CTBL1_RAT
ID CTBL1_RAT Reviewed; 563 AA.
AC Q4V8K2;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Beta-catenin-like protein 1;
DE AltName: Full=Nuclear-associated protein;
DE Short=NAP;
GN Name=Ctnnbl1;
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 [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Component of the PRP19-CDC5L complex that forms an integral
CC part of the spliceosome and is required for activating pre-mRNA
CC splicing. Participates in AID/AICDA-mediated Ig class switching
CC recombination (CSR). May induce apoptosis (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the PRP19-CDC5L splicing complex composed of a
CC core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and
CC BCAS2, and at least three less stably associated proteins CTNNBL1,
CC CWC15 and HSPA8. Interacts directly with CWC15 and CDC5L in the
CC complex. Interacts with AICDA; the interaction is important for the
CC antibody diversification activity of AICDA. Interacts with PRPF31 (via
CC its NLS). Interacts (via its N-terminal NLS) with KPNA1 and KPNA2 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The surface residues of the concave side of the superhelical
CC ARM repeat region contribute to, but are not essential for NLS binding.
CC {ECO:0000250}.
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DR EMBL; BC097352; AAH97352.1; -; mRNA.
DR RefSeq; NP_001020041.1; NM_001024870.1.
DR AlphaFoldDB; Q4V8K2; -.
DR SMR; Q4V8K2; -.
DR STRING; 10116.ENSRNOP00000060192; -.
DR iPTMnet; Q4V8K2; -.
DR PhosphoSitePlus; Q4V8K2; -.
DR jPOST; Q4V8K2; -.
DR PaxDb; Q4V8K2; -.
DR PRIDE; Q4V8K2; -.
DR GeneID; 296320; -.
DR KEGG; rno:296320; -.
DR UCSC; RGD:1563558; rat.
DR CTD; 56259; -.
DR RGD; 1563558; Ctnnbl1.
DR VEuPathDB; HostDB:ENSRNOG00000012021; -.
DR eggNOG; KOG2734; Eukaryota.
DR HOGENOM; CLU_017098_2_1_1; -.
DR InParanoid; Q4V8K2; -.
DR OMA; TDWREQE; -.
DR OrthoDB; 724270at2759; -.
DR PhylomeDB; Q4V8K2; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q4V8K2; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000012021; Expressed in thymus and 20 other tissues.
DR Genevisible; Q4V8K2; RN.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0016445; P:somatic diversification of immunoglobulins; ISO:RGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039678; CTNNBL1.
DR InterPro; IPR013180; CTNNBL1_N.
DR PANTHER; PTHR14978; PTHR14978; 1.
DR Pfam; PF08216; CTNNBL; 1.
DR SMART; SM01156; DUF1716; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Coiled coil; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Spliceosome.
FT CHAIN 1..563
FT /note="Beta-catenin-like protein 1"
FT /id="PRO_0000239450"
FT REPEAT 79..129
FT /note="HEAT 1"
FT REPEAT 134..176
FT /note="HEAT 2"
FT REPEAT 178..228
FT /note="ARM 1"
FT REPEAT 229..273
FT /note="ARM 2"
FT REPEAT 274..323
FT /note="ARM 3"
FT REPEAT 325..363
FT /note="ARM 4"
FT REPEAT 364..417
FT /note="ARM 5"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 476..540
FT /evidence="ECO:0000250"
FT MOTIF 16..33
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 130..140
FT /note="Nuclear export signal (NES)"
FT /evidence="ECO:0000250"
FT COMPBIAS 14..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYA6"
FT MOD_RES 91
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYA6"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYA6"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 563 AA; 64948 MW; 7363EFB389CFFD80 CRC64;
MDVGELLSYQ PNRGTKRPRD DEEEELKTRR KQTGPRERGR YREDEATAAE DADDDKKRLL
QIIDRDGEEE EEEEEPLDES SVKKMILTFE KRSYKNQELR IKFPDNPEKF MESELDLNDI
IQEMHVVATM PDLYHLLVEL SAVQSLLGLL GHDNTDVSIA VVDLLQELTD IDTLHESEEG
AEVLIDALVD GQVVALLVQN LERLDESVRE EADGVHNTLA IVENMAEFRP EMCTEAAQQG
LLQWLLKRLK AKMPFDANKL YCSEVLAILL QDNDENRELL GELDGIDVLL QQLSVFKRHN
PSTAEEQEMM ENLFDALCSC LMLSSNRERF LKGEGLQLMN LMLREKKISR SSALKVLDHA
MIGPEGADNC HKFVDILGLR TIFPLFMKSP RKIKKVGTTE KEHEEHVCSI LASLLRNLRG
QQRTRLLNKF TENDSEKVDR LMELHFKYLG AMQVADKKIE GEKHDIVRRG EIIDNDMEDE
FYLRRLDAGL FILQHICYIM AEICNANVPQ IRQRVHQILN MRGSSIKIVR HIIKEYAENI
GDGRSPEFRE TEQKRILGLL ENF
