CTNB_TRIGR
ID CTNB_TRIGR Reviewed; 820 AA.
AC P35223;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Catenin beta;
DE AltName: Full=Beta-catenin;
OS Tripneustes gratilla (Hawaian sea urchin) (Echinus gratilla).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Temnopleuroida; Toxopneustidae; Tripneustes.
OX NCBI_TaxID=7673;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8318544; DOI=10.1016/0167-4781(93)90134-y;
RA Rosenthal E.T.;
RT "Identification of homologues to beta-catenin/plakoglobin/armadillo in two
RT invertebrates, Urechis caupo and Tripneustes gratilla.";
RL Biochim. Biophys. Acta 1173:337-341(1993).
CC -!- FUNCTION: Binds to the cytoplasmic domain of the cell-cell adhesion
CC molecule E-cadherin, and perhaps to other (membrane) proteins. The
CC association of catenins to cadherins produces a complex which is linked
CC to the actin filament network, and which seems to be of primary
CC importance for cadherins cell-adhesion properties.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L10354; AAA30089.1; -; mRNA.
DR PIR; S33794; S33794.
DR AlphaFoldDB; P35223; -.
DR SMR; P35223; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR013284; Beta-catenin.
DR PANTHER; PTHR45976; PTHR45976; 1.
DR Pfam; PF00514; Arm; 3.
DR PRINTS; PR01869; BCATNINFAMLY.
DR SMART; SM00185; ARM; 12.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 9.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cytoplasm; Cytoskeleton; Repeat.
FT CHAIN 1..820
FT /note="Catenin beta"
FT /id="PRO_0000064274"
FT REPEAT 157..196
FT /note="ARM 1"
FT REPEAT 199..239
FT /note="ARM 2"
FT REPEAT 241..280
FT /note="ARM 3"
FT REPEAT 283..322
FT /note="ARM 4"
FT REPEAT 367..405
FT /note="ARM 5"
FT REPEAT 406..445
FT /note="ARM 6"
FT REPEAT 448..489
FT /note="ARM 7"
FT REPEAT 495..535
FT /note="ARM 8"
FT REPEAT 603..642
FT /note="ARM 9"
FT REPEAT 644..683
FT /note="ARM 10"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 89361 MW; 57255E0F57795FD3 CRC64;
MEQARYSNQQ SVNPQQKGFG GPGLQDLPKQ DPMQNTMEWQ HHGYGMDSGF QSSATSHPPS
VSSKSRHEDG GEEAQAQGMF EWDAGYGQAY TQEQVDEMNQ QLTQTRSQRV RAAMFPETLE
EGVQIPSTQF DPAHPTAVQR LSEPSQMLKH AVVNLINYQD DADLATRAIP ELTKLLNDDD
LVVVNQAAMM VHQLSKKEAS RHAIMNSPQM VAALVRAMSN SNDAETTRCA AGTLHNLSHH
RAGLLQIFKS GGIPALIKLL SSPVESVLFY AITTLHNLLL HQEGSKMAVR LAGGLQKMVA
LLSRNNPKFL AITTDCLQIL AYGNQESKLI ILASGGPAAL VHIMRTYDYE KLLWTTSRVL
KVLSVCHNNK PAIVEAGGMS ALGLHLGHHS NRLVQNCLWT LRNLSDCHRG TDDIEPLLQM
LVQLLASNDI NVVTCACGIL SNLTCNNSRN KMIVSQMAGV EALVQTLMKA GDREEITEPA
VCALRHVTSR HPGAEMGQNT VRLNYGIPVI VKLLHPPSRW PLIKATVGLI RNLALCSANH
APLREQGALH RLVQLLMRAH QDTQRRSSMG STGSQGGNYA DGVRMEDIVE GTTGALHILA
RDSHNRALIQ GLNCIPLFVQ LLYNNIENIQ RVAAGVLSEL SLEKQGAEMI EQEGATAPLT
ELLHSRNEGV ATYAAAVLYR MSDDKPQDYK KRISVELGNS LFRGDSVPWG DPLDMPSDNQ
ILPPSSMGGH PPDPGYPQPG SVHSLHSNHG EYRQPPPPMQ GYHDGTGPIE PMMQDLDLGG
GGDFGMDPGL PDMGPPASDL NLDSIPPADN TGLAFFDTDL