Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Calcium-binding and coiled-coil domain-containing protein 1

Gene

Calcoco1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). Recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. Involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. Coactivator function for nuclear receptors and LEF1/CTNNB1 involves differential utilization of two different activation regions. In association with CCAR1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781).3 Publications

GO - Molecular functioni

GO - Biological processi

  • intracellular steroid hormone receptor signaling pathway Source: HGNC
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • signal transduction Source: HGNC
  • transcription, DNA-templated Source: HGNC
  • Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation, Wnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-binding and coiled-coil domain-containing protein 1
Alternative name(s):
Coiled-coil coactivator protein
Gene namesi
Name:Calcoco1
Synonyms:CocoA, Kiaa1536
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1914738. Calcoco1.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

  • Note: Shuttles between nucleus and cytoplasm.

GO - Cellular componenti

  • cytoplasm Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • nuclear chromatin Source: MGI
  • nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 171F → A: Loss of interaction with p300 KIX domain; eliminated the autonomous transactivation function. 1 Publication
Mutagenesisi20 – 201V → A: Reduced binding to p300 KIX domain; severe reduction in the autonomous transactivation function. 1 Publication
Mutagenesisi20 – 201V → P: Reduced binding to p300 KIX domain; severe reduction in the autonomous transactivation function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 691691Calcium-binding and coiled-coil domain-containing protein 1PRO_0000308900Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8CGU1.
MaxQBiQ8CGU1.
PaxDbiQ8CGU1.
PRIDEiQ8CGU1.

PTM databases

iPTMnetiQ8CGU1.
PhosphoSiteiQ8CGU1.

Expressioni

Tissue specificityi

Expressed in all tissues examined except spleen, with high levels of expression in the heart and kidney.2 Publications

Gene expression databases

BgeeiQ8CGU1.
CleanExiMM_CALCOCO1.
ExpressionAtlasiQ8CGU1. baseline and differential.
GenevisibleiQ8CGU1. MM.

Interactioni

Subunit structurei

Part of a calphoglin complex consisting of CALCOCO1, PPA1 and PGM (By similarity). Interacts with the bHLH-PAS domains of GRIP1, AHR and ARNT. Interacts with CTNNB1 via both its N- and C-terminal regions. Interacts with EP300. Interacts with CCAR1 (via N-terminus) and GATA1.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
chBcatO424864EBI-972374,EBI-972394From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi212224. 2 interactions.
IntActiQ8CGU1. 1 interaction.
STRINGi10090.ENSMUSP00000023818.

Structurei

3D structure databases

ProteinModelPortaliQ8CGU1.
SMRiQ8CGU1. Positions 15-119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 190190N-terminal AD (CTNNB1 binding site)Add
BLAST
Regioni1 – 3030p300 KIX-bindingAdd
BLAST
Regioni45 – 12581Interaction with GATA11 PublicationAdd
BLAST
Regioni501 – 691191C-terminal AD (CTNNB1 binding site); interaction with CCAR11 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili145 – 20561Sequence analysisAdd
BLAST
Coiled coili232 – 339108Sequence analysisAdd
BLAST
Coiled coili417 – 51498Sequence analysisAdd
BLAST

Domaini

The C-terminal activation region (AD) is used for downstream signaling. Seems to be essential for coactivator function with nuclear receptors and with the aryl hydrocarbon receptor.
The N-terminal activation region (AD) is necessary and sufficient for synergistic activation of LEF1-mediated transcription by CTNNB1. Contains a EP3000 binding region which is important for synergistic cooperation.
Recruitment by nuclear receptors is accomplished by the interaction of the coiled-coiled domain with p160 coactivators.

Sequence similaritiesi

Belongs to the CALCOCO family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IHKH. Eukaryota.
ENOG410ZVZ6. LUCA.
GeneTreeiENSGT00530000063216.
HOGENOMiHOG000111283.
HOVERGENiHBG107573.
InParanoidiQ8CGU1.
OMAiYDMASGF.
OrthoDBiEOG7RRF8H.
PhylomeDBiQ8CGU1.
TreeFamiTF329501.

Family and domain databases

InterProiIPR012852. CALCOCO1-like.
[Graphical view]
PfamiPF07888. CALCOCO1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CGU1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEESSLSRAP SRGGVNFLNV ARTYIPNTKV ECHYTLPPGT MPSASDWIGI
60 70 80 90 100
FKVEAACVRD YHTFVWSSVP ESTTDGSPTH ASVQFQASYL PKPGAQLYQF
110 120 130 140 150
RYVNRQGRVC GQSPPFQFRE PRPMDELVTL EEADGGSDIL LVVPKATVLQ
160 170 180 190 200
NQLDESQQER NDLMQLKLQL EDQVTELRSR VQELEAALAT ARQEHSELTE
210 220 230 240 250
QYKGLSRSHG ELSEERDILS QQQGDHVARI LELEDDIQTM SDKVLMKEVE
260 270 280 290 300
LDRVRDTVKA LTREQEKLLR QLKEFQADKE QSEAELQTVR EENCCLNTEL
310 320 330 340 350
EEAKSRQEEQ GAQVQRLKDK LAHMKDTLGQ AQQKVAELEP LKEQLRGVQE
360 370 380 390 400
LAASSQQKAA LLGEELASAA GARDRTIAEL HRSRLEVAEV NGRLAELSLH
410 420 430 440 450
MKEEKCQWSK ERTGLLQSME AEKDKILKLS AEILRLEKTV QEERTQSHVF
460 470 480 490 500
KTELAREKDS SLVQLSESKR ELTELRSALR VLQKEKEQLQ TEKQELLEYM
510 520 530 540 550
RKLEARLEKV ADEKWTEDAA TEDEEATAGL SCPASLTDSE DESPEDMRLP
560 570 580 590 600
SYGLCESGNT SSSPPGPREP SSLVVINQPA PIAPQFSGPG EASSSDSEAE
610 620 630 640 650
DEKSVLMAAV QSGGEEASLL LPELGSAFYD VASAFTVSSL SEASPGVPAN
660 670 680 690
PPWKECPICK ERFPAESDKD ALEGHMDGHF FFSTQDPFTF E
Length:691
Mass (Da):77,280
Last modified:October 23, 2007 - v2
Checksum:i4759E5478839D9B7
GO

