CHK1_DROME
ID CHK1_DROME Reviewed; 512 AA.
AC O61661; A4V0S9; Q960N7;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Serine/threonine-protein kinase grp;
DE EC=2.7.11.1;
DE AltName: Full=Chk1 homolog;
DE AltName: Full=Protein grapes;
GN Name=grp {ECO:0000312|FlyBase:FBgn0261278};
GN ORFNames=CG17161 {ECO:0000312|FlyBase:FBgn0261278};
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 {ECO:0000312|EMBL:AAK93385.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=9197245; DOI=10.1016/s0960-9822(06)00189-8;
RA Fogarty P., Campbell S.D., Abu-Shumays R., de Saint Phalle B., Yu K.R.,
RA Uy G.L., Goldberg M.L., Sullivan W.;
RT "The Drosophila grapes gene is related to checkpoint gene chk1/rad27 and is
RT required for late syncytial division fidelity.";
RL Curr. Biol. 7:418-426(1997).
RN [2] {ECO:0000305}
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 [3] {ECO:0000305}
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 [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
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 [5]
RP FUNCTION.
RX PubMed=7925016; DOI=10.1242/dev.120.8.2131;
RA Fogarty P., Kalpin R.F., Sullivan W.;
RT "The Drosophila maternal-effect mutation grapes causes a metaphase arrest
RT at nuclear cycle 13.";
RL Development 120:2131-2142(1994).
RN [6]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=9214509; DOI=10.1038/40439;
RA Sibon O.C.M., Stevenson V.A., Theurkauf W.E.;
RT "DNA-replication checkpoint control at the Drosophila midblastula
RT transition.";
RL Nature 388:93-97(1997).
RN [7]
RP FUNCTION.
RX PubMed=10209095; DOI=10.1016/s0960-9822(99)80138-9;
RA Sibon O.C.M., Laurencon A., Hawley R., Theurkauf W.E.;
RT "The Drosophila ATM homologue Mei-41 has an essential checkpoint function
RT at the midblastula transition.";
RL Curr. Biol. 9:302-312(1999).
RN [8]
RP FUNCTION.
RX PubMed=10469601; DOI=10.1016/s0960-9822(99)80399-6;
RA Su T.T., Campbell S.D., O'Farrell P.H.;
RT "Drosophila grapes/CHK1 mutants are defective in cyclin proteolysis and
RT coordination of mitotic events.";
RL Curr. Biol. 9:919-922(1999).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10980701; DOI=10.1038/35023555;
RA Yu K.R., Saint R.B., Sullivan W.;
RT "The grapes checkpoint coordinates nuclear envelope breakdown and
RT chromosome condensation.";
RL Nat. Cell Biol. 2:609-615(2000).
RN [10]
RP MUTAGENESIS OF ASP-143.
RX PubMed=12172011; DOI=10.1073/pnas.172382899;
RA Peters M., DeLuca C., Hirao A., Stambolic V., Potter J., Zhou L., Liepa J.,
RA Snow B., Arya S., Wong J., Bouchard D., Binari R., Manoukian A.S.,
RA Mak T.W.;
RT "Chk2 regulates irradiation-induced, p53-mediated apoptosis in
RT Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11305-11310(2002).
RN [11]
RP FUNCTION.
RX PubMed=12919679; DOI=10.1016/s1534-5807(03)00208-9;
RA Grosshans J., Mueller H.A.J., Wieschaus E.;
RT "Control of cleavage cycles in Drosophila embryos by fruhstart.";
RL Dev. Cell 5:285-294(2003).
RN [12]
RP FUNCTION.
RX PubMed=14711410; DOI=10.1016/j.cub.2003.12.032;
RA Jaklevic B.R., Su T.T.;
RT "Relative contribution of DNA repair, cell cycle checkpoints, and cell
RT death to survival after DNA damage in Drosophila larvae.";
RL Curr. Biol. 14:23-32(2004).
RN [13]
RP FUNCTION.
RX PubMed=15723794; DOI=10.1016/j.cub.2005.02.026;
RA Royou A., Macias H., Sullivan W.;
RT "The Drosophila Grp/Chk1 DNA damage checkpoint controls entry into
RT anaphase.";
RL Curr. Biol. 15:334-339(2005).
