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Fat-like cadherin-related tumor suppressor homolog (Protein kugelei)

 FAT2_DROME              Reviewed;        4699 AA.
Q9VW71; A4V252; Q95S51;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
14-MAY-2014, sequence version 3.
12-SEP-2018, entry version 162.
RecName: Full=Fat-like cadherin-related tumor suppressor homolog;
AltName: Full=Protein kugelei;
Flags: Precursor;
Name=kug; Synonyms=fat2; ORFNames=CG7749;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000312|EMBL:AAL28503.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3360-4401 (ISOFORMS C/D),
AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3821-4699 (ISOFORM C).
STRAIN=Berkeley; TISSUE=Embryo, and Ovary;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=19906848; DOI=10.1242/dev.039099;
Viktorinova I., Konig T., Schlichting K., Dahmann C.;
"The cadherin Fat2 is required for planar cell polarity in the
Drosophila ovary.";
Development 136:4123-4132(2009).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23369713; DOI=10.1016/j.devcel.2012.12.005;
Lerner D.W., McCoy D., Isabella A.J., Mahowald A.P., Gerlach G.F.,
Chaudhry T.A., Horne-Badovinac S.;
"A Rab10-dependent mechanism for polarized basement membrane secretion
during organ morphogenesis.";
Dev. Cell 24:159-168(2013).
-!- FUNCTION: Required for the planar polarity of actin filament
orientation at the basal side of ovarian follicle cells
(PubMed:19906848, PubMed:23369713). Required for proper egg
chamber shape and elongation of the egg chamber during oogenesis
(PubMed:19906848, PubMed:23369713). Required for the correct
planar polarization of Rab10 within the basal follicle cell
epithelium and is therefore indirectly involved in the Rab10-
dependent remodeling of the basal membrane during egg chamber
elongation (PubMed:23369713). {ECO:0000269|PubMed:19906848,
ECO:0000269|PubMed:23369713}.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Note=Accumulates on cell membranes where the planar
oriented actin filaments terminate.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=D;
IsoId=Q9VW71-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=C;
IsoId=Q9VW71-2; Sequence=VSP_054450;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Localizes where basal actin filaments
terminate. {ECO:0000269|PubMed:19906848}.
-!- DISRUPTION PHENOTYPE: Defects in actin filament orientation
correlate with a failure of egg chambers to elongate during
oogenesis (PubMed:19906848). In follicle cells, Rab10 protein
polarizes normally along the apical-basal axis, but is
mislocalized within the epithelial plane (PubMed:23369713).
Epithelia migration is impaired and the structure of the basal
membrane is disrupted (PubMed:23369713).
{ECO:0000269|PubMed:19906848, ECO:0000269|PubMed:23369713}.
-!- SEQUENCE CAUTION:
Sequence=AAL28503.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAM50035.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAM50035.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AE014296; AAF49078.3; -; Genomic_DNA.
EMBL; AE014296; AAZ66056.2; -; Genomic_DNA.
EMBL; AY060955; AAL28503.1; ALT_INIT; mRNA.
EMBL; AY118666; AAM50035.1; ALT_SEQ; mRNA.
RefSeq; NP_001027138.2; NM_001031967.2. [Q9VW71-1]
RefSeq; NP_001287126.1; NM_001300197.1. [Q9VW71-2]
RefSeq; NP_649171.3; NM_140914.3. [Q9VW71-2]
UniGene; Dm.3778; -.
SMR; Q9VW71; -.
BioGrid; 65458; 4.
DIP; DIP-24050N; -.
IntAct; Q9VW71; 7.
STRING; 7227.FBpp0304968; -.
PaxDb; Q9VW71; -.
PRIDE; Q9VW71; -.
EnsemblMetazoa; FBtr0332721; FBpp0304967; FBgn0261574. [Q9VW71-2]
EnsemblMetazoa; FBtr0332722; FBpp0304968; FBgn0261574. [Q9VW71-1]
EnsemblMetazoa; FBtr0346077; FBpp0311915; FBgn0261574. [Q9VW71-2]
GeneID; 40191; -.
KEGG; dme:Dmel_CG7749; -.
UCSC; CG7749-RA; d. melanogaster. [Q9VW71-1]
CTD; 40191; -.
FlyBase; FBgn0261574; kug.
eggNOG; KOG1219; Eukaryota.
eggNOG; ENOG410XPEI; LUCA.
