CACO1_MOUSE
ID CACO1_MOUSE Reviewed; 691 AA.
AC Q8CGU1; Q5DTX0; Q9D935;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Calcium-binding and coiled-coil domain-containing protein 1;
DE AltName: Full=Coiled-coil coactivator protein;
GN Name=Calcoco1; Synonyms=CocoA, Kiaa1536;
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], FUNCTION, INTERACTION WITH GRIP1, AND TISSUE
RP SPECIFICITY.
RX PubMed=14690606; DOI=10.1016/s1097-2765(03)00450-7;
RA Kim J.H., Li H., Stallcup M.R.;
RT "CoCoA, a nuclear receptor coactivator which acts through an N-terminal
RT activation domain of p160 coactivators.";
RL Mol. Cell 12:1537-1549(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas, and Urinary bladder;
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 TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=15522220; DOI=10.1016/j.bbrc.2004.10.021;
RA Takahashi K., Inuzuka M., Ingi T.;
RT "Cellular signaling mediated by calphoglin-induced activation of IPP and
RT PGM.";
RL Biochem. Biophys. Res. Commun. 325:203-214(2004).
RN [6]
RP INTERACTION WITH AHR AND ARNT.
RX PubMed=15383530; DOI=10.1074/jbc.m408535200;
RA Kim J.H., Stallcup M.R.;
RT "Role of the coiled-coil coactivator (CoCoA) in aryl hydrocarbon receptor-
RT mediated transcription.";
RL J. Biol. Chem. 279:49842-49848(2004).
RN [7]
RP INTERACTION WITH CTNNB; GRIP1 AND P300.
RX PubMed=16344550; DOI=10.1074/jbc.m510403200;
RA Yang C.K., Kim J.H., Li H., Stallcup M.R.;
RT "Differential use of functional domains by coiled-coil coactivator in its
RT synergistic coactivator function with beta-catenin or GRIP1.";
RL J. Biol. Chem. 281:3389-3397(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CTNNB, AND MUTAGENESIS OF
RP PHE-17 AND VAL-20.
RX PubMed=16931570; DOI=10.1210/me.2006-0200;
RA Yang C.K., Kim J.H., Stallcup M.R.;
RT "Role of the N-terminal activation domain of the coiled-coil coactivator in
RT mediating transcriptional activation by beta-catenin.";
RL Mol. Endocrinol. 20:3251-3262(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, 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).
RN [10]
RP FUNCTION, AND INTERACTION WITH CCAR1 AND GATA1.
RX PubMed=24245781; DOI=10.1111/gtc.12104;
RA Mizuta S., Minami T., Fujita H., Kaminaga C., Matsui K., Ishino R.,
RA Fujita A., Oda K., Kawai A., Hasegawa N., Urahama N., Roeder R.G., Ito M.;
RT "CCAR1/CoCoA pair-mediated recruitment of the Mediator defines a novel
RT pathway for GATA1 function.";
RL Genes Cells 19:28-51(2014).
CC -!- FUNCTION: Functions as a coactivator for aryl hydrocarbon and nuclear
CC receptors (NR). Recruited to promoters through its contact with the N-
CC terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of
CC transcription factors or coactivators, such as NCOA2. During ER-
CC activation acts synergistically in combination with other NCOA2-binding
CC proteins, such as EP300, CREBBP and CARM1. Involved in the
CC transcriptional activation of target genes in the Wnt/CTNNB1 pathway.
CC Functions as a secondary coactivator in LEF1-mediated transcriptional
CC activation via its interaction with CTNNB1. Coactivator function for
CC nuclear receptors and LEF1/CTNNB1 involves differential utilization of
CC two different activation regions. In association with CCAR1 enhances
CC GATA1- and MED1-mediated transcriptional activation from the gamma-
CC globin promoter during erythroid differentiation of K562
CC erythroleukemia cells (PubMed:24245781). {ECO:0000269|PubMed:14690606,
CC ECO:0000269|PubMed:16931570, ECO:0000269|PubMed:24245781}.
