CACO1_PONAB
ID CACO1_PONAB Reviewed; 691 AA.
AC Q5RD60; Q5R8A3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Calcium-binding and coiled-coil domain-containing protein 1;
GN Name=CALCOCO1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250|UniProtKB:Q8CGU1}.
CC -!- FUNCTION: Seems to enhance inorganic pyrophosphatase thus activating
CC phosphogluomutase (PMG). Probably functions as component of the
CC calphoglin complex, which is involved in linking cellular metabolism
CC (phosphate and glucose metabolism) with other core functions including
CC protein synthesis and degradation, calcium signaling and cell growth
CC (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250|UniProtKB:Q8CGU1,
CC ECO:0000250|UniProtKB:Q9P1Z2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Shuttles between nucleus and cytoplasm. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RD60-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RD60-2; Sequence=VSP_029054;
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 (By similarity).
CC {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- DOMAIN: Recruitment by nuclear receptors is accomplished by the
CC interaction of the coiled-coiled domain with p160 coactivators.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CALCOCO family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR858058; CAH90297.1; -; mRNA.
DR EMBL; CR859850; CAH92007.1; -; mRNA.
DR RefSeq; NP_001125137.1; NM_001131665.1. [Q5RD60-1]
DR RefSeq; NP_001128845.1; NM_001135373.1.
DR AlphaFoldDB; Q5RD60; -.
DR SMR; Q5RD60; -.
DR GeneID; 100189762; -.
DR KEGG; pon:100189762; -.
DR CTD; 57658; -.
DR eggNOG; ENOG502QR9J; Eukaryota.
DR InParanoid; Q5RD60; -.
DR OrthoDB; 179838at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Activator; Alternative splicing; Coiled coil; Cytoplasm; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; 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_0000308901"
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 /evidence="ECO:0000250"
FT REGION 1..30
FT /note="p300 KIX-binding"
FT /evidence="ECO:0000250"
FT REGION 45..125
FT /note="Interaction with GATA1"
FT /evidence="ECO:0000250|UniProtKB:Q8CGU1"
FT REGION 501..691
FT /note="C-terminal AD (CTNNB1 binding site); interaction
FT with CCAR1"
FT /evidence="ECO:0000250|UniProtKB:Q8CGU1"
FT REGION 513..604
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 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 VAR_SEQ 463..464
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_029054"
FT CONFLICT 136
FT /note="S -> G (in Ref. 1; CAH92007)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="L -> P (in Ref. 1; CAH92007)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 691 AA; 77427 MW; 4898EBB59BE27B24 CRC64;
MEESPLSRAP SRGGVNFLNV ARTYIPNTKV ECHYTLPPGT MPSASDWIGI FKVEAACVRD
YHTFVWSSVP ESTADGSPIH TSVQFQASYL PKPGAQLYQF RYVNRQGRVC GQSPPFQFRE
PRPMDELVTL EEADGSSDIL LVVPKATVLQ NQLDESQQER NDLMQLKLQL EGQVTELRSR
VQELERALAT ARQEHTELME QYKGISRSHG EITEERDILS RQQGDHVARI LELEDDIQTI
SEKVLTKEVE LDRLRDTVKA LTREQEKLLG QLKEVQADKE QSEAELQVAQ QENHRLNLDL
KEAKSWQKEQ SAQAQRLKDK VAQMKDTLGQ AQQRVAELEP LKEQLRGAQE LATSSQQKAT
LLGEELASAA AARDRTIAEL HRSRLEVAEV NGRLAELGLH LKEEKCQWSK ERAGLLQSVE
AEKDKILKLS AEILRLEKAV QEERTQNHVF KTELAREKDS SLVQLSESKR ELTELRSALR
VLQKEKEQLQ EEKQELLEYM RKLEARLEKV ADEKWNEDAT TEDEEATAGL SCPAALTDSE
DESPEDMRLP PYGLCEHGDP GSSPAGPREA SPLVVISQPA PISPHLSGPA EDSSSDSEAE
DEKSVLMAAV QSGGEEANLL LPELGNAFYD MASGFTVGPL SETSTGGPAT PTWKECPICK
ERFPAESDKD ALEDHMDGHF FFSTQDPFTF E
