FAT_DROME
ID FAT_DROME Reviewed; 5147 AA.
AC P33450; Q9VQX5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Cadherin-related tumor suppressor;
DE AltName: Full=Protein fat;
DE Contains:
DE RecName: Full=Ft-mito {ECO:0000305|PubMed:25215488};
DE Flags: Precursor;
GN Name=ft {ECO:0000312|FlyBase:FBgn0001075};
GN ORFNames=CG3352 {ECO:0000312|FlyBase:FBgn0001075};
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 [GENOMIC DNA].
RX PubMed=1959133; DOI=10.1016/0092-8674(91)90359-7;
RA Mahoney P.A., Weber U., Onofrechuk P., Biessmann H., Bryant P.J.,
RA Goodman C.S.;
RT "The fat tumor suppressor gene in Drosophila encodes a novel member of the
RT cadherin gene superfamily.";
RL Cell 67:853-868(1991).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11893338; DOI=10.1016/s0092-8674(02)00658-x;
RA Yang C.H., Axelrod J.D., Simon M.A.;
RT "Regulation of Frizzled by fat-like cadherins during planar polarity
RT signaling in the Drosophila compound eye.";
RL Cell 108:675-688(2002).
RN [5]
RP FUNCTION.
RX PubMed=12540853; DOI=10.1038/nature01366;
RA Ma D., Yang C.H., McNeill H., Simon M.A., Axelrod J.D.;
RT "Fidelity in planar cell polarity signalling.";
RL Nature 421:543-547(2003).
RN [6]
RP FUNCTION.
RX PubMed=15240556; DOI=10.1242/dev.01254;
RA Matakatsu H., Blair S.S.;
RT "Interactions between Fat and Dachsous and the regulation of planar cell
RT polarity in the Drosophila wing.";
RL Development 131:3785-3794(2004).
RN [7]
RP FUNCTION.
RX PubMed=15548581; DOI=10.1242/dev.01550;
RA Simon M.A.;
RT "Planar cell polarity in the Drosophila eye is directed by graded Four-
RT jointed and Dachsous expression.";
RL Development 131:6175-6184(2004).
RN [8]
RP DOMAIN.
RX PubMed=16687445; DOI=10.1242/dev.02401;
RA Matakatsu H., Blair S.S.;
RT "Separating the adhesive and signaling functions of the Fat and Dachsous
RT protocadherins.";
RL Development 133:2315-2324(2006).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16996265; DOI=10.1016/j.cub.2006.09.005;
RA Willecke M., Hamaratoglu F., Kango-Singh M., Udan R., Chen C.L., Tao C.,
RA Zhang X., Halder G.;
RT "The fat cadherin acts through the hippo tumor-suppressor pathway to
RT regulate tissue size.";
RL Curr. Biol. 16:2090-2100(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4843; SER-5054 AND SER-5061,
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).
RN [11]
RP PHOSPHORYLATION.
RX PubMed=18635802; DOI=10.1126/science.1158159;
RA Ishikawa H.O., Takeuchi H., Haltiwanger R.S., Irvine K.D.;
RT "Four-jointed is a Golgi kinase that phosphorylates a subset of cadherin
RT domains.";
RL Science 321:401-404(2008).
RN [12]
RP PHOSPHORYLATION, AND CLEAVAGE.
RX PubMed=19574458; DOI=10.1073/pnas.0811540106;
RA Feng Y., Irvine K.D.;
RT "Processing and phosphorylation of the Fat receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:11989-11994(2009).
RN [13]
RP FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-273.
RX PubMed=20434335; DOI=10.1016/j.cub.2010.04.016;
RA Simon M.A., Xu A., Ishikawa H.O., Irvine K.D.;
RT "Modulation of fat:dachsous binding by the cadherin domain kinase four-
RT jointed.";
RL Curr. Biol. 20:811-817(2010).
RN [14]
RP FUNCTION.
RX PubMed=23667559; DOI=10.1371/journal.pone.0062998;
RA Zhao X., Yang C.H., Simon M.A.;
RT "The Drosophila Cadherin Fat regulates tissue size and planar cell polarity
RT through different domains.";
RL PLoS ONE 8:E62998-E62998(2013).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, CLEAVAGE, DISRUPTION PHENOTYPE, AND
RP INTERACTION WITH ATPSYNC AND ND-24.
