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Protocadherin Fat 2 (hFat2) (Cadherin family member 8) (Multiple epidermal growth factor-like domains protein 1) (Multiple EGF-like domains protein 1)

 FAT2_HUMAN              Reviewed;        4349 AA.
Q9NYQ8; O75091; Q9NSR7;
02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
22-NOV-2017, entry version 162.
RecName: Full=Protocadherin Fat 2;
Short=hFat2;
AltName: Full=Cadherin family member 8;
AltName: Full=Multiple epidermal growth factor-like domains protein 1;
Short=Multiple EGF-like domains protein 1;
Flags: Precursor;
Name=FAT2; Synonyms=CDHF8, KIAA0811, MEGF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10716726; DOI=10.1073/pnas.97.7.3124;
Wu Q., Maniatis T.;
"Large exons encoding multiple ectodomains are a characteristic
feature of protocadherin genes.";
Proc. Natl. Acad. Sci. U.S.A. 97:3124-3129(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 3777-4349, AND VARIANT LEU-4117.
TISSUE=Brain;
PubMed=9693030; DOI=10.1006/geno.1998.5341;
Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
"Identification of high-molecular-weight proteins with multiple EGF-
like motifs by motif-trap screening.";
Genomics 51:27-34(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4142-4349.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3904.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[6]
TISSUE SPECIFICITY.
PubMed=16865240;
Katoh Y., Katoh M.;
"Comparative integromics on FAT1, FAT2, FAT3 and FAT4.";
Int. J. Mol. Med. 18:523-528(2006).
[7]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17900869; DOI=10.1016/j.jdermsci.2007.07.010;
Matsui S., Utani A., Takahashi K., Mukoyama Y., Miyachi Y.,
Matsuyoshi N.;
"Human Fat2 is localized at immature adherens junctions in epidermal
keratinocytes.";
J. Dermatol. Sci. 48:233-236(2007).
[8]
FUNCTION.
PubMed=18534823; DOI=10.1016/j.jdermsci.2008.04.006;
Matsui S., Utani A., Takahashi K., Mukoyama Y., Miyachi Y.,
Matsuyoshi N.;
"Knockdown of Fat2 by siRNA inhibits the migration of human squamous
carcinoma cells.";
J. Dermatol. Sci. 51:207-210(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- FUNCTION: Plays a role in the migration of epidermal cells. May
modulate the extracellular space surronding parallel fibers of
cerebellar during development (By similarity). {ECO:0000250,
ECO:0000269|PubMed:18534823}.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
type I membrane protein {ECO:0000305}. Cell junction
{ECO:0000269|PubMed:17900869}. Nucleus
{ECO:0000269|PubMed:17900869}. Note=Localized at adhesion zippers
(early state of adherens junctions) of keratinocytes.
-!- TISSUE SPECIFICITY: Expressed in epidermal keratinocytes, infant
brain, cerebellum, and also in a variety of tumors, such as
pancreatic cancer, diffuse type gastric cancer, ovarian cancer,
esophageal cancer, skin squamous cell carcinoma, head and neck
cancer. Not expressed in melanoma cell line A375 cells, normal
epidermal melanocytes or normal dermal fibroblasts. Expressed in
epidermal keratinocytes and squamous cell carcinoma (at protein
level). {ECO:0000269|PubMed:16865240,
ECO:0000269|PubMed:17900869}.
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EMBL; AF231022; AAF61928.1; -; mRNA.
EMBL; AB011535; BAA32463.1; -; mRNA.
EMBL; AL157443; CAB75663.1; -; mRNA.
EMBL; AC011337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC034205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS4317.1; -.
PIR; T46927; T46927.
RefSeq; NP_001438.1; NM_001447.2.
RefSeq; XP_006714824.1; XM_006714761.3.
RefSeq; XP_011535902.1; XM_011537600.2.
RefSeq; XP_011535905.1; XM_011537603.2.
RefSeq; XP_016864713.1; XM_017009224.1.
RefSeq; XP_016864714.1; XM_017009225.1.
UniGene; Hs.591255; -.
ProteinModelPortal; Q9NYQ8; -.
SMR; Q9NYQ8; -.
MINT; MINT-2819753; -.
STRING; 9606.ENSP00000261800; -.
iPTMnet; Q9NYQ8; -.
PhosphoSitePlus; Q9NYQ8; -.
BioMuta; FAT2; -.
DMDM; 296434503; -.
EPD; Q9NYQ8; -.
MaxQB; Q9NYQ8; -.
PaxDb; Q9NYQ8; -.
PeptideAtlas; Q9NYQ8; -.
PRIDE; Q9NYQ8; -.
