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O57539 (NCOA3_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear receptor coactivator 3

EC=2.3.1.48
Alternative name(s):
Retinoid X receptor-interacting coactivator xSRC-3
Gene names
Name:ncoa3
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length1391 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ncoa3O57539-12EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13911391Nuclear receptor coactivator 3
PRO_0000094409

Regions

Domain27 – 8458bHLH
Domain112 – 18271PAS
Region1088 – 1274187Acetyltransferase
Motif680 – 6845LXXLL motif 1
Motif736 – 7405LXXLL motif 2
Motif1048 – 10525LXXLL motif 3
Compositional bias503 – 666164Ser-rich
Compositional bias515 – 5228Poly-Ser
Compositional bias968 – 9714Poly-Gln
Compositional bias1241 – 12488Poly-Gln

Amino acid modifications

Modified residue6141N6-acetyllysine By similarity
Modified residue6171N6-acetyllysine By similarity
Modified residue6181N6-acetyllysine By similarity

Experimental info

Mutagenesis6221L → A: Weakly impairs interaction with nuclear receptors. Ref.1
Mutagenesis6831L → A: Strongly impairs interaction with nuclear receptors. Ref.1
Mutagenesis7391L → A: Strongly impairs interaction with nuclear receptors. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: AD28F5CD934AC33D

FASTA1,391152,532
        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 

« Hide

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.
RefSeqNP_001081732.1. NM_001088263.1. [O57539-1]
UniGeneXl.268.

3D structure databases

ProteinModelPortalO57539.
SMRO57539. Positions 1036-1082.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID398021.
KEGGxla:398021.

Organism-specific databases

CTD8202.
XenbaseXB-GENE-865628. ncoa3.

Phylogenomic databases

HOVERGENHBG052583.
KOK11256.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
4.10.630.10. 2 hits.
InterProIPR011598. bHLH_dom.
IPR010011. DUF1518.
IPR028818. NCOA3.
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]
PANTHERPTHR10684. PTHR10684. 1 hit.
PTHR10684:SF3. PTHR10684:SF3. 1 hit.
PfamPF07469. DUF1518. 1 hit.
PF08815. Nuc_rec_co-act. 1 hit.
PF00989. PAS. 1 hit.
PF08832. SRC-1. 1 hit.
[Graphical view]
PIRSFPIRSF038181. Nuclear_receptor_coactivator. 1 hit.
SMARTSM00353. HLH. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNCOA3_XENLA
AccessionPrimary (citable) accession number: O57539
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: June 1, 1998
Last modified: June 11, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families