ID A0A7L3Q7Q6_9SYLV Unreviewed; 1405 AA.
AC A0A7L3Q7Q6;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 14.
DE RecName: Full=Nuclear receptor coactivator 3 {ECO:0000256|ARBA:ARBA00067176};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
DE Flags: Fragment;
GN Name=Ncoa3 {ECO:0000313|EMBL:NXU99536.1};
GN ORFNames=CETCET_R05445 {ECO:0000313|EMBL:NXU99536.1};
OS Cettia cetti.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sylvioidea; Sylviidae; Acrocephalinae; Cettia.
OX NCBI_TaxID=68486 {ECO:0000313|EMBL:NXU99536.1, ECO:0000313|Proteomes:UP000524451};
RN [1] {ECO:0000313|EMBL:NXU99536.1, ECO:0000313|Proteomes:UP000524451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OUT-0056 {ECO:0000313|EMBL:NXU99536.1};
RC TISSUE=Blood {ECO:0000313|EMBL:NXU99536.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein]
CC + CoA + H(+); Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000256|ARBA:ARBA00048017};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
CC family. {ECO:0000256|ARBA:ARBA00009933}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NXU99536.1}.
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DR EMBL; VZUI01034310; NXU99536.1; -; Genomic_DNA.
DR Proteomes; UP000524451; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0016922; F:nuclear receptor binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEA:TreeGrafter.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:TreeGrafter.
DR CDD; cd18949; bHLH-PAS_NCoA3_SRC3; 1.
DR CDD; cd00130; PAS; 1.
DR FunFam; 3.30.450.20:FF:000008; Nuclear receptor coactivator; 1.
DR FunFam; 4.10.280.10:FF:000008; Nuclear receptor coactivator; 1.
DR FunFam; 3.30.450.20:FF:000027; Nuclear receptor coactivator 3; 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; IPR056193; bHLH_NCOA1-3.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR010011; NCO_DUF1518.
DR InterPro; IPR032565; NCOA2/3_DUF4927.
DR InterPro; IPR056194; NCOA3_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:SF3; NUCLEAR RECEPTOR COACTIVATOR 3; 1.
DR Pfam; PF23172; bHLH_NCOA; 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; 1.
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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000524451};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT DOMAIN 31..88
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT DOMAIN 123..187
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..525
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..677
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1264
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXU99536.1"
FT NON_TER 1405
FT /evidence="ECO:0000313|EMBL:NXU99536.1"
SQ SEQUENCE 1405 AA; 153372 MW; 3B55F5A883EA83BC CRC64;
CMVKMSGLGE NSLDSLTNES RKRKPLPCDT PGASLVCSGE KRRREQESKY IEELAELISA
NLSDIDNFNV KPDKCAILKE TVRQIRQIKE QGKTVSNDDD VQKADVSSTG QGVIDKDSLG
PLLLQAALDG FLFVVNRDGN IVFVSENVTQ YLQYKQEDLV NTSVYGILHE EDRTDFLKNL
PKSSVNGVAW TNETPRQKSH TFNCRMMVKS SHDLLEDVGG YQDIHQRYET MQCFALSQPR
AMMEEGEDLQ SCMICVARRI TTAERVFPAN PESFITRHDL SGKLVNIDTN SLRSSMRPGF
EDIIRRCIQR FLCHNDGQSW SNKRHYHEAY TQGHAETPLY RFSLADGTIV TAQTKSKLFR
NPVTNDRHGF VSTHFLHREQ NGYWPNPNSI GQNIRTPVTG NTNSVNGLMN VSPGQAMLTQ
NRNYGMGDPN AVGQLTSTRY GGPGNMGPVN SGPGMQSFAY QSNSFGLNIS SPPHGSPGLT
SNQQNLMVSP RNRGSPKMSS HQYSPVTGMH SPMGSASNTS NSTFSSSSLS ALQAISEGVG
NSLLSTLSSP GPKLDNSPNI SITQQSKTST EDSKSPSGLY CEQNQVESSI CQSNSRDLFS
EKDSKEGNLE ASESQRGPSE SKGHKKLLQL LTCSSDERGH STASNSPLDS NCKESSTSVT
SPSGVSSSTS GGVSSSSNMH GSLLQEKHRI LHKLLQNGNS PAEVAKITAE ATGKDTYDAS
NTASCGEGTV KHEQLSPKKK ENNALLRYLL DKDDIKDPLS KELKPKVEGV DNKIGQCTSS
TIPTSSQEKE MKIKMEPAEE VNGDLDNLDA ILGDLTSSEF YNNAMSANGN NPGTKQALFQ
GNALLGVKSP QSVQTTRPPF NRALSLESPV GSGASVRNVS AFSMLQKQNV MGGSPRMIEN
QENFGANLGF TPNRNVAMNQ HQSGDWGLPN SKVNRLESAS SASMLRPGPE FSTTLPRPSE
GGSVSGLPVR SNSIPGARPM LQQQMIHMRP NEINIDMGGN LYGQPGPSNQ PGLWADNMMS
MEQASRGSQN RQLVRSSLDD LLCSATNVEG QNDERALLDQ LHTLLSNTDV TGLEEIDRAL
GIPDLVNQGQ ALEPKQDSFQ GQQSSVMIDQ KPLLYGQPYQ GQGAAMPGGF SNIQGQQPSF
NSVMNQMSQL SNFPLQSMHP RANVMRPRTN SQKQLRMQLQ QRLQGQQFMN QTRQTLEIKM
ENPVSGTNSV MRPVMQPQVG SQQGFLNAQM VAQRNRELIS HHFRQQRMAM MMQQQQQPQA
FSQPPNVTAS GSMDSALTGP PMAQVPSQQF PYPPNYGISQ QPDPAFSRVS SPPNPMISPR
IGPSQNPMLQ HSQSATMYQS SEMKGWPSGS MPRNSSFPQQ QFSHQGSPAA YSMMHMNGSS
GHIGQMSINT MPVSGLPMGP DQVSC
//
