CTND2_MOUSE
ID CTND2_MOUSE Reviewed; 1247 AA.
AC O35927; B2RR80;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 176.
DE RecName: Full=Catenin delta-2;
DE AltName: Full=Neural plakophilin-related ARM-repeat protein;
DE Short=NPRAP;
DE AltName: Full=Neurojungin;
GN Name=Ctnnd2; Synonyms=Catnd2, Nprap;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RC TISSUE=Fetal brain;
RX PubMed=9342840; DOI=10.1046/j.1432-0436.1997.6150293.x;
RA Paffenholz R., Franke W.W.;
RT "Identification and localization of a neurally expressed member of the
RT plakoglobin/armadillo multigene family.";
RL Differentiation 61:293-304(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND INTERACTION WITH E-CADHERIN.
RC TISSUE=Brain;
RX PubMed=9971746; DOI=10.1083/jcb.144.3.519;
RA Lu Q., Paredes M., Medina M., Zhou J., Cavallo R., Peifer M., Orecchio L.,
RA Kosik K.S.;
RT "Delta-catenin, an adhesive junction-associated protein which promotes cell
RT scattering.";
RL J. Cell Biol. 144:519-532(1999).
RN [4]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), AND INDUCTION.
RX PubMed=10626844; DOI=10.1016/s0304-3940(99)00875-7;
RA Kawamura Y., Fan Q.W., Hayashi H., Michikawa M., Yanagisawa K., Komano H.;
RT "Expression of the mRNA for two isoforms of neural plakophilin-related arm-
RT repeat protein/delta-catenin in rodent neurons and glial cells.";
RL Neurosci. Lett. 277:185-188(1999).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=10753311;
RX DOI=10.1002/(sici)1096-9861(20000501)420:2<261::aid-cne8>3.0.co;2-q;
RA Ho C., Zhou J., Medina M., Goto T., Jacobson M., Bhide P.G., Kosik K.S.;
RT "Delta-catenin is a nervous system-specific adherens junction protein which
RT undergoes dynamic relocalization during development.";
RL J. Comp. Neurol. 420:261-276(2000).
RN [6]
RP FUNCTION, INTERACTION WITH ZBTB33, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15282317; DOI=10.1128/mcb.24.16.7188-7196.2004;
RA Rodova M., Kelly K.F., VanSaun M., Daniel J.M., Werle M.J.;
RT "Regulation of the rapsyn promoter by kaiso and delta-catenin.";
RL Mol. Cell. Biol. 24:7188-7196(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1098, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452088; DOI=10.1074/mcp.t500040-mcp200;
RA Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A.,
RA Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A.,
RA Schoepfer R., Burlingame A.L.;
RT "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT preparations using lectin weak affinity chromatography and mass
RT spectrometry.";
RL Mol. Cell. Proteomics 5:923-934(2006).
RN [10]
RP FUNCTION, AND INTERACTION WITH ARHGEF28.
RX PubMed=17993462; DOI=10.1074/jbc.m707158200;
RA Kim H., Han J.-R., Park J., Oh M., James S.E., Chang S., Lu Q., Lee K.Y.,
RA Ki H., Song W.-J., Kim K.;
RT "Delta-catenin-induced dendritic morphogenesis. An essential role of
RT p190RhoGEF interaction through Akt1-mediated phosphorylation.";
RL J. Biol. Chem. 283:977-987(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-513, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [12]
RP INTERACTION WITH GSK3A AND GSK3B, AND PHOSPHORYLATION BY GSK3B.
RX PubMed=19706605; DOI=10.1074/jbc.m109.002659;
RA Oh M., Kim H., Yang I., Park J.H., Cong W.T., Baek M.C., Bareiss S., Ki H.,
RA Lu Q., No J., Kwon I., Choi J.K., Kim K.;
RT "GSK-3 phosphorylates delta-catenin and negatively regulates its stability
RT via ubiquitination/proteosome-mediated proteolysis.";
RL J. Biol. Chem. 284:28579-28589(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-264; SER-273; SER-324;
RP SER-357; SER-412; SER-458; SER-511 AND SER-1087, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
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 expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP FUNCTION, AND INTERACTION WITH GSK3B.
RX PubMed=20623542; DOI=10.1002/jnr.22414;
RA Bareiss S., Kim K., Lu Q.;
RT "Delta-catenin/NPRAP: A new member of the glycogen synthase kinase-3beta
RT signaling complex that promotes beta-catenin turnover in neurons.";
RL J. Neurosci. Res. 88:2350-2363(2010).
RN [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-209; ARG-261; ARG-279 AND
RP ARG-293, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [16]
RP FUNCTION.
RX PubMed=25807484; DOI=10.1038/nature14186;
RA Turner T.N., Sharma K., Oh E.C., Liu Y.P., Collins R.L., Sosa M.X.,
RA Auer D.R., Brand H., Sanders S.J., Moreno-De-Luca D., Pihur V., Plona T.,
RA Pike K., Soppet D.R., Smith M.W., Cheung S.W., Martin C.L., State M.W.,
RA Talkowski M.E., Cook E., Huganir R., Katsanis N., Chakravarti A.;
RT "Loss of delta-catenin function in severe autism.";
RL Nature 520:51-56(2015).
