FER_DROME
ID FER_DROME Reviewed; 1325 AA.
AC P18106; Q27576; Q86P62; Q8INP1; Q8INP2; Q9TYI1; Q9VHE7; Q9VHE8;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 3.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Tyrosine-protein kinase Fer;
DE EC=2.7.10.2;
GN Name=FER {ECO:0000312|FlyBase:FBgn0000723};
GN Synonyms=fps {ECO:0000312|FlyBase:FBgn0000723},
GN Fps85D {ECO:0000312|FlyBase:FBgn0000723},
GN HD-179 {ECO:0000312|FlyBase:FBgn0000723};
GN ORFNames=CG8874 {ECO:0000312|FlyBase:FBgn0000723};
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] (ISOFORM B), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo, and Head;
RX PubMed=1898762; DOI=10.1128/mcb.11.1.226-239.1991;
RA Katzen A.L., Montarras D., Jackson J., Paulson R.F., Kornberg T.,
RA Bishop J.M.;
RT "A gene related to the proto-oncogene fps/fes is expressed at diverse times
RT during the life cycle of Drosophila melanogaster.";
RL Mol. Cell. Biol. 11:226-239(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND D), AND SUBCELLULAR LOCATION.
RC TISSUE=Embryo, and Head;
RX PubMed=9038371; DOI=10.1038/sj.onc.1200875;
RA Paulson R.F., Jackson J., Immergluck K., Bishop J.M.;
RT "The DFer gene of Drosophila melanogaster encodes two membrane-associated
RT proteins that can both transform vertebrate cells.";
RL Oncogene 14:641-652(1997).
RN [3]
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1191-1241.
RX PubMed=9731193; DOI=10.1006/bbrc.1998.9003;
RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.;
RT "Sampling the genomic pool of protein tyrosine kinase genes using the
RT polymerase chain reaction with genomic DNA.";
RL Biochem. Biophys. Res. Commun. 249:660-667(1998).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16831834; DOI=10.1242/dev.02467;
RA Murray M.J., Davidson C.M., Hayward N.M., Brand A.H.;
RT "The Fes/Fer non-receptor tyrosine kinase cooperates with Src42A to
RT regulate dorsal closure in Drosophila.";
RL Development 133:3063-3073(2006).
CC -!- FUNCTION: Tyrosine-protein kinase which is required during
CC embryogenesis for formation of the actin cable in leading edge cells of
CC the dorsal epidermis and for the timely progression of dorsal closure.
CC May play a role in regulation of adherens junctions and cell adhesion
CC through phosphorylation of the beta-catenin arm.
CC {ECO:0000269|PubMed:16831834}.
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=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9038371}; Peripheral
CC membrane protein {ECO:0000269|PubMed:9038371}. Cell junction, adherens
CC junction {ECO:0000269|PubMed:9038371}. Note=At stages 11-12 of
CC embryogenesis, localizes to adherens junctions in epidermal cells. At
CC stages 13-14, is no longer detected in the epidermal cell junctions
CC which border with the amnioserosa. {ECO:0000269|PubMed:16831834}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A;
CC IsoId=P18106-4; Sequence=Displayed;
CC Name=B; Synonyms=p92;
CC IsoId=P18106-1; Sequence=VSP_004988;
CC Name=C;
CC IsoId=P18106-3; Sequence=VSP_004987, VSP_004988;
CC Name=D; Synonyms=p45;
CC IsoId=P18106-2; Sequence=VSP_004986;
CC -!- TISSUE SPECIFICITY: Expressed in a subset of cells in the embryonic
CC central nervous system (CNS) (PubMed:16831834). In the embryo,
CC expressed in leading edge cells of the dorsal epidermis (at protein
CC level) (PubMed:16831834). Expressed in many tissues during embryonic
CC development, some expression is transient and absent from most of
CC nervous system (PubMed:1898762). In the embryo, strong expression in
CC the leading edge cells from late stage 13 and throughout dorsal closure
CC to the end of stage 15 (PubMed:16831834). In the embryonic CNS,
CC expressed in the midline glia from stage 13, and by stage 16 expressed
CC in a segmentally repeated subset of cells and in the dMP2 neurons
CC (PubMed:16831834). Larvae exhibit expression in neural tissues and
CC graded expression in all imaginal disks (PubMed:1898762). Pupal
CC expression is seen in muscles and varies during development
CC (PubMed:1898762). Expression in adults is strong in the retina and
CC present in ovaries, no expression is present in the adult brain
CC (PubMed:1898762). {ECO:0000269|PubMed:16831834,
CC ECO:0000269|PubMed:1898762}.