CC -!- SUBUNIT: Part of a calphoglin complex consisting of CALCOCO1, PPA1 and
CC PGM (By similarity). Interacts with the bHLH-PAS domains of GRIP1, AHR
CC and ARNT. Interacts with CTNNB1 via both its N- and C-terminal regions.
CC Interacts with EP300. Interacts with CCAR1 (via N-terminus) and GATA1.
CC {ECO:0000250|UniProtKB:Q9P1Z2, ECO:0000269|PubMed:14690606,
CC ECO:0000269|PubMed:15383530, ECO:0000269|PubMed:16344550,
CC ECO:0000269|PubMed:16931570, ECO:0000269|PubMed:24245781}.
CC -!- INTERACTION:
CC Q8CGU1; O42486: Bcat; Xeno; NbExp=4; IntAct=EBI-972374, EBI-972394;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16931570}. Nucleus
CC {ECO:0000269|PubMed:16931570}. Note=Shuttles between nucleus and
CC cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined except spleen,
CC with high levels of expression in the heart and kidney.
CC {ECO:0000269|PubMed:14690606, ECO:0000269|PubMed:15522220}.
CC -!- DOMAIN: The C-terminal activation region (AD) is used for downstream
CC signaling. Seems to be essential for coactivator function with nuclear
CC receptors and with the aryl hydrocarbon receptor.
CC -!- DOMAIN: The N-terminal activation region (AD) is necessary and
CC sufficient for synergistic activation of LEF1-mediated transcription by
CC CTNNB1. Contains a EP3000 binding region which is important for
CC synergistic cooperation.
CC -!- DOMAIN: Recruitment by nuclear receptors is accomplished by the
CC interaction of the coiled-coiled domain with p160 coactivators.
CC -!- SIMILARITY: Belongs to the CALCOCO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90452.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY131329; AAN10148.1; -; mRNA.
DR EMBL; AK007393; BAB25009.1; -; mRNA.
DR EMBL; AK035598; BAC29119.1; -; mRNA.
DR EMBL; AK220400; BAD90452.1; ALT_INIT; mRNA.
DR EMBL; BC054783; AAH54783.1; -; mRNA.
DR CCDS; CCDS27889.1; -.
DR RefSeq; NP_080468.1; NM_026192.3.
DR AlphaFoldDB; Q8CGU1; -.
DR SMR; Q8CGU1; -.
DR BioGRID; 212224; 6.
DR IntAct; Q8CGU1; 2.
DR STRING; 10090.ENSMUSP00000023818; -.
DR iPTMnet; Q8CGU1; -.
DR PhosphoSitePlus; Q8CGU1; -.
DR jPOST; Q8CGU1; -.
DR MaxQB; Q8CGU1; -.
DR PaxDb; Q8CGU1; -.
DR PRIDE; Q8CGU1; -.
DR ProteomicsDB; 281739; -.
DR Antibodypedia; 27237; 107 antibodies from 22 providers.
DR Ensembl; ENSMUST00000023818; ENSMUSP00000023818; ENSMUSG00000023055.
DR GeneID; 67488; -.
DR KEGG; mmu:67488; -.
DR UCSC; uc007xws.2; mouse.
DR CTD; 57658; -.
DR MGI; MGI:1914738; Calcoco1.
DR VEuPathDB; HostDB:ENSMUSG00000023055; -.
DR eggNOG; ENOG502QR9J; Eukaryota.
DR GeneTree; ENSGT00950000183025; -.
DR InParanoid; Q8CGU1; -.
DR OMA; GLCEHGD; -.
DR OrthoDB; 179838at2759; -.
DR PhylomeDB; Q8CGU1; -.
DR TreeFam; TF329501; -.
DR BioGRID-ORCS; 67488; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Calcoco1; mouse.
DR PRO; PR:Q8CGU1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8CGU1; protein.
DR Bgee; ENSMUSG00000023055; Expressed in ascending aorta and 212 other tissues.
DR ExpressionAtlas; Q8CGU1; baseline and differential.
DR Genevisible; Q8CGU1; MM.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0070016; F:armadillo repeat domain binding; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:HGNC-UCL.
