NCOA2_XENTR
ID NCOA2_XENTR Reviewed; 1440 AA.
AC B5DE09;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Nuclear receptor coactivator 2 {ECO:0000250|UniProtKB:Q9W705};
DE Short=NCoA-2 {ECO:0000250|UniProtKB:Q9W705};
DE AltName: Full=Transcriptional intermediary factor 2 {ECO:0000250|UniProtKB:Q9W705};
GN Name=ncoa2 {ECO:0000250|UniProtKB:Q9W705};
GN Synonyms=tif2 {ECO:0000250|UniProtKB:Q9W705};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAI68483.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAI68483.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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). Required in a nuclear receptor
CC pathway to suppress expression of dorsal mesoderm genes. May play a
CC role in the positive regulation of the circadian clock.
CC {ECO:0000250|UniProtKB:Q15596, ECO:0000250|UniProtKB:Q61026,
CC ECO:0000250|UniProtKB:Q9W705}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15596}.
CC -!- DOMAIN: Contains three Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. The LXXLL
CC motifs are essential for the association with nuclear receptors and
CC are, at least in part, functionally redundant.
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:0000255}.
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DR EMBL; BC168483; AAI68483.1; -; mRNA.
DR RefSeq; NP_001135631.1; NM_001142159.1.
DR AlphaFoldDB; B5DE09; -.
DR SMR; B5DE09; -.
DR STRING; 8364.ENSXETP00000034772; -.
DR GeneID; 100216190; -.
DR KEGG; xtr:100216190; -.
DR CTD; 10499; -.
DR Xenbase; XB-GENE-482311; ncoa2.
DR eggNOG; KOG3561; Eukaryota.
DR InParanoid; B5DE09; -.
DR OrthoDB; 59971at2759; -.
DR Reactome; R-XTR-159418; Recycling of bile acids and salts.
DR Reactome; R-XTR-192105; Synthesis of bile acids and bile salts.
DR Reactome; R-XTR-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-XTR-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR Reactome; R-XTR-211976; Endogenous sterols.
DR Reactome; R-XTR-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016922; F:nuclear receptor binding; IBA:GO_Central.
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:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 4.10.280.10; -; 1.
DR Gene3D; 6.10.140.20; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR010011; NCO_DUF1518.
DR InterPro; IPR028822; NCOA2.
DR InterPro; IPR032565; NCOA2/3_DUF4927.
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; PTHR10684; 1.
DR PANTHER; PTHR10684:SF2; PTHR10684:SF2; 1.
DR Pfam; PF07469; DUF1518; 1.
DR Pfam; PF16279; DUF4927; 1.
DR Pfam; PF08815; Nuc_rec_co-act; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08832; SRC-1; 1.
DR PIRSF; PIRSF038181; Nuclear_receptor_coactivator; 1.
DR SMART; SM01151; DUF1518; 1.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR SUPFAM; SSF69125; SSF69125; 1.
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..1440
FT /note="Nuclear receptor coactivator 2"
FT /id="PRO_0000356222"
FT DOMAIN 26..83
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 112..183
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 631..635
FT /note="LXXLL motif 1"
FT /evidence="ECO:0000255"
FT MOTIF 684..688
FT /note="LXXLL motif 2"
FT /evidence="ECO:0000255"
FT MOTIF 739..743
FT /note="LXXLL motif 3"
FT /evidence="ECO:0000255"
FT MOTIF 1074..1082
FT /note="LLXXLXXXL motif"
FT /evidence="ECO:0000255"
FT COMPBIAS 11..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1440 AA; 157293 MW; 3B21201CD6CFD7F3 CRC64;
MSGMGENPSD PSRAEPRKRK ESIDQLGPSP KRSTEKRNRE QENKYIEELA ELIFANFNDI
DNLNFKPDKC AILKETVKQI RQIKEHEKTA AANEDEVQKA DVSSTGQSVI DKDALGPMML
EALDGFFFVV NREGNVVFVS ENVTQYLRYN QEELMNTSVY SILHVGDHSE FIKNLLPKSI
VNGGPRRNSH TFNCRMLVKP MMECEEEGHD GQETHQKYET MQCFAVSQPK SIKEEGEDFQ
SCLICVARRV PMKERPVPPP SESFTTRQDL QGKITSLDTT NMRALMRPGW EDLVRRCIQR
FHSQHDGEIS YSKRHHQEVL RQGHATSPFY RFALSDGTTV LAHTKSKLMR SQTTNEPQLV
LSLHVLQREQ NMCGLNQDLA GQAMGKTLNP VQSSSPAHQA MYGGNPGQDT TISSNMNYAI
TGPKEQMGMA AGRFVGSGGM NHISSLQATT PQGNNYALKI NSPSQGSPGM GQGQPNSMLS
PRHRVSPGVA GSPRIAPSQF SPAGSLHSPV SVCSSTGNSH SYTNSSLNAL QALSEGHGVP
LAPPLSSPDL KVGNVQHSPV NMNPPQLRKM GSIDSKESFG LYGEQPESAA GQGESGCHSN
EQKDCSENLS SVGDQTEGQS RLLDSKGQQK LLKLLTTKSD QMEPSPLPSN TLGDMNKDSL
SNFASNSMSA SAHGTSLKEK HKILHRLLQD SSSPVDLAKL TAEATGKELS QESNSTGPGS
EVTIKQEPVS PKKKEHALLR YLLDKDDTKD NVADITPKLE RPDVKVEPTS CPKLLSVKAE
KEEPSFGHSD QLMPPGSDLD NLDEILDDLQ NSQLSQLFPD ARHDGSNSAD KQAIMNDLMQ
LAGDNSTGLP AGAHKQRMIR IQQNNGFSSQ LAAQLGRLPN QSLPLDINLQ SQVSAGSFPP
MRNSAPYTTV SQSVVMNNQA MMGSQGNVSN SSPGIIGVNG PRPALKPGDW GSQASAVRPA
CPTPSTAINR PIQDLTRSPT ASIPMRPGGQ VCPRQVLQSP VINMGSSELD MNIGGPQYTQ
QQAPPNQTAP WPDSILPIDQ PSFNNQNRQP FGSPADDLIC QPIASQSPTD DGNLLDQLYM
ALRNFDGLEE IDRALGIPEM VSQGQAVEQE SFVSPESNLM MEQKPPLYNH AYANQGQMAQ
NSYTPMQDPG FNPMGQRPSY GILRMQNRPG LRPTGMVQNQ PNQLRLQLQH RLQAQNRQPI
MNPINNVSNM NLAMRPGVPG QLREQGPINA QMLAQRQREL LSQHLRQKQL QQQQQQQQQQ
QQQVQQHRAM MMRGQGLAMP PNMVGSGGIP ASINSPRIPQ GNTQQFPFPP NYGMSQQSDP
GFTGATTPQS PIMSPRMGHI QSPMMQQSQA SPAYQSELNG WAQGNPAGNS MFSQQSPPHF
GQQSGTSMYN SNNMNISVSM AANGNGMNSM NQMTGQINMT SVTSVPTSGL SSMGPEQKYC
