CTNB_URECA
ID CTNB_URECA Reviewed; 818 AA.
AC P35224;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Catenin beta;
DE AltName: Full=Beta-catenin;
OS Urechis caupo (Innkeeper worm) (Spoonworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Echiura; Xenopneusta; Urechidae; Urechis.
OX NCBI_TaxID=6431;
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}.
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DR EMBL; L10355; AAA30330.1; -; mRNA.
DR PIR; S33793; S33793.
DR AlphaFoldDB; P35224; -.
DR SMR; P35224; -.
DR PRIDE; P35224; -.
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..818
FT /note="Catenin beta"
FT /id="PRO_0000064275"
FT REPEAT 164..203
FT /note="ARM 1"
FT REPEAT 248..287
FT /note="ARM 2"
FT REPEAT 412..451
FT /note="ARM 3"
FT REPEAT 454..495
FT /note="ARM 4"
FT REPEAT 501..541
FT /note="ARM 5"
FT REPEAT 543..582
FT /note="ARM 6"
FT REPEAT 648..687
FT /note="ARM 7"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..818
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 48..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 89070 MW; 1DF174BEEF745C1D CRC64;
METYQQMNSG SGPRSVGTPQ GQYMDVGEMP PMDAKQQTML WQQNQYMGDS GIQSGATTQA
PPSVSSKHGL DDMDTGEGMD TSRMMFDFDQ GFSTQAFTQE QVDEMNQQLN QTRSQRVRAA
MFPETLEEGV QIPSTQLDPG QPTAVQRLSE PSQMLKHAVV NLINYQDDAD LATRAIPELT
KLLNDEDQVV VSQAAMMVHQ LSKKEASRHA IMNSPQMVAA LVRAMTNTND LETTRCAAGT
LHNLSHHRQG LLTIFKSGGI PALVKLLSSP VESVLFYAIT TLHNLLLHQE GSKMAVRLAG
GLQKMVLLLQ RNNLKFLAIT TDCLQILAYG NQESKLIILA SGGPGELVRI MRSYTYEKLL
WTTSRVLKVL SVCASNKPAI VEAGSAGPSM HLGHQSQRLV QNCLWTLRNL SDAATKSSDI
EGLLQMLVQL LASNDINIVT CAAGILSNLT CNNQRNKVTV CQVGGIEALV RTILQAGDRE
DITEPAVCAL RHLTSRHGEA EMAQNAVRLH YGLPVLVKLL HPPSRWPLIK AVVGLIRNLA
LCPANHAPLR EHGAIPRIVQ LLIRAHQDTQ RRATAGSGNT SAYVDGVRME EIVEGTVGAL
HIMAREAHNR AVIRGLNCIS LFAQLLYSPI DNIQRVAAGV LCELAADKEG AEMIEQEGTT
APLTELLHSR NEGVATYAAA VLFRMSEDKP QDYKKRLSVE LTSSLFRGEQ VPWGEPPGLD
DMDSSQLLPE EQGFRGYQGS GPGSVPSGPP HDMNRQDSMQ GLELGSQQGT AYGSHMPDLG
PNTDLHFDPM DGGGSSMGGP HTPTDPQNQM AAWFDTDL