ID PLK4_DROME Reviewed; 769 AA.
AC O97143; Q86NL8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 191.
DE RecName: Full=Serine/threonine-protein kinase PLK4;
DE EC=2.7.11.21;
DE AltName: Full=Polo-like kinase 4;
DE Short=PLK-4;
DE AltName: Full=Serine/threonine-protein kinase SAK;
GN Name=SAK; ORFNames=CG7186;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hudson J.W., Dennis J.W.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16326102; DOI=10.1016/j.cub.2005.11.042;
RA Bettencourt-Dias M., Rodrigues-Martins A., Carpenter L., Riparbelli M.,
RA Lehmann L., Gatt M.K., Carmo N., Balloux F., Callaini G., Glover D.M.;
RT "SAK/PLK4 is required for centriole duplication and flagella development.";
RL Curr. Biol. 15:2199-2207(2005).
RN [6]
RP FUNCTION.
RX PubMed=17463247; DOI=10.1126/science.1142950;
RA Rodrigues-Martins A., Riparbelli M., Callaini G., Glover D.M.,
RA Bettencourt-Dias M.;
RT "Revisiting the role of the mother centriole in centriole biogenesis.";
RL Science 316:1046-1050(2007).
RN [7]
RP FUNCTION.
RX PubMed=18555779; DOI=10.1016/j.cell.2008.05.039;
RA Basto R., Brunk K., Vinadogrova T., Peel N., Franz A., Khodjakov A.,
RA Raff J.W.;
RT "Centrosome amplification can initiate tumorigenesis in flies.";
RL Cell 133:1032-1042(2008).
RN [8]
RP SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=19171756; DOI=10.1083/jcb.200808049;
RA Rogers G.C., Rusan N.M., Roberts D.M., Peifer M., Rogers S.L.;
RT "The SCF Slimb ubiquitin ligase regulates Plk4/Sak levels to block
RT centriole reduplication.";
RL J. Cell Biol. 184:225-239(2009).
RN [9]
RP UBIQUITINATION, AND MUTAGENESIS OF SER-293 AND THR-297.
RX PubMed=19084407; DOI=10.1016/j.cub.2008.11.037;
RA Cunha-Ferreira I., Rodrigues-Martins A., Bento I., Riparbelli M., Zhang W.,
RA Laue E., Callaini G., Glover D.M., Bettencourt-Dias M.;
RT "The SCF/Slimb ubiquitin ligase limits centrosome amplification through
RT degradation of SAK/PLK4.";
RL Curr. Biol. 19:43-49(2009).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=20946984; DOI=10.1016/j.cell.2010.09.022;
RA Goodwin S.S., Vale R.D.;
RT "Patronin regulates the microtubule network by protecting microtubule minus
RT ends.";
RL Cell 143:263-274(2010).
RN [11]
RP INTERACTION WITH ALMS1A, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=32965218; DOI=10.7554/elife.59368;
RA Chen C., Yamashita Y.M.;
RT "Alstrom syndrome gene is a stem-cell-specific regulator of centriole
RT duplication in the Drosophila testis.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Serine/threonine-protein kinase that plays a central role in
CC centriole duplication. Able to trigger procentriole formation on the
CC surface of the mother centriole cylinder, using mother centriole as a
CC platform, leading to the recruitment of centriole biogenesis proteins
CC such as Sas-6. When overexpressed, it is able to induce centrosome
CC amplification through the simultaneous generation of multiple
CC procentrioles adjoining each parental centriole during S phase.
CC Centrosome amplification following overexpression can initiate
CC tumorigenesis, highlighting the importance of centrosome regulation in
CC cancers. {ECO:0000269|PubMed:16326102, ECO:0000269|PubMed:17463247,
CC ECO:0000269|PubMed:18555779}.
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=2.7.11.21;
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=2.7.11.21;
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with Alms1a
CC (PubMed:32965218). {ECO:0000250|UniProtKB:Q64702,
CC ECO:0000269|PubMed:32965218}.
CC -!- INTERACTION:
CC O97143; Q9VNE4: asl; NbExp=13; IntAct=EBI-162366, EBI-108604;
CC O97143; O97143: SAK; NbExp=10; IntAct=EBI-162366, EBI-162366;
CC O97143; Q9VDE3: slmb; NbExp=2; IntAct=EBI-162366, EBI-91763;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:16326102,
CC ECO:0000269|PubMed:19171756, ECO:0000269|PubMed:20946984,
CC ECO:0000269|PubMed:32965218}. Note=Colocalizes with Sas-4 and Patronin
CC at the microtubule organizing center (PubMed:20946984). Colocalizes
CC with Alms1a at the mother centrosome in male germ stem cells
CC (PubMed:32965218). {ECO:0000269|PubMed:20946984,
CC ECO:0000269|PubMed:32965218}.
