ID   NCOA2_XENLA             Reviewed;        1516 AA.
AC   Q9W705;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Nuclear receptor coactivator 2;
DE            Short=NCoA-2;
DE   AltName: Full=Transcriptional intermediary factor 2;
DE            Short=xTIF2;
GN   Name=ncoa2; Synonyms=tif2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=10704837; DOI=10.1016/s0925-4773(99)00280-4;
RA   de la Calle-Mustienes E., Gomez-Skarmeta J.L.;
RT   "XTIF2, a Xenopus homologue of the human transcription intermediary factor,
RT   is required for a nuclear receptor pathway that also interacts with CBP to
RT   suppress Brachyury and XMyoD.";
RL   Mech. Dev. 91:119-129(2000).
CC   -!- FUNCTION: Transcriptional coactivator for steroid receptors and nuclear
CC       receptors. Coactivator of the steroid binding domain (AF-2) but not of
CC       the modulating N-terminal domain (AF-1) (By similarity). Required in a
CC       nuclear receptor pathway to suppress expression of dorsal mesoderm
CC       genes. May play a role in the positive regulation of the circadian
CC       clock (By similarity). {ECO:0000250|UniProtKB:Q15596,
CC       ECO:0000250|UniProtKB:Q61026, ECO:0000269|PubMed:10704837}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15596}.
CC   -!- TISSUE SPECIFICITY: Expressed homogeneously during late blastula-early
CC       gastrula stages, becoming highly expressed in the notochord in the late
CC       gastrula and neurula stages. At hatching, restricted to a few areas
CC       including the blood precursor region, prospective pronephros and
CC       retina. {ECO:0000269|PubMed:10704837}.
CC   -!- DOMAIN: Contains three Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. The LXXLL
CC       motifs are essential for the association with nuclear receptors and, at
CC       least in part, functionally redundant (By similarity).
CC       {ECO:0000250|UniProtKB:Q15596}.
CC   -!- DOMAIN: The LLXXLXXXL motif is involved in transcriptional coactivation
CC       and CREBBP/CBP binding. {ECO:0000250|UniProtKB:Q15596}.
CC   -!- DOMAIN: Contains 2 C-terminal transcription activation domains (AD1 and
CC       AD2) that can function independently. {ECO:0000250|UniProtKB:Q15596}.
CC   -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
CC       family. {ECO:0000305}.
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DR   EMBL; AJ243119; CAB45389.1; -; mRNA.
DR   RefSeq; NP_001081139.1; NM_001087670.1.
DR   AlphaFoldDB; Q9W705; -.
DR   SMR; Q9W705; -.
DR   BioGRID; 99007; 1.
DR   IntAct; Q9W705; 1.
DR   GeneID; 394405; -.
DR   KEGG; xla:394405; -.
DR   AGR; Xenbase:XB-GENE-864856; -.
DR   CTD; 394405; -.
DR   Xenbase; XB-GENE-864856; ncoa2.S.
DR   OrthoDB; 4230728at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 394405; Expressed in spleen and 19 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR   GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISS:UniProtKB.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IMP:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:UniProtKB.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   CDD; cd18950; bHLH-PAS_NCoA2_SRC2; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR   Gene3D; 6.10.140.20; Nuclear receptor coactivator, Ncoa-type, interlocking domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR010011; NCO_DUF1518.
DR   InterPro; IPR032565; NCOA2/3_DUF4927.
DR   InterPro; IPR028822; NCOA2_bHLH.
DR   InterPro; IPR009110; Nuc_rcpt_coact.
DR   InterPro; IPR014920; Nuc_rcpt_coact_Ncoa-typ.
DR   InterPro; IPR037077; Nuc_rcpt_coact_Ncoa_int_sf.
DR   InterPro; IPR017426; Nuclear_rcpt_coactivator.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR014935; SRC/p160_LXXLL.
DR   PANTHER; PTHR10684; NUCLEAR RECEPTOR COACTIVATOR; 1.
DR   PANTHER; PTHR10684:SF2; NUCLEAR RECEPTOR COACTIVATOR 2; 1.
DR   Pfam; PF07469; DUF1518; 2.
DR   Pfam; PF16279; DUF4927; 1.
DR   Pfam; PF16665; NCOA_u2; 1.
DR   Pfam; PF08815; Nuc_rec_co-act; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF14598; PAS_11; 1.
DR   Pfam; PF08832; SRC-1; 1.
DR   PIRSF; PIRSF038181; Nuclear_receptor_coactivator; 1.
DR   SMART; SM01151; DUF1518; 2.
