GenomeNet

Database: UniProt
Entry: Q5F226
LinkDB: Q5F226
Original site: Q5F226 
ID   FAT2_MOUSE              Reviewed;        4351 AA.
AC   Q5F226; Q3V1D4; Q69ZY7;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   16-JAN-2019, entry version 109.
DE   RecName: Full=Protocadherin Fat 2;
DE   AltName: Full=FAT tumor suppressor homolog 2;
DE   Flags: Precursor;
GN   Name=Fat2; Synonyms=Fath2, Kiaa0811;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2698-4351.
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3590-4351.
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Involved in the regulation of cell migration (By
CC       similarity). May be involved in mediating the organization of the
CC       parallel fibers of granule cells during cerebellar development (By
CC       similarity). {ECO:0000250|UniProtKB:O88277,
CC       ECO:0000250|UniProtKB:Q9NYQ8}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}. Cell junction
CC       {ECO:0000250|UniProtKB:Q9NYQ8}. Golgi apparatus, trans-Golgi
CC       network {ECO:0000250|UniProtKB:O88277}. Note=Localized at adhesion
CC       zippers (early state of adherens junctions) of keratinocytes.
CC       {ECO:0000250|UniProtKB:Q9NYQ8}.
DR   EMBL; AL713870; CAI52049.1; -; Genomic_DNA.
DR   EMBL; CH466575; EDL33495.1; -; Genomic_DNA.
DR   EMBL; AK173031; BAD32309.1; -; mRNA.
DR   EMBL; AK132523; BAE21217.1; -; mRNA.
DR   CCDS; CCDS36157.1; -.
DR   RefSeq; NP_001025159.1; NM_001029988.2.
DR   RefSeq; XP_006533385.1; XM_006533322.3.
DR   RefSeq; XP_006533386.1; XM_006533323.3.
DR   UniGene; Mm.339363; -.
DR   ProteinModelPortal; Q5F226; -.
DR   SMR; Q5F226; -.
DR   IntAct; Q5F226; 1.
DR   STRING; 10090.ENSMUSP00000067556; -.
DR   iPTMnet; Q5F226; -.
DR   PhosphoSitePlus; Q5F226; -.
DR   MaxQB; Q5F226; -.
DR   PaxDb; Q5F226; -.
DR   PeptideAtlas; Q5F226; -.
DR   PRIDE; Q5F226; -.
DR   Ensembl; ENSMUST00000068853; ENSMUSP00000067556; ENSMUSG00000055333.
DR   Ensembl; ENSMUST00000108864; ENSMUSP00000104492; ENSMUSG00000055333.
DR   GeneID; 245827; -.
DR   KEGG; mmu:245827; -.
DR   UCSC; uc007izf.1; mouse.
DR   CTD; 2196; -.
DR   MGI; MGI:2685369; Fat2.
DR   eggNOG; KOG1219; Eukaryota.
DR   eggNOG; ENOG410XPEI; LUCA.
DR   GeneTree; ENSGT00940000158507; -.
DR   HOGENOM; HOG000046499; -.
DR   HOVERGEN; HBG005641; -.
DR   InParanoid; Q5F226; -.
DR   KO; K16506; -.
DR   OMA; MVRDQEM; -.
DR   OrthoDB; 12779at2759; -.
DR   PhylomeDB; Q5F226; -.
DR   TreeFam; TF316403; -.
DR   PRO; PR:Q5F226; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000055333; Expressed in 84 organ(s), highest expression level in cerebellum.
DR   Genevisible; Q5F226; MM.
DR   GO; GO:0005913; C:cell-cell adherens junction; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0031589; P:cell-substrate adhesion; ISS:UniProtKB.
DR   GO; GO:0010631; P:epithelial cell migration; ISS:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR001791; Laminin_G.
DR   Pfam; PF00028; Cadherin; 28.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 33.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00282; LamG; 1.
DR   SUPFAM; SSF49313; SSF49313; 33.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00232; CADHERIN_1; 13.
DR   PROSITE; PS50268; CADHERIN_2; 32.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Cell junction; Cell membrane;
KW   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Golgi apparatus; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19   4351       Protocadherin Fat 2.
FT                                /FTId=PRO_0000406601.
FT   TOPO_DOM     19   4050       Extracellular. {ECO:0000255}.
FT   TRANSMEM   4051   4071       Helical. {ECO:0000255}.