GeneTree; ENSGT00760000118805; -.
InParanoid; Q9VW71; -.
KO; K16506; -.
OMA; YELMPRV; -.
OrthoDB; EOG091G00A0; -.
GenomeRNAi; 40191; -.
PRO; PR:Q9VW71; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0261574; Expressed in 30 organ(s), highest expression level in eye disc (Drosophila).
ExpressionAtlas; Q9VW71; baseline and differential.
Genevisible; Q9VW71; DM.
GO; GO:0098858; C:actin-based cell projection; IDA:FlyBase.
GO; GO:0009925; C:basal plasma membrane; IDA:FlyBase.
GO; GO:0031254; C:cell trailing edge; IDA:FlyBase.
GO; GO:0005925; C:focal adhesion; IDA:FlyBase.
GO; GO:0005887; C:integral component of plasma membrane; ISS:FlyBase.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; ISM:FlyBase.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:FlyBase.
GO; GO:0044877; F:protein-containing complex binding; IPI:FlyBase.
GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:FlyBase.
GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISM:FlyBase.
GO; GO:0060269; P:centripetally migrating follicle cell migration; IMP:FlyBase.
GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
GO; GO:0042247; P:establishment of planar polarity of follicular epithelium; IMP:UniProtKB.
GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:FlyBase.
GO; GO:0007440; P:foregut morphogenesis; IMP:FlyBase.
GO; GO:0007295; P:growth of a germarium-derived egg chamber; IMP:UniProtKB.
GO; GO:0007442; P:hindgut morphogenesis; IMP:FlyBase.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:FlyBase.
GO; GO:0048477; P:oogenesis; IMP:FlyBase.
GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:FlyBase.
GO; GO:0045089; P:positive regulation of innate immune response; HMP:FlyBase.
GO; GO:1902463; P:protein localization to cell leading edge; IMP:FlyBase.
GO; GO:0007431; P:salivary gland development; IMP:FlyBase.
InterPro; IPR002126; Cadherin.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR020894; Cadherin_CS.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR001791; Laminin_G.
Pfam; PF00028; Cadherin; 26.
Pfam; PF02210; Laminin_G_2; 1.
PRINTS; PR00205; CADHERIN.
SMART; SM00112; CA; 34.
SMART; SM00181; EGF; 6.
SMART; SM00179; EGF_CA; 4.
SMART; SM00282; LamG; 1.
SUPFAM; SSF49313; SSF49313; 34.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00232; CADHERIN_1; 18.
PROSITE; PS50268; CADHERIN_2; 34.
PROSITE; PS00022; EGF_1; 5.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 5.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS50025; LAM_G_DOMAIN; 1.
2: Evidence at transcript level;
Alternative splicing; Calcium; Cell adhesion; Cell membrane;
Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
Membrane; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 38 {ECO:0000255}.
CHAIN 39 4699 Fat-like cadherin-related tumor
suppressor homolog.
/FTId=PRO_0000004016.
TOPO_DOM 39 4285 Extracellular. {ECO:0000255}.
TRANSMEM 4286 4306 Helical. {ECO:0000255}.
TOPO_DOM 4307 4699 Cytoplasmic. {ECO:0000255}.
DOMAIN 63 183 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 184 291 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 288 400 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 401 507 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 508 613 Cadherin 5. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 614 716 Cadherin 6. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 773 877 Cadherin 7. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 878 980 Cadherin 8. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 981 1088 Cadherin 9. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1089 1198 Cadherin 10. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1194 1299 Cadherin 11. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1300 1405 Cadherin 12. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1408 1506 Cadherin 13. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1507 1612 Cadherin 14. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1613 1717 Cadherin 15. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1718 1815 Cadherin 16. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1816 1932 Cadherin 17. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1933 2033 Cadherin 18. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2034 2140 Cadherin 19. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2141 2241 Cadherin 20. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2242 2341 Cadherin 21. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2342 2449 Cadherin 22. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2450 2551 Cadherin 23. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2552 2654 Cadherin 24. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2655 2763 Cadherin 25. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2764 2860 Cadherin 26. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2861 2967 Cadherin 27. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2968 3072 Cadherin 28. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3068 3169 Cadherin 29. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3170 3273 Cadherin 30. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3274 3378 Cadherin 31. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3379 3483 Cadherin 32. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3484 3588 Cadherin 33. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3589 3696 Cadherin 34. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3865 3903 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3921 4105 Laminin G-like. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 4113 4150 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4152 4189 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4190 4225 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4227 4263 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 159 159 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 367 367 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 782 782 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 846 846 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 926 926 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1109 1109 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1201 1201 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1315 1315 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1442 1442 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1476 1476 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1514 1514 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 3807 3819 {ECO:0000255}.