RX PubMed=25215488; DOI=10.1016/j.cell.2014.07.036;
RA Sing A., Tsatskis Y., Fabian L., Hester I., Rosenfeld R., Serricchio M.,
RA Yau N., Bietenhader M., Shanbhag R., Jurisicova A., Brill J.A.,
RA McQuibban G.A., McNeill H.;
RT "The atypical cadherin fat directly regulates mitochondrial function and
RT metabolic state.";
RL Cell 158:1293-1308(2014).
RN [16]
RP SUBCELLULAR LOCATION, INTERACTION WITH FBXL7, AND MUTAGENESIS OF THR-4854.
RX PubMed=25107277; DOI=10.7554/elife.03383;
RA Bosch J.A., Sumabat T.M., Hafezi Y., Pellock B.J., Gandhi K.D.,
RA Hariharan I.K.;
RT "The Drosophila F-box protein Fbxl7 binds to the protocadherin fat and
RT regulates Dachs localization and Hippo signaling.";
RL Elife 3:E03383-E03383(2014).
CC -!- FUNCTION: Involved in regulation of planar cell polarity in the
CC compound eye where it is required for correct specification of the R3
CC and R4 photoreceptor cells by regulating Fz activity in the R3/R4
CC precursor cells (PubMed:11893338). This is likely to occur through
CC creation of an ft gradient so that the equatorial R3/R4 precursor cell
CC has a higher level of ft function than its polar neighbor
CC (PubMed:15548581). Also required for planar cell polarity of wing hairs
CC (PubMed:12540853, PubMed:15240556). Mediates heterophilic cell adhesion
CC in vitro and is required to stabilize ds on the cell surface
CC (PubMed:15240556). Involved in regulation of eye imaginal disk size
CC (PubMed:23667559). Upstream component of the Hippo pathway where it is
CC likely to act as a cell surface receptor involved in regulation of
CC tissue size and is required for the localization and stability of ex
CC (PubMed:16996265). Probably acts as a cell surface receptor for ds
CC (PubMed:20434335). {ECO:0000269|PubMed:11893338,
CC ECO:0000269|PubMed:12540853, ECO:0000269|PubMed:15240556,
CC ECO:0000269|PubMed:15548581, ECO:0000269|PubMed:16996265,
CC ECO:0000269|PubMed:20434335, ECO:0000269|PubMed:23667559}.
CC -!- FUNCTION: [Ft-mito]: Regulates mitochondrial electron transport chain
CC integrity and promotes oxidative phosphorylation.
CC {ECO:0000269|PubMed:25215488}.
CC -!- SUBUNIT: Interacts with Fbxl7 (PubMed:25107277). Ft-mito interacts with
CC NADH dehydrogenase subunit ND-24 and with ATP synthase subunit ATPsynC
CC (PubMed:25215488). {ECO:0000269|PubMed:25107277,
CC ECO:0000269|PubMed:25215488}.
CC -!- INTERACTION:
CC P33450; Q6NN09: ATPsynC; NbExp=2; IntAct=EBI-135374, EBI-153383;
CC P33450; Q8IQA6: Gug; NbExp=3; IntAct=EBI-135374, EBI-153156;
CC P33450; Q9VX36: ND-24; NbExp=4; IntAct=EBI-135374, EBI-189196;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11893338};
CC Single-pass type I membrane protein {ECO:0000250}. Apical cell membrane
CC {ECO:0000269|PubMed:25107277}.
CC -!- SUBCELLULAR LOCATION: [Ft-mito]: Mitochondrion
CC {ECO:0000269|PubMed:25215488}.
CC -!- DOMAIN: The extracellular domain is required for correct subcellular
CC localization and for cell adhesion. {ECO:0000269|PubMed:16687445}.
CC -!- DOMAIN: The intracellular domain is sufficient for viability, growth
CC control and planar cell polarity. {ECO:0000269|PubMed:16687445}.
CC -!- PTM: Phosphorylated by fj on Ser/Thr of cadherin domains
CC (PubMed:18635802). Phosphorylation by fj enhances binding to ds
CC (PubMed:20434335). Phosphorylated in the cytoplasmic domain in a dco-
CC dependent manner which is promoted by ds (PubMed:19574458).
CC {ECO:0000269|PubMed:18635802, ECO:0000269|PubMed:19574458,
CC ECO:0000269|PubMed:20434335}.
