LOCUS       NP_075243               4351 aa            linear   ROD 02-APR-2024
DEFINITION  protocadherin Fat 2 precursor [Rattus norvegicus].
ACCESSION   NP_075243 XP_346394
VERSION     NP_075243.1
DBSOURCE    REFSEQ: accession NM_022954.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 4351)
  AUTHORS   Nibbeling,E.A.R., Duarri,A., Verschuuren-Bemelmans,C.C.,
            Fokkens,M.R., Karjalainen,J.M., Smeets,C.J.L.M., de
            Boer-Bergsma,J.J., van der Vries,G., Dooijes,D., Bampi,G.B., van
            Diemen,C., Brunt,E., Ippel,E., Kremer,B., Vlak,M., Adir,N.,
            Wijmenga,C., van de Warrenburg,B.P.C., Franke,L., Sinke,R.J. and
            Verbeek,D.S.
  TITLE     Exome sequencing and network analysis identifies shared mechanisms
            underlying spinocerebellar ataxia
  JOURNAL   Brain 140 (11), 2860-2878 (2017)
   PUBMED   29053796
REFERENCE   2  (residues 1 to 4351)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   3  (residues 1 to 4351)
  AUTHORS   Matsui,S., Utani,A., Takahashi,K., Mukoyama,Y., Miyachi,Y. and
            Matsuyoshi,N.
  TITLE     Human Fat2 is localized at immature adherens junctions in epidermal
            keratinocytes
  JOURNAL   J Dermatol Sci 48 (3), 233-236 (2007)
   PUBMED   17900869
REFERENCE   4  (residues 1 to 4351)
  AUTHORS   Nakayama,M., Nakajima,D., Yoshimura,R., Endo,Y. and Ohara,O.
  TITLE     MEGF1/fat2 proteins containing extraordinarily large extracellular
            domains are localized to thin parallel fibers of cerebellar granule
            cells
  JOURNAL   Mol Cell Neurosci 20 (4), 563-578 (2002)
   PUBMED   12213440
REFERENCE   5  (residues 1 to 4351)
  AUTHORS   Nakayama,M., Nakajima,D., Nagase,T., Nomura,N., Seki,N. and
            Ohara,O.
  TITLE     Identification of high-molecular-weight proteins with multiple
            EGF-like motifs by motif-trap screening
  JOURNAL   Genomics 51 (1), 27-34 (1998)
   PUBMED   9693030
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB011527.1.
            
            On Jan 12, 2005 this sequence version replaced XP_346394.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB011527.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..4351
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..4351
                     /product="protocadherin Fat 2 precursor"
                     /note="protocadherin Fat 2; multiple epidermal growth
                     factor-like domains 1; multiple EGF-like domains protein
                     1; FAT tumor suppressor homolog 2; multiple epidermal
                     growth factor-like domains protein 1; MEGF1"
                     /calculated_mol_wt=478752
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1921
     mat_peptide     19..4351
                     /product="Protocadherin Fat 2. /id=PRO_0000004019"
                     /note="propagated from UniProtKB/Swiss-Prot (O88277.1)"
                     /calculated_mol_wt=478752
     Region          38..143
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Site            order(44..45,108,110,140,142..143)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          152..249
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Site            330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          366..454
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(373..374,422,424,450,452..453)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            459
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          462..560
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(469..470,521,523,556,558..559)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            568
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          570..661
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            627
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          719..816
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(726..727,779,781,812,814..815)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            789
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          825..921
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(831..832,882,884,917,919..920)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          931..1026
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(936..937,988,990,1022,1024..1025)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            996
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          1036..1133
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1043..1044,1096,1098,1129,1131..1132)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          1141..1238
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1148..1149,1201,1203,1234,1236..1237)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            1175
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          1247..1335
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            1276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          1354..1444
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1360..1361,1409,1411,1440,1442..1443)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            1417
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          1452..1551
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1459..1460,1513,1547,1549..1550)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          1560..1650
