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Database: UniProt
Entry: A0A5A9NEZ0_9TELE
LinkDB: A0A5A9NEZ0_9TELE
Original site: A0A5A9NEZ0_9TELE 
ID   A0A5A9NEZ0_9TELE        Unreviewed;      1480 AA.
AC   A0A5A9NEZ0;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   18-JUN-2025, entry version 22.
DE   RecName: Full=Nuclear receptor coactivator 3 {ECO:0000256|ARBA:ARBA00067176};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   ORFNames=E1301_Tti010456 {ECO:0000313|EMBL:KAA0707785.1};
OS   Triplophysa tibetana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Nemacheilidae; Triplophysa.
OX   NCBI_TaxID=1572043 {ECO:0000313|EMBL:KAA0707785.1, ECO:0000313|Proteomes:UP000324632};
RN   [1] {ECO:0000313|EMBL:KAA0707785.1, ECO:0000313|Proteomes:UP000324632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TTIB1903HZAU {ECO:0000313|EMBL:KAA0707785.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:KAA0707785.1};
RX   PubMed=30977968;
RA   Yang X., Liu H., Ma Z., Zou Y., Zou M., Mao Y., Li X., Wang H., Chen T.,
RA   Wang W., Yang R.;
RT   "Chromosome-level genome assembly of Triplophysa tibetana, a fish adapted
RT   to the harsh high-altitude environment of the Tibetan Plateau.";
RL   Mol. Ecol. Resour. 19:1027-1036(2019).
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:KAA0707785.1}.
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DR   EMBL; SOYY01000019; KAA0707785.1; -; Genomic_DNA.
DR   Proteomes; UP000324632; Chromosome 19.
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; 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; 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; 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   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   Receptor {ECO:0000313|EMBL:KAA0707785.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000324632};
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          22..79
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   DOMAIN          114..177
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   REGION          488..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          568..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..626
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        699..721
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        776..797
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        805..827
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..847
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1480 AA;  158300 MW;  4D94B946D8A9AD65 CRC64;
     MSRVGENSLE PLCSDRKRKL STCDTPGQGC DKRRREQESK YIEELAELIS ANLGDIDSFN
     VKPDKCAILK ETVRQIRQIK EQGKSSCGDD DVQKADVSST GQGVIDKDHL GPLLLQALDG
     FLFVVSREGS IVFVSDNVTQ YLQYKQEELI NTSIYNILHE EDRGELLKNL PKSNGSNSVS
     WGGDASRQKS HTFNCRMLMK FGHGGPGGEE GGGGPRYETM QCFALTQPKA MMEEGEDLQS
     CMICVARRVT AVERTERFST RHELSGKLIE IEQQSLLHTT MRPGWEDLVR RCMQMFLHRS
     EGQPWSYKRH YQEAYVHGRA ETPLYRFSLS DGTPVTAQTR SELCRNTVTN EPLTFLSTHL
     LQREQNGYRP NQGGVMRSVM SNTNPNAQLS MPPGGGMGMG NTRAYGMNEQ AHMGPRGGPM
     YGPGNRMNQI NPMHQMNQMN MNQMNSMTQM GSMNQMNSMG QMNHMGHPGM NQHQPGQFHG
     GSYGMGMTSP SQGSPALNPP QQNLIGSPRI RGSPKMGASP FSPGGMNSPM GPVSMGGTGG
     SSAPTVGNTF SSSSLNALQA ISEGVGSSLP SALNSPAHKS DSSPSINSTQ TSQQGQTGNN
     KPGNSDSKSP SSSHSSAVDQ QQASSSETTM EKPDSQSSKD VSAGPEVNRR LSDGKGHKKL
     LQLLTSPTED IGHATGGPVP GRASTPMSLE SKETGGGMMS PSSTGVSSSS GSSSGNNANQ
     QGSGGVSSTA CPSGSHTVQE KHKILHKLLK NGNTPDEVAR ITAEATGKAS LGAEHPGAEA
     RNLELKQEQL SPKEVKKPAL LHYLLNKDDS KDPNPTEAKP KLEELEGRGS MGGQGSGVTT
     SNSNNQEGKV KLEPPDEMDS LESILGGLRN PTSGLFADSR TGGSVGGNKQ GNGPNSTAHD
     REGVGMVSSQ RVPFQRAVSV DGKPLIGPGM SGRRSAPSSL VKQEHTENQM AMGGPNRPMG
     MNRPPMAGAG DWGMSSSSPV GHPGMGRPGM DHNPKGMMGA PMVNRSNSVP ANRSILQQQL
     MEMGPYEVGI GMTAFRGQGP PPRSPSWPDN GMGMEGAQNT NRLPFNNSLD DLLVPPSTTE
     GQSDERALLD QLDSLLNNTD VMALEEIDRA LGIPDLVSQG HSTEQAPPTD PFSAPCPDST
     LGMDPKGMYG QGYPGPPSMG MQGGYGHGPS PGPGPMQGQS GPGFNPIMNP MNQQGAFPGM
     GGMGGMHPRA TMMRPRMMNP TKPLRLQLQQ RLQGQQFLNQ NRQGMGMGMR PDNSPAGNPN
     MRPNMQPGMA GQPGFLNAQM MAQRSREMLN LSEMRRQRMM MVMQQQQQQQ QQVAPGGFSP
     PPNVTAPTVM DNPMGGPPMN QSSQQAFNYG GNYGMGQQGD PSFVGTGTSP PNNMMCGRMG
     GPQNPMMQQH PQSNPMYQSA EMKGWGQGPM PMNSSYSQQQ QYPQQGAQGQ YGGMMMNGSM
     QGVVNGNSAG QMPPMQGQMG MNGMGMGRMP MGPDQVHNVI
//
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