CC -!- DEVELOPMENTAL STAGE: Expressed during all stages of development.
CC {ECO:0000269|PubMed:1898762}.
CC -!- DISRUPTION PHENOTYPE: 53% of mutants die during embryogenesis with the
CC remainder dying during larval and pupal development. In embryos the
CC rate of dorsal closure is reduced and complete closure is delayed until
CC after stage 16. During dorsal closure, filopodia are normal but the
CC actomyosin cable is reduced and the leading edge cells have an
CC irregular morphology. After dorsal closure, a very small percentage of
CC embryos display a small anterior hole in their cuticle. Reduced
CC phosphorylation of arm. {ECO:0000269|PubMed:16831834}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fes/fps subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA93470.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA37036.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X52844; CAA37036.1; ALT_FRAME; mRNA.
DR EMBL; U50450; AAA93470.1; ALT_FRAME; mRNA.
DR EMBL; AE014297; AAF54366.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54367.3; -; Genomic_DNA.
DR EMBL; AE014297; AAN13420.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13421.1; -; Genomic_DNA.
DR EMBL; BT003462; AAO39465.1; -; mRNA.
DR EMBL; AJ002916; CAA05751.1; -; Genomic_DNA.
DR PIR; A39670; OKFFPS.
DR RefSeq; NP_524288.3; NM_079564.4. [P18106-4]
DR RefSeq; NP_731341.1; NM_169274.2. [P18106-1]
DR RefSeq; NP_731342.1; NM_169275.2. [P18106-3]
DR RefSeq; NP_731343.1; NM_169276.2. [P18106-2]
DR AlphaFoldDB; P18106; -.
DR SMR; P18106; -.
DR BioGRID; 66283; 8.
DR IntAct; P18106; 11.
DR STRING; 7227.FBpp0081530; -.
DR PaxDb; P18106; -.
DR PRIDE; P18106; -.
DR EnsemblMetazoa; FBtr0082051; FBpp0081529; FBgn0000723. [P18106-1]
DR EnsemblMetazoa; FBtr0082052; FBpp0081530; FBgn0000723. [P18106-4]
DR EnsemblMetazoa; FBtr0082053; FBpp0081531; FBgn0000723. [P18106-3]
DR EnsemblMetazoa; FBtr0082054; FBpp0081532; FBgn0000723. [P18106-2]
DR GeneID; 41118; -.
DR KEGG; dme:Dmel_CG8874; -.
DR CTD; 2241; -.
DR FlyBase; FBgn0000723; FER.
DR VEuPathDB; VectorBase:FBgn0000723; -.
DR eggNOG; KOG0194; Eukaryota.
DR GeneTree; ENSGT00940000168715; -.
DR HOGENOM; CLU_005265_1_0_1; -.
DR InParanoid; P18106; -.
DR PhylomeDB; P18106; -.
DR BRENDA; 2.7.10.2; 1994.
DR Reactome; R-DME-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-DME-399956; CRMPs in Sema3A signaling.
DR SignaLink; P18106; -.
DR BioGRID-ORCS; 41118; 0 hits in 3 CRISPR screens.
DR ChiTaRS; FER; fly.
DR GenomeRNAi; 41118; -.
DR PRO; PR:P18106; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0000723; Expressed in crop (Drosophila) and 26 other tissues.
DR ExpressionAtlas; P18106; baseline and differential.
DR Genevisible; P18106; DM.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; ISM:FlyBase.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:FlyBase.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0051017; P:actin filament bundle assembly; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007391; P:dorsal closure; IGI:FlyBase.
DR GO; GO:0046664; P:dorsal closure, amnioserosa morphology change; IMP:FlyBase.
DR GO; GO:0007394; P:dorsal closure, elongation of leading edge cells; IMP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd10361; SH2_Fps_family; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR035849; Fes/Fps/Fer_SH2.
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; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell junction; Coiled coil;
KW Developmental protein; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; SH2 domain; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..1325
FT /note="Tyrosine-protein kinase Fer"
FT /id="PRO_0000088095"
FT DOMAIN 1..264
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 960..1051
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 1063..1318
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 453..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..928
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1185
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 1069..1077
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1092
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1213
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..932
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|PubMed:9038371"
FT /id="VSP_004986"
FT VAR_SEQ 1..329
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_004987"
FT VAR_SEQ 426..946
FT /note="Missing (in isoform B and isoform C)"
FT /evidence="ECO:0000303|PubMed:1898762,
FT ECO:0000303|PubMed:9038371"
FT /id="VSP_004988"
FT CONFLICT 58
FT /note="I -> T (in Ref. 1; CAA37036)"
FT /evidence="ECO:0000305"
FT CONFLICT 230..248
FT /note="ILQEAAQYGDLTADKYKEI -> TCRRRPSMATSRPTSTRRF (in Ref.