FT   TOPO_DOM   4072   4351       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       34    148       Cadherin 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      149    256       Cadherin 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      363    458       Cadherin 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      459    564       Cadherin 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      565    669       Cadherin 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      716    820       Cadherin 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      821    925       Cadherin 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      926   1032       Cadherin 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1033   1142       Cadherin 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1138   1242       Cadherin 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1243   1346       Cadherin 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1350   1448       Cadherin 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1449   1555       Cadherin 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1556   1660       Cadherin 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1661   1758       Cadherin 15. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1759   1872       Cadherin 16. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1873   1968       Cadherin 17. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     1969   2070       Cadherin 18. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2071   2171       Cadherin 19. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2172   2272       Cadherin 20. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2273   2379       Cadherin 21. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2380   2481       Cadherin 22. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2482   2585       Cadherin 23. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2586   2692       Cadherin 24. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2693   2799       Cadherin 25. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2800   2908       Cadherin 26. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     2909   3013       Cadherin 27. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3014   3115       Cadherin 28. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3116   3220       Cadherin 29. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3221   3323       Cadherin 30. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3324   3428       Cadherin 31. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3429   3533       Cadherin 32. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3534   3631       Cadherin 33. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN     3775   3946       Laminin G-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     3949   3986       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     3988   4024       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS   4147   4261       Pro-rich.
FT   COMPBIAS   4286   4289       Poly-Gly.
FT   CARBOHYD     39     39       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    210    210       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    280    280       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    330    330       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    459    459       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    568    568       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    627    627       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    789    789       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    996    996       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1175   1175       