RN [14]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=15860729; DOI=10.1242/jcs.02309;
RA de Vries H.I., Uyetake L., Lemstra W., Brunsting J.F., Su T.T.,
RA Kampinga H.H., Sibon O.C.M.;
RT "Grp/DChk1 is required for G2-M checkpoint activation in Drosophila S2
RT cells, whereas Dmnk/DChk2 is dispensable.";
RL J. Cell Sci. 118:1833-1842(2005).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16079276; DOI=10.1242/jcs.02454;
RA Purdy A., Uyetake L., Cordeiro M.G., Su T.T.;
RT "Regulation of mitosis in response to damaged or incompletely replicated
RT DNA require different levels of grapes (Drosophila Chk1).";
RL J. Cell Sci. 118:3305-3315(2005).
RN [16]
RP MUTAGENESIS OF PRO-189.
RX PubMed=22796626; DOI=10.1016/j.dnarep.2012.06.007;
RA Lee E.M., Trinh T.T., Shim H.J., Park S.Y., Nguyen T.T., Kim M.J.,
RA Song Y.H.;
RT "Drosophila Claspin is required for the G2 arrest that is induced by DNA
RT replication stress but not by DNA double-strand breaks.";
RL DNA Repair 11:741-752(2012).
RN [17]
RP DISRUPTION PHENOTYPE.
RX PubMed=34644293; DOI=10.1371/journal.pgen.1009834;
RA Yang Y., Kong R., Goh F.G., Somers W.G., Hime G.R., Li Z., Cai Y.;
RT "dRTEL1 is essential for the maintenance of Drosophila male germline stem
RT cells.";
RL PLoS Genet. 17:e1009834-e1009834(2021).
CC -!- FUNCTION: Serine/threonine-protein kinase which is required for
CC checkpoint-mediated cell cycle arrest and activation of DNA repair in
CC response to the presence of DNA damage or unreplicated DNA. May also
CC negatively regulate cell cycle progression during unperturbed cell
CC cycles. May phosphorylate the CDC25 phosphatase stg, which promotes its
CC degradation. This results in increased inhibitory tyrosine
CC phosphorylation of Cdk1-cyclin complexes and consequent inhibition of
CC cell cycle progression. {ECO:0000269|PubMed:10209095,
CC ECO:0000269|PubMed:10469601, ECO:0000269|PubMed:10980701,
CC ECO:0000269|PubMed:12919679, ECO:0000269|PubMed:14711410,
CC ECO:0000269|PubMed:15723794, ECO:0000269|PubMed:15860729,
CC ECO:0000269|PubMed:16079276, ECO:0000269|PubMed:7925016,
CC ECO:0000269|PubMed:9197245, ECO:0000269|PubMed:9214509}.
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:0000250|UniProtKB:O14757};
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:0000250|UniProtKB:O14757};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10980701,
CC ECO:0000269|PubMed:16079276}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Maternally supplied mRNA is degraded during progression from nuclear
CC stage 12 to nuclear stage 13. Zygotic expression is seen at reduced
CC levels later in embryogenesis and during larval development. Higher
CC expression is seen in pupae, coincident with ovarian differentiation.
CC May be activated during the syncytial blastoderm divisions which
CC precede cellularization, the Drosophila equivalent of the mid-blastula
CC transition (MBT). Developmentally regulated activation of the DNA
CC replication checkpoint may occur as the nucleo-cytoplasmic ratio
CC increases and maternal replication factors are depleted. Elongation of
CC the embryonic cell cycle may allow time for the transcription of genes
CC that initiate the switch from maternal to zygotic control of
CC embryogenesis. {ECO:0000269|PubMed:9197245,
CC ECO:0000269|PubMed:9214509}.
CC -!- PTM: Phosphorylated in a MEI-41/ATR dependent manner in response to DNA
CC damage or the presence of unreplicated DNA.
CC {ECO:0000269|PubMed:15860729}.
CC -!- DISRUPTION PHENOTYPE: In the germline, simultaneous RNAi-mediated
CC knockdown of grp and Rtel1 results in partial rescue of loss of
CC germline stem cell observed in the single Rtel1 knockdown.
CC {ECO:0000269|PubMed:9214509}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. NIM1 subfamily. {ECO:0000305}.
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DR EMBL; AF057041; AAC13566.1; -; mRNA.
DR EMBL; AE014134; AAF53551.2; -; Genomic_DNA.
DR EMBL; AE014134; AAF53552.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN10952.1; -; Genomic_DNA.
DR EMBL; AY051961; AAK93385.1; -; mRNA.
DR RefSeq; NP_477011.1; NM_057663.4.
DR RefSeq; NP_723985.1; NM_165171.3.
DR RefSeq; NP_723986.1; NM_165172.3.
DR AlphaFoldDB; O61661; -.
DR SMR; O61661; -.
DR BioGRID; 61001; 50.
DR IntAct; O61661; 25.
DR STRING; 7227.FBpp0080441; -.
