TRC_DROME
ID TRC_DROME Reviewed; 463 AA.
AC Q9NBK5; Q24464; Q9NGW6; Q9VW46;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Serine/threonine-protein kinase tricornered {ECO:0000303|PubMed:15479641, ECO:0000312|FlyBase:FBgn0003744};
DE EC=2.7.11.1 {ECO:0000269|PubMed:15479641, ECO:0000305|PubMed:32022690};
DE AltName: Full=NDR protein kinase {ECO:0000303|PubMed:7761441};
DE AltName: Full=Serine/threonine-protein kinase 38-like;
DE AltName: Full=Serine/threonine-protein kinase tricorner {ECO:0000312|FlyBase:FBgn0003744};
GN Name=trc {ECO:0000303|PubMed:15479641, ECO:0000312|FlyBase:FBgn0003744};
GN ORFNames=CG8637 {ECO:0000312|FlyBase:FBgn0003744};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA84486.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC STRAIN=Canton-S {ECO:0000312|EMBL:CAA84486.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:7761441};
RX PubMed=7761441; DOI=10.1073/pnas.92.11.5022;
RA Millward T.A., Cron P., Hemmings B.A.;
RT "Molecular cloning and characterization of a conserved nuclear
RT serine/threonine protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5022-5026(1995).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF97511.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS B; C AND D), FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11102376; DOI=10.1093/genetics/156.4.1817;
RA Geng W., He B., Wang M., Adler P.N.;
RT "The tricornered gene, which is required for the integrity of epidermal
RT cell extensions, encodes the Drosophila nuclear DBF2-related kinase.";
RL Genetics 156:1817-1828(2000).
RN [3] {ECO:0000312|EMBL:AAF49104.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAF49104.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAK93304.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK93304.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6] {ECO:0000305}
RP FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-292
RP AND THR-453, MUTAGENESIS OF SER-292 AND THR-453, AND DISRUPTION PHENOTYPE.
RX PubMed=15479641; DOI=10.1016/j.cell.2004.09.036;
RA Emoto K., He Y., Ye B., Grueber W.B., Adler P.N., Jan L.Y., Jan Y.-N.;
RT "Control of dendritic branching and tiling by the Tricornered-kinase/Furry
RT signaling pathway in Drosophila sensory neurons.";
RL Cell 119:245-256(2004).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MOB1, AND SUBCELLULAR LOCATION.
RX PubMed=15975907; DOI=10.1091/mbc.e05-01-0018;
RA He Y., Emoto K., Fang X., Ren N., Tian X., Jan Y.-N., Adler P.N.;
RT "Drosophila Mob family proteins interact with the related tricornered (Trc)
RT and warts (Wts) kinases.";
RL Mol. Biol. Cell 16:4139-4152(2005).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-122 AND THR-453.
RX PubMed=32022690; DOI=10.7554/elife.52009;
RA Norkett R., Del Castillo U., Lu W., Gelfand V.I.;
RT "Ser/Thr kinase Trc controls neurite outgrowth in Drosophila by modulating
RT microtubule-microtubule sliding.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in controlling cell
CC structure and proliferation of a variety of polarized outgrowths
CC including epidermal hairs, bristles, arista laterals, and dendrites
CC (PubMed:11102376, PubMed:15479641, PubMed:32022690). Together with fry,
CC maintains the integrity of epidermal hairs and is an essential
CC component of the signaling pathway regulating dendritic branching of
CC sensory neurons (PubMed:15479641). Reduces neurite outgrowth by
CC phosphorylating pav, thereby inhibiting its function in microtubule-
CC microtubule sliding (PubMed:32022690). {ECO:0000269|PubMed:11102376,
CC ECO:0000269|PubMed:15479641, ECO:0000269|PubMed:32022690}.
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:0000269|PubMed:15479641, ECO:0000305|PubMed:32022690};
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:0000269|PubMed:15479641,
CC ECO:0000305|PubMed:32022690};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15479641};
CC -!- ACTIVITY REGULATION: Activated by fry. {ECO:0000269|PubMed:32022690}.
CC -!- SUBUNIT: Interacts with, and is activated by, Mob1.