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Region          1664..1754
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1671..1672,1719,1721,1750,1752..1753)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          1766..1867
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1769..1770,1829,1831,1864,1866..1867)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          1877..1959
                     /region_name="CA_like"
                     /note="Cadherin repeat-like domain; cl46864"
                     /db_xref="CDD:481204"
     Site            1899
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          1972..2066
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1979..1980,2029,2031,2062,2064..2065)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            1998
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Site            2007
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          2074..2163
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            2102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Site            2165
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          2176..2268
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2182..2183,2232,2234,2264,2266..2267)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            2183
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          2276..2375
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2283..2284,2338,2340,2371,2373..2374)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            2325
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Site            2368
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          2383..2475
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            2387
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Site            2430
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Site            2470
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          2485..2581
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2492..2493,2544,2546,2577,2579..2580)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            2547
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          2590..2683
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            2597
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          2697..2795
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2703..2704,2757,2759,2791,2793..2794)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          2803..2904
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2810..2811,2866,2868,2900,2902..2903)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          2913..3009
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2919..2920,2975,2977,3005,3007..3008)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          3018..3111
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(3024..3025,3076,3078,3107,3109..3110)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          3122..3211
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            3127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          3226..3319
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(3231..3232,3282,3284,3315,3317..3318)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            3278
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Site            3312
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          3328..3424
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(3334..3335,3387,3389,3420,3422..3423)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            3432
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          3433..3524
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Region          3535..3621
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            3603
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Site            3770
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Site            3774
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          3802..3923
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Site            3815
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Site            3842
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Site            3875
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Site            3906
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          3953..3986
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            3991
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88277.1)"
     Region          3992..4022
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Site            4051..4071
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88277.1)"
     Region          4084..>4268
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          4316..4340
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88277.1)"
     CDS             1..4351
                     /gene="Fat2"
                     /gene_synonym="Fath2"
                     /coded_by="NM_022954.1:127..13182"
                     /db_xref="GeneID:65048"
                     /db_xref="RGD:620656"
ORIGIN      
        1 mtlvllglai lllhraacek sleetippls wrfthslyna tiyensapkt yvespvkmgm
       61 ylaephwvvk yriisgdaag vfkteehvvg nfcflrirtk ssntallnre vrdsytlivq
