NEDD4_DROME
ID NEDD4_DROME Reviewed; 1007 AA.
AC Q9VVI3; Q7KUR2; Q8IQR6; Q95R64; Q95TQ0; Q95ZF9;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=E3 ubiquitin-protein ligase Nedd-4;
DE Short=DNedd4;
DE EC=2.3.2.26 {ECO:0000250|UniProtKB:P46934};
DE AltName: Full=HECT-type E3 ubiquitin transferase NEDD4;
GN Name=Nedd4; ORFNames=CG7555;
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 1), FUNCTION, INTERACTION WITH COMM,
RP MUTAGENESIS OF CYS-974, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=12165468; DOI=10.1016/s0896-6273(02)00795-x;
RA Myat A., Henry P., McCabe V., Flintoft L., Rotin D., Tear G.;
RT "Drosophila Nedd4, a ubiquitin ligase, is recruited by Commissureless to
RT control cell surface levels of the roundabout receptor.";
RL Neuron 35:447-459(2002).
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, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 98-1007 (ISOFORM 2).
RC STRAIN=Berkeley; TISSUE=Embryo;
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, INTERACTION WITH N, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15620649; DOI=10.1016/j.cub.2004.12.028;
RA Sakata T., Sakaguchi H., Tsuda L., Higashitani A., Aigaki T., Matsuno K.,
RA Hayashi S.;
RT "Drosophila Nedd4 regulates endocytosis of notch and suppresses its ligand-
RT independent activation.";
RL Curr. Biol. 14:2228-2236(2004).
RN [6]
RP FUNCTION.
RX PubMed=15657595; DOI=10.1038/nn1388;
RA Keleman K., Ribeiro C., Dickson B.J.;
RT "Comm function in commissural axon guidance: cell-autonomous sorting of
RT Robo in vivo.";
RL Nat. Neurosci. 8:156-163(2005).
RN [7]
RP STRUCTURE BY NMR OF 526-566 IN COMPLEX WITH COMM PY-MOTIF 2.
RX PubMed=16531238; DOI=10.1016/j.str.2005.11.018;
RA Kanelis V., Bruce M.C., Skrynnikov N.R., Rotin D., Forman-Kay J.D.;
RT "Structural determinants for high-affinity binding in a Nedd4 WW3* domain-
RT Comm PY motif complex.";
RL Structure 14:543-553(2006).
CC -!- FUNCTION: Essential E3 ubiquitin-protein ligase which accepts ubiquitin
CC from an E2 ubiquitin-conjugating enzyme in the form of a thioester and
CC then directly transfers the ubiquitin to targeted substrates. Down-
CC regulates Notch/N signaling pathway by promoting Notch ubiquitination,
CC endocytosis and degradation. {ECO:0000269|PubMed:12165468,
CC ECO:0000269|PubMed:15620649, ECO:0000269|PubMed:15657595}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000250|UniProtKB:P46934};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts (via WW2 domain) with comm (via PY-motifs)
CC (PubMed:12165468, PubMed:16531238). Interacts with N (PubMed:15620649).
CC {ECO:0000269|PubMed:12165468, ECO:0000269|PubMed:15620649,
CC ECO:0000269|PubMed:16531238}.
CC -!- INTERACTION:
CC Q9VVI3; Q24139: comm; NbExp=3; IntAct=EBI-498113, EBI-118294;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15620649}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9VVI3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9VVI3-2; Sequence=VSP_015440, VSP_015441, VSP_015443;
CC Name=3;
CC IsoId=Q9VVI3-3; Sequence=VSP_015442;
CC Name=4;
CC IsoId=Q9VVI3-4; Sequence=VSP_015440, VSP_015441, VSP_015442;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12165468, ECO:0000269|PubMed:15620649}.