CC {ECO:0000269|PubMed:15975907}.
CC -!- INTERACTION:
CC Q9NBK5-2; Q8T0S6: hpo; NbExp=2; IntAct=EBI-15596484, EBI-101858;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11102376,
CC ECO:0000269|PubMed:15975907}. Nucleus {ECO:0000269|PubMed:11102376,
CC ECO:0000269|PubMed:15975907}. Note=Trc colocalizes with Mob1 to the
CC cell periphery in wing cells and wing hairs.
CC {ECO:0000269|PubMed:11102376, ECO:0000269|PubMed:15975907}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=D {ECO:0000269|PubMed:11102376};
CC IsoId=Q9NBK5-1; Sequence=Displayed;
CC Name=A {ECO:0000269|PubMed:12537569};
CC IsoId=Q9NBK5-2; Sequence=VSP_052342;
CC Name=B {ECO:0000269|PubMed:11102376}; Synonyms=trc-S
CC {ECO:0000269|PubMed:11102376};
CC IsoId=Q9NBK5-3; Sequence=VSP_052342, VSP_052343, VSP_052344;
CC Name=C {ECO:0000269|PubMed:11102376}; Synonyms=trc-L
CC {ECO:0000269|PubMed:11102376};
CC IsoId=Q9NBK5-4; Sequence=VSP_052343, VSP_052344;
CC -!- TISSUE SPECIFICITY: Expressed in the peripheral and central nervous
CC system (at protein level) (PubMed:15479641, PubMed:32022690). Expressed
CC in the wing imaginal disk (PubMed:11102376).
CC {ECO:0000269|PubMed:11102376, ECO:0000269|PubMed:15479641,
CC ECO:0000269|PubMed:32022690}.
CC -!- DISRUPTION PHENOTYPE: Results in splitting or branching of epidermal
CC hairs, supernumerary terminal branching and defective dendritic tiling
CC (PubMed:11102376, PubMed:15479641). RNAi-mediated knockdown in neurons
CC increases dendrite length of sensory neurons (PubMed:32022690).
CC {ECO:0000269|PubMed:11102376, ECO:0000269|PubMed:15479641,
CC ECO:0000269|PubMed:32022690}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; Z35103; CAA84486.1; -; mRNA.
DR EMBL; AF238490; AAF67167.1; -; mRNA.
DR EMBL; AF239171; AAF67168.1; -; mRNA.
DR EMBL; AF247814; AAF97511.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49104.1; -; Genomic_DNA.
DR EMBL; AY051880; AAK93304.1; -; mRNA.
DR RefSeq; NP_001262071.1; NM_001275142.1. [Q9NBK5-1]
DR RefSeq; NP_524170.2; NM_079446.4. [Q9NBK5-2]
DR AlphaFoldDB; Q9NBK5; -.
DR SMR; Q9NBK5; -.
DR BioGRID; 65434; 19.
DR DIP; DIP-21479N; -.
DR IntAct; Q9NBK5; 3.
DR MINT; Q9NBK5; -.
DR STRING; 7227.FBpp0304464; -.
DR iPTMnet; Q9NBK5; -.
DR PaxDb; Q9NBK5; -.
DR PRIDE; Q9NBK5; -.
DR DNASU; 40165; -.
DR EnsemblMetazoa; FBtr0074922; FBpp0074691; FBgn0003744. [Q9NBK5-2]
DR EnsemblMetazoa; FBtr0332154; FBpp0304464; FBgn0003744. [Q9NBK5-1]
DR GeneID; 40165; -.
DR KEGG; dme:Dmel_CG8637; -.
DR CTD; 40165; -.
DR FlyBase; FBgn0003744; trc.
DR VEuPathDB; VectorBase:FBgn0003744; -.
DR eggNOG; KOG0605; Eukaryota.
DR GeneTree; ENSGT00940000153544; -.
DR InParanoid; Q9NBK5; -.
DR OMA; PERYSEN; -.
DR PhylomeDB; Q9NBK5; -.
DR Reactome; R-DME-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-DME-9013422; RHOBTB1 GTPase cycle.
DR SignaLink; Q9NBK5; -.
