LOCUS       NP_001029156            2622 aa            linear   ROD 03-JUN-2025
DEFINITION  ankyrin-3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001029156
VERSION     NP_001029156.1
DBSOURCE    REFSEQ: accession NM_001033984.1
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 2622)
  AUTHORS   Dorrego-Rivas,A., Ezan,J., Moreau,M.M., Poirault-Chassac,S.,
            Aubailly,N., De Neve,J., Blanchard,C., Castets,F., Freal,A.,
            Battefeld,A., Sans,N. and Montcouquiol,M.
  TITLE     The core PCP protein Prickle2 regulates axon number and AIS
            maturation by binding to AnkG and modulating microtubule bundling
  JOURNAL   Sci Adv 8 (36), eabo6333 (2022)
   PUBMED   36083912
REFERENCE   2  (residues 1 to 2622)
  AUTHORS   Jung,G., Hernandez-Illan,E., Lozano,J.J., Sidorova,J., Munoz,J.,
            Okada,Y., Quintero,E., Hernandez,G., Jover,R., Carballal,S.,
            Cuatrecasas,M., Moreno,L., Diaz,M., Ocana,T., Sanchez,A.,
            Rivero,L., Ortiz,O., Llach,J., Castells,A., Pellise,M., Goel,A.,
            Batlle,E. and Balaguer,F.
  TITLE     Epigenome-Wide DNA Methylation Profiling of Normal Mucosa Reveals
            HLA-F Hypermethylation as a Biomarker Candidate for Serrated
            Polyposis Syndrome
  JOURNAL   J Mol Diagn 24 (6), 674-686 (2022)
   PUBMED   35447336
REFERENCE   3  (residues 1 to 2622)
  AUTHORS   Toma,C., Shaw,A.D., Heath,A., Pierce,K.D., Mitchell,P.B.,
            Schofield,P.R. and Fullerton,J.M.
  TITLE     A linkage and exome study of multiplex families with bipolar
            disorder implicates rare coding variants of ANK3 and additional
            rare alleles at 10q11-q21
  JOURNAL   J Psychiatry Neurosci 46 (2), E247-E257 (2021)
   PUBMED   33729739
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2622)
  AUTHORS   Yang,H.Q., Perez-Hernandez,M., Sanchez-Alonso,J., Shevchuk,A.,
            Gorelik,J., Rothenberg,E., Delmar,M. and Coetzee,W.A.
  TITLE     Ankyrin-G mediates targeting of both Na+ and KATP channels to the
            rat cardiac intercalated disc
  JOURNAL   Elife 9, e52373 (2020)
   PUBMED   31934859
  REMARK    GeneRIF: Ankyrin-G mediates targeting of both Na(+) and KATP
            channels to the rat cardiac intercalated disc.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2622)
  AUTHORS   Freal,A., Rai,D., Tas,R.P., Pan,X., Katrukha,E.A., van de
            Willige,D., Stucchi,R., Aher,A., Yang,C., Altelaar,A.F.M.,
            Vocking,K., Post,J.A., Harterink,M., Kapitein,L.C., Akhmanova,A.
            and Hoogenraad,C.C.
  TITLE     Feedback-Driven Assembly of the Axon Initial Segment
  JOURNAL   Neuron 104 (2), 305-321 (2019)
   PUBMED   31474508
REFERENCE   6  (residues 1 to 2622)
  AUTHORS   Zhou,D., Lambert,S., Malen,P.L., Carpenter,S., Boland,L.M. and
            Bennett,V.
  TITLE     AnkyrinG is required for clustering of voltage-gated Na channels at
            axon initial segments and for normal action potential firing
  JOURNAL   J Cell Biol 143 (5), 1295-1304 (1998)
   PUBMED   9832557
REFERENCE   7  (residues 1 to 2622)
  AUTHORS   Zhang,X. and Bennett,V.
  TITLE     Restriction of 480/270-kD ankyrin G to axon proximal segments
            requires multiple ankyrin G-specific domains
  JOURNAL   J Cell Biol 142 (6), 1571-1581 (1998)
   PUBMED   9744885
REFERENCE   8  (residues 1 to 2622)
  AUTHORS   Thevananther,S., Kolli,A.H. and Devarajan,P.
  TITLE     Identification of a novel ankyrin isoform (AnkG190) in kidney and
            lung that associates with the plasma membrane and binds alpha-Na,
            K-ATPase
  JOURNAL   J Biol Chem 273 (37), 23952-23958 (1998)
   PUBMED   9727010
REFERENCE   9  (residues 1 to 2622)
  AUTHORS   Kordeli,E., Ludosky,M.A., Deprette,C., Frappier,T. and Cartaud,J.
  TITLE     AnkyrinG is associated with the postsynaptic membrane and the
            sarcoplasmic reticulum in the skeletal muscle fiber
  JOURNAL   J Cell Sci 111 (Pt 15), 2197-2207 (1998)
   PUBMED   9664041
REFERENCE   10 (residues 1 to 2622)
  AUTHORS   Peters,L.L., John,K.M., Lu,F.M., Eicher,E.M., Higgins,A.,
            Yialamas,M., Turtzo,L.C., Otsuka,A.J. and Lux,S.E.
