ID F1SBF0_PIG Unreviewed; 1338 AA.
AC F1SBF0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 5.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Nuclear receptor coactivator 3 {ECO:0000313|Ensembl:ENSSSCP00000007946.5};
GN Name=NCOA3 {ECO:0000313|Ensembl:ENSSSCP00000007946.5,
GN ECO:0000313|VGNC:VGNC:96434};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000007946.5, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000007946.5, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000007946.5,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000007946.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
CC family. {ECO:0000256|ARBA:ARBA00009933}.
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DR STRING; 9823.ENSSSCP00000007946; -.
DR Ensembl; ENSSSCT00000008162.5; ENSSSCP00000007946.5; ENSSSCG00000007458.5.
DR VGNC; VGNC:96434; NCOA3.
DR eggNOG; KOG3561; Eukaryota.
DR GeneTree; ENSGT00950000183021; -.
DR HOGENOM; CLU_001988_0_0_1; -.
DR InParanoid; F1SBF0; -.
DR TreeFam; TF332652; -.
DR Reactome; R-SSC-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SSC-9018519; Estrogen-dependent gene expression.
DR Proteomes; UP000008227; Chromosome 17.
DR Bgee; ENSSSCG00000007458; Expressed in oocyte and 44 other cell types or tissues.
DR ExpressionAtlas; F1SBF0; baseline and differential.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0016922; F:nuclear receptor binding; IBA:GO_Central.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 6.10.140.410; -; 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding 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; 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:SF3; NUCLEAR RECEPTOR COACTIVATOR 3; 1.
DR Pfam; PF07469; DUF1518; 1.
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; 2.
DR SMART; SM01151; DUF1518; 1.
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 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 27..84
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT DOMAIN 101..164
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1338 AA; 145747 MW; FFC8A37975A97C21 CRC64;
MMSGLGENSL DPLAPDSRKR KLPCDTPGQG LTCSGEKWRR EQESKYIEEL AELISANLSD
IDNFNVKPDK CAILKETVRQ IRQIKEQGQG VIDKDSLGPL LLQALDGFLF VVNREGNIVF
VSENVTQYLQ YKQEDLVNTS VYSILHEEDR KDFLKNLPKS TVNGVTWTNE TQRQKSHTFN
CRMLMKIPHD ILEDMNTSPE MRQRYETMQC FALSQPRAMM EEGEDLVYFI QFVSIDTNSL
RSSMRPGFED IIRRCIQRFF SLNDGQSWSQ KRHYQEAYIH GHAETPVYRF SLADGTIVTA
QTKSKLFRNP VTNDRHSFVS THFLQREQNG YRPNPNPVGQ GVRPPAAGCN SSVGSMNMSP
NQGLQMLSSR TYGLADPSTT GQMTGARYGA AGSIASMNPG PGMQSPSSYQ NSNYGLNMSS
PPHGSPGLGS NQQNIMISPR NRGSPKMASH QFSPVAGVHS PMGSSGSTGN HSFSSSSLSA
LQAISEGVGT SLLSTLSSPG PKLDNSPNMN ITQPSKVSSQ DSKSPLGLYC DQNPVESSMC
QSNSRDHLND KESKESSVEG SENQRGPLES KGHKKLLQLL TCSSDDRGHS SLTNSPLDSG
CKDSAISVTS PSGVSSSTSG GVSSTSNMHG SLLQEKHRIL HKLLQNGNSP AEVAKITAEA
TGKDTSSTAS CVEGNVKQEQ LSPKKKENNA LLRYLLDRDD PSDTLSKELQ PKVEGVDGKM
SQCSSSALPS SSQEKDSKIK TETNEEGSGD LDNLDAILGD LTSSDFYNNS ISTNGSNLGT
KQQMFQGTNS LGLRSPQSVQ SVRPPYNRAV SLDSPVSAFP MLTKQPLMGG NPRMMDGQEN
YGSAMGGPNR NVAVNQTPSS GDWGLPNSKA SRMEPMNPNS MGRPGTDFNA SLPRPAVGGS
MPTMPLRSNS IPGARPVLQQ QQQQQQQMLQ MRPGEIPVGM GVGPYGQGAP SNQPGSWPDG
MLSMEQGPHG TQNRPLLRNS LDDLLGPPSN LEGQSDERAL LDQLHTLLSN TDATGLEEID
RALGIPELVN QGQALEPKQD AFQGQEAAVM MEQKAALYGQ TYPAQGPPMQ GGFNLQGQSP
SFNSMMNQMN QQGSFPLQGM HPRANIMRPR TNTPKQLRMQ LQQRLQGQQF LNQNRQALEM
KMESPSAGGA AVMRPMMQPQ VSSQGFLNAQ MVAQRSRELL SHHFRQQRVA MMMQQQQQQQ
QQTQAFSPPP NVTASPSMDG VLAGPSMPQA PPQQFPYPPN YGMGQQPDPA FGRVSSPSNA
MMSSRMGPSQ NPMMQHPQTA PMYQSSDMKG WPSGTLARNS SFPQQQFAPQ GNPAAYSMMN
MNSVPMTGMP MGPDQKYC
//