CC -!- CAUTION: According to some authors (PubMed:12165468) it is involved in
CC axon guidance by promoting ubiquitination of comm and subsequent
CC endocytosis of the comm/robo complex. However, according to others
CC (PubMed:15657595), it is not the case. {ECO:0000305|PubMed:12165468,
CC ECO:0000305|PubMed:15657595}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13848.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ278468; CAC42101.1; -; mRNA.
DR EMBL; AE014296; AAF49328.2; -; Genomic_DNA.
DR EMBL; AE014296; AAS64973.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11694.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11695.1; -; Genomic_DNA.
DR EMBL; AY061595; AAL29143.1; -; mRNA.
DR EMBL; AY058619; AAL13848.1; ALT_INIT; mRNA.
DR RefSeq; NP_648993.1; NM_140736.3. [Q9VVI3-1]
DR RefSeq; NP_730282.1; NM_168736.4. [Q9VVI3-3]
DR RefSeq; NP_730283.1; NM_168737.2. [Q9VVI3-2]
DR RefSeq; NP_996116.1; NM_206394.2.
DR PDB; 2EZ5; NMR; -; W=526-566.
DR PDBsum; 2EZ5; -.
DR AlphaFoldDB; Q9VVI3; -.
DR SMR; Q9VVI3; -.
DR BioGRID; 65246; 15.
DR DIP; DIP-29040N; -.
DR IntAct; Q9VVI3; 7.
DR STRING; 7227.FBpp0289746; -.
DR TCDB; 8.A.30.1.5; the nedd4-family interacting protein-2 (nedd4) family.
DR PaxDb; Q9VVI3; -.
DR DNASU; 39958; -.
DR EnsemblMetazoa; FBtr0299645; FBpp0288920; FBgn0259174. [Q9VVI3-2]
DR EnsemblMetazoa; FBtr0300519; FBpp0289746; FBgn0259174. [Q9VVI3-1]
DR EnsemblMetazoa; FBtr0300520; FBpp0289747; FBgn0259174. [Q9VVI3-3]
DR GeneID; 39958; -.
DR KEGG; dme:Dmel_CG42279; -.
DR UCSC; CG42279-RC; d. melanogaster. [Q9VVI3-1]
DR CTD; 4734; -.
DR FlyBase; FBgn0259174; Nedd4.
DR VEuPathDB; VectorBase:FBgn0259174; -.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00940000168483; -.
DR InParanoid; Q9VVI3; -.
DR PhylomeDB; Q9VVI3; -.
DR Reactome; R-DME-1253288; Downregulation of ERBB4 signaling.
DR Reactome; R-DME-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-DME-8948747; Regulation of PTEN localization.
DR Reactome; R-DME-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9VVI3; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 39958; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Nedd4; fly.
DR EvolutionaryTrace; Q9VVI3; -.
DR GenomeRNAi; 39958; -.
DR PRO; PR:Q9VVI3; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0259174; Expressed in adult Malpighian tubule (Drosophila) and 27 other tissues.
DR ExpressionAtlas; Q9VVI3; baseline and differential.
DR Genevisible; Q9VVI3; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0071212; C:subsynaptic reticulum; IMP:FlyBase.
DR GO; GO:0017022; F:myosin binding; IPI:FlyBase.
DR GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IDA:FlyBase.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:FlyBase.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; NAS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0016199; P:axon midline choice point recognition; IMP:UniProtKB.
DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:BHF-UCL.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IDA:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IGI:FlyBase.
DR GO; GO:2000650; P:negative regulation of sodium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:1905306; P:positive regulation of cardiac myofibril assembly; IMP:BHF-UCL.
DR GO; GO:1905062; P:positive regulation of cardioblast proliferation; IMP:BHF-UCL.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:FlyBase.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:FlyBase.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IMP:FlyBase.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IMP:FlyBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase.