  TITLE     Ank3 (epithelial ankyrin), a widely distributed new member of the
            ankyrin gene family and the major ankyrin in kidney, is expressed
            in alternatively spliced forms, including forms that lack the
            repeat domain
  JOURNAL   J Cell Biol 130 (2), 313-330 (1995)
   PUBMED   7615634
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF102552.1 and AJ812023.1.
            
            Transcript Variant: This variant (2) represents the longest variant
            and it encodes the longest protein (isoform 2). Isoform 2 is also
            known as '270 kDa ankyrin-G'.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF102552.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2622
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p11"
     Protein         1..2622
                     /product="ankyrin-3 isoform 2"
                     /note="ankyrin 3 (G); ankyrin 3, epithelial; ankyrin-G;
                     ankyrin 3, node of Ranvier (ankyrin G)"
                     /calculated_mol_wt=284313
     Region          1..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12955; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Region          54..379
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(73,75,79..80,83..85,87..88,92,95,104,106,108,
                     112..113,116..118,120..121,125,128,137,139,141,145..146,
                     149..151,153..154,158,161)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          73..104
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          73..102
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          106..137
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          106..135
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          139..168
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          139..164
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          172..201
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          203..230
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          205..240
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(242,244,248..249,252..254,256..257,261,264,273,275,
                     277,281..282,285..287,289..290,294,297,306,308,310,
                     314..315,318..320,322..323,327,330)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          242..273
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          242..271
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          256..544
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          275..306
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          275..304
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          308..337
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          308..333
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          341..372
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          341..370
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          374..403
                     /region_name="ANK 10"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          377..405
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          407..438
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          407..436
                     /region_name="ANK 11"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          421..709
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          440..471
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          440..469
                     /region_name="ANK 12"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Site            order(473,475,479..480,483..485,487..488,492,495,504,506,
                     508,512..513,516..518,520..521,525,528,537,539,541,
                     545..546,549..551,553..554,558,561)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          473..504
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          473..502
                     /region_name="ANK 13"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          506..537
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          506..535
                     /region_name="ANK 14"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          539..568
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          539..568
                     /region_name="ANK 15"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          572..601
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          572..601
                     /region_name="ANK 16"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          605..634
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          605..634
                     /region_name="ANK 17"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          608..>817
                     /region_name="PHA03100"
                     /note="ankyrin repeat protein; Provisional; cl39094"
                     /db_xref="CDD:476869"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Region          638..669
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          638..667
                     /region_name="ANK 18"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          671..702
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          671..700
                     /region_name="ANK 19"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Site            order(704,706,710..711,714..716,718..719,723,726,735,737,
                     739,743..744,747..749,751..752,756,759,768,770,772,
                     776..777,780..782,784..785,789,792)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          704..735
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          704..733
                     /region_name="ANK 20"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          737..768
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          737..766
                     /region_name="ANK 21"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          770..799
                     /region_name="ANK 22"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          770..798
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          803..832
                     /region_name="ANK 23"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Site            851
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Site            855
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Region          868..889