DR PaxDb; O61661; -.
DR PRIDE; O61661; -.
DR DNASU; 34993; -.
DR EnsemblMetazoa; FBtr0080884; FBpp0080441; FBgn0261278.
DR EnsemblMetazoa; FBtr0080885; FBpp0080442; FBgn0261278.
DR EnsemblMetazoa; FBtr0080886; FBpp0080443; FBgn0261278.
DR GeneID; 34993; -.
DR KEGG; dme:Dmel_CG17161; -.
DR UCSC; CG17161-RB; d. melanogaster.
DR CTD; 2922; -.
DR FlyBase; FBgn0261278; grp.
DR VEuPathDB; VectorBase:FBgn0261278; -.
DR eggNOG; KOG0590; Eukaryota.
DR GeneTree; ENSGT00940000159682; -.
DR HOGENOM; CLU_000288_59_8_1; -.
DR InParanoid; O61661; -.
DR OMA; KRSQGHV; -.
DR OrthoDB; 698464at2759; -.
DR PhylomeDB; O61661; -.
DR Reactome; R-DME-176187; Activation of ATR in response to replication stress.
DR Reactome; R-DME-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-DME-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DME-69473; G2/M DNA damage checkpoint.
DR Reactome; R-DME-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-DME-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; O61661; -.
DR BioGRID-ORCS; 34993; 2 hits in 3 CRISPR screens.
DR ChiTaRS; gpp; fly.
DR GenomeRNAi; 34993; -.
DR PRO; PR:O61661; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0261278; Expressed in ovary and 11 other tissues.
DR ExpressionAtlas; O61661; baseline and differential.
DR Genevisible; O61661; DM.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:BHF-UCL.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0051299; P:centrosome separation; IMP:FlyBase.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IMP:FlyBase.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:FlyBase.
DR GO; GO:0007348; P:regulation of syncytial blastoderm mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0051225; P:spindle assembly; IMP:FlyBase.
DR GO; GO:0042060; P:wound healing; HMP:FlyBase.
DR CDD; cd14069; STKc_Chk1; 1.
DR InterPro; IPR034670; Chk1_catalytic_dom.
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; 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 ATP-binding; Cell cycle; Developmental protein; DNA damage; Kinase;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..512
FT /note="Serine/threonine-protein kinase grp"
FT /id="PRO_0000085855"
FT DOMAIN 22..279
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 335..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O14757,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O14757,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 143
FT /note="D->A: Abolishes kinase activity."
FT /evidence="ECO:0000269|PubMed:12172011"
FT MUTAGEN 189
FT /note="P->L: Impaired cell cycle arrest in response to the
FT DNA synthesis inhibitor hydroxyurea (HU)."
FT /evidence="ECO:0000269|PubMed:22796626"
FT CONFLICT 46..49
FT /note="EAVA -> GGCG (in Ref. 1; AAC13566)"
FT /evidence="ECO:0000305"
FT CONFLICT 197..198
FT /note="HA -> QP (in Ref. 1; AAC13566)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="L -> LL (in Ref. 1; AAC13566)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="S -> T (in Ref. 1; AAC13566)"
FT /evidence="ECO:0000305"
FT CONFLICT 352..359
FT /note="SKEDGGDR -> IQGGWRRP (in Ref. 1; AAC13566)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 57833 MW; 504CAB3C0B642EA0 CRC64;
MAATLTEAGT GPAATREFVE GWTLAQTLGE GAYGEVKLLI NRQTGEAVAM KMVDLKKHPD
AANSVRKEVC IQKMLQDKHI LRFFGKRSQG SVEYIFLEYA AGGELFDRIE PDVGMPQHEA
QRYFTQLLSG LNYLHQRGIA HRDLKPENLL LDEHDNVKIS DFGMATMFRC KGKERLLDKR
CGTLPYVAPE VLQKAYHAQP ADLWSCGVIL VTMLAGELPW DQPSTNCTEF TNWRDNDHWQ
LQTPWSKLDT LAISLLRKLL ATSPGTRLTL EKTLDHKWCN MQFADNERSY DLVDSAAALE
ICSPKAKRQR LQSSAHLSNG LDDSISRNYC SQPMPTMRSD DDFNVRLGSG RSKEDGGDRQ
TLAQEARLSY SFSQPALLDD LLLATQMNQT QNASQNYFQR LVRRMTRFFV TTRWDDTIKR
LVGTIERLGG YTCKFGDDGV VTVSTVDRNK LRLVFKAHII EMDGKILVDC RLSKGCGLEF
KRRFIKIKNA LEDIVLKGPT TWPIAIATNS VP
