O57539 (NCOA3_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear receptor coactivator 3
EC=2.3.1.48

Alternative name(s):
Retinoid X receptor-interacting coactivator xSRC-3

Gene names

Name:

ncoa3

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	1391 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, probably via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as retinoids (RAR and RXR), thyroid hormone (TR) and orphan nuclear receptor (hepatocyte nuclear receptor 4 (HNF4) and constitutive androstane receptor (CAR)). Displays histone acetyltransferase activity.
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Interacts with the histone acetyltransferase protein EP300. Ref.1
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Note: Mainly cytoplasmic and weakly nuclear By similarity.
Tissue specificity	Highly expressed in liver and in early stages of oocyte development.
Developmental stage	Expressed only in early stages of oocyte development. Expression is more prominent in stage I, strongly decreases in stage II and then, gradually disappears.
Domain	Contains three Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Motifs 1 and 2 are essential for the association with nuclear receptors, and constitute the RID domain (Receptor-interacting domain).
Post-translational modification	Phosphorylated and acetylated By similarity.
Sequence similarities	Belongs to the SRC/p160 nuclear receptor coactivator family. Contains 1 bHLH (basic helix-loop-helix) domain. Contains 1 PAS (PER-ARNT-SIM) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Molecular function	Activator Acyltransferase Transferase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological_process	histone acetylation Inferred from electronic annotation. Source: GOC regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	histone acetyltransferase activity Inferred from electronic annotation. Source: EC signal transducer activity Inferred from electronic annotation. Source: InterPro transcription coactivator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ncoa3	O57539-1	2	EBI-301587,EBI-301595

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms may be produced.

Isoform 1 (identifier: O57539-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1391	1391	Nuclear receptor coactivator 3		PRO_0000094409
Regions
	Domain	27 – 84	58	bHLH
	Domain	112 – 182	71	PAS
	Region	1088 – 1274	187	Acetyltransferase
	Motif	680 – 684	5	LXXLL motif 1
	Motif	736 – 740	5	LXXLL motif 2
	Motif	1048 – 1052	5	LXXLL motif 3
	Compositional bias	503 – 666	164	Ser-rich
	Compositional bias	515 – 522	8	Poly-Ser
	Compositional bias	968 – 971	4	Poly-Gln
	Compositional bias	1241 – 1248	8	Poly-Gln
Amino acid modifications
	Modified residue	614	1	N6-acetyllysine By similarity
	Modified residue	617	1	N6-acetyllysine By similarity
	Modified residue	618	1	N6-acetyllysine By similarity
Experimental info
	Mutagenesis	622	1	L → A: Weakly impairs interaction with nuclear receptors. Ref.1
	Mutagenesis	683	1	L → A: Strongly impairs interaction with nuclear receptors. Ref.1
	Mutagenesis	739	1	L → A: Strongly impairs interaction with nuclear receptors. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: AD28F5CD934AC33D	FASTA	1,391	152,532
	10 20 30 40 50 60 MSGLGENSLD PLASETRKRK PSSCDTPGPG LTCSGEKRRR EQESKYIEEL ADLISANLSD 70 80 90 100 110 120 IDNFNVKPDK CAILKETVRQ IRQIKEQGKA SSNDDDVQKA DVSSTGQGVI DKDSLGPLLL 130 140 150 160 170 180 QALDGFLYVV NREGSIVFVS ENVTQYLQYK QEDLVNTSVY SILHEEDRKD FLKNLPKSTV 190 200 210 220 230 240 NGVPWFSETP RQKSHTFNCR MLVKTSHDHL EDGSNLDARQ RYETMQCFAL SQPRAMIEEG 250 260 270 280 290 300 EDLQSCMICV ARRITTAERA FSANPESFIT RHDLTGKVVN IDANSLRSSM RPGFEDTIRR 310 320 330 340 350 360 CIQRFLFHSE GQPWTYKRHY QEAYVHGLSE TPLYRFSLAD GTMVTAQTKS KLFRNPVTND 370 380 390 400 410 420 PHGFVSTHFL QREQNGYRPN PNPMAQGIRP QMNPNLPNTM NSMPPQAMQQ QNRNYGMGDP 430 440 450 460 470 480 NSMAQMQGMR YKSPGNMAPV NQAPGVQQSP YQNNSNYGLN MNSPPHGSPG MNANQPNLMV 490 500 510 520 530 540 SPRNRASPKM ASNQFSPVPG MNSPMGSSGN AGGGSFSSSS LSALHAISEG VGSSLLSSLS 550 560 570 580 590 600 SPGQKVENNS NMNMPQQGKI CNQDCKSPSG LYCEQGQVES SVCQSSGREH LGEKDVKENI 610 620 630 640 650 660 FEGSESQRSQ AESKGHKKLL QLLTCFTEER GQSLMSSSSM DCKDSSNVTS PSGVSSSTSI 670 680 690 700 710 720 GVSSTSNLHG SMLQEKHRIL HKLLQNGNSP AEVAKITAEA TGKDVFQETV SSAPCTEATV 730 740 750 760 770 780 KREQLSPKKK ENNALLRHLL DKDDWKDPLA KDIKPKVEHM DIKMGSCSSS NVPTSSQDKE 790 800 810 820 830 840 VKIKTEPGEE VPGDLDNLDA ILGDLAGSDF YSNSMSSRAS DLGPKQPVFQ DSPTLAMRSP 850 860 870 880 890 900 DSMQGSRPPF NRAMSLDSRS STPPVRNVNS FPMLPKQGMI GSPRMMDGQD NFGVMMGSGP 910 920 930 940 950 960 NRSMNQHPGG DWAMQNSAVN RLEPPNVGSV GRPGPDYSSA MTRPAMGGNM PGLLTRSNSI 970 980 990 1000 1010 1020 PGSRPVMQQQ QHILPMRPND MAMSMGSNPY GQQAPSNPPG SWPDAIMMNQ GRGGAQNRQL 1030 1040 1050 1060 1070 1080 GRNSLDDLLC PPSTVEGQTD EIALLDQLHT LLSNTDATGL EEIDRALGIP DLVSQGQALE 1090 1100 1110 1120 1130 1140 PQPDSYQPQG SPVMIDQKPP MYGQHYAGQG AAMSAGGFNN MQGQHPPFNT VMGQMNQQQG 1150 1160 1170 1180 1190 1200 MHPLQGMHPR ANLIRPRNNI PKQLRMQLQQ RLQGQQFLNQ NRQALEMKVD PMNPGGAGVM 1210 1220 1230 1240 1250 1260 RPVMQTPVSQ QGFLNAQMVA QKNRELISHQ IRQHRMAMMM QQQQGQPQAF SPPPNVTASA 1270 1280 1290 1300 1310 1320 SMDNPLGGPP MPQAPPQQFS YPPNYGINQQ TDPTFGRVSS PPNAMMSSRM APSQNPHPQT 1330 1340 1350 1360 1370 1380 TQMYPSPDMK GWPSGNMARP NSFPQQQYSH QTNPATYNMM HMNGNGNHMG QMNINSLPMS 1390 GMPMGPDQKY C