DR BioGRID-ORCS; 40165; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 40165; -.
DR PRO; PR:Q9NBK5; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0003744; Expressed in adult abdomen and 21 other tissues.
DR ExpressionAtlas; Q9NBK5; baseline and differential.
DR Genevisible; Q9NBK5; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0044297; C:cell body; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0070451; C:cell hair; IDA:FlyBase.
DR GO; GO:0071944; C:cell periphery; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0048800; P:antennal morphogenesis; IMP:FlyBase.
DR GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0070593; P:dendrite self-avoidance; IGI:FlyBase.
DR GO; GO:0035317; P:imaginal disc-derived wing hair organization; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0051012; P:microtubule sliding; IMP:UniProtKB.
DR GO; GO:0150013; P:negative regulation of neuron projection arborization; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0050773; P:regulation of dendrite development; IMP:UniProtKB.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..463
FT /note="Serine/threonine-protein kinase tricornered"
FT /id="PRO_0000279717"
FT DOMAIN 93..394
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 395..463
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 119..180
FT /note="Interaction with mats and Mob1"
FT /evidence="ECO:0000269|PubMed:15975907"
FT ACT_SITE 216
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 99..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15479641"
FT MOD_RES 453
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15479641"
FT VAR_SEQ 267..270
FT /note="Missing (in isoform A and isoform B)"
FT /evidence="ECO:0000303|PubMed:11102376,
FT ECO:0000303|PubMed:12537569, ECO:0000303|PubMed:7761441"
FT /id="VSP_052342"
FT VAR_SEQ 357..358
FT /note="EI -> RD (in isoform B and isoform C)"
FT /evidence="ECO:0000303|PubMed:11102376,
FT ECO:0000303|PubMed:7761441"
FT /id="VSP_052343"
FT VAR_SEQ 403..411
FT /note="RERPAAIPV -> LAAPYL (in isoform B and isoform C)"
FT /evidence="ECO:0000303|PubMed:11102376,
FT ECO:0000303|PubMed:7761441"
FT /id="VSP_052344"
FT MUTAGEN 122
FT /note="K->A: Loss of catalytic activity; increases
FT microtubule sliding (in vitro)."
FT /evidence="ECO:0000269|PubMed:32022690"
FT MUTAGEN 292
FT /note="S->A: Excessive dendritic branching."
FT /evidence="ECO:0000269|PubMed:15479641"
FT MUTAGEN 453
FT /note="T->A: Excessive dendritic branching."
FT /evidence="ECO:0000269|PubMed:15479641"
FT MUTAGEN 453
FT /note="T->E: Constitutively active kinase; reduces
FT microtubule sliding to similar levels of wild-type (in
FT vitro)."
FT /evidence="ECO:0000269|PubMed:32022690"
FT CONFLICT 379..390
FT /note="LGSQRGLEDLKS -> WVPASSGGSEV (in Ref. 1; CAA84486 and
FT 2; AAF67167/AAF67168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 53333 MW; 8079BBEC09F6B037 CRC64;
MMSSRTQDAD GASIRFSDHT LDKATKAKVT LENYYSNLVT QYGERKQRLA KLEAQLKDES
LSEAQRQEKR LQHAQKETEY LRLKRLRLGV EDFEALKVIG RGAFGEVRLV QKKDTGHVYA
MKVLRKADML EKEQVAHVRA ERDVLVEADH QWVVKMYYSF QDPVNLYLIM EFLPGGDMMT
LLMKKDTLSE EGTQFYISET ALAIDSIHKL GFIHRDIKPD NLLLDARGHL KLSDFGLCTG
LKKSHRTDFY RDLSQAKPSD FIGTCASLSC SPMDSKRRAE SWKRNRRALA YSTVGTPDYI
APEVFLQTGY GPACDWWSLG VIMYEMLMGY PPFCSDNPQD TYRKVMNWRE TLIFPPEIPI
SEEAKETIIN FCCEADRRLG SQRGLEDLKS VPFFRGVDWE HIRERPAAIP VEVRSIDDTS
NFDEFPDVSL EIPSAPIPQG GEIAKDWVFI NYTYKRFEVR NLE