Sequence cautioni

The sequence BAD90452.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti301 – 3011E → Q in AAN10148 (PubMed:14690606).Curated
Sequence conflicti301 – 3011E → Q in BAD90452 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY131329 mRNA. Translation: AAN10148.1.
AK007393 mRNA. Translation: BAB25009.1.
AK035598 mRNA. Translation: BAC29119.1.
AK220400 mRNA. Translation: BAD90452.1. Different initiation.
BC054783 mRNA. Translation: AAH54783.1.
CCDSiCCDS27889.1.
RefSeqiNP_080468.1. NM_026192.3.
UniGeneiMm.71682.

Genome annotation databases

EnsembliENSMUST00000023818; ENSMUSP00000023818; ENSMUSG00000023055.
GeneIDi67488.
KEGGimmu:67488.
UCSCiuc007xws.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY131329 mRNA. Translation: AAN10148.1.
AK007393 mRNA. Translation: BAB25009.1.
AK035598 mRNA. Translation: BAC29119.1.
AK220400 mRNA. Translation: BAD90452.1. Different initiation.
BC054783 mRNA. Translation: AAH54783.1.
CCDSiCCDS27889.1.
RefSeqiNP_080468.1. NM_026192.3.
UniGeneiMm.71682.

3D structure databases

ProteinModelPortaliQ8CGU1.
SMRiQ8CGU1. Positions 15-119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212224. 2 interactions.
IntActiQ8CGU1. 1 interaction.
STRINGi10090.ENSMUSP00000023818.

PTM databases

iPTMnetiQ8CGU1.
PhosphoSiteiQ8CGU1.

Proteomic databases

EPDiQ8CGU1.
MaxQBiQ8CGU1.
PaxDbiQ8CGU1.
PRIDEiQ8CGU1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023818; ENSMUSP00000023818; ENSMUSG00000023055.
GeneIDi67488.
KEGGimmu:67488.
UCSCiuc007xws.2. mouse.

Organism-specific databases

CTDi57658.
MGIiMGI:1914738. Calcoco1.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IHKH. Eukaryota.
ENOG410ZVZ6. LUCA.
GeneTreeiENSGT00530000063216.
HOGENOMiHOG000111283.
HOVERGENiHBG107573.
InParanoidiQ8CGU1.
OMAiYDMASGF.
OrthoDBiEOG7RRF8H.
PhylomeDBiQ8CGU1.
TreeFamiTF329501.

Miscellaneous databases

PROiQ8CGU1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CGU1.
CleanExiMM_CALCOCO1.
ExpressionAtlasiQ8CGU1. baseline and differential.
GenevisibleiQ8CGU1. MM.

Family and domain databases

InterProiIPR012852. CALCOCO1-like.
[Graphical view]
PfamiPF07888. CALCOCO1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CoCoA, a nuclear receptor coactivator which acts through an N-terminal activation domain of p160 coactivators."
    Kim J.H., Li H., Stallcup M.R.
    Mol. Cell 12:1537-1549(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH GRIP1, TISSUE SPECIFICITY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pancreas and Urinary bladder.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal brain.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "Cellular signaling mediated by calphoglin-induced activation of IPP and PGM."
    Takahashi K., Inuzuka M., Ingi T.
    Biochem. Biophys. Res. Commun. 325:203-214(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Role of the coiled-coil coactivator (CoCoA) in aryl hydrocarbon receptor-mediated transcription."
    Kim J.H., Stallcup M.R.
    J. Biol. Chem. 279:49842-49848(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AHR AND ARNT.
  7. "Differential use of functional domains by coiled-coil coactivator in its synergistic coactivator function with beta-catenin or GRIP1."
    Yang C.K., Kim J.H., Li H., Stallcup M.R.
    J. Biol. Chem. 281:3389-3397(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTNNB; GRIP1 AND P300.
  8. "Role of the N-terminal activation domain of the coiled-coil coactivator in mediating transcriptional activation by beta-catenin."
    Yang C.K., Kim J.H., Stallcup M.R.
    Mol. Endocrinol. 20:3251-3262(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CTNNB, MUTAGENESIS OF PHE-17 AND VAL-20.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Lung and Testis.
  10. "CCAR1/CoCoA pair-mediated recruitment of the Mediator defines a novel pathway for GATA1 function."
    Mizuta S., Minami T., Fujita H., Kaminaga C., Matsui K., Ishino R., Fujita A., Oda K., Kawai A., Hasegawa N., Urahama N., Roeder R.G., Ito M.
    Genes Cells 19:28-51(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CCAR1 AND GATA1.

Entry informationi

Entry nameiCACO1_MOUSE
AccessioniPrimary (citable) accession number: Q8CGU1
Secondary accession number(s): Q5DTX0, Q9D935
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: October 23, 2007
Last modified: July 6, 2016
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.