CC -!- PTM: Proteolytically cleaved to yield stably associated N- and C-
CC terminal fragments (PubMed:19574458). The C-terminal fragment is
CC processed further to release a 68 kDa mitochondrial fragment, Ft-mito
CC (PubMed:25215488). {ECO:0000269|PubMed:19574458,
CC ECO:0000269|PubMed:25215488}.
CC -!- DISRUPTION PHENOTYPE: Severe overgrown imaginal disk derivatives and
CC pupal death (PubMed:16996265). Overall larval growth is reduced
CC (PubMed:25215488). Cells are round, swollen and have abnormal
CC mitochondrial cristae due to defects in assembly of the mitochondrial
CC electron chain complexes I and V (CI and CV) (PubMed:25215488). Loss of
CC CI activity results in a switch to aerobic glycosis which increases
CC lactate levels (PubMed:25215488). RNAi-mediated knockdown results in
CC dorsal-ventral inversions in ommatidia planar cell polarity
CC (PubMed:25215488). {ECO:0000269|PubMed:16996265,
CC ECO:0000269|PubMed:25215488}.
CC -!- MISCELLANEOUS: The name 'fat' originates from weak mutant alleles that
CC exhibit a broadening of the abdomen. {ECO:0000305}.
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DR EMBL; M80537; AAA28530.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF51036.1; -; Genomic_DNA.
DR PIR; A41087; IJFFTM.
DR RefSeq; NP_477497.1; NM_058149.4.
DR SMR; P33450; -.
DR BioGRID; 59824; 76.
DR DIP; DIP-21094N; -.
DR IntAct; P33450; 52.
DR STRING; 7227.FBpp0077167; -.
DR GlyGen; P33450; 38 sites.
DR iPTMnet; P33450; -.
DR SwissPalm; P33450; -.
DR PaxDb; P33450; -.
DR EnsemblMetazoa; FBtr0077478; FBpp0077167; FBgn0001075.
DR GeneID; 33627; -.
DR KEGG; dme:Dmel_CG3352; -.
DR CTD; 33627; -.
DR FlyBase; FBgn0001075; ft.
DR VEuPathDB; VectorBase:FBgn0001075; -.
DR eggNOG; KOG1219; Eukaryota.
DR HOGENOM; CLU_000042_1_0_1; -.
DR InParanoid; P33450; -.
DR OMA; YREAGGM; -.
DR OrthoDB; 34489at2759; -.
DR PhylomeDB; P33450; -.
DR Reactome; R-DME-350379; Homo-/heterophilic binding of transmembrane components.
DR Reactome; R-DME-390023; Subcellular localisation of D.
DR Reactome; R-DME-390150; DS ligand bound to FT receptor.
DR SignaLink; P33450; -.
DR BioGRID-ORCS; 33627; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33627; -.
DR PRO; PR:P33450; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0001075; Expressed in wing disc and 38 other tissues.
DR ExpressionAtlas; P33450; baseline and differential.
DR Genevisible; P33450; DM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045296; F:cadherin binding; IPI:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:FlyBase.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:FlyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:FlyBase.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IDA:FlyBase.
DR GO; GO:0045317; P:equator specification; IMP:UniProtKB.
DR GO; GO:0048105; P:establishment of body hair planar orientation; IMP:FlyBase.
DR GO; GO:0001737; P:establishment of imaginal disc-derived wing hair orientation; IMP:FlyBase.
DR GO; GO:0042067; P:establishment of ommatidial planar polarity; IMP:UniProtKB.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:FlyBase.
DR GO; GO:0007164; P:establishment of tissue polarity; IMP:FlyBase.
DR GO; GO:0016336; P:establishment or maintenance of polarity of larval imaginal disc epithelium; IMP:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IPI:FlyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0007446; P:imaginal disc growth; IMP:FlyBase.
DR GO; GO:0007447; P:imaginal disc pattern formation; IMP:UniProtKB.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:UniProtKB.
DR GO; GO:0090176; P:microtubule cytoskeleton organization involved in establishment of planar polarity; IMP:FlyBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045926; P:negative regulation of growth; IMP:FlyBase.
DR GO; GO:0045571; P:negative regulation of imaginal disc growth; IMP:FlyBase.
DR GO; GO:0046621; P:negative regulation of organ growth; IMP:FlyBase.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:0090251; P:protein localization involved in establishment of planar polarity; IMP:FlyBase.
DR GO; GO:0035209; P:pupal development; IMP:UniProtKB.