Ensembl; ENST00000261800; ENSP00000261800; ENSG00000086570.
GeneID; 2196; -.
KEGG; hsa:2196; -.
UCSC; uc003lue.5; human.
CTD; 2196; -.
DisGeNET; 2196; -.
EuPathDB; HostDB:ENSG00000086570.12; -.
GeneCards; FAT2; -.
H-InvDB; HIX0005330; -.
HGNC; HGNC:3596; FAT2.
HPA; CAB033680; -.
MIM; 604269; gene.
neXtProt; NX_Q9NYQ8; -.
OpenTargets; ENSG00000086570; -.
PharmGKB; PA28009; -.
eggNOG; KOG1219; Eukaryota.
eggNOG; ENOG410XPEI; LUCA.
GeneTree; ENSGT00760000118805; -.
HOGENOM; HOG000046499; -.
HOVERGEN; HBG005641; -.
InParanoid; Q9NYQ8; -.
KO; K16506; -.
OMA; CTVKIIL; -.
OrthoDB; EOG091G00A0; -.
PhylomeDB; Q9NYQ8; -.
TreeFam; TF316403; -.
GenomeRNAi; 2196; -.
PRO; PR:Q9NYQ8; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000086570; -.
CleanEx; HS_FAT2; -.
ExpressionAtlas; Q9NYQ8; baseline and differential.
Genevisible; Q9NYQ8; HS.
GO; GO:0005913; C:cell-cell adherens junction; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0010631; P:epithelial cell migration; IMP:UniProtKB.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
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; IPR001791; Laminin_G.
Pfam; PF00028; Cadherin; 29.
Pfam; PF00008; EGF; 2.
Pfam; PF02210; Laminin_G_2; 1.
PRINTS; PR00205; CADHERIN.
SMART; SM00112; CA; 33.
SMART; SM00181; EGF; 2.
SMART; SM00179; EGF_CA; 2.
SMART; SM00282; LamG; 1.
SUPFAM; SSF49313; SSF49313; 33.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS00232; CADHERIN_1; 14.
PROSITE; PS50268; CADHERIN_2; 32.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS50025; LAM_G_DOMAIN; 1.
1: Evidence at protein level;
Calcium; Cell adhesion; Cell junction; Cell membrane;
Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
Membrane; Nucleus; Polymorphism; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 4349 Protocadherin Fat 2.
/FTId=PRO_0000004018.
TOPO_DOM 19 4048 Extracellular. {ECO:0000255}.
TRANSMEM 4049 4069 Helical. {ECO:0000255}.
TOPO_DOM 4070 4349 Cytoplasmic. {ECO:0000255}.
DOMAIN 34 148 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 149 256 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 363 458 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 459 564 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 565 669 Cadherin 5. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 716 820 Cadherin 6. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 821 925 Cadherin 7. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 926 1032 Cadherin 8. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1033 1137 Cadherin 9. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1138 1242 Cadherin 10. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1243 1346 Cadherin 11. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1350 1448 Cadherin 12. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1449 1555 Cadherin 13. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1556 1660 Cadherin 14. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1661 1758 Cadherin 15. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1759 1872 Cadherin 16. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1969 2070 Cadherin 17. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2071 2171 Cadherin 18. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2172 2272 Cadherin 19. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2273 2379 Cadherin 20. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2380 2481 Cadherin 21. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2482 2585 Cadherin 22. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2586 2691 Cadherin 23. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2692 2797 Cadherin 24. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2798 2906 Cadherin 25. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2907 3011 Cadherin 26. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3012 3113 Cadherin 27. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3114 3218 Cadherin 28. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3219 3321 Cadherin 29. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3322 3426 Cadherin 30. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3427 3531 Cadherin 31. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3532 3642 Cadherin 32. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3773 3944 Laminin G-like. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 3947 3984 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3986 4022 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
COMPBIAS 3297 3302 Poly-Ser.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 210 210 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 280 280 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 459 459 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 568 568 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 627 627 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 655 655 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 789 789 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 996 996 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1175 1175 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1383 1383 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1417 1417 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1904 1904 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1998 1998 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2007 2007 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2165 2165 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2183 2183 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2325 2325 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2368 2368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2387 2387 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2430 2430 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2470 2470 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2547 2547 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2597 2597 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2654 2654 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3125 3125 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3276 3276 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3310 3310 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3430 3430 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3471 3471 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3601 3601 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3772 3772 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3813 3813 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3840 3840 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3873 3873 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3904 3904 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 3989 3989 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 3912 3944 {ECO:0000250}.
DISULFID 3951 3962 {ECO:0000250}.