FT 1; CAA37036)"
FT /evidence="ECO:0000305"
FT CONFLICT 320..341
FT /note="GAVRDCQEKQMKMIEHVNGGSP -> EPSGLPGEADEDDRACEWWLA (in
FT Ref. 1; CAA37036)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="S -> D (in Ref. 1; CAA37036)"
FT /evidence="ECO:0000305"
FT CONFLICT 940
FT /note="V -> W (in Ref. 2; AAA93470)"
FT /evidence="ECO:0000305"
FT CONFLICT 1050
FT /note="P -> T (in Ref. 1; CAA37036 and 2; AAA93470)"
FT /evidence="ECO:0000305"
FT CONFLICT 1161
FT /note="Q -> E (in Ref. 1; CAA37036 and 2; AAA93470)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1325 AA; 150263 MW; 7DFC98D9B9776E78 CRC64;
MGFSSALQSR AAHEALIVRQ DAELRLMETM KRSIQMKAKC DKEYAISLTA VAQQGLKIDR
ADEMQGSLIS KSWRSYMDEL DHQAKQFKFN AEQLEVVCDK LTHLSQDKRK ARKAYQEEHA
KIAARLNHLT DEVVRKKSEY QKHLEGYKAL RTRFEENYIK APSRSGRKLD DVRDKYQKAC
RKLHLTHNEY VLSITEAIEV EKDFRNVLLP GLLEHQQSVQ ESFILLWRNI LQEAAQYGDL
TADKYKEIQK RIDTVIGSIN PTEEYGEFTE KYKTSPTTPL LFQFDETLIQ DIPGKLQSST
LTVDNLTVDW LRNRLQELEG AVRDCQEKQM KMIEHVNGGS PVANGSIISN GSNTSNGIQS
NKDSLCRQSK DLNALRCQEK QKQKLVDMIK CALNEVGCEE LPSGCDDDLT LEQNFIENGY
NNEQQRSNST SSPGLGIMNE LMRRGGVLTL LRGRGRHFKR KSTPQPATPM TRSRQGRFNK
LQPRSQSLGS LSVIRDGNGP SPARYEPITN HRLRQAASVH YLGEEIATSS TNPPDLTRLR
RTQCSMLCLG EDEEPVVLAS PAPLTQLTAA VLTNTNNNHI YADLELDKKK DTSPSPECKG
EQIQPKKEQI RIEINQTAPQ NSIDAHLDRI DELNRVLDDR LKRTLQPSDD VNAIESAEEN
HIQTRKLAKD PDSQTKRSSS SSSECRSSKD TSHSKKRSLS FSQKSISNIF SNLKEFSKSP
LVRMGKNHIL NEEQDAKRTQ PSQHHHSSGS DCPTNSSSSS SNNNNNNKNT SSNSNHSASQ
STIITSTITT TITTTTTTTP SKENSRLKFK VPKIQKKSKA IRNTFRSKLL NFQLKRSKPC
KQCTKRRRIH PSKSVFDFAK EFEVEQPAGS AADEQFCNCP PAGQKPVKPS VQISGHKDHP
FESSSGELDE NSDRDIDNDE EEEDSASDDV LSMKDHCYCV PSLAASISLS TNRPLYEEEW
FHGVLPREEV VRLLNNDGDF LVRETIRNEE SQIVLSVCWN GHKHFIVQTT GEGNFRFEGP
PFASIQELIM HQYHSELPVT VKSGAILRRP VCRERWELSN DDVVLLERIG RGNFGDVYKA
KLKSTKLDVA VKTCRMTLPD EQKRKFLQEG RILKQYDHPN IVKLIGICVQ KQPIMIVMEL
VLGGSLLTYL RKNSNGLTTR QQMGMCRDAA AGMRYLESKN CIHRDLAARN CLVDLEHSVK
ISDFGMSREE EEYIVSDGMK QIPVKWTAPE ALNFGKYTSL CDVWSYGILM WEIFSKGDTP
YSGMTNSRAR ERIDTGYRMP TPKSTPEEMY RLMLQCWAAD AESRPHFDEI YNVVDALILR
LDNSH