DR GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IDA:HGNC-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:HGNC-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IDA:HGNC-UCL.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR012852; CALCOCO1-like.
DR InterPro; IPR041641; CALCOCO1/2_Zn_UBZ1.
DR InterPro; IPR041611; SKICH.
DR Pfam; PF07888; CALCOCO1; 1.
DR Pfam; PF17751; SKICH; 1.
DR Pfam; PF18112; Zn-C2H2_12; 1.
DR PROSITE; PS51905; ZF_UBZ1; 1.
PE 1: Evidence at protein level;
KW Activator; Coiled coil; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Wnt signaling pathway; Zinc; Zinc-finger.
FT CHAIN 1..691
FT /note="Calcium-binding and coiled-coil domain-containing
FT protein 1"
FT /id="PRO_0000308900"
FT ZN_FING 653..679
FT /note="UBZ1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT REGION 1..190
FT /note="N-terminal AD (CTNNB1 binding site)"
FT REGION 1..30
FT /note="p300 KIX-binding"
FT REGION 45..125
FT /note="Interaction with GATA1"
FT /evidence="ECO:0000269|PubMed:24245781"
FT REGION 501..691
FT /note="C-terminal AD (CTNNB1 binding site); interaction
FT with CCAR1"
FT /evidence="ECO:0000269|PubMed:24245781"
FT REGION 512..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 145..205
FT /evidence="ECO:0000255"
FT COILED 232..339
FT /evidence="ECO:0000255"
FT COILED 417..514
FT /evidence="ECO:0000255"
FT COMPBIAS 554..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 656
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 659
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 675
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 679
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Z2"
FT MUTAGEN 17
FT /note="F->A: Loss of interaction with p300 KIX domain;
FT eliminated the autonomous transactivation function."
FT /evidence="ECO:0000269|PubMed:16931570"
FT MUTAGEN 20
FT /note="V->A: Reduced binding to p300 KIX domain; severe
FT reduction in the autonomous transactivation function."
FT /evidence="ECO:0000269|PubMed:16931570"
FT MUTAGEN 20
FT /note="V->P: Reduced binding to p300 KIX domain; severe
FT reduction in the autonomous transactivation function."
FT /evidence="ECO:0000269|PubMed:16931570"
FT CONFLICT 301
FT /note="E -> Q (in Ref. 1; AAN10148 and 3; BAD90452)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 691 AA; 77280 MW; 4759E5478839D9B7 CRC64;
MEESSLSRAP SRGGVNFLNV ARTYIPNTKV ECHYTLPPGT MPSASDWIGI FKVEAACVRD
YHTFVWSSVP ESTTDGSPTH ASVQFQASYL PKPGAQLYQF RYVNRQGRVC GQSPPFQFRE
PRPMDELVTL EEADGGSDIL LVVPKATVLQ NQLDESQQER NDLMQLKLQL EDQVTELRSR
VQELEAALAT ARQEHSELTE QYKGLSRSHG ELSEERDILS QQQGDHVARI LELEDDIQTM
SDKVLMKEVE LDRVRDTVKA LTREQEKLLR QLKEFQADKE QSEAELQTVR EENCCLNTEL
EEAKSRQEEQ GAQVQRLKDK LAHMKDTLGQ AQQKVAELEP LKEQLRGVQE LAASSQQKAA
LLGEELASAA GARDRTIAEL HRSRLEVAEV NGRLAELSLH MKEEKCQWSK ERTGLLQSME
AEKDKILKLS AEILRLEKTV QEERTQSHVF KTELAREKDS SLVQLSESKR ELTELRSALR
VLQKEKEQLQ TEKQELLEYM RKLEARLEKV ADEKWTEDAA TEDEEATAGL SCPASLTDSE
DESPEDMRLP SYGLCESGNT SSSPPGPREP SSLVVINQPA PIAPQFSGPG EASSSDSEAE
DEKSVLMAAV QSGGEEASLL LPELGSAFYD VASAFTVSSL SEASPGVPAN PPWKECPICK
ERFPAESDKD ALEGHMDGHF FFSTQDPFTF E
