FYV1_DROME
ID FYV1_DROME Reviewed; 1809 AA.
AC O96838; A4UZM3; Q8SZX0; Q95SX9; Q9V886;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Putative 1-phosphatidylinositol 3-phosphate 5-kinase;
DE Short=Phosphatidylinositol 3-phosphate 5-kinase;
DE EC=2.7.1.150 {ECO:0000305|PubMed:16837550};
DE AltName: Full=Type III PIP kinase;
DE Short=PIPkin-III;
GN Name=fab1; ORFNames=CG6355;
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:AAL39881.1};
RN [1] {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 [2]
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 [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R {ECO:0000269|PubMed:10731137};
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 979-1809.
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569},
RC Larva {ECO:0000269|PubMed:12537569}, and
RC Pupae {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, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16837550; DOI=10.1091/mbc.e06-03-0239;
RA Rusten T.E., Rodahl L.M.W., Pattni K., Englund C., Samakovlis C., Dove S.,
RA Brech A., Stenmark H.;
RT "Fab1 phosphatidylinositol 3-phosphate 5-kinase controls trafficking but
RT not silencing of endocytosed receptors.";
RL Mol. Biol. Cell 17:3989-4001(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-755; THR-760 AND SER-1530,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Regulates both the synthesis and turnover of
CC phosphatidylinositol 3,5-bisphosphate (1,2-diacyl-sn-glycero-3-phospho-
CC (1D-myo-inositol-3,5-bisphosphate) or PtdIns(3,5)P2) (PubMed:16837550).
CC Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate (1,2-
CC diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)) on the fifth
CC hydroxyl of the myo-inositol ring, to form PtdIns(3,5)P2
CC (PubMed:16837550). Required for endocytic-vacuolar pathway and nuclear
CC migration. Has a role at a late stage in endosome-related membrane
CC trafficking, at a point when signal termination has occurred. Is not
CC required for receptor silencing. {ECO:0000269|PubMed:16837550}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:13609,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57923,
CC ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.150;
CC Evidence={ECO:0000305|PubMed:16837550};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13610;
CC Evidence={ECO:0000305|PubMed:16837550};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:16837550}.
CC Note=Mainly associated with membranes of the late endocytic pathway.
CC -!- DISRUPTION PHENOTYPE: Flies contain undetectable phosphatidylinositol
CC 3,5-bisphosphate levels, show profound increases in cell and organ
CC size, and die at the pupal stage. Mutant larvae contain highly enlarged
CC multivesicular bodies and late endosomes that are inefficiently
CC acidified. Even though endocytic receptor trafficking is impaired in
CC fab1 mutants, Notch, Wingless, and Dpp signaling is unaffected.
CC {ECO:0000269|PubMed:16837550}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL25475.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL39881.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA22949.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF57789.1; -; Genomic_DNA.
DR EMBL; AE013599; AAS64818.1; -; Genomic_DNA.
DR EMBL; AL035311; CAA22949.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY060436; AAL25475.1; ALT_INIT; mRNA.
DR EMBL; AY069736; AAL39881.1; ALT_INIT; mRNA.
DR PIR; T13576; T13576.
DR RefSeq; NP_611269.1; NM_137425.4.
DR RefSeq; NP_995880.1; NM_206158.3.
DR AlphaFoldDB; O96838; -.
DR SMR; O96838; -.
DR BioGRID; 62718; 1.
DR IntAct; O96838; 2.
DR STRING; 7227.FBpp0088523; -.
DR iPTMnet; O96838; -.
DR PaxDb; O96838; -.
DR PRIDE; O96838; -.
DR EnsemblMetazoa; FBtr0089554; FBpp0088523; FBgn0028741.
DR EnsemblMetazoa; FBtr0089555; FBpp0088952; FBgn0028741.
DR GeneID; 37033; -.
DR KEGG; dme:Dmel_CG6355; -.
DR CTD; 37033; -.
DR FlyBase; FBgn0028741; fab1.
DR VEuPathDB; VectorBase:FBgn0028741; -.
DR eggNOG; KOG0230; Eukaryota.
DR GeneTree; ENSGT00940000156307; -.
DR HOGENOM; CLU_000480_2_1_1; -.
DR InParanoid; O96838; -.
DR OMA; HRQYVHG; -.
DR PhylomeDB; O96838; -.
DR SignaLink; O96838; -.
DR BioGRID-ORCS; 37033; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37033; -.
DR PRO; PR:O96838; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0028741; Expressed in saliva-secreting gland and 10 other tissues.
DR Genevisible; O96838; DM.
DR GO; GO:0005768; C:endosome; IDA:FlyBase.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0012506; C:vesicle membrane; ISS:UniProtKB.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IMP:FlyBase.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; IMP:FlyBase.
DR GO; GO:0008333; P:endosome to lysosome transport; IMP:FlyBase.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IMP:FlyBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd17300; PIPKc_PIKfyve; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.800.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR044769; PIKfyve_PIPKc.
