTION.
RX PubMed=30115939; DOI=10.1038/s41598-018-30115-3;
RA Wang L., Buckley A.F., Spurney R.F.;
RT "Regulation of cofilin phosphorylation in glomerular podocytes by testis
RT specific kinase 1 (TESK1).";
RL Sci. Rep. 8:12286-12286(2018).
CC -!- FUNCTION: Dual specificity protein kinase activity catalyzing
CC autophosphorylation and phosphorylation of exogenous substrates on both
CC serine/threonine and tyrosine residues (By similarity). Regulates the
CC cellular cytoskeleton by enhancing actin stress fiber formation via
CC phosphorylation of cofilin and by preventing microtubule breakdown via
CC inhibition of TAOK1/MARKK kinase activity (By similarity). Inhibits
CC podocyte motility via regulation of actin cytoskeletal dynamics and
CC phosphorylation of CFL1 (PubMed:30115939). Positively regulates
CC integrin-mediated cell spreading, via phosphorylation of cofilin (By
CC similarity). Suppresses ciliogenesis via multiple pathways;
CC phosphorylation of CFL1, suppression of ciliary vesicle directional
CC trafficking to the ciliary base, and by facilitating YAP1 nuclear
CC localization where it acts as a transcriptional corepressor of the
CC TEAD4 target genes AURKA and PLK1 (By similarity). Probably plays a
CC central role at and after the meiotic phase of spermatogenesis (By
CC similarity). {ECO:0000250|UniProtKB:Q15569,
CC ECO:0000250|UniProtKB:Q63572, ECO:0000269|PubMed:30115939}.
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=2.7.12.1;
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=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by autophosphorylation on Ser-215.
CC Kinase activity is inhibited by SPRED1. {ECO:0000250|UniProtKB:Q63572}.
CC -!- SUBUNIT: Interacts (via both C- and N-termini) with SPRY4 (via C-
CC terminus); the interaction inhibits TESK1 kinase activity (By
CC similarity). Interacts with TAOK1; the interaction inhibits TAOK1
CC kinase activity (By similarity). Interacts (via C-terminus) with SPRED1
CC (via C-terminus); the interaction inhibits TESK1 kinase activity (By
CC similarity). Interacts (via C-terminus) with PARVA/PARVIN (via C-
CC terminus); the interaction inhibits TESK1 kinase activity (By
CC similarity). Interacts with YWHAB/14-3-3 beta; the interaction is
CC dependent on the phosphorylation of TESK1 Ser-439 and inhibits TESK1
CC kinase activity (By similarity). Interacts with SPRY1, SPRY3 and SPRED2
CC (By similarity). Interacts (via C-terminus) with SPRY2 (via C-
CC terminus); the interaction disrupts SPRY2 interaction with PPP2CA/PP2A-
CC C, possibly by vesicular sequestration of SPRY2 (PubMed:17974561).
CC Therefore dephosphorylation of SPRY2 by the serine/threonine-protein
CC phosphatase 2A (PP2A) holoenzyme is lost, inhibiting its interaction
CC with GRB2 (By similarity). {ECO:0000250|UniProtKB:Q15569,
CC ECO:0000250|UniProtKB:Q63572, ECO:0000269|PubMed:17974561}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15569}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63572}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q15569}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q63572}. Note=Colocalizes with SPRY4 in
CC vesicular spots in the cytoplasm (By similarity). Localized to F-actin-
CC rich lamellipodia at the cell periphery following fibronectin-mediated
CC cell adhesion of Schwann cells (By similarity).
CC {ECO:0000250|UniProtKB:Q15569, ECO:0000250|UniProtKB:Q63572}.
CC -!- TISSUE SPECIFICITY: Expressed in testes and brain (at protein level).
CC {ECO:0000269|PubMed:17974561, ECO:0000269|PubMed:9469938}.
CC -!- DOMAIN: The extracatalytic C-terminal part is highly rich in proline
CC residues.
CC -!- PTM: Autophosphorylated on serine and tyrosine residues.
CC {ECO:0000250|UniProtKB:Q63572}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AB003493; BAA25124.1; -; Genomic_DNA.
DR EMBL; AB003494; BAA25125.1; -; mRNA.
DR EMBL; AK144302; BAE25822.1; -; mRNA.
DR EMBL; AL732506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC099699; AAH99699.1; -; mRNA.
DR CCDS; CCDS18094.1; -.
DR PIR; JC6534; JC6534.
DR RefSeq; NP_035701.3; NM_011571.3.
DR AlphaFoldDB; O70146; -.
DR SMR; O70146; -.
DR BioGRID; 204120; 2.
DR STRING; 10090.ENSMUSP00000050087; -.