DISULFID 3814 3851 {ECO:0000255}.
DISULFID 3853 3862 {ECO:0000255}.
DISULFID 3869 3880 {ECO:0000255}.
DISULFID 3874 3891 {ECO:0000255}.
DISULFID 3893 3902 {ECO:0000255}.
DISULFID 4071 4105 {ECO:0000250}.
DISULFID 4117 4128 {ECO:0000255}.
DISULFID 4122 4138 {ECO:0000255}.
DISULFID 4140 4149 {ECO:0000255}.
DISULFID 4156 4167 {ECO:0000255}.
DISULFID 4161 4177 {ECO:0000255}.
DISULFID 4179 4188 {ECO:0000255}.
DISULFID 4194 4205 {ECO:0000250}.
DISULFID 4199 4214 {ECO:0000250}.
DISULFID 4216 4224 {ECO:0000250}.
DISULFID 4231 4242 {ECO:0000255}.
DISULFID 4236 4251 {ECO:0000255}.
DISULFID 4253 4262 {ECO:0000255}.
VAR_SEQ 4601 4611 VPLPSKVSHSC -> G (in isoform C).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_054450.
CONFLICT 3946 3946 G -> E (in Ref. 3; AAL28503).
{ECO:0000305}.
SEQUENCE 4699 AA; 523781 MW; 1798A54345758C36 CRC64;
MFTMKIKKYV TPVKRKAFTI LQWISLLCSL WLIPTVQSKA DEKHTATLEY RLENQLQDLY
RFSHSVYNVT IPENSLGKTY AKGVLHERLA GLRVGLNAEV KYRIISGDKE KLFKAEEKLV
GDFAFLAIRT RTNNVVLNRE KTEEYVIRVK AHVHLHDRNV SSYETEANIH IKVLDRNDLS
PLFYPTQYTV VIPEDTPKYQ SILKVTADDA DLGINGEIYY SLLMDSEYFA IHPTTGEITL
LQQLQYAENS HFELTVVAYD RGSWVNHQNH QASKTKVSIS VKQVNFYAPE IFTKTFSSVT
PTSNPLIYGI VRVNDKDTGI NGNIGRLEIV DGNPDGTFLL KAAETKDEYY IELNQFAHLN
QQHFIYNLTL LAEDLGTPRR FAYKSVPIQI KPESKNIPIF TQEIYEVSIP ETAPINMPVI
RLKVSDPDLG KNALVYLEIV GGNEGDEFRI NPDSGMLYTA KQLDAEKKSS YTLTVSAIDQ
ANVGSRKQSS AKVKISVQDM NDNDPIFENV NKVISINENN LAGSFVVKLT AKDRDSGENS
YISYSIANLN AVPFEIDHFS GIVKTTSLLD FETMKRNYEL IIRASDWGLP YRRQTEIKLS
IVVKDINDNR PQFERVNCYG KVTKSAPMGT EVFVTSAIDF DAGDIISYRL SDGNEDGCFN
LDPTSGSLSI SCDLKKTTLT NRILKVSATD GTHFSDDLII NVHLMPEDLG GDSSILHGFG
SFECRETGVA RRLAETLSLA EKNNVKSASP SVFSDLSLTP SRYGQNVHRP EFVNFPQELS
INESVQLGET VAWIEAKDRD LGYNGKLVFA ISDGDYDSVF RIDPDRGELQ IIGYLDRERQ
NEYVLNITVY DLGNPTKSTS KMLPITILDV NDNRPVIQKT LATFRLTESA RIGTVVHCLH
ATDADSGINA QVTYALSVEC SDFTVNATTG CLRLNKPLDR EKQDNYALHI TAKDGGSPVL
SSEALVYVLV DDVNDNAPVF GVQEYIFKVR EDLPRGTVLA VIEAVDEDIG PNAEIQFSLK
EETQDEELFR IDKHTGAIRT QGYLDYENKQ VHNLIVSAID GGDPSLTSDM SIVIMIIDVN