References

[1]

"Molecular cloning of xSRC-3, a novel transcription coactivator from Xenopus, that is related to AIB1, p/CIP and TIF2." Kim H.-J., Lee S.-K., Na S.-Y., Choi H.-S., Lee J.W. Mol. Endocrinol. 12:1038-1047(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RXRA; THRA AND EP300, MUTAGENESIS OF LEU-622; LEU-683 AND LEU-739. Tissue: Oocyte.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF044080 mRNA. Translation: AAC12927.1.
RefSeq	NP_001081732.1. NM_001088263.1.
UniGene	Xl.268.
3D structure databases
ProteinModelPortal	O57539.
SMR	O57539. Positions 1036-1082.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	398021.
KEGG	xla:398021.
Organism-specific databases
CTD	8202.
Xenbase	XB-GENE-865628. ncoa3.
Phylogenomic databases
HOVERGEN	HBG052583.
KO	K11256.
Family and domain databases
Gene3D	4.10.280.10. 1 hit. 4.10.630.10. 2 hits.
InterPro	IPR011598. bHLH_dom. IPR010011. DUF1518. IPR009110. Nuc_rcpt_coact. IPR014920. Nuc_rcpt_coact_Ncoa-typ. IPR017426. Nuclear_rcpt_coactivator. IPR000014. PAS. IPR013767. PAS_fold. IPR014935. SRC-1. IPR008955. Src1_rcpt_coact. [Graphical view]
Pfam	PF07469. DUF1518. 1 hit. PF08815. Nuc_rec_co-act. 1 hit. PF00989. PAS. 1 hit. PF08832. SRC-1. 1 hit. [Graphical view]
PIRSF	PIRSF038181. Nuclear_receptor_coactivator. 1 hit.
SMART	SM00353. HLH. 1 hit. SM00091. PAS. 1 hit. [Graphical view]
SUPFAM	SSF47459. HLH_basic. 1 hit. SSF69125. Nuc_recept_coact. 1 hit.
PROSITE	PS50888. BHLH. 1 hit. PS50112. PAS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NCOA3_XENLA

Accession

Primary (citable) accession number: O57539

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program