DR GO; GO:0090175; P:regulation of establishment of planar polarity; IMP:FlyBase.
DR GO; GO:0040008; P:regulation of growth; IMP:FlyBase.
DR GO; GO:0045570; P:regulation of imaginal disc growth; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IMP:FlyBase.
DR GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
DR GO; GO:0009888; P:tissue development; IMP:UniProtKB.
DR GO; GO:0035220; P:wing disc development; IMP:UniProtKB.
DR CDD; cd00110; LamG; 2.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00028; Cadherin; 33.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 34.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; SSF49313; 34.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS00232; CADHERIN_1; 22.
DR PROSITE; PS50268; CADHERIN_2; 34.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Mitochondrion; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..5147
FT /note="Cadherin-related tumor suppressor"
FT /id="PRO_0000004015"
FT CHAIN ?..5147
FT /note="Ft-mito"
FT /evidence="ECO:0000269|PubMed:25215488"
FT /id="PRO_0000434022"
FT TOPO_DOM 36..4583
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 4584..4609
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 4610..5147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..156
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 157..270
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 271..382
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 383..494
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 495..599
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 600..708
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 709..820
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 821..942
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 943..1049
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1050..1153
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1154..1278
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1279..1384
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1385..1489
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1490..1601
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1602..1713
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1714..1823
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1824..1922
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1923..2027
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2028..2167
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2168..2278
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2279..2385
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2386..2491
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2492..2596
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2597..2703
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2704..2810
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2811..2913
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2914..3013
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3014..3124
FT /note="Cadherin 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3125..3229
FT /note="Cadherin 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3230..3334
FT /note="Cadherin 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3335..3439
FT /note="Cadherin 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3440..3545
FT /note="Cadherin 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3546..3651
FT /note="Cadherin 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3652..3756
FT /note="Cadherin 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3950..4011
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4013..4049
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4052..4090
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4092..4128
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4129..4320
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 4321..4362
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4402..4569
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 4744..4771
FT /note="Essential for stability of mitochondrial electron
FT chain complexes I and V, and promotes interaction with ND-
FT 24"
FT /evidence="ECO:0000269|PubMed:25215488"
FT REGION 4787..4850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4871..4921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4967..5041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5113..5147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4788..4815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4829..4850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4969..5012
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 5114..5137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4843
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 5054
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 5061
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1831
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1880
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2080
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2799
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2920
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2946
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2967
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3852
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3865
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3905
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 3954..3966
FT /evidence="ECO:0000250"
FT DISULFID 3960..3999
FT /evidence="ECO:0000250"
FT DISULFID 4001..4010
FT /evidence="ECO:0000250"
FT DISULFID 4017..4028
FT /evidence="ECO:0000250"
FT DISULFID 4022..4037
FT /evidence="ECO:0000250"
FT DISULFID 4039..4048
FT /evidence="ECO:0000250"
FT DISULFID 4056..4067
FT /evidence="ECO:0000250"
FT DISULFID 4061..4078
FT /evidence="ECO:0000250"
FT DISULFID 4080..4089
FT /evidence="ECO:0000250"
FT DISULFID 4096..4107
FT /evidence="ECO:0000250"
FT DISULFID 4101..4116
FT /evidence="ECO:0000250"
FT DISULFID 4118..4127
FT /evidence="ECO:0000250"
FT DISULFID 4294..4320
FT /evidence="ECO:0000250"
FT DISULFID 4325..4341
FT /evidence="ECO:0000250"
FT DISULFID 4334..4350
FT /evidence="ECO:0000250"
FT DISULFID 4352..4361
FT /evidence="ECO:0000250"
FT DISULFID 4536..4569
FT /evidence="ECO:0000250"
FT VARIANT 1229
FT /note="S -> G"
FT VARIANT 1233
FT /note="G -> S"
FT MUTAGEN 273
FT /note="S->A,D: Blocks ability of fj to enhance binding to
FT ds."
FT /evidence="ECO:0000269|PubMed:20434335"
FT MUTAGEN 4854
FT /note="T->I: In ft61; strong overgrowth of eye imaginal
FT disks. Binding to Fbxl7 is not affected."