CC -!- TISSUE SPECIFICITY: Expressed in testis (at protein level).
CC {ECO:0000269|PubMed:32965218}.
CC -!- PTM: Ubiquitinated by the SCF-slmb ubiquitin ligase complex; leading to
CC its degradation by the proteasome during interphase and regulating
CC centriole number and ensuring the block to centriole reduplication.
CC {ECO:0000269|PubMed:19084407, ECO:0000269|PubMed:19171756}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU01328,
CC ECO:0000255|PROSITE-ProRule:PRU01329}.
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DR EMBL; AF106952; AAD19607.1; -; mRNA.
DR EMBL; AE014296; AAF51737.1; -; Genomic_DNA.
DR EMBL; BT004846; AAO45202.1; -; mRNA.
DR EMBL; BT044561; ACI15756.1; -; mRNA.
DR RefSeq; NP_649324.1; NM_141067.3.
DR PDB; 4G7N; X-ray; 2.30 A; A/B=382-602.
DR PDB; 4NK7; X-ray; 3.23 A; A=383-601.
DR PDB; 5LHX; X-ray; 1.53 A; A/B=657-745.
DR PDB; 7RL3; X-ray; 1.75 A; A/B=657-745.
DR PDBsum; 4G7N; -.
DR PDBsum; 4NK7; -.
DR PDBsum; 5LHX; -.
DR PDBsum; 7RL3; -.
DR AlphaFoldDB; O97143; -.
DR SMR; O97143; -.
DR BioGRID; 65629; 74.
DR DIP; DIP-49071N; -.
DR ELM; O97143; -.
DR IntAct; O97143; 65.
DR STRING; 7227.FBpp0078042; -.
DR iPTMnet; O97143; -.
DR PaxDb; 7227-FBpp0078042; -.
DR DNASU; 40384; -.
DR EnsemblMetazoa; FBtr0078387; FBpp0078042; FBgn0026371.
DR GeneID; 40384; -.
DR KEGG; dme:Dmel_CG7186; -.
DR UCSC; CG7186-RA; d. melanogaster.
DR AGR; FB:FBgn0026371; -.
DR CTD; 40384; -.
DR FlyBase; FBgn0026371; SAK.
DR VEuPathDB; VectorBase:FBgn0026371; -.
DR eggNOG; KOG0575; Eukaryota.
DR GeneTree; ENSGT00940000156316; -.
DR HOGENOM; CLU_008726_2_0_1; -.
DR InParanoid; O97143; -.
DR OMA; LPSKHWK; -.
DR OrthoDB; 5471704at2759; -.
DR PhylomeDB; O97143; -.
DR BRENDA; 2.7.11.21; 1994.
DR SignaLink; O97143; -.
DR BioGRID-ORCS; 40384; 0 hits in 3 CRISPR screens.
DR ChiTaRS; SAK; fly.
DR GenomeRNAi; 40384; -.
DR PRO; PR:O97143; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0026371; Expressed in mouthpart and 30 other cell types or tissues.
DR Genevisible; O97143; DM.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
DR GO; GO:0007099; P:centriole replication; IDA:FlyBase.
DR GO; GO:0007098; P:centrosome cycle; IMP:FlyBase.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:FlyBase.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:FlyBase.
DR GO; GO:0046599; P:regulation of centriole replication; IDA:FlyBase.
DR GO; GO:0031647; P:regulation of protein stability; IMP:FlyBase.
DR GO; GO:0007288; P:sperm axoneme assembly; IMP:FlyBase.
DR GO; GO:0035186; P:syncytial blastoderm mitotic cell cycle; IMP:FlyBase.
DR CDD; cd13114; POLO_box_Plk4_1; 1.
DR CDD; cd13115; POLO_box_Plk4_2; 1.
DR CDD; cd13116; POLO_box_Plk4_3; 1.
DR CDD; cd14186; STKc_PLK4; 1.
DR Gene3D; 2.40.50.930; -; 1.
DR Gene3D; 3.30.1120.120; -; 1.
DR Gene3D; 3.30.1120.130; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR047108; Plk4-like_POLO_box_2_sf.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR033699; POLO_box_Plk4_1.
DR InterPro; IPR033698; POLO_box_Plk4_2.
DR InterPro; IPR033696; POLO_box_Plk4_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR046437; Ser_Thr-PK_POLO_box_1_sf.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF94; SERINE_THREONINE-PROTEIN KINASE PLK4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF18190; Plk4_PB1; 1.
DR Pfam; PF18409; Plk4_PB2; 1.
DR SUPFAM; SSF82615; Polo-box domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51984; CPB1; 1.
DR PROSITE; PS51985; CPB2; 1.
DR PROSITE; PS50078; POLO_BOX; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Ubl conjugation.