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1276   1276       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1417   1417       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1899   1899       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1998   1998       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2007   2007       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2102   2102       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2165   2165       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2183   2183       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2325   2325       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2368   2368       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2387   2387       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2430   2430       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2470   2470       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2547   2547       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2597   2597       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3127   3127       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3278   3278       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3312   3312       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3432   3432       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3603   3603       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3770   3770       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3774   3774       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3815   3815       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3842   3842       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3875   3875       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3906   3906       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3991   3991       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID   3914   3946       {ECO:0000250}.
FT   DISULFID   3953   3964       {ECO:0000250}.
FT   DISULFID   3958   3974       {ECO:0000250}.
FT   DISULFID   3976   3985       {ECO:0000250}.
FT   DISULFID   3992   4003       {ECO:0000250}.
FT   DISULFID   3997   4012       {ECO:0000250}.
FT   DISULFID   4014   4023       {ECO:0000250}.
FT   CONFLICT   4010   4010       T -> N (in Ref. 4; BAE21217).
FT                                {ECO:0000305}.
SQ   SEQUENCE   4351 AA;  480109 MW;  72F9DADAAA5467D5 CRC64;
     MTLVLLGVAM VLLHRAACEK PLEETITPLT WRFTHSLYNA TIYENSAPKT YVESPVKMGM
     YLAEPHWVVK YRIISGDAAG VFKTEEHVVG NFCFLRIRTK SSNTALLNRE VRDSYTLVVQ
     ASDKSLEFEA LTQVVVHILD QNDLKPLFSP PSYRFTISED RPLKSPICKV TATDADLGQN
     AEFYYAFNAR SEVFAIHPTS GVVTVAGKLN VTWRGKYELQ VLAVDRMRKI SEGNGFGNLA
     PLVIYVEPVH RKPPVITLVV LNPPEGDEGD IYATVTVDTN GSGAEVDSLE VVGGDPGKYF
     KVLKSYAQGN EFNLVAVRDI NWAEHLHGFN ISLQTHSRSR FPSRSIIRAF HLPPYTLANL
     RFEKAVYRVK LSEFSPPGSR VALVRVTTAL PTLRYALKPS SGSTVFKLNA RTGLITTTKP
     VDFHEQNQYQ LHVKTSLGQA TTTVIIDIVD CNNHAPVFNR SSYEGTLDEN IPPGTSVLTV
     TATDQDHGDN GHITYSIAGP KAVPFSIDPY LGVISTTKSM DYELMKRIYT FRVRASDWGS
     PFRQEKEVSV SLRLKNLNDN QPMFEEVNCT VSLRQDAPVG KSIMAVSAID MDELQNLKYE
     IVSGNEQDYF HLNHFSGVIS LKRSFMNLTA VRPTVYSLKI TASDGKNYAS PTTLKVTVVK
     DPRSEVPVQC DKTGVLTHIT KTILQSAGLQ GQEMGEEDFT SLGNYQINHH APQFEDHFPQ
     SIDILEQVPV NTPLAHLAAT DPDPGFHGRL VYVIADGNEE GCFDIELETG LLTVAAALDY
     ETTSFYVLNV TVYDLGTPPK SSWKLLTVTV KDWNDKPPRF PPGGYQLTIS EDTEVGTTVA
     ELKTRDTDSE DNGRVRYTLL TPTEKFSLHP LTGELVVTGQ LDRESEPQYI LKAEARDQPT
     KGHQLFSVTD VIVTLEDIND NPPQCITEHS SLKVPEDMPL GTVLTFLDAS DPDLGPAGEV
     KYILVDDVHG TFRVDPMTGA LSLEKELDFE RRAGYNLSFW ASDSGRPLAR RTLCHVEVLV
     MDVNENLHSP HFSSFVYQGQ VQENSPAGTQ VMVVTAQDDD SGLDGELQYF LRAGTGLEAF
     SINQDTGMLE TLAPLDREFT PYYWLTVLAV DRGSVPLSAV TEVYIEVTDI NDNIPSMSRP