      121 asdkslefea ltqvvvhild qndlkplfsp psyrvtised rplkspickv tatdadlgqn
      181 aefyyafnar sevfaihpts gvvtvagkln vtrrgkyelq vlavdrmrki segngfgnla
      241 slvirvepvh rkppainlvv lnppegdegd iyaivtvdtn gsgaevdsle vvggdpgkyf
      301 kvlrsyaqgn efnlvavrdi nwaehphgfn islqthswsr fpphsiiraf hlpswklanl
      361 rfekavyrvk lsefsppgsr valvkvttal pnlryslkps srntafklna rtglitttkl
      421 vdfheqnqyq lhvktslgqa tttviidivd cnnhapvfnr ssyegtlden ippgtsvltv
      481 tatdqdhgdn ghitysiagp kavpfsidpl lgvisttkpm dyelmkriyt frvrasdwgs
      541 pfrqekevsv slrlknlndn qpmfeevnct vslrqdvpvg ksimavsaid mdelqnlkye
      601 ivsgneqdyf hlnhfsgvis lkrsfmnlta vrptiyslki tasdgknyas pttlkvtvvk
      661 dphsevpvqc dktgvlthit ktilqsaglq sqelgeeeft slsnyqinhh spqfedhfpq
      721 sidileqvpi ntplarlaat dpdtgfhgkl vyvisdgnee gcfdieletg llmvaaaldy
      781 ettsfyvlnv tvydlgtppk sswklltvtv kdwndnpprf ppggyqltis edtevgttia
      841 elktedadse dnrrvrytll tptekfslhp ftgelvvtgh ldresesqyi lkaeardqpt
      901 kghqlfsvtd livtledind nppqcitehr rlkvpedmpl gtvltfldas dpdlgpagev
      961 kyilvedahg tfqvhpmtga lslekeldfe rragynlsfw asdsgkplsr rtlchvevlv
     1021 mdvnenlhsp hfssfvyqgq vqenspagtp vmvvtaqddd sgldgelqyf lragtgletf
     1081 sinqdtgmle tlapldreft pyywltvlav drgsvplsav tevyievtdi ndnipsmsrp
     1141 vfypsvleda plgtsvlqle awdpdsssqg kltfnltsgn hlghfivhpf tgllttakql
     1201 drenkdeyvl evtvqdngdp slrstsrvvv cildvndnpp mfshklfnvr lserlsplsp
     1261 epvyrlvasd pdeglngsvt ysieesdees fridpvtgvv sssstfaage yniltikatd
     1321 sgqpalstsv rlhiewipqp rpssiplsfd esyysftvme tdpvnhmvgv isvegrpglf
     1381 wfhisdgdkd mdfdiekttg siviarpldt rrkssynltv evtdgfhtia tqvhifmian
     1441 inhhrpqflq dhyeirvpqd tlpgvellrv qatdqdhgkg liytilssqd pgsanlfqld
     1501 pssgvlvtvg tlelhsgpsq hiltvmvrdq empikrnfvw vtihvedgnl hsphftqlry
     1561 eanvpdttap gtellqvrav dadrganaei hysflkgnsd gffnidsllg iitvaqrlyh
     1621 vhltrhaltv kaedqgsprr hdlalvvihv hpsdssapvf skdeyfieip esvpigspil
     1681 llsagsssev tyelregnkd svfsmnsysg listqkrldh ekvpsyrlri rgsnmagvft
     1741 evvalvyiid endnppafgk ptflghisea aplhslilge dnsplvvras dsdreansll
     1801 vykilepeal kffkidpsmg tltttseldf edtplfqfni yvhdqgtpil faprsakvii
     1861 hvrdvndspp rfseqiyeva vvepihpgmg lltvqaednd srvtysikts nadeavtihp
     1921 ttgqisvvnp atlrlfqkfs irasdglyhd tavvkisltq vldkslqfdq dvyrarvten
     1981 tphrkalvil gvhgnhlndt lsyfllngtd lfhmiesagv lqtrggtfdr eqqdthevav
     2041 evrdnrvpqr vaqalvrvsv edvndnipef qhlpyytviq dgtepgdvlf qvsatdkdlg
     2101 angsvtygfa edyayfridp yvgdislkkp fdyqalnkyh lrviardsgi pplqtevevh
     2161 vtvrnksnpl fqspyykvkv penitlytpi lhtqarspeg lrliynivee eplmlfttdf
     2221 ktgvltvtgp ldyesknkhv ftvratdtal gsfseatvev lvedindnpp tfsqlvytts
     2281 vsegspaqtp viqllasdqd sgqnqdvsyq ivedgsdvsk ffringstge iftiqeldye
     2341 thqhfrvkvr amdkgdpplt getlvvvnvs dindnppkfr epqyeanvse latcghlvlk
     2401 vqaldpdigd tsrleylils gnqdrhfsin stsgiismfn lckkqldssy nlrvgasdgv
     2461 fratvpvyin ttnankyspe fqqnvyeael aenakvgtkv iellaidkds gpygtvdyti
     2521 inklagerff inprgqittl qkldrenste rviaikvmar dgggkvafct vkiiltdend
     2581 napqfkasgy tvsipsnvsr dspiiqvlay dadegrnadv tysvdstedl aeeiievnpt
     2641 tgvvkvkesl vglenravdf nikaqdggpp hwdslvpvrl qvvpneiplp kfseplytfs
     2701 apedlpegse igsvkavaaq dpiiyslvqg ttpesnsddv fsldqdtgvl kvrkamdhes
     2761 tkwyqidlma hcphedtdlv slvsvsiqve dvndnrpvfe adpykaflte nmpggttviq
     2821 vtandqdtgs dgqvsyrlsv epgsnihelf avdsesgwit tlqeldcetq qtyrfyvvaf
     2881 dhgqtiqlss qalvevsitd endnpprfas edyrgsvven nepgelvatl ktldadvsdq
     2941 nrqvtcyite gdplgqfsis qvgdewriss rktldrehia kyllrvtasd gkfqasvpve
     3001 vfvvdindns pqcsqllytg kvredvtpgh filkvsaidv dmdtnaqity slhgpgaqef
     3061 kldphtgelt tltvldrerk dvynlvakat dgggqscqae vtlhiedvnd naprffpshc
     3121 dvavfdnttv ktpvavvfar dpdqganaqv vysltdsadg qfsidatsgv irlekplqvr
     3181 assaveltvr asdlgtpipl stlgtvtvsv vgledylpif lnaehstqvp edapidmevl
     3241 hlatltrpgs ektgyhitgg neqgkfrlda htgilyvngs ldfetnpkyf lsiecsrkss
     3301 sslsdvttiv invtdvnehh prfthdlytv rvlenavvgd viltvsasdd dgpvnsaity
     3361 slvggnqlgh ftinpkkgkl qvakaldweq tpsyslrlra tdsgqpplhe dtevavevvd
     3421 vndnpprffq lnystsvqen spigikvlql ilddpdspqn gppyffrite gntgsvfrvt
     3481 pdgwlvtaas lskkarewyq lhievsdsgl pplssstlvr vqvteqsryp pstlpleisi
     3541 tkgeeefqgg migkihatdr dpqdtltysl eqeggldryf tvgasdgkii asqglphgry
     3601 sfnvtvsdgt fttttgvhvh vwhmepevpq qavwlgfhql tpeelvsdhw rnlqrflsnl
     3661 ldvkranihl aslqpaevta gvdvllvfer hsgtsydlqe lasaiahsvr eiehsvgirm
     3721 rsalpvvpcq gqscqdqtcq etvsleprvg psystarlsi ltprhhlgrn cscngttlrf
     3781 sgqsyvqyrp leaqnwqihf ylktlqpwal lmftnetasi slklangfsh leyhcpggfy
     3841 gnlssrypvn dgqwhsmlle erdtsvhllv ditdnaslvi peecqglrte rqlllgglvp
     3901 snpssnvslg fegcldavvv ngerlellgr ekkmegrlet walsqccwpg tacsqspcln
     3961 ggscspalgs gylcrcpppf sgrncelgre nctsapcqeg gtcvsspegt scncphpytg
     4021 drcemeargc sgghclitpe ikrgdwgqqe flvitvalpl viiatvglll ycrrrkshkp
     4081 vtmedpdlla rsigvdtqas paieldplnt sscnnlnqpe psktsvpnel vtfgpsskqr
     4141 pmvcsvpprl ppaavsshpg hepiikrtws geelvypsga avwpptysrk khweyphpet
     4201 mqgtlppspr rhvgpavmpd ptglyggfpf plelenkrap lpprysnqnl edlmpprpps
     4261 prehllapcl neytaisyyh sqfrqggggp claeggykgv smrlsragps yadcevnggp
     4321 atgrsqprap pnyegsdmve sdygsceevm f
//
