ID   CBY1_MOUSE              Reviewed;         127 AA.
AC   Q9D1C2;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 150.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Huang C.-H.;
RT   "A novel cytosolic leucine-rich protein.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=17261658; DOI=10.1161/circulationaha.106.642298;
RA   Singh A.M., Li F.-Q., Hamazaki T., Kasahara H., Takemaru K., Terada N.;
RT   "Chibby, an antagonist of the Wnt/beta-catenin pathway, facilitates
RT   cardiomyocyte differentiation of murine embryonic stem cells.";
RL   Circulation 115:617-626(2007).
RN   [5]
RP   FUNCTION.
RX   PubMed=17403895; DOI=10.1128/mcb.01640-06;
RA   Li F.-Q., Singh A.M., Mofunanya A., Love D., Terada N., Moon R.T.,
RA   Takemaru K.;
RT   "Chibby promotes adipocyte differentiation through inhibition of beta-
RT   catenin signaling.";
RL   Mol. Cell. Biol. 27:4347-4354(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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, ECO:0000269|PubMed:17261658,
CC       ECO:0000269|PubMed:17403895}.
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}.
CC   -!- TISSUE SPECIFICITY: Found in heart, brain, lung, liver, muscle, kidney
CC       and testis. Levels are approximately 3-fold higher in embryonic and
CC       adult heart than in lung or liver. {ECO:0000269|PubMed:17261658}.
CC   -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in early stages of
CC       embryonic stem cell differentiation but decreases at later stages when
CC       high expression is restricted to cardiomyocytes.
CC       {ECO:0000269|PubMed:17261658}.
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; AF331040; AAL56061.1; -; mRNA.
DR   EMBL; AK003719; BAB22956.1; -; mRNA.
DR   EMBL; BC005733; AAH05733.1; -; mRNA.
DR   CCDS; CCDS27645.1; -.
DR   RefSeq; NP_082910.1; NM_028634.3.
DR   AlphaFoldDB; Q9D1C2; -.
DR   SMR; Q9D1C2; -.
DR   BioGRID; 216224; 3.
DR   IntAct; Q9D1C2; 1.
DR   STRING; 10090.ENSMUSP00000023064; -.
DR   iPTMnet; Q9D1C2; -.
DR   PhosphoSitePlus; Q9D1C2; -.
DR   jPOST; Q9D1C2; -.
DR   MaxQB; Q9D1C2; -.
DR   PaxDb; 10090-ENSMUSP00000023064; -.
DR   PeptideAtlas; Q9D1C2; -.
DR   ProteomicsDB; 279934; -.
DR   Pumba; Q9D1C2; -.
DR   Antibodypedia; 26394; 194 antibodies from 27 providers.
DR   DNASU; 73739; -.
DR   Ensembl; ENSMUST00000023064.9; ENSMUSP00000023064.8; ENSMUSG00000022428.9.
DR   GeneID; 73739; -.
DR   KEGG; mmu:73739; -.
DR   UCSC; uc007wuc.1; mouse.
DR   AGR; MGI:1920989; -.
DR   CTD; 25776; -.
DR   MGI; MGI:1920989; Cby1.
DR   VEuPathDB; HostDB:ENSMUSG00000022428; -.
DR   eggNOG; ENOG502S6C8; Eukaryota.
DR   GeneTree; ENSGT00940000153137; -.
DR   HOGENOM; CLU_134504_0_0_1; -.
DR   InParanoid; Q9D1C2; -.
DR   OMA; IWMHSAR; -.
DR   OrthoDB; 2903420at2759; -.
DR   PhylomeDB; Q9D1C2; -.
DR   TreeFam; TF324419; -.
DR   Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
DR   BioGRID-ORCS; 73739; 7 hits in 77 CRISPR screens.
DR   PRO; PR:Q9D1C2; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q9D1C2; Protein.
DR   Bgee; ENSMUSG00000022428; Expressed in cortical plate and 248 other cell types or tissues.
DR   GO; GO:0005814; C:centriole; IDA:MGI.
DR   GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR   GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
DR   GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR   GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
DR   GO; GO:0033504; P:floor plate development; IGI:MGI.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISO:MGI.
DR   GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
DR   GO; GO:0008104; P:protein localization; ISO:MGI.
DR   CDD; cd07429; Cby_like; 1.
DR   InterPro; IPR028118; Chibby_fam.
DR   Pfam; PF14645; Chibby; 1.
DR   Genevisible; Q9D1C2; MM.
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_0000058355"
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:0000250|UniProtKB:Q8K4I6"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y3M2"
SQ   SEQUENCE   127 AA;  14535 MW;  7CE38A48D045CCC7 CRC64;
     MPLFGSIFSP KKTPPRKSAS LSNLHSLDRS TRELELGLDY GTPTMNLAGQ SLKFENGQWV
     ADSVISGGVD RRETQRLRKR NQQLEEENNL LRLKVDILLD MLSETTAESH LKDKELDELK
     VTNRRRK
//