CC -!- FUNCTION: Has a critical role in neuronal development, particularly in
CC the formation and/or maintenance of dendritic spines and synapses
CC (PubMed:17993462) (PubMed:25807484). Involved in the regulation of
CC canonical Wnt signaling (By similarity). It probably acts on beta-
CC catenin turnover, facilitating beta-catenin interaction with GSK3B,
CC phosphorylation, ubiquitination and degradation (PubMed:20623542). May
CC be involved in neuronal cell adhesion and tissue morphogenesis and
CC integrity by regulating adhesion molecules. Functions as a
CC transcriptional activator when bound to ZBTB33 (PubMed:15282317).
CC {ECO:0000250|UniProtKB:Q9UQB3, ECO:0000269|PubMed:15282317,
CC ECO:0000269|PubMed:17993462, ECO:0000269|PubMed:20623542,
CC ECO:0000269|PubMed:25807484, ECO:0000269|PubMed:9971746}.
CC -!- SUBUNIT: Binds to E-cadherin at a juxtamembrane site within the
CC cytoplasmic domain. Binds to PSEN1. Interacts with PDZD2 (By
CC similarity). Interacts (via the extreme C-terminus) with FRMPD2 (via
CC the PDZ 2 domain) (By similarity). Interacts with ZBTB33. Interacts
CC with ARHGEF28 (PubMed:17993462). Interacts with CDK5 (By similarity).
CC Interacts with CTNNB1 (By similarity). Interacts with GSK3A and GSK3B
CC (PubMed:20623542) (PubMed:19706605). Interacts with DNM2 (By
CC similarity). Interacts with CCDC85B (By similarity).
CC {ECO:0000250|UniProtKB:O35116, ECO:0000250|UniProtKB:Q9UQB3,
CC ECO:0000269|PubMed:15282317, ECO:0000269|PubMed:17993462,
CC ECO:0000269|PubMed:19706605, ECO:0000269|PubMed:20623542,
CC ECO:0000269|PubMed:9971746}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15282317}. Cell
CC junction, adherens junction {ECO:0000269|PubMed:10753311}. Cell
CC projection, dendrite {ECO:0000250|UniProtKB:O35116}. Perikaryon
CC {ECO:0000250|UniProtKB:O35116}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=NPRAPa;
CC IsoId=O35927-1; Sequence=Displayed;
CC Name=2; Synonyms=NPRAPb;
CC IsoId=O35927-2; Sequence=VSP_006747;
CC -!- TISSUE SPECIFICITY: Expressed in neurons and glial cells. Isoform 2 was
CC found to be the most predominant isoform in various brain regions.
CC Expressed at neuromuscular junctions. {ECO:0000269|PubMed:10753311,
CC ECO:0000269|PubMed:15282317}.
CC -!- DEVELOPMENTAL STAGE: Increasingly expressed by 10 dpc. Expression peaks
CC at postnatal day P7 and stays at lower levels in adulthood. First
CC expressed within proliferating neuronal progenitor cells of the
CC neuroepithelium, becomes down-regulated during neuronal migration, and
CC is later reexpressed in the dendritic compartment of postmitotic
CC neurons. In the developing neocortex, it is strongly expressed in the
CC proliferative ventricular zone and the developing cortical plate, yet
CC is conspicuously less prominent in the intermediate zone, which
CC contains migrating cortical neurons, it forms a honeycomb pattern in
CC the neuroepithelium by labeling the cell periphery in a typical
CC adherens junction pattern. By 18 dpc, its expression shifts primarily
CC to nascent apical dendrites, a pattern that continues through
CC adulthood.
CC -!- INDUCTION: By retinoic acid. {ECO:0000269|PubMed:10626844}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:16452088}.
CC -!- PTM: Phosphorylated by CDK5 (By similarity). Phosphorylated by GSK3B
CC (PubMed:19706605). {ECO:0000250|UniProtKB:O35116,
CC ECO:0000269|PubMed:19706605}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
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DR EMBL; U90331; AAB82409.1; -; mRNA.
DR EMBL; BC138260; AAI38261.1; -; mRNA.
DR EMBL; BC138261; AAI38262.1; -; mRNA.
DR PIR; T42209; T42209.
DR RefSeq; NP_032755.2; NM_008729.2.
DR AlphaFoldDB; O35927; -.
DR SMR; O35927; -.
DR BioGRID; 201832; 16.
DR IntAct; O35927; 9.
DR MINT; O35927; -.
DR STRING; 10090.ENSMUSP00000080427; -.
DR iPTMnet; O35927; -.
DR PhosphoSitePlus; O35927; -.
DR SwissPalm; O35927; -.
DR MaxQB; O35927; -.
DR PaxDb; O35927; -.
DR PRIDE; O35927; -.
