CBY1_RAT
ID CBY1_RAT Reviewed; 127 AA.
AC Q8K4I6;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein chibby homolog 1;
DE AltName: Full=Cytosolic leucine-rich protein;
DE AltName: Full=PIGEA-14;
DE AltName: Full=PKD2 interactor, Golgi and endoplasmic reticulum-associated 1;
GN Name=Cby1; Synonyms=Cby, Pgea1;
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].
RA Huang C.-H.;
RT "A conserved cytosolic leucine-rich protein (LRP) in vertebrate animals.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-20, AND
RP IDENTIFICATION BY 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: Inhibits the Wnt/Wingless pathway by binding to CTNNB1/beta-
CC catenin and inhibiting beta-catenin-mediated transcriptional activation
CC through competition with TCF/LEF transcription factors. Has also been
CC shown to play a role in regulating the intracellular trafficking of
CC polycystin-2/PKD2 and possibly of other intracellular proteins.
CC Promotes adipocyte and cardiomyocyte differentiation.
CC {ECO:0000250|UniProtKB:Q9Y3M2}.
CC -!- SUBUNIT: Homodimer. Interacts with polycystin-2/PKD2 and GM130.
CC Interacts with the C-terminal region of CTNNB1. Interacts (C-terminus)
CC with TCIM (C-terminus), TCIM competes with CTNNB1 for the interaction
CC with CBY1. Interacts with FAM92A; this interaction facilitates
CC targeting of FAM92A to cilium basal body. Interacts with CIBAR2.
CC {ECO:0000250|UniProtKB:Q9Y3M2}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q9Y3M2}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q9Y3M2}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q9Y3M2}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9Y3M2}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q9Y3M2}. Note=Nuclear, in a punctate manner (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y3M2}.
CC -!- MISCELLANEOUS: 'Chibby' is Japanese for 'small'; the gene was so named
CC for the RNAi phenotype seen in flies.
CC -!- SIMILARITY: Belongs to the chibby family. {ECO:0000305}.
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DR EMBL; AF393211; AAM73679.1; -; mRNA.
DR RefSeq; NP_663709.1; NM_145676.1.
DR RefSeq; XP_006242029.1; XM_006241967.3.
DR AlphaFoldDB; Q8K4I6; -.
DR SMR; Q8K4I6; -.
DR STRING; 10116.ENSRNOP00000018787; -.
DR iPTMnet; Q8K4I6; -.
DR PhosphoSitePlus; Q8K4I6; -.
DR PaxDb; Q8K4I6; -.
DR PRIDE; Q8K4I6; -.
DR GeneID; 246768; -.
DR KEGG; rno:246768; -.
DR UCSC; RGD:708481; rat.
DR CTD; 25776; -.
DR RGD; 708481; Cby1.
DR eggNOG; ENOG502S6C8; Eukaryota.
DR HOGENOM; CLU_134504_0_0_1; -.
DR InParanoid; Q8K4I6; -.
DR OMA; IWMHSAR; -.
DR OrthoDB; 1492677at2759; -.
DR PhylomeDB; Q8K4I6; -.
DR TreeFam; TF324419; -.
DR Reactome; R-RNO-3769402; Deactivation of the beta-catenin transactivating complex.
DR PRO; PR:Q8K4I6; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000013892; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q8K4I6; RN.
DR GO; GO:0005814; C:centriole; ISO:RGD.
DR GO; GO:0036064; C:ciliary basal body; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0033504; P:floor plate development; ISO:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISO:RGD.
DR GO; GO:0051289; P:protein homotetramerization; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR CDD; cd07429; Cby_like; 1.
DR InterPro; IPR028118; Chibby_fam.
DR Pfam; PF14645; Chibby; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW Cytoskeleton; Differentiation; Golgi apparatus; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..127
FT /note="Protein chibby homolog 1"
FT /id="PRO_0000058356"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..112
FT /note="Minimal region for the interaction with PKD2"
FT /evidence="ECO:0000250"
FT COILED 68..110
FT /evidence="ECO:0000255"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 127 AA; 14549 MW; 7CE38A48D045DE57 CRC64;
MPLFGSIFSP KKTPPRKSAS LSNLHSLDRS TRELELGLDY GTPTMNLAGQ SLKFENGQWV
ADSVISGGVD RRETQRLRKR NQQLEEENNL LRLKVDILLD MLSETTAESH LKDKELDELK
ITNRRRK