ENRFAPEFDD FVYEGKVKEN KPKGTFVMNV TARDMDTVDL NSKITYSITG GDGLGIFAVN
DQGSITSLSQ LDAETKNFYW LTLCAQDCAI VPLSNCVEVY IQVENENDNI PLTDKPVYYV
NVTEASVENV EIITLKAFDP DIDPTQTITY NIVSGNLVGY FEIDSKTGVI KTTERKLDRE
NQAEHILEVA ISDNGSPVLS STSRIVVSVL DINDNSPEFD QRVYKVQVPS SATVNQSIFQ
VHAIDSDSGE NGRITYSIKS GKGKNKFRID SQRGHIHIAK PLDSDNEFEI HIKAEDNGIP
KKSQTARVNI VVVPVNPNSQ NAPLIVRKTS ENVVDLTEND KPGFLVTQIL AVDDDNDQLW
YNISNGNDDN TFYIGQDNGN ILLSKYLDYE TQQSYNLTIS VTDGTFTAFT NLLVQVIDIN
DNPPQFAKDV YHVNISENIE EESVIMQLHA TDRDEDKKLF YHLHATQDPS SLALFRIDSI
SGNVIVTQRL DFEKTAQHIL IVFVKDQGAP GKRNYAKIIV NVHDHNDHHP EFTAKIIQSK
VPESAAIGSK LAEVRAIDRD SGHNAEIQYS IITGNVGSVF EIDPTFGIIT LAGNLNINKI
QEYMLQVKAV DLGNPPLSSQ IPVHIIVTMS ENDPPKFPTN NIAIEIFENL PIGTFVTQVT
ARSSSSIFFN IISGNINESF RINPSTGVIV INGNIDYESI KVFNLTVKGT NMAAESSCQN
IIIHILDAND NIPYFVQNEY VGALPESAAI GSYVLKVHDS SKDHLTLQVK DADVGVNGMV
EYHIVDDLAK NFFKIDSTTG AIELLRQLDY ETNAGYTFDV TVSDMGKPKL HSTTTAHVTI
RVINVNDCPP VFNERELNVT LFLPTFENVF VRQVSAKDAD NDTLRFDIVD GNTNECFQIE
KYTGIITTRN FEILNNENDR DYALHVRASD GIFSAILIVK IKVLSAIDSN FAFQRESYRF
SAFENNTKVA TIGLVNVIGN TLDENVEYRI LNPTQLFDIG ISSGALKTTG VIFDREVKDL
YRLFVEAKSM LYDGMNSNVR RAVTSIDISV LDVNDNCPLF VNMPYYATVS IDDPKGTIIM
QVKAIDLDSA ENGEVRYELK KGNGELFKLD RKSGELSIKQ HVEGHNRNYE LTVAAYDGAI
TPCSSEAPLQ VKVIDRSMPV FEKQFYTVSV KEDVEMYSAL SVSIEAESPL GRSLIYTISS
ESQSFEIDYN TGSIFVVNEL DYEKISSHDV SIRATDSLSG VYAEVVLSVS IMDVNDCYPE
IESDIYNLTI PENASFGTQI LKINATDNDS GANAKLSYYI ESINGQNNSE LFYIDVTDGN
LYLKTPLDYE QIKYHHIVVN VKDHGSPSLS SRSNVFITVK DLNDNAPCFV EPSYFTKVSV
AAVRGQFVAL PKAYDKDISD TDSLEYKIVY GNELQTYSID KLTGVISLQN MLNFTDKSST
VLNISVSDGV HTAYARLKIS LLPENVYSPL FDQSTYEAQV PENLLHGHNI ITVKASDGDF
GTYANLYYEI VSEEMKKIFL IDQTTGVITS KVTFDREKKD EYVVLLKVSD GGGKFGFASL
KVIVVDVNDN VPYFLLKEYK MVVSTTVEAN QTILTVKAKD DDIVDNGSVH FQIVQKSNDK
AVKDVIEINE KTGDIVFKSK AESYGVNSYQ FFVRASDRGE PQFHSEVPVS IEIIETDANI
PTFEKSSVLL KIIESTPPGT VLTKLHMIGN YTFKFSIAAD QDHFMISDSG ELILQQTLDR
EQQESHNLIV VAETSTVPVF FAYADVLIDV RDENDNYPKF DNTFYSASVA ENSEKVISLV
KVSATDADTG PNGDIRYYLE SDTENIQNIF DIDIYSGWIT LLTSLDREVQ SEYNFKVIAA