DR GO; GO:0031623; P:receptor internalization; IMP:UniProtKB.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IBA:GO_Central.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 3.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 3.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51045; SSF51045; 3.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 3.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Notch signaling pathway; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..1007
FT /note="E3 ubiquitin-protein ligase Nedd-4"
FT /id="PRO_0000120322"
FT DOMAIN 52..175
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 246..279
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 529..562
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 580..613
FT /note="WW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 672..1006
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 15..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 974
FT /note="Glycyl thioester intermediate"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_015440"
FT VAR_SEQ 39..63
FT /note="SVAGQQQTRQEFGNGYTPRRSLAAV -> MAESTTTSPSVTSEDGQIHGCNN
FT SD (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_015441"
FT VAR_SEQ 314..486
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_015442"
FT VAR_SEQ 375..387
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_015443"
FT MUTAGEN 974
FT /note="C->A: Abolishes activity; no effect on interaction
FT with comm."
FT /evidence="ECO:0000269|PubMed:12165468"
FT CONFLICT 185..188
FT /note="RSVG -> S (in Ref. 2; AAS64973)"
FT /evidence="ECO:0000305"
FT STRAND 535..539
FT /evidence="ECO:0007829|PDB:2EZ5"
FT STRAND 543..549
FT /evidence="ECO:0007829|PDB:2EZ5"
FT TURN 550..553
FT /evidence="ECO:0007829|PDB:2EZ5"
FT STRAND 554..558
FT /evidence="ECO:0007829|PDB:2EZ5"
FT TURN 560..562
FT /evidence="ECO:0007829|PDB:2EZ5"
SQ SEQUENCE 1007 AA; 114875 MW; DC5994BD19543760 CRC64;
MSARSSGLVA AAALPVPSSS SSVAGGDVPR PPPRRRAASV AGQQQTRQEF GNGYTPRRSL
AAVNDSGDSC HLRIVVLTGQ SLAKKDIFGA SDPYVRIDLN TINGDINIDS VLTKTKKKTL
NPTWNEEFIF RVKPSEHKLV FQVFDENRLT RDDFLGMVEL TLVNLPTEQE GRTIGEQSYT
LRPRRSVGAK SRIKGTLRIY HAFIRETREQ SEPSSGNSDG EWEHVEATNA GETSAQPHPF
PTGGHDALPA GWEERQDANG RTYYVNHTAR TTQWDRPTVL NSHSSQSTDD QLASDFQRRF
HISVDDTESG RSADSISHNS IEDNNNAAGL AYTPKTAATS SAPPNTPTNN NGILAQIAMQ
YRAEEDQDPT VDHTSFVYNS LRHPVAHRQP EISATSLQND LRPVREAPGV PDIAITNPFT
RRAAGNMAGG AGWQQERRRQ QMQLHIQQHQ QRQQQQQQNR ILLDVDHRQQ EPQHRGQRHQ
QQHRPSNEDT DHTDSHNPSD ISAPSTRRNS EEDNAAVPPM EQNTGGEEEP LPPRWSMQVA
PNGRTFFIDH ASRRTTWIDP RNGRASPMPN QTRRVEDDLG PLPEGWEERV HTDGRVFYID
HNTRTTQWED PRLSNPNIAG QAVPYSRDYK QKYEYFKSHI RKPTNVPNKF EIRIRRTSIL
EDSYRIISSV TKTDLLKTKL WVEFEGETGL DYGGLAREWF YLLSKEMFNP YYGLFEYSAM
DNYTLQINNG SGLCNEEHLS YFKFIGRIAG MAVYHGKLLD AFFIRPFYKM MLQKPIDLKD
MESVDTEYYN SLMWIKENDP RILELTFCLD EDVFGQKSQH ELKPGGANID VTNENKDEYI
KLVIEWRFVA RVKEQMSSFL DGFGSIIPLN LIKIFDEHEL ELLMCGIQNI DVKDWRENTL
YKGDYHMNHI IIQWFWRAVL SFSNEMRSRL LQFVTGTSRV PMNGFKELYG SNGPQMFTIE
KWGTPNNFPR AHTCFNRLDL PPYEGYLQLK DKLIKAIEGS QGFAGVD