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Site            869
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Site            875
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Site            921
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Site            924
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Site            930
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:G5E8K5; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Site            965
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Site            967
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Region          990..1094
                     /region_name="ZU5"
                     /note="Domain present in ZO-1 and Unc5-like netrin
                     receptors; smart00218"
                     /db_xref="CDD:128514"
     Site            1121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Region          1316..1445
                     /region_name="UPA_2"
                     /note="UPA domain; pfam17809"
                     /db_xref="CDD:375346"
     Site            1458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Site            1469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:G5E8K5; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Region          <1472..1879
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          1510..1539
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Site            1621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:G5E8K5; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Site            1624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:G5E8K5; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Site            1679
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Region          1968..1992
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Site            1984
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Region          <2045..2317
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          2099..2147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Site            2102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Site            2114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Site            2117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Region          2292..2312
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     Region          2334..2417
                     /region_name="Death_ank3"
                     /note="Death domain of Ankyrin-3; cd08803"
                     /db_xref="CDD:176781"
     Site            2457
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Site            2475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12955; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Site            2544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70511.3)"
     Region          2568..2622
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70511.3)"
     CDS             1..2622
                     /gene="Ank3"
                     /gene_synonym="ANK-3"
                     /coded_by="NM_001033984.1:1..7869"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361833"
                     /db_xref="RGD:620157"
ORIGIN      
        1 mahaasqlkk nrdleinaee etekkkkhrk rsrdrkkksd anasylraar aghlekaldy
       61 ikngvdvnic nqnglnalhl askeghvevv sellqreanv daatkkgnta lhiaslagqa
      121 evvkvlvtng anvnaqsqng ftplymaaqe nhlevvrfll dngasqslat edgftplava
      181 lqqghdqvvs lllendtkgk vrlpalhiaa rkddtkaaal llqndtnadi eskmvvnrat
      241 esgftplhia ahygninvat lllnraaavd ftarnditpl hvaskrgnan mvkllldrga
      301 kidaktrdgl tplhcgarsg heqvvemlld raapilsktk nglsplhmat qgdhlncvql
      361 llqhnvpvdd vtndyltalh vaahcghykv akvlldkkan pnakalngft plhiackknr
      421 irvmelllkh gasiqavtes gltpihvaaf mghvnivsql mhhgaspntt nvrgetalhm
      481 aarsgqaevv rylvqdgaqv eakakddqtp lhisarlgka divqqllqqg aspnaattsg
      541 ytplhlsare ghedvaafll dhgaslsitt kkgftplhva akygklevas lllqksaspd
      601 aagksgltpl hvaahydnqk valllldqga sphaaakngy tplhiaakkn qmdiatslle
      661 ygadanavtr qgiasvhlaa qeghvdmvsl llsrnanvnl snksgltplh laaqedrvnv
      721 aevlvnqgah vdaqtkmgyt plhvgchygn ikivnfllqh sakvnaktkn gytplhqaaq
      781 qghthiinvl lqnnaspnel tvngntalai arrlgyisvv dtlkvvteei mttttitekh
      841 kmnvpetmne vldmsddevg kasapeklsd geyisdgeeg edaitgdtdk ylgpqdlkel
      901 gddslpaegy vgfslgarsa slrsfssdrs ytlnrssyar dsmmieellv pskeqhlpft
      961 refdsdslrh yswaadtldn vnlvsspvhs gflvsfmvda rggsmrgsrh hgmriiippr
     1021 kctaptritc rlvkrhklan pppmvegegl asrlvemgpa gaqflgpviv eiphfgsmrg
     1081 kerelivlrs engetwkehq fdsknedlse llngmdeeld speelgtkri criitkdfpq
     1141 yfavvsrikq esnqigpegg ilssttvplv qasfpegalt krirvglqaq pvpeetvkki
     1201 lgnkatfspi vtveprrrkf hkpitmtipv pppsgegvsn gykgdttpsl rllcsitggt
     1261 spaqweditg ttpltfikdc vsfttnvsar fwladchqvl etvglasqly relicvpyma
     1321 kfvvfaktnd pvesslrcfc mtddrvdktl eqqenfeeva rskdievleg kpiyvdcygn
     1381 lapltkggqq lvfnfysfke nrlpfsikvr dtsqepcgrl sflkepkttk glpqtavcnl
     1441 nitlpahkka ekadrrqsft slalrkrysy ltepsmktve rssgtarslp ttyshkpffs
     1501 trpyqswttt pitvpgpaks gslssspsnt psasplksiw svstpspiks tlgasttssv
     1561 ksisdvaspi rsfrtisspi rtvaspspyn tqvasgtlgr vptiteatpi kgvapnstls
     1621 srtspvttag sllekssitm tppaspkani tmyssslpfk siitsaapli ssplksvvsp
     1681 tksaadvist akaamastls splkqmsgha evalvngsvs plkypsssal ingckatatl
     1741 qdkistatna vssvvsaapd tvekalsttt ampfsplrsy vsaaapsafq slrapsasal
     1801 ynslgpsvgv ttssvtssii tvpvysvgnv laepalkklp dsnsltksaa allspiktlt
     1861 tetrpqphfn rtsspvkssl flassalkps vpsslsssqe ilkdvaemke dlmrmtailq
     1921 tdvpeekpfq tdlpregrid deepfkivek vkedlvkvse ilkkdvcves kgppkspksd
     1981 kghspeddwt efsseeirea rqaaashaps lpervhgkan ltrvidyltn digsssltnl
     2041 kykfeeakke geerqkrilk pamalqehkl kmppasmrps tsekelckma dsffgtdail
     2101 espddfsqhd qdksplsdsg fetrsektps apqsaestgp kplfhevpip pvitetrtev
     2161 vhvirsyeps tgeipqsqpe dpvspkpppt fmelepkpta lsikekvkaf qmkasseeed
     2221 hsrvlskgmr vkeethittt trmvyhsppg secaseriee tmsvhdimka fqsgrdpske
     2281 laglfehksa mspdvaksaa etsaqhaekd nqmkpkleri ievhiekgpq spcertdirm
     2341 aivadhlgls wtelarelnf svdeinqirv enpnslisqs fmllkkwvtr dgknattdal
     2401 tsvltkinri divtllegpi fdygnisgtr sfadennvfh dpvdgwqnet psgslespaq
     2461 arritgglld rlddssdqvr dpitsyltge agkfeangnh aevipeakak ayfpesqndi
     2521 gkqsikenlk pkthgcgrae epvspltayq ksleetsklv iedapkpcvp vgmkkmtrtp
     2581 adgkarlnlq eeegsarsep kqgegykvkt kkeirnvekk ah
//