DISULFID 3956 3972 {ECO:0000250}.
DISULFID 3974 3983 {ECO:0000250}.
DISULFID 3990 4001 {ECO:0000250}.
DISULFID 3995 4010 {ECO:0000250}.
DISULFID 4012 4021 {ECO:0000250}.
VARIANT 201 201 G -> A (in dbSNP:rs11739693).
/FTId=VAR_055595.
VARIANT 248 248 P -> S (in dbSNP:rs3734061).
/FTId=VAR_055596.
VARIANT 574 574 R -> C (in dbSNP:rs1432862).
/FTId=VAR_055597.
VARIANT 686 686 F -> S (in dbSNP:rs9324700).
/FTId=VAR_055598.
VARIANT 992 992 R -> Q (in dbSNP:rs3734056).
/FTId=VAR_055599.
VARIANT 1004 1004 G -> S (in dbSNP:rs3734055).
/FTId=VAR_055600.
VARIANT 1164 1164 P -> L (in dbSNP:rs2304053).
/FTId=VAR_055601.
VARIANT 1181 1181 Y -> H (in dbSNP:rs6872614).
/FTId=VAR_061076.
VARIANT 1295 1295 L -> P (in dbSNP:rs35640822).
/FTId=VAR_058286.
VARIANT 1462 1462 V -> M (in dbSNP:rs2278371).
/FTId=VAR_055602.
VARIANT 1515 1515 G -> S (in dbSNP:rs2278370).
/FTId=VAR_055603.
VARIANT 1571 1571 G -> S (in dbSNP:rs10044879).
/FTId=VAR_055604.
VARIANT 1895 1895 R -> W (in dbSNP:rs34464977).
/FTId=VAR_055605.
VARIANT 2054 2054 G -> A (in dbSNP:rs34493925).
/FTId=VAR_055606.
VARIANT 2428 2428 F -> S (in dbSNP:rs6892335).
/FTId=VAR_061077.
VARIANT 2907 2907 A -> T (in dbSNP:rs3734053).
/FTId=VAR_055607.
VARIANT 3318 3318 R -> Q (in dbSNP:rs7718054).
/FTId=VAR_055608.
VARIANT 3318 3318 R -> W (in dbSNP:rs2304024).
/FTId=VAR_055609.
VARIANT 3514 3514 L -> S (in dbSNP:rs2053028).
/FTId=VAR_055610.
VARIANT 3631 3631 M -> I (in dbSNP:rs6650971).
/FTId=VAR_055611.
VARIANT 3664 3664 A -> G (in dbSNP:rs35963695).
/FTId=VAR_055612.
VARIANT 3953 3953 Q -> H (in dbSNP:rs2304029).
/FTId=VAR_055613.
VARIANT 4117 4117 P -> L (in dbSNP:rs1105168).
{ECO:0000269|PubMed:9693030}.
/FTId=VAR_055614.
CONFLICT 1287 1287 D -> Y (in Ref. 1; AAF61928).
{ECO:0000305}.
CONFLICT 1303 1303 S -> N (in Ref. 1; AAF61928).
{ECO:0000305}.
CONFLICT 4160 4160 E -> G (in Ref. 2; BAA32463).
{ECO:0000305}.
SEQUENCE 4349 AA; 479317 MW; FCEDBB52E252A996 CRC64;
MTIALLGFAI FLLHCATCEK PLEGILSSSA WHFTHSHYNA TIYENSSPKT YVESFEKMGI
YLAEPQWAVR YRIISGDVAN VFKTEEYVVG NFCFLRIRTK SSNTALLNRE VRDSYTLIIQ
ATEKTLELEA LTRVVVHILD QNDLKPLFSP PSYRVTISED MPLKSPICKV TATDADLGQN
AEFYYAFNTR SEMFAIHPTS GVVTVAGKLN VTWRGKHELQ VLAVDRMRKI SEGNGFGSLA
ALVVHVEPAL RKPPAIASVV VTPPDSNDGT TYATVLVDAN SSGAEVESVE VVGGDPGKHF