DR ProteomicsDB; 284144; -. [O35927-1]
DR ProteomicsDB; 284145; -. [O35927-2]
DR DNASU; 18163; -.
DR GeneID; 18163; -.
DR KEGG; mmu:18163; -.
DR CTD; 1501; -.
DR MGI; MGI:1195966; Ctnnd2.
DR eggNOG; KOG1048; Eukaryota.
DR InParanoid; O35927; -.
DR OrthoDB; 233858at2759; -.
DR PhylomeDB; O35927; -.
DR BioGRID-ORCS; 18163; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Ctnnd2; mouse.
DR PRO; PR:O35927; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O35927; protein.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR GO; GO:0060997; P:dendritic spine morphogenesis; ISO:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0001763; P:morphogenesis of a branching structure; IDA:MGI.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR GO; GO:0050808; P:synapse organization; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR028435; Plakophilin/d_Catenin.
DR PANTHER; PTHR10372; PTHR10372; 1.
DR Pfam; PF00514; Arm; 4.
DR SMART; SM00185; ARM; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell projection;
KW Coiled coil; Developmental protein; Glycoprotein; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..1247
FT /note="Catenin delta-2"
FT /id="PRO_0000064300"
FT REPEAT 391..433
FT /note="ARM 1"
FT REPEAT 537..576
FT /note="ARM 2"
FT REPEAT 579..618
FT /note="ARM 3"
FT REPEAT 623..663
FT /note="ARM 4"
FT REPEAT 679..721
FT /note="ARM 5"
FT REPEAT 725..770
FT /note="ARM 6"
FT REPEAT 832..872
FT /note="ARM 7"
FT REPEAT 904..943
FT /note="ARM 8"
FT REPEAT 997..1040
FT /note="ARM 9"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 49..84
FT /evidence="ECO:0000255"
FT COMPBIAS 22..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 209
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 261
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 279
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 293
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 513
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT VAR_SEQ 878..902
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006747"
SQ SEQUENCE 1247 AA; 135000 MW; D4A7A6B6A27D2919 CRC64;
MFARKQSGAA PFGAMPVPDQ PPSASEKNSS LSPGLNTSNG DGSETETTSA ILASVKEQEL
QFERLTRELE AERQIVASQL ERCKLGSETG SMSSISSAGE QFHWQTQDGQ KDIEDELTTG
LELVDSCIRS LQESGILDPQ DYSTSERPSL LSQSALQLNS KPEGSFQYPA SYHSNQTLAL
GDTAPSQLPA RSTQARAAGQ SFSQGTTGRA GHLAGSEPAP PPPPPREPFA PSLGSAFHLP
DAPPAAAALY YSSSTLPAPP RGGSPLTTTQ GGSPTKLQRG GSAPEGAAYA APRGSSPKQS
PSRLAKSYST SSPINIVVSS AGLSPIRVTS PPTVQSTISS SPIHQLSSTI GTYATLSPTK
RLVHASEQYS KHSQELYATA TLQRPGSLAA GSRASYSSQH GHLAPELRAL QSPEHHIDPI
YEDRVYQKPP MRSLSQSQGD PLPPAHTGTF RTSTAPSSPG VDSVPLQRTG SQHGPQNAAA
ATFQRASYAA GPASNYADPY RQLQYCASVD SPYSKSGPAL PPEGTLARSP SIDSIQKDPR
EFGWRDPELP EVIQMLQHQF PSVQSNAAAY LQHLCFGDNK IKAEIRRQGG IQLLVDLLDH
RMTEVHRSAC GALRNLVYGK ANDDNKIALK NCGGIPALVR LLRKTTDLEI RELVTGVLWN
LSSCDALKMP IIQDALAVLT NAVIIPHSGW ENSPLQDDRK IQLHSSQVLR NATGCLRNVS
SAGEEARRRM RECDGLTDAL LYVIQSALGS SEIDSKTVEN CVCILRNLSY RLAAETSQGQ
HMGTDELDGL LCGETNGKDT ESSGCWGKKK KKKKSQDQWD GVGPLPDCAE PPKGIQMLWH
PSIVKPYLTL LSECSNPDTL EGAAGALQNL AAGSWKGWAE DVAGMAYALR SLPEGAPCLP
QWSVYIRAAV RKEKGLPILV ELLRIDNDRV VCAVATALRN MALDVRNKEL IGKYAMRDLV
HRLPGGNNSN NSGSKAMSDD TVTAVCCTLH EVITKNMENA KALRDAGGIE KLVGISKSKG
DKHSPKVVKA ASQVLNSMWQ YRDLRSLYKK DGWSQYHFVA SSSTIERDRQ RPYSSSRTPS
ISPVRVSPNN RSASAPASPR EMISLKERKT DYESAGNNAT YHGTKGEHTS RKDTMTAQNT
GVSTLYRNSY GAPAEDIKQN QVSTQPVPQE PSRKDYETYQ PFPNSTRNYD ESFFEDQVHH
RPPASEYTMH LGLKSTGNYV DFYSAARPYS ELNYETSHYP ASPDSWV