DR iPTMnet; O70146; -.
DR PhosphoSitePlus; O70146; -.
DR SwissPalm; O70146; -.
DR EPD; O70146; -.
DR MaxQB; O70146; -.
DR PaxDb; O70146; -.
DR PRIDE; O70146; -.
DR ProteomicsDB; 258856; -.
DR Antibodypedia; 2068; 152 antibodies from 27 providers.
DR DNASU; 21754; -.
DR Ensembl; ENSMUST00000060864; ENSMUSP00000050087; ENSMUSG00000028458.
DR GeneID; 21754; -.
DR KEGG; mmu:21754; -.
DR UCSC; uc008spq.2; mouse.
DR CTD; 7016; -.
DR MGI; MGI:1201675; Tesk1.
DR VEuPathDB; HostDB:ENSMUSG00000028458; -.
DR eggNOG; ENOG502QTCP; Eukaryota.
DR GeneTree; ENSGT00940000157807; -.
DR HOGENOM; CLU_018577_0_0_1; -.
DR InParanoid; O70146; -.
DR OMA; SPPTWGD; -.
DR OrthoDB; 219904at2759; -.
DR PhylomeDB; O70146; -.
DR TreeFam; TF318014; -.
DR BRENDA; 2.7.10.2; 3474.
DR Reactome; R-MMU-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR BioGRID-ORCS; 21754; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Tesk1; mouse.
DR PRO; PR:O70146; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O70146; protein.
DR Bgee; ENSMUSG00000028458; Expressed in seminiferous tubule of testis and 231 other tissues.
DR ExpressionAtlas; O70146; baseline and differential.
DR Genevisible; O70146; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; 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:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051650; P:establishment of vesicle localization; ISS:UniProtKB.
DR GO; GO:1902018; P:negative regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:0042326; P:negative regulation of phosphorylation; IMP:UniProtKB.
DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISO:MGI.
DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0090521; P:podocyte cell migration; IMP:UniProtKB.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
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; IPR015782; TESK1.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR46485:SF3; PTHR46485:SF3; 1.
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; Cell projection; Cytoplasm; Cytoskeleton; Kinase; Magnesium;
KW Manganese; Metal-binding; Methylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..627
FT /note="Dual specificity testis-specific protein kinase 1"
FT /id="PRO_0000086747"
FT DOMAIN 52..309
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..525
FT /note="Required for interaction with YWHAB"
FT /evidence="ECO:0000250|UniProtKB:Q63572"
FT REGION 436..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..627
FT /note="Required for interaction with SPRED1 and SPRY2.
FT Required for TESK1-mediated dephosphorylation of SPRY2 and
FT SPRY2 inhibition of ERK phosphorylation"
FT /evidence="ECO:0000250|UniProtKB:Q63572"
FT REGION 528..625
FT /note="Required for interaction with PARVA"
FT /evidence="ECO:0000250|UniProtKB:Q63572"
FT REGION 532..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 170
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 58..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 215
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q63572"
FT MOD_RES 338
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT 550
FT /note="R -> Q (in Ref. 1; BAA25124/BAA25125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 627 AA; 68052 MW; 091ADA8CF52A2B50 CRC64;
MAGERPPLRG PGPGEAPGEG PGGAGGGPGR GRPSSYRALR SAVSSLARVD DFDCAEKIGA
GFFSEVYKVR HRQSGQVMVL KMNKLPSNRS NTLREVQLMN RLRHPNILRF MGVCVHQGQL
HALTEYMNGG TLEQLLSSPE PLSWPVRLHL ALDIAQGLRY LHAKGVFHRD LTSKNCLVRR
EDRGFTAVVG DFGLAEKIPV YREGTRKEPL AVVGSPYWMA PEVLRGELYD EKADVFAFGI
VLCELIARVP ADPDYLPRTE DFGLDVPAFR TLVGNDCPLP FLLLAIHCCS MEPSTRAPFT
EITQHLEQIL EQQPEATPLA KPPLTKAPLT YNQGSVPRGG PSATLPRPDP RLSRSRSDLF
LPPSPESPPS WGDNLTRVNP FSLREDLRGG KIKLLDTPCK PATPLPLVPP SPLTSTQLPL
VTTPDILVQP ETPVRRCRSL PSSPELPRRM ETALPGPGPS PMGPTEERMD CEGSSPEPEP
PGLAPQLPLA VATDNFISTC SSASQPWSPR SGPPLNNNPP AVVVNSPQGW AREPWNRAQH
SLPRAAALER TEPSPPPSAP REPEEGLPCP GCCLGPFSFG FLSMCPRPTP AVARYRNLNC
EAGSLLCHRG HHAKPPTPSL QLPGARS