DR InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Endosome; Kinase; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1809
FT /note="Putative 1-phosphatidylinositol 3-phosphate 5-
FT kinase"
FT /id="PRO_0000185454"
FT DOMAIN 323..399
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066,
FT ECO:0000305"
FT DOMAIN 1473..1796
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT ZN_FING 186..246
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091,
FT ECO:0000305"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1269..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1399..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1552..1809
FT /note="Catalytic"
FT COMPBIAS 84..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 760
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1530
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 1403
FT /note="A -> ASSASA (in Ref. 3; CAA22949)"
FT /evidence="ECO:0000305"
FT CONFLICT 1420
FT /note="V -> I (in Ref. 3; CAA22949)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1809 AA; 204635 MW; B5A111FAD317B05F CRC64;
MTSNNQNNSS SHQHLHSPSK LTEFARNFED KPESLFGRVV NKIQNVYNQS YNTVNDISSG
SSSSSSTQPV QVVGKSQFFS DSQTSTAEIA DVETSSQSSV RPQPPTTLSI RTNSETRGTS
TSSNTAAEDS ETSDRVETLP LPTSEANQGR TVSNVLKHIS NIVATKNNND LRNYKDTELQ
RFWMPDSKAK ECYDCSQKFS TFRRKHHCRL CGQIFCSKCC NQVVPGMIIR CDGDLKVCNY
CSKIVLTFLK SSSSEMGQDM QELQQHLSNK LEVQDSGSSL AKHPQMQRAP LPRKTSVGYQ
EERFSSHPTY TTLSIDDRKN ILQQSNSLIT LHEEMQRDLP AQNCGQRLIE FLNSNNKSAN
EVQAVAILNA MLAAGFLEPI VPDPEQMDFD SSLHYKFSKS SSSDTSRTMS PQFEANPHAE
PQPPKSMDQS AEEKEKELEN ELENDRCYTT ATSKLLASYC EHEEQLLAQM LRAHNLDQEW
DKVLQMLCST AANHFKPEHC SNDLMDIRNY VNFKKVPGGR RKDSKIVHGV AFSKNVAHKD
MATHVPFPRI LLLQCPIVYE RIEGKFVTIE TVLLQEKEYL RNVCARIMSF KPNVVLVHKN
VAGIAQDLLR SYEVTLVLDV KLSVMERLSR TLQCDIVSSI ESNITMPKLG YCNDFYIRNY
NGKTLMFFEK LTNPRGYTCL LRGGSNAELT RVKRVASALL FARYNWRLEM SFLLNEFAQP
LSPKPSIFDS KETSPKTETE AELRSKRPII LERKSEDKIT TIVSENVSDF TDPLRASQAE
ALSTSPCAPP VVEALAVEPR YDNRFRTALS STLLSVSPFL TFPLPYLETE QGRKCKLRKL
FPAELYFSKQ WSRTGLERPD SMGDGEAGKS EPGNKENQMQ LLPAHDFVLM KITAPASSRD
IQSKLAEFRS FGGRLPKGKA PMLRPKKKNA EVIQRPQKVS EEQLYKDALD PQNHQRLPVL
FCSFHYNPKG VSSFCKLPML LDMKFYGQYD IMLEQFLQRY CCLFNSMCPS CNLPMLGHVR
RYVHSLGCVH VYLTEDLTRS DPTRIYFTSW CSICNATTPT IPLSDAAKCL SLAKYLEMRF
HGHAYKRRPP STDAEQGGTV CEHSLHRDYV HHFSFRGVGA KFQYTPVEVW ETDLPSLTVQ
LDLPQPFQSA QVQEEIKNFS IKGHEVYNRI HERIADLATE EENSPLVQHL KTMLTHDQFI
FKQKIEIVHT LLTDNRATAY DTSDALAMAR RALAESIELW GPRLQEIEKL TAKQAHHIDS
GTICTEELRP EQVQTADSSK VTTSSLPKEN DPLECPSEDT ETGASNSQTV LDKNFSIDQM
LASTVNVYSD KKSIRKILTQ LLPSGNQVNP LQSPFPAQDH LTLPLGSIPI HVRETDLSSV
IAYSLTSMDY QKAIDEAEAN SNAAHSSPQL KRKIPLAESV SDAEDSPSLS RTSSNTSAAP
NASVPSPATA ASESEEKSKE RIKQPPSPHI TLAFQDHSCQ FQCKIYFARE FDAMRSKSLK
PPKLDKSLYR RLEKSKMREE LRISQSRTGS EMELVRKPSD VGAPRTTEDD SNQEEDARIA
LARSLCKSVQ WEARGGKSGS RFCKTLDDRF VLKEMNSRDM TIFEPFAPKY FEYIDRCQQQ
QQPTLLAKIF GVFRVSVKKK DSFVERSVMV MENLFYGCNI ENKFDLKGSE RNRLVDPSNQ
QGEIVLLDEN LVQMSWSKPL YVLSHSKTVL RDAIQRDSSF LEKNLVMDYS LLVGLDKKNG
VLVLGIIDYI RTFTLDKRVE SIIKGSGILG GKGKDPTVVN PERYKQRFID AMDRYFLTVP
DRWEGLSKV