     VFYPSVKEDA PLGTSVLQLE AWDPDFSSQG KLTFNLTSGN HMGHFIVHPF TGLLSTAKQL
     DRENKDEYVL EVTVQDNGDP PLRSTSRVVV CVLDVNDNSP MFSHKLFNVR LSERLSPLSP
     EPVYRLVASD PDEGLNGSIT YSIEESDEES FRIDPVTGVV SSSSTFAAGE YNILTIKATD
     SGQPALSTSV RLHIEWIPQP RPSSIPLSFD ESHYSFAVME TDPVNHMLGV ISVEGRPGLF
     WFHISDGDKD MDFDIEKTTG SIVIARPLDT RRKSSYNLTV EVTDGFHTIA TQVHILMIAN
     INHHRPQFLQ DHYDIRVPQD TLPGVELLRV QATDQDHGKG LIYTIHSSRD PGSANLFQLD
     PSSGVLVTVG TLDLHSGPSQ HILTVMVRDQ EMPIKRNFVW VTIHVEDGNL HSPHFTQPRY
     EANVPDTTTP GTELLQVRAV DADRGANAEV HYSFLKGNSE GFFNIDSLLG IITVAQRLDH
     VHLNRHALTV KAEDQGSPQR HDLAMVVVHV HPSDSSAPIF SKDEYFIEIP ESVPIGSPIL
     LISAASSSDV TYELREGNKN SVFSMNSYSG LISTQKRLDH EKVSSYQLKI RGSNMAGVFT
     EVVALVYIID ENDNAPAFLK STFVGHISEA APLHSLILGE DNSPLVIRAS DSDQEANSLL
     VYKILEPEAL KFFKIDPSMG TLTITSELDY ETTPLFQFSI YVHDQGTPIL FAPRSARVII
     HVRDVNDSPP RFSEQIYEVA VVEPIHPGME LLTVQAEDND SKVTYSIKTS NTDEAVTIHP
     ITGQISVVNP AALRLFPKLN IRAFDGLYQD TAVVKISLTQ ALDKSLQFDQ DIYRARVTEN
     TPHSNVLVIL GVHGNHLNDT LSYFLLNGTD LFHMVKSAGV LQTRGVTFDR EQQDTHEVAV
     EVRDNRVPRR VAQALVRVSV EDVNDNIPEF QHLPYYTVIQ DGTEPGDVLF QVSATDKDLG
     ANGTVTYGFA EDYAYFRIDP YVGDISLKKP FDYQALNKYH LRVTARDAGT PPLQTEVEVH
     VTVRNKSNPL FQSPYYKVKV PENITLYTPI LHTQARSPEG LRLIYNIVEE EPLMLFTTDF
     KTGVLTVTGP LDYESKNKHV FTVRATDTAL GSFSEATVEV LVEDINDNPP TFSQLVYSTS
     VSEGSPAQTP VIQLLASDQD SGQNQDVSYQ IVEDGSDVSK FFRINGSTGE MFTIQELDYE
     AHQHFRVKVR ATDRGDPPLT GETLVVVNVS DINDNPPEFR EPQYEANVSE LATCGHLVLK
     VQALDPDIGD TSRLEYLILS GNQDRHFSIN STSGIISMFN LCKKQLDSSY NLRVGASDGV
     FQATVPVYIN TTNANKYSPE FQQNVYEAEL AENAKVGTKV IELLAIDKDS GPYGTVDYTI
     INKLAGERFF INPSGQITTL QKLDRENSTE RVIAIKIMAR DGGGKVAFCT VKIILTDEND
     NAPQFKASGY TVSIPSNVSR DSPIIQVLAY DADEGRNADV TYSVDSTEDL AEEIIEVNPT
     TGVVKVKESL VGLENKAVDF NIKAQDGGPP HWDSLVPVRL QVVPNEIPLP KFSEPLYTFS
     ASEDLPEGSE IGSVKAVAAQ DPIIYSLVQG TTPESNSDDV FSLDQDTGVL KVKKAMDHES
     TKWYQIDLMA HCPHEDTDLV SLVSVNIQVE DVNDNRPVFE ADPYKAFLTE NMPGGTTVIQ
     VTANDQDTGS DGQVSYRLSV EPGSNIHQLF AVDSESGWIT TLQELDCETQ QTYRFYVVAF
     DHGQTIQLSS QALVEVSITD ENDNPPRFAS EDYRGSVVEN NEPGELVATL KTLDADISEQ
     NRQVTCYITE GDPLGQFSIS QVGDEWRITS RKTLDREHIA KYLLRITASD GKFQASVPVE
     VFVLDINDNS PQCSQLLYTG KVREDVTPGH FILKVSAIDV DMDTNAQITY SLHGPGAQEF
     KLDPHTGELT TLSVLDRERK DVYNLVAKAT DGGGQSCQAE VTLHIEDVND NAPRFFPSHC
     AVAVFDNTTV KTPVAVVFAR DPDQGVNAQV VYSLTDSADG QFSIDATSGV IRLEKPLQVR
     SSSAVELTVR ASDLGTPIPL STLGTVTVSI VGLEDYLPIF LNSEHSTQVP EDALIDMEVL
     YLATLTRPGS EKTGYHITGG NEQGKFRLDA HTGILYVNGS LDFETNPKYF LSIECSRKSS
     SSLSDVTTIV INVTDVNEHH PRFTHDLYTV RVLENAIVGD VILTVSASDD DGPVNSVITY
     SLVGGNQLGH FTIDPKKGKL QVAKALDWEQ TPSYSLRIRA TDSGQPPLHE DTEVAVEVVD
     VNDNPPRFFQ LNYSTAVQEN SPIGIKVLQL ILDDPDSPQN GPPYFFRITE GNTGSVFRVT
     PDGWLVTAGS LSRRAQEWYQ LHIEVSDSGL PPLSSSTLVR VHITEQSRYP PSTLPLEIFI
     TKGEEEFQGG MVGKIHATDR DPQDTLTYSL DREGSLGKYF TVGASDGKII ASQGLPRGRY
     LFNVTVSDGT FTTTTGVHVH VWHMGQEAPQ QAVWLGFHQL TPEELVSDHW RNLQRFLSNI
     LDIKRANIHL ASLQPAEVTA GVDVLLAFEG HSGTSYDLQE LASAIAHSAK EMEHSVGIQM
     RSALPVVPCQ GPSCQDQTCQ ETVSLEPRVG PSYSTARLSI LTPRHHLGKN CSCNGTTWRF
     SGQSYMRYRP LEAQNWQIHF YLKTLQPWAL LMFTNETASI SLKLANGFLH LEYRCPGGFY
     GNLSSHRPVN DGQWHSMLLE ERDTSVHLLV DITDNTSLVI PEECQGLRTE RHLLLGGLVP
     SNPSSNVSLG FEGCLDAVVV NSERLELLGH RKKMAGYLET WALSQCCWPG TTCSQNPCLN
     GGSCSPALGS GYLCRCPPLF SGRNCELGRE NCTSAPCQEG GTCVSSPEGT SCSCPHPYTG
     DRCEMEARGC SGGHCLITPE IKRGDWGQQE FLVIIVALPL LIIATVGLLL YCRRCKSHKP
     VAMEDPDLLA RSIGVDTQAS PAIELDPLNA GSCNDLNQLE PSKTSVPNEL VTFGPSSKQR
     PMVCSVPPRL PPAVVSSHPG HEPIIKRTWS GEELVYPSGA AVWPPTYSRK EHWEYPHPEA
     MQGPLPPSPR RHVSPAVMPD PAGLYGGFPF PLELENKRAP LPPRYSNQNL EDLIPPRPPS
     PREHLLAPCL NEYTAISYYH SQFRQGGGGP CLAEGGYKGV SMRLSRAGPS YADCEVNGGP
     APGRSQPRAP PNYEGSDMVE SDYGSCEEVM F
//
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