DNGHPKHDAK VPVTIKIVDY NDNAPVFKLP IEGLSVFENA LPGTVLINLL LIDPDIEKQE
MDFFIVSGDK QAQFQIGKSG ELFIAKPLDR EQLMFYNLSI IATDGKFTAK ANVEIDVKDI
NDNTPYCLKP RYHISTNESI SIGTTLVEVK AIDFDFQSKL RFYLSGKGAD DFSIGKESGI
LKVASALDRE TTPKYKLVAH VQDGKDFTQE CFSEIIITVN DINDNMPIFS MAQYRVSVPE
DAQLNTLITK VHAMDKDFGV NRQIKYSLMG ENHDYFKISK STGIIRLHKS LDRETISLFN
LTVKAEDCGV PKLHSIATVA VNILDINDNP PEFSMRQYSC KILENATHGT EVCKVYATSI
DIGVNADIHY FIMSGNEQGK FKMDSTTGDL VLNATLDYEM SKFYFLTIQA IDGGTPPLSN
NAYVNISILD INDNSPTFLQ NLYRINVNED IFVGSKILDV KATDEDSDVN GLVTYNIERG
DNIGQFSIDP KNGTISVSRP LDRETISHYT LEIQACDQGD PQRCNSVPIN INILDTNDNA
PIFSSSNYSV VLQENRLLGY VFLTFKISDA DETPNTTPYT FDIRSGNEGG LFRLEQDGSL
RTASRFNHNL QDEFVIQVRV FDNGTPPLYS DAWVVVKIIE ESQYPPIVTP LEVTINSFED
DFSGAFIGKV HASDQDKYDE LNFSLVSGPD DMYQSSKLFN ISNNTGKIYA ISNLDIGLYK
LNVSVSDGKF HVFSIVKINV ELVTNDMLKE SVVIRFRRIS ASEFLLSHRK TFMRSIRNIM
RCRQKDVILI TLQSDYQKAS QHAVGNRRAR SIDSDLNVVF AVRKQQIIPD SDEFFTSDEI
RQTLIDKKNE IENETNLVVE DVLPSTCQSN KNDCVHGECK QILQILKNNV TTTFTDVISF
AAPSYIPVNT CVCRPGFDGK HCKETVNACS TDPCSPQRIC MPSGSALGYQ CVCPKGFSGT
YCERKSSKCS NESCDMGLFT AVSFGGKSYA HYKINKVKAK FTLENGFSYS LQIRTVQQTG
TLLYASGKVD YNILEIINGA VQYRFDLGSG EGVISVSSIN ISDGEWHQIS LERSLNSAKV
MVDNKHVSHG SAPGVNGILN IQSNDIFVGA EVRPHPSIIG YEDIQRGFIG CMANIKIAKE
SLPLYISGGS TIAALKRFTN VEFKCDPSNV LVRLGICGSQ PCANSGICKE LDTDVFECAC
QPRYSGKHCE IDLDPCSSGP CLFGGRCDYH GPNNYSCTCP IHLSGKRCEY GKFCTPNPCK
NGGICEEGDG ISHCMCRGYT GPTCEIDVDE CENQPCGNGA TCINEPGSFR CICPSYLTGA
SCGDPLYSNS ISTKLKNFSI EHISGIISGV AVVLVIISCV LCCVVLKRSS SSKRRNRLEK
DKNKSSYKEA NLNSLVDKDN YCKPNVKLSN LEVNQRPISY TAVPNDNLVL SNRNFVNNLD
ILRSYGSAGD ELENVPFEYQ KVNRNKQHVN INSCHSTDAD NAYKQEWCEQ MHLRTFSENK
LNNELKRDFG PSVSRFSTGK LIQVEMPNVC HSSSANFVDY SALANGQYHW DCSDWVRKSH
NPLPDITEVP GAEIADSSSL HSNDSNESKS KKAFFVHRED GDVDPTRDIA ALNEDIGSEY
LDSEAESCLE PFMLPRSSNQ PLSRLSSFNN IENEDYKSNT VPLPSKVSHS CKVYLRHPDS
YLPTMHFPSE TDGESSMTEG PISRMEIKTR RTISENSEEA YLFPCTVGEI GSNSNISVRL
CEIEDSELEE FLPQQQTNN


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