FT /evidence="ECO:0000269|PubMed:25107277"
FT CONFLICT 676
FT /note="S -> P (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 718
FT /note="A -> T (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 889
FT /note="T -> S (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 1298
FT /note="T -> M (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 1338
FT /note="G -> A (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 1366
FT /note="S -> T (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 1408
FT /note="A -> G (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 1755
FT /note="T -> V (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 2168
FT /note="I -> V (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 2266
FT /note="I -> V (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 2665
FT /note="H -> T (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 2712
FT /note="A -> T (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 2816
FT /note="N -> T (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 2893
FT /note="M -> L (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 3359
FT /note="A -> T (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 3674
FT /note="I -> M (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 3722
FT /note="I -> V (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 3869
FT /note="Y -> N (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 4187
FT /note="G -> D (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
FT CONFLICT 4309
FT /note="L -> S (in Ref. 1; AAA28530)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 5147 AA; 564791 MW; 6A5A4743FC7E07D0 CRC64;
MERLLLLFFL LLAGRESLCQ TGDTKLELLA PRGRSYATTY EQYAAFPRRR SSSSSPSGEM
QSRAVDTSAD FEVLEGQPRG TTVGFIPTKP KFSYRFNEPP REFTLDPVTG EVKTNVVLDR
EGMRDHYDLV VLSSQPTYPI EVRIKVLDVN DNSPEFPEPS IAISFSESAT SGTRLLLDAA
TDADVGENGV TDQYEIVAGN VDNKFRLVTT ANPSGDTSYL HLETTGNLDR ESRGSYQLNI
SARDGGSPPR FGYLQVNVTI LDVNDNPPIF DHSDYNVSLN ETALPGTPVV TVMASDNDLG
DNSKITYYLA ETEHQFTVNP ETGVISTTER VNCPQQTNVK SSASQKSCVF TVFARDHGSP
RQDGRTYVTV NLLDTNDHDP IISFRFFPDG GKVATVDENA VNGTVVAAVA VKDSDSGLNG
RTSVRIVSGN ELGHFRLEEA ADLHIVRVNG VLDREEIGKY NLTVVAMDQG TPARTTTAHL
IIDVNDVNDH EPVFEKSEYS AVLSELAPTG SFVASITATD EDTGVNAQVH YDILSGNELK
WFSMDPLTGL IVTTGPLDRE IRDTVELSIS ARDGGPNPKF AYTQLKVIIL DENDEAPQFS
QREQNVTLGE DAPPQTIVAL MTATDHDQGT NGSVTFALAP SVERLYPLQF ALDALTGQLT
TRRPLDREKM SQYEISVIAR DQGAPTPQSA TATVWLNVAD VNDNDPQFYP RHYIYSLADD