KAIKSYARSN EFSLVSVKDI NWMEYLHGFN LSLQARSGSG PYFYSQIRGF HLPPSKLSSL
KFEKAVYRVQ LSEFSPPGSR VVMVRVTPAF PNLQYVLKPS SENVGFKLNA RTGLITTTKL
MDFHDRAHYQ LHIRTSPGQA STVVVIDIVD CNNHAPLFNR SSYDGTLDEN IPPGTSVLAV
TATDRDHGEN GYVTYSIAGP KALPFSIDPY LGIISTSKPM DYELMKRIYT FRVRASDWGS
PFRREKEVSI FLQLRNLNDN QPMFEEVNCT GSIRQDWPVG KSIMTMSAID VDELQNLKYE
IVSGNELEYF DLNHFSGVIS LKRPFINLTA GQPTSYSLKI TASDGKNYAS PTTLNITVVK
DPHFEVPVTC DKTGVLTQFT KTILHFIGLQ NQESSDEEFT SLSTYQINHY TPQFEDHFPQ
SIDVLESVPI NTPLARLAAT DPDAGFNGKL VYVIADGNEE GCFDIELETG LLTVAAPLDY
EATNFYILNV TVYDLGTPQK SSWKLLTVNV KDWNDNAPRF PPGGYQLTIS EDTEVGTTIA
ELTTKDADSE DNGRVRYTLL SPTEKFSLHP LTGELVVTGH LDRESEPRYI LKVEARDQPS
KGHQLFSVTD LIITLEDVND NSPQCITEHN RLKVPEDLPP GTVLTFLDAS DPDLGPAGEV
RYVLMDGAHG TFRVDLMTGA LILERELDFE RRAGYNLSLW ASDGGRPLAR RTLCHVEVIV
LDVNENLHPP HFASFVHQGQ VQENSPSGTQ VIVVAAQDDD SGLDGELQYF LRAGTGLAAF
SINQDTGMIQ TLAPLDREFA SYYWLTVLAV DRGSVPLSSV TEVYIEVTDA NDNPPQMSQA
VFYPSIQEDA PVGTSVLQLD AWDPDSSSKG KLTFNITSGN YMGFFMIHPV TGLLSTAQQL
DRENKDEHIL EVTVLDNGEP SLKSTSRVVV GILDVNDNPP IFSHKLFNVR LPERLSPVSP
GPVYRLVASD LDEGLNGRVT YSIEDSDEEA FSIDLVTGVV SSSSTFTAGE YNILTIKATD
SGQPPLSASV RLHIEWIPWP RPSSIPLAFD ETYYSFTVME TDPVNHMVGV ISVEGRPGLF
WFNISGGDKD MDFDIEKTTG SIVIARPLDT RRRSNYNLTV EVTDGSRTIA TQVHIFMIAN
INHHRPQFLE TRYEVRVPQD TVPGVELLRV QAIDQDKGKS LIYTIHGSQD PGSASLFQLD
PSSGVLVTVG KLDLGSGPSQ HTLTVMVRDQ EIPIKRNFVW VTIHVEDGNL HPPRFTQLHY
EASVPDTIAP GTELLQVRAM DADRGVNAEV HYSLLKGNSE GFFNINALLG IITLAQKLDQ
ANHAPHTLTV KAEDQGSPQW HDLATVIIHV YPSDRSAPIF SKSEYFVEIP ESIPVGSPIL
LVSAMSPSEV TYELREGNKD GVFSMNSYSG LISTQKKLDH EKISSYQLKI RGSNMAGAFT
DVMVVVDIID ENDNAPMFLK STFVGQISEA APLYSMIMDK NNNPFVIHAS DSDKEANSLL
VYKILEPEAL KFFKIDPSMG TLTIVSEMDY ESMPSFQFCV YVHDQGSPVL FAPRPAQVII
HVRDVNDSPP RFSEQIYEVA IVGPIHPGME LLMVRASDED SEVNYSIKTG NADEAVTIHP
VTGSISVLNP AFLGLSRKLT IRASDGLYQD TALVKISLTQ VLDKSLQFDQ DVYWAAVKEN
LQDRKALVIL GAQGNHLNDT LSYFLLNGTD MFHMVQSAGV LQTRGVAFDR EQQDTHELAV
EVRDNRTPQR VAQGLVRVSI EDVNDNPPKF KHLPYYTIIQ DGTEPGDVLF QVSATDEDLG
TNGAVTYEFA EDYTYFRIDP YLGDISLKKP FDYQALNKYH LKVIARDGGT PSLQSEEEVL
VTVRNKSNPL FQSPYYKVRV PENITLYTPI LHTQARSPEG LRLIYNIVEE EPLMLFTTDF
KTGVLTVTGP LDYESKTKHV FTVRATDTAL GSFSEATVEV LVEDVNDNPP TFSQLVYTTS
ISEGLPAQTP VIQLLASDQD SGRNRDVSYQ IVEDGSDVSK FFQINGSTGE MSTVQELDYE