DR   SMART; SM00353; HLH; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   SUPFAM; SSF69125; Nuclear receptor coactivator interlocking domain; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50888; BHLH; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   2: Evidence at transcript level;
KW   Activator; Biological rhythms; Developmental protein; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation.
FT   CHAIN           1..1516
FT                   /note="Nuclear receptor coactivator 2"
FT                   /id="PRO_0000094405"
FT   DOMAIN          23..80
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   DOMAIN          116..180
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          700..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          775..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          955..979
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1284..1311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1324..1350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           628..632
FT                   /note="LXXLL motif 1"
FT   MOTIF           680..684
FT                   /note="LXXLL motif 2"
FT   MOTIF           735..739
FT                   /note="LXXLL motif 3"
FT   MOTIF           1064..1072
FT                   /note="LLXXLXXXL motif"
FT   COMPBIAS        8..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..518
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..719
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..975
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1324..1339
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1516 AA;  166156 MW;  09851C00AB439A4A CRC64;
     MGENLSDPSR AEPRKRKESL DQLGPSPKRS TEKRNREQEN KYIEELAELI FANFNDIDNL
     NFKPDKCAIL KETVKQIRQI KEHEKTAAAN EDEVQKADVS STGQSVIDKD ALGPMMLEAL
     DGFFFVVNRE GNVVFVSENV TQYLRYNQEE LMNTSVYSIL HVGDHSEFIK NLLPKSLVNG
     VPRRNSHTFN CRMLVKPMME CEEERHDGQE THQKYESMQC FAVSQPKSIK EEGEDFQSCL
     ICVARRVPVK ERPVPPPSES FTTRQDFQGK ITSLDTTSMR ALMRPGWEDM VRRCIQRFHS
     QHDGEISYSR RHHQEVLRQG HATSPFYRFS LSDGTTVVAQ TKSRLMRSQT NNEPPLVLSL
     HVLQREQNVC GLNQDLAGQA MGKTLNPVQS SSPAHQAMYG GNPGQDTTIS SNMNYAISGP
     KEQMGLATGR FVGSGGMNHI SSLQATTPQG NNYALKMNSP SHGSPGMGQG QPNSMLSPRH
     RVSPGVAGSP RIAPSPFSPA GSLHSPVSVC SSTGNSHSYT NSSLNALQAL SEGQGPLAPP
     LSSPDLKGGN LQHSPGNMNP PQLRKMGSID SKESFGLYEE QPESATGQGE SGCHSNEQKD
     CGENLSSVVD KTEGQSRLLD GKGQQKLLKL LTTKSDQMEP STLPSNTLGD MNKDSLSNFA
     SNSMSASAHG TSLKEKHKIL HRLLQDSSSP VDLAKLTAEA TGKELSQESN STGPGSEVTI
     KQEPVSPKKK EHALLRYLLD KDDTTDNVAD ITPKLERADN KVDPSSCPKL SAVKAEKEEP
     NFGHTDQPGS DFDNLDEILD DLQNSQLSQL FSDTRHDGNS ADKQAIMNDL MQLAGENSTG
     LPAWAQKQRM LRMQQNNGFN SQLAAQLGRL PNQNLPLDIH FQSQASAGSF AQMRSSGPYT
     TVPQSGVINN QAMMGSQGNV RNSSPGIVGV NGPRPPLKPG DWGSQASAVR PACPTTSTAM
     NRHDMSRSPT ASIPMRPGSQ VCPRQVLQSA VMNMGSSELD MNISGPQYTQ QQAPPNQTAP
     WPNRILTIEQ PSFNNQNRQP FGSPADDLIC QPIVSESPAD DGNLLDQLYM ALRNFDGLEE
     IDRALGIPEM VSQGQAVEQE SFGSPESNLM MEQKPPVYNH AYANQGQMAQ NSYQPMQDPG
     FNPMGQRPSY GILRMQNRPG LRPTGMVQNQ PNQLRLQLQH RLQAQNRQQL MNPINNVSNM
     NLAMRPGVPG QLREQGPINA QMLAQRQREI LSQHLRQKQL QQQQQQQQQQ QQQQQQQQQQ
     QQQQQQQQQQ QQQHRAMMMR SQGLAMPPNM VGSGGIPASI NSPRIPQGST QQFPFPPNYG
     TGIPSPPPFT SPFSPVPPSP GSQSLSHSSL HGSQMNLANQ GIMGSMGGQY GPVMNPQMQH
     NAFQFANSGM SQQSDPGFTG ATTPQSPIMS PRMGHIQSSM MQQSQANPAY QSELNGWAQG
     NPAGNSMFSQ QSPPHFGQQS GTSMYNSNNM NISVSMAANG NGMNNMNQMT GQINMTSVTS
     VPTSGLSSMG PEQKYC
//