DDDIKLKKEV EKERILLHVT ASDKDDGDNA LIEYRLESGG EGLFQLDARS GAISLRGDAP
ASMHWKPHYK LLVSARDAGQ RRSQQDAIVE IVLKSKLEML ECGQAQAGGY EFQMVEDHEQ
QRNSQPNREV GIVQVKSTNG KANSHIEYDI IQGDRAQNFR IDTRSGRITT ARPLDREEQA
NYRLTILASS SSSSSAAASS VSYGQCIVNI AIIDLNDNAP VFALDRESEP TISLPENAAV
GQEIYLSRVR DRDAGVNSRI SYSLTNNPNQ QFRIGPVTGV LYLQRPIRAE PGSLIHVELM
ATDAGSPPLS SKLSLSVLIA DVNDHTPVFD HTSYETSLPE TTKVNTRFFA LAATDIDLGD
NGRISYEIIE GNTERMFGVF PDGYLFVRAP LDREERDYYA LTVSCRDAGQ PSRSSVVPVV
IHVIDENDNA PQFTNSTFTF SIPENAPADT FVGKLTAVDR DIGRNAELSF TLSSQTQDFT
IDTRNGFIKT LRPFDREALV KVSRNAEASG EDGSLRGSMA GNYMLLEATV SDNGIPRLQD
KVKVKVIVTD VNDNAPEFLR APYHVTISEG ASEGTHITHV FTQDADEGLN GDVYYSLAKG
NEAGQFNLDS ATGQLSLGRR LDRESQEIHH LIVVAKDAAL KHPLSSNASI TIVVLDENDN
APEFTQSSSE VSVLETSPTG TELMRFRASD ADQGVNSQVV FSISAGNRRD TFHIDSITGS
LYLHKPLDYE DITSYTLNIT ASDCGTPSLS TTVLYNVLVV DDNDNPPIFP STAIVRQIKE
GIPLKTPIVT VTADDPDSGL NGKVSYAISK QEPQLPQGRH FGINTETGVI HTLREIDRES
IDTFRLTVVA TDRAQPSERQ LSTEKLVTVI VEDINDNAPV FVSMNAAILP PKFSTSKGSS
TAVMQVHAKD ADSSSNGLVT YEIVSGPQEL FKLQRNTGII TFTPGPQFKQ EVRYQLTLKS
TDEAVQSERR SSEVYITIIT PGSGGSESSV PQFEQRSKLS GSVYENEPIG TSILTVTAHL
ASAEIEYFVT NVTATGSRGQ VDRLFDIDAK LGILSTAAEL DREAGPEEYE VEVYAIALGG
QPRTSRTKVR VTVLDKNDSP PQFLDTPFVY NVSEDLQIGH TISTLRAHDP DTLGSVTFLL
MDGHDGKFLL EPSTGKLILN DTLDRETKSK YELRIRVSDG VQYTEAYATI QVSDTNDNPP
LFEDTVYSFD IPENAQRGYQ VGQIVARDAD LGQNAQLSYG VVSDWANDVF SLNPQTGMLT
LTARLDYEEV QHYILIVQAQ DNGQPSLSTT ITVYCNVLDL NDNAPIFDPM SYSSEVFENV
PIATEVVTVS AKDIDSGNNG LIEYSITAGD VDSEFGIDSN GTIRTRRNLD REHRSTYTLT
VTARDCADEF ASFSELEETQ LKLKYRSPRK YQQTRQEFLA HQKQQRLSST VKVTILIKDV
NDEVPVFISA NETAIMENVA INTVVIAVKA VDNDEGRNGY IDYLMKEARD EDMGQSDPLP
FSLNPTDGQL RVVDALDREL RSSYLLNITA RDRGEPPQST ESQLLIRILD ENDNSPVFDP
KQYSASVAEN ASIGAMVLQV SATDVDEGAN GRIRYSIVLG DQNHDFSISE DTGVVRVAKN
LNYERLSRYS LTVRAEDCAL ENPAGDTAEL TINILDINDN RPTFLDSPYL ARVMENTVPP
NGGYVLTVNA YDADTPPLNS QVRYFLKEGD SDLFRINASS GDIALLKPLD REQQSEYTLT
LVAMDTGSPP LTGTGIVRVE VQDINDNDPV FELQSYHATV RENLPSGTHV LTPRATDKDE
GLNAKLRFNL LGEHMHRFHI DSETGEISTA TTLDREETSV YHLTLMAQDS SITEPRASSV
NLTISVSDVN DNIPKFDSTT YNVAVPERIS KGEFVFGARA LDLDDGENAV VHYTISGRDQ
HYFDINTKTG VVSTKLELKT KTKSHDDLTY TIVISAMDQG EQSLSSKAEL TVILRPPELF
PTFAYMANSH FAMSEDVRPG KMITKVSATS PKKGLVGKIR YAIAGGIMGD SLRVDPNSGL
LSVGQDGLDY ELTHLYEIWI EAADGDTPSL RSVTLITLNV TDANDNAPVM EQLIYNAEVL
EEESPPQLIA VVKASDRDSG DNGNVIYRLQ NDFDGTFEIT ESGEIYTRMR LDREEIGDYA
FVVEAVDQGV PHMTGTASVL LHLLDKNDNP PKFTRLFSLN VTENAEIGSF VIRVTSSDLD