AQQHFHVKVR AMDKGDPPLT GETLVVVNVS DINDNPPEFR QPQYEANVSE LATCGHLVLK
VQAIDPDSRD TSRLEYLILS GNQDRHFFIN SSSGIISMFN LCKKHLDSSY NLRVGASDGV
FRATVPVYIN TTNANKYSPE FQQHLYEAEL AENAMVGTKV IDLLAIDKDS GPYGTIDYTI
INKLASEKFS INPNGQIATL QKLDRENSTE RVIAIKVMAR DGGGRVAFCT VKIILTDEND
NPPQFKASEY TVSIQSNVSK DSPVIQVLAY DADEGQNADV TYSVNPEDLV KDVIEINPVT
GVVKVKDSLV GLENQTLDFF IKAQDGGPPH WNSLVPVRLQ VVPKKVSLPK FSEPLYTFSA
PEDLPEGSEI GIVKAVAAQD PVIYSLVRGT TPESNKDGVF SLDPDTGVIK VRKPMDHEST
KLYQIDVMAH CLQNTDVVSL VSVNIQVGDV NDNRPVFEAD PYKAVLTENM PVGTSVIQVT
AIDKDTGRDG QVSYRLSADP GSNVHELFAI DSESGWITTL QELDCETCQT YHFHVVAYDH
GQTIQLSSQA LVQVSITDEN DNAPRFASEE YRGSVVENSE PGELVATLKT LDADISEQNR
QVTCYITEGD PLGQFGISQV GDEWRISSRK TLDREHTAKY LLRVTASDGK FQASVTVEIF
VLDVNDNSPQ CSQLLYTGKV HEDVFPGHFI LKVSATDLDT DTNAQITYSL HGPGAHEFKL
DPHTGELTTL TALDRERKDV FNLVAKATDG GGRSCQADIT LHVEDVNDNA PRFFPSHCAV
AVFDNTTVKT PVAVVFARDP DQGANAQVVY SLPDSAEGHF SIDATTGVIR LEKPLQVRPQ
APLELTVRAS DLGTPIPLST LGTVTVSVVG LEDYLPVFLN TEHSVQVPED APPGTEVLQL
ATLTRPGAEK TGYRVVSGNE QGRFRLDART GILYVNASLD FETSPKYFLS IECSRKSSSS
LSDVTTVMVN ITDVNEHRPQ FPQDPYSTRV LENALVGDVI LTVSATDEDG PLNSDITYSL
IGGNQLGHFT IHPKKGELQV AKALDREQAS SYSLKLRATD SGQPPLHEDT DIAIQVADVN
DNPPRFFQLN YSTTVQENSP IGSKVLQLIL SDPDSPENGP PYSFRITKGN NGSAFRVTPD
GWLVTAEGLS RRAQEWYQLQ IQASDSGIPP LSSLTSVRVH VTEQSHYAPS ALPLEIFITV
GEDEFQGGMV GKIHATDRDP QDTLTYSLAE EETLGRHFSV GAPDGKIIAA QGLPRGHYSF
NVTVSDGTFT TTAGVHVYVW HVGQEALQQA MWMGFYQLTP EELVSDHWRN LQRFLSHKLD
IKRANIHLAS LQPAEAVAGV DVLLVFEGHS GTFYEFQELA SIITHSAKEM EHSVGVQMRS
AMPMVPCQGP TCQGQICHNT VHLDPKVGPT YSTARLSILT PRHHLQRSCS CNGTATRFSG
QSYVRYRAPA ARNWHIHFYL KTLQPQAILL FTNETASVSL KLASGVPQLE YHCLGGFYGN
LSSQRHVNDH EWHSILVEEM DASIRLMVDS MGNTSLVVPE NCRGLRPERH LLLGGLILLH
SSSNVSQGFE GCLDAVVVNE EALDLLAPGK TVAGLLETQA LTQCCLHSDY CSQNTCLNGG
KCSWTHGAGY VCKCPPQFSG KHCEQGRENC TFAPCLEGGT CILSPKGASC NCPHPYTGDR
CEMEARGCSE GHCLVTPEIQ RGDWGQQELL IITVAVAFII ISTVGLLFYC RRCKSHKPVA
MEDPDLLARS VGVDTQAMPA IELNPLSASS CNNLNQPEPS KASVPNELVT FGPNSKQRPV
VCSVPPRLPP AAVPSHSDNE PVIKRTWSSE EMVYPGGAMV WPPTYSRNER WEYPHSEVTQ
GPLPPSAHRH STPVVMPEPN GLYGGFPFPL EMENKRAPLP PRYSNQNLED LMPSRPPSPR
ERLVAPCLNE YTAISYYHSQ FRQGGGGPCL ADGGYKGVGM RLSRAGPSYA VCEVEGAPLA
GQGQPRVPPN YEGSDMVESD YGSCEEVMF


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