FT CHAIN 1..769
FT /note="Serine/threonine-protein kinase PLK4"
FT /id="PRO_0000385291"
FT DOMAIN 14..267
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 381..498
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01328"
FT DOMAIN 499..602
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01329"
FT DOMAIN 660..739
FT /note="POLO box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 20..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 293
FT /note="S->A: In SAK-ND; impairs interaction with SCF-slmb
FT ubiquitin ligase complex and subsequent ubiquitination;
FT when associated with A-297."
FT /evidence="ECO:0000269|PubMed:19084407"
FT MUTAGEN 297
FT /note="T->A: In SAK-ND; impairs interaction with SCF-slmb
FT ubiquitin ligase complex and subsequent ubiquitination;
FT when associated with A-292."
FT /evidence="ECO:0000269|PubMed:19084407"
FT CONFLICT 145
FT /note="L -> V (in Ref. 4; AAO45202)"
FT /evidence="ECO:0000305"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:4G7N"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:4G7N"
FT STRAND 414..421
FT /evidence="ECO:0007829|PDB:4G7N"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:4G7N"
FT STRAND 426..436
FT /evidence="ECO:0007829|PDB:4G7N"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:4G7N"
FT TURN 449..452
FT /evidence="ECO:0007829|PDB:4G7N"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:4G7N"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:4G7N"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:4G7N"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:4G7N"
FT HELIX 482..496
FT /evidence="ECO:0007829|PDB:4G7N"
FT STRAND 499..505
FT /evidence="ECO:0007829|PDB:4G7N"
FT STRAND 507..514
FT /evidence="ECO:0007829|PDB:4G7N"
FT STRAND 520..524
FT /evidence="ECO:0007829|PDB:4G7N"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:4G7N"
FT TURN 534..536
FT /evidence="ECO:0007829|PDB:4G7N"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:4G7N"
FT HELIX 554..578
FT /evidence="ECO:0007829|PDB:4G7N"
FT STRAND 589..593
FT /evidence="ECO:0007829|PDB:4G7N"
FT STRAND 660..666
FT /evidence="ECO:0007829|PDB:5LHX"
FT TURN 667..669
FT /evidence="ECO:0007829|PDB:5LHX"
FT STRAND 670..675
FT /evidence="ECO:0007829|PDB:5LHX"
FT STRAND 680..684
FT /evidence="ECO:0007829|PDB:5LHX"
FT STRAND 689..692
FT /evidence="ECO:0007829|PDB:5LHX"
FT HELIX 695..697
FT /evidence="ECO:0007829|PDB:5LHX"
FT STRAND 701..704
FT /evidence="ECO:0007829|PDB:5LHX"
FT STRAND 710..713
FT /evidence="ECO:0007829|PDB:5LHX"
FT HELIX 723..727
FT /evidence="ECO:0007829|PDB:5LHX"
FT HELIX 730..738
FT /evidence="ECO:0007829|PDB:5LHX"
SQ SEQUENCE 769 AA; 85887 MW; F050BF60A5D94AA4 CRC64;
MLSNRAFGET IEDYEVQHLL GKGGFATVYK ARCLHTHQDV AIKMIDKKLI QGTGLTNRVR
QEVEIHSRLK HPSVLQLYTF FQDANYVYLV LELAHNGELH RYMNHIARPF TETEAASILK
QVVAGLLYLH SHNIMHRDIS LSNLLLSREM HVKIADFGLA TQLKRPDERH MTMCGTPNYI
SPEVVSRTSH GLPADVWSVG CMLYTLLVGR PPFETDAVQS TLNKVVMSEY IMPAHLSYEA
QDLINKLLKK LPHERITLEA VLCHPFMLKC SNGGHSAPGA LNVFSQSMES GDSGIITFAS
SDSRNSQQIR SVENSGPQQV LPQIREEFKQ VHHKLPYEQT GLFGQASTGL AEPNWPGAAK
SSAFCMEAGN VPNSKQASLK EDRISVPPLN TKRLLPTRYK TKNAIMSILR NGEVVLEFLK
FRPTYNEDRI NDICRISDDG QRIIIYQPDP GRGLPVREQP PDLQIPSGDC VYNYDNLPSK
HWKKYIYGAR FVGLVKSKTP KVTYFSTLGK CQLMETMTDF EIRFYSGAKL LKTPSEGLKV
YDRNGMLLSD YSCSESRSLI EHGNECFTHC VNISNALEVA QTKDNSCFPV TIGRRPITDV
QPAQRLDGLR DTTNIAFSTP KSNQGSINFS LSTISSTRNT SDFGTNCSRS NMLAAHQNIP
IKRINVPEIG IATELSHGVV QVQFYDGSVV SVIPSMQGGG ITYTQPNGTS THFGKGDDLP
FPVRDRVGQI PNIQLKLKTA PLLGSGRKTD YNNAMTPKTT TPYYNRMLL
//