LGANANASYS FSENPGEKFR IEPQSGNITV AGHLDREQQD EYILKVVASD GAWRAETPIT
ITIQDQNDNA PEFEHSFYSF SFPELQQSIA LVGQIIATDR DKQGPNSVIS YSLQQPSPMF
SIDPATGEVF SKKAVRFKHS QYVRSPENMY ALTVLATDNG KPPLYSECLV NINIVDAHNN
PPKFEQAEYL APLPQDAVRG QRIVRVHAND KQDLGTNEMD YSLMTFNLSS IFSVGRHDGW
ITLVKPIQVP PNTRYELVVR ATDRGVPPQS DETRVVIVVT GENMDTPRFS VNSYQVIVPE
NEPVGSTILT VGATDDDTGP NGMLRYSISG GNERQDFSVD ERTGGIVIQQ QLDYDLIQEY
HLNITVQDLG YHPLSSVAML TIILTDVNDN PPVFNHKEYH CYIPENKPVG TFVFQAHAAD
KDSPKNAIIH YAFLPSGPDR HFFIMNQSNG TISSAVSFDY EERRIYTLQI KAKNPDSSME
SYANLYVHVL GVNEFYPQFL QPVFHFDVSE TSAVGTRVGA VQATDKDSGE DGRVYYLLVG
SSNDKGFRID TNTGLIYVAR HLDRETQNRV VLTVMAKNYG SIRGNDTDEA QVIISIQDGN
DPPEFIKHYY TSTISEAAPV GTKVTTVKAI DKDVRTQNNQ FSYSIINGNL KQSFKIDVQT
GEISTASRLD REETSTYNLV IGAIDTGLPP QTGSATVHIE LEDVNDNGPT FTPEGLNGYI
SENEPAGTSI MTLIASDPDL PRNGGPFTYQ LIGGKHKSWL SVDRNSGVVR STTSFDREMT
PILEAIIEVE DSGKPKQKSQ HLLTITVLDQ NDNPSTTRSL HIAVSLFNGD LPSNVKLADV
RPNDIDIVGD YRCRLQKNPA QSQLQLAIPR ACDLITTSHT TPIASVFSYT GNDGKHGDVS
SKVSVAFQSF NNETLANSVS IMVRNMTAYH FLANHYRPIL EMIKSRMSNE DEVILYSLLE
GGSGNSTNLQ LLMAVRLAKT SYQQPKYLIE RLREKRSAFS ELLQKEVIVG YEPCSEPDVC
ENGGVCSATM RLLDAHSFVI QDSPALVLSG PRVVHDYSCQ CTSGFSGEQC SRRQDPCLPN
PCHSQVQCRR LGSDFQCMCP ANRDGKHCEK ERSDVCYSKP CRNGGSCQRS PDGSSYFCLC
RPGFRGNQCE SVSDSCRPNP CLHGGLCVSL KPGYKCNCTP GRYGRHCERF SYGFQPLSYM
TFPALDVTTN DISIVFATTK PNSLLLYNYG MQSGGRSDFL AIELVHGRAY FSSGGARTAI
STVIAGRNLA DGGWHKVTAT RNGRVMSLSV AKCADSGDVC TECLPGDSSC YADEVGPVGT
LNFNKQPLMI GGLSSADPIL ERPGQVHSDD LVGCLHSVHI GGRALNLSLP LQQKGILAGC
NRQACQPALA AERCGGFAGQ CIDRWSSSLC QCGGHLQSPD CSDSLEPITL GEGAFVEFRI
SEIYRRMQLL DNLYNSKSAW LDNQQMRERR AVSNFSTASQ IYEAPKMLSM LFRTYKDQGQ
ILYAATNQMF TSLSLREGRL VYYSKQHLTI NMTVQETSTL NDGKWHNVSL FSESRSLRLI
VDGRQVGDEL DIAGVHDFLD PYLTILNVGG EAFVGCLANV TVNNELQPLN GSGSIFPEVR
YHGKIESGCR GDIGQDAAQV ADPLSIGFTL VIVFFVILVV AILGSYVIYR FRGKQEKIGS
LSCGVPGFKI KHPGGPVTQS QVDHVLVRNL HPSEAPSPPV GAGDHMRPPV GSHHLVGPEL
LTKKFKEPTA EMPQPQQQQQ RPQRPDIIER ESPLIREDHH LPIPPLHPLP LEHASSVDMG
SEYPEHYDLE NASSIAPSDI DIVYHYKGYR EAAGLRKYKA SVPPVSAYTH HKHQNSGSQQ
QQQQHRHTAP FVTRNQGGQP PPPPTSASRT HQSTPLARLS PSSELSSQQP RILTLHDISG
KPLQSALLAT TSSSGGVGKD VHSNSERSLN SPVMSQLSGQ SSSASRQKPG VPQQQAQQTS
MGLTAEEIER LNGRPRTCSL ISTLDAVSSS SEAPRVSSSA LHMSLGGDVD AHSSTSTDES
GNDSFTCSEI EYDNNSLSGD GKYSTSKSLL DGRSPVSRAL SGGETSRNPP TTVVKTPPIP
PHAYDGFESS FRGSLSTLVA SDDDIANHLS GIYRKANGAA SPSATTLGWE YLLNWGPSYE
NLMGVFKDIA ELPDTNGPSQ QQQQQTQVVS TLRMPSSNGP AAPEEYV
