CTND2_RAT
ID CTND2_RAT Reviewed; 264 AA.
AC O35116;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Catenin delta-2;
DE Flags: Fragment;
GN Name=Ctnnd2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RA Tanahashi H.;
RT "cDNAs encoding presenilin associated proteins.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH PDZD2.
RX PubMed=10896674; DOI=10.1074/jbc.m005384200;
RA Deguchi M., Iizuka T., Hata Y., Nishimura W., Hirao K., Yao I., Kawabe H.,
RA Takai Y.;
RT "A novel multiple PSD-95/Dlg-A/ZO-1 protein interacting with neural
RT plakophilin-related armadillo repeat protein/delta-catenin and p0071.";
RL J. Biol. Chem. 275:29875-29880(2000).
RN [3]
RP PHOSPHORYLATION BY CDK5, INTERACTION WITH CDK5, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17009320; DOI=10.1002/jcb.21041;
RA Munoz J.P., Huichalaf C.H., Orellana D., Maccioni R.B.;
RT "cdk5 modulates beta- and delta-catenin/Pin1 interactions in neuronal
RT cells.";
RL J. Cell. Biochem. 100:738-749(2007).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [5]
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:25807484). Involved in the regulation of canonical Wnt
CC signaling (By similarity). It probably acts on beta-catenin turnover,
CC facilitating beta-catenin interaction with GSK3B, phosphorylation,
CC ubiquitination and degradation (PubMed:20623542). May be involved in
CC neuronal cell adhesion and tissue morphogenesis and integrity by
CC regulating adhesion molecules. Functions as a transcriptional activator
CC when bound to ZBTB33 (By similarity). {ECO:0000250|UniProtKB:O35927,
CC ECO:0000250|UniProtKB:Q9UQB3, ECO:0000269|PubMed:20623542,
CC ECO:0000269|PubMed:25807484}.
CC -!- SUBUNIT: Binds to E-cadherin at a juxtamembrane site within the
CC cytoplasmic domain (By similarity). Binds to PSEN1 (By similarity).
CC Interacts with ZBTB33 (By similarity). Interacts with ARHGEF28 (By
CC similarity). Interacts (via the extreme C-terminus) with FRMPD2 (via
CC the PDZ 2 domain) (By similarity). Interacts with PDZD2
CC (PubMed:10896674). Interacts with CDK5 (PubMed:17009320). Interacts
CC with CTNBB1 (By similarity). Interacts with GSK3A and GSK3B (By
CC similarity). Interacts with DNM2 (By similarity). Interacts with
CC CCDC85B (By similarity). {ECO:0000250|UniProtKB:O35927,
CC ECO:0000250|UniProtKB:Q9UQB3, ECO:0000269|PubMed:10896674,
CC ECO:0000269|PubMed:17009320}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O35927}. Cell
CC junction, adherens junction {ECO:0000250|UniProtKB:O35927}. Cell
CC projection, dendrite {ECO:0000269|PubMed:17009320,
CC ECO:0000269|PubMed:20623542}. Perikaryon {ECO:0000269|PubMed:17009320,
CC ECO:0000269|PubMed:20623542}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain; accumulates in
CC cortical neurons (at protein level). {ECO:0000269|PubMed:17009320}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- PTM: Phosphorylated by CDK5 (PubMed:17009320). Phosphorylated by GSK3B
CC (By similarity). {ECO:0000250|UniProtKB:O35927,
CC ECO:0000269|PubMed:17009320}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
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DR EMBL; AB008752; BAA23384.1; -; mRNA.
DR AlphaFoldDB; O35116; -.
DR SMR; O35116; -.
DR IntAct; O35116; 1.
DR MINT; O35116; -.
DR STRING; 10116.ENSRNOP00000045121; -.
DR SwissPalm; O35116; -.
DR PaxDb; O35116; -.
DR PRIDE; O35116; -.
DR UCSC; RGD:620734; rat.
DR RGD; 620734; Ctnnd2.
DR eggNOG; KOG1048; Eukaryota.
DR InParanoid; O35116; -.
DR PhylomeDB; O35116; -.
DR Proteomes; UP000002494; Unplaced.
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:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
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:RGD.
DR GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
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:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0001763; P:morphogenesis of a branching structure; ISO:RGD.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
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; 2.
DR SMART; SM00185; ARM; 4.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cell projection; Developmental protein;
KW Glycoprotein; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN <1..>264
FT /note="Catenin delta-2"
FT /id="PRO_0000064301"
FT REPEAT 20..59
FT /note="ARM 1"
FT REPEAT 64..104
FT /note="ARM 2"
FT REPEAT 120..162
FT /note="ARM 3"
FT REPEAT 166..211
FT /note="ARM 4"
FT REGION 238..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT NON_TER 264
SQ SEQUENCE 264 AA; 28928 MW; 065A886B8D2F58E0 CRC64;
FPSVQSNAAA YLQHLCFGDN KIKAEIRRQG GIQLLVDLLD HRMTEVHRSA CGALRNLVYG
KANDDNKIAL KNCGGIPALV RLLRKTTDLE IRELVTGVLW NLSSCDALKM PIIQDALAVL
TNAVIIPHSG WENSPLQDDR KIQLHSSQVL RNATGCLRNV SSAGEEARRR MRECDGLTDA
LLYVIQSALG SSEIDSKTVE NCVCILRNLS YRLAAETSQG QHMGTDELDG LLCGEANGKD
AESSGCWGKK KKKKKSQDQW DGVG
