GenomeNet

Database: UniProt
Entry: Q5F393_CHICK
LinkDB: Q5F393_CHICK
Original site: Q5F393_CHICK 
ID   Q5F393_CHICK            Unreviewed;      1510 AA.
AC   Q5F393; E1BRL1;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Nuclear receptor coactivator {ECO:0000256|PIRNR:PIRNR038181};
GN   Name=NCOA1 {ECO:0000313|Ensembl:ENSGALP00010014582.1};
GN   ORFNames=RCJMB04_27h20 {ECO:0000313|EMBL:CAH65391.1};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031 {ECO:0000313|EMBL:CAH65391.1};
RN   [1] {ECO:0000313|EMBL:CAH65391.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CB {ECO:0000313|EMBL:CAH65391.1};
RC   TISSUE=Bursa {ECO:0000313|EMBL:CAH65391.1};
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
RN   [2] {ECO:0000313|Ensembl:ENSGALP00010014582.1}
RP   IDENTIFICATION.
RC   STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010014582.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR038181}.
CC   -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
CC       family. {ECO:0000256|ARBA:ARBA00009933, ECO:0000256|PIRNR:PIRNR038181}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ851757; CAH65391.1; -; mRNA.
DR   RefSeq; NP_001012900.1; NM_001012882.1.
DR   RefSeq; XP_015140590.1; XM_015285104.1.
DR   STRING; 9031.ENSGALP00000050346; -.
DR   PaxDb; 9031-ENSGALP00000026768; -.
DR   Ensembl; ENSGALT00010025906.1; ENSGALP00010014582.1; ENSGALG00010010826.1.
DR   GeneID; 422016; -.
DR   KEGG; gga:422016; -.
DR   CTD; 8648; -.
DR   VEuPathDB; HostDB:geneid_422016; -.
DR   GeneTree; ENSGT00950000183021; -.
DR   HOGENOM; CLU_001988_0_0_1; -.
DR   OMA; AQHVNIG; -.
DR   OrthoDB; 4230728at2759; -.
DR   Reactome; R-GGA-159418; Recycling of bile acids and salts.
DR   Reactome; R-GGA-192105; Synthesis of bile acids and bile salts.
DR   Reactome; R-GGA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR   Reactome; R-GGA-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR   Reactome; R-GGA-211976; Endogenous sterols.
DR   Reactome; R-GGA-3214847; HATs acetylate histones.
DR   Reactome; R-GGA-3899300; SUMOylation of transcription cofactors.
DR   Reactome; R-GGA-400206; Regulation of lipid metabolism by PPARalpha.
DR   Reactome; R-GGA-9018519; Estrogen-dependent gene expression.
DR   Reactome; R-GGA-9707564; Cytoprotection by HMOX1.
DR   Proteomes; UP000000539; Chromosome 3.
DR   Bgee; ENSGALG00000016617; Expressed in cerebellum and 12 other cell types or tissues.
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:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR   GO; GO:0030331; F:nuclear estrogen receptor binding; 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:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR   GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; IEA:Ensembl.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; IEA:Ensembl.
DR   GO; GO:0002155; P:regulation of thyroid hormone mediated signaling pathway; IEA:Ensembl.
DR   CDD; cd18948; bHLH-PAS_NCoA1_SRC1; 1.
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; IPR028819; NCOA1_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   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR10684; NUCLEAR RECEPTOR COACTIVATOR; 1.
DR   PANTHER; PTHR10684:SF1; NUCLEAR RECEPTOR COACTIVATOR 1; 1.
DR   Pfam; PF07469; DUF1518; 2.
DR   Pfam; PF00010; HLH; 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; 2.
DR   SMART; SM00353; HLH; 1.
DR   SMART; SM00091; PAS; 2.
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 {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|PIRNR:PIRNR038181};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR038181};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000539};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR038181};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PIRNR:PIRNR038181}.
FT   DOMAIN          22..79
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   DOMAIN          107..178
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          667..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          901..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1230..1259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1306..1348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1484..1510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..554
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..735
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1233..1247
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1306..1323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1324..1347
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1495..1510
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1510 AA;  161987 MW;  FCACDEB9186207EC CRC64;
     MSGLGDSSTD PANPDSRKRK GSPCDTAQSN EKRRREQENK YLEELAELLS ANIGDIDTLS
     VKPDKCKILK KTVDQIQQMK RLEQEKAADD EVQKSDISSS SQGVIEKESL GPLLLEALDG
     FFFVVNREGR IVFVSENVTS YLGYNQEELM NTSVYSILHV GDHTEFVKNL LPKSLVNGVP
     WPQEATRRNS HTFSCRMLIR PPDEPGTENQ EARQRYEVMQ CFTVSQPKSF KEEGEDFQSC
     LICIARRLPR PAAVTPSESF VTKQDTTGKI ISIDTSSLRA AGRTGWEDLV RKCIYAFFQP
     QGREPSYAKQ LFQEVMTRGT AFSPSYRFTL SDGTVLSAHT KCKLCYPSSP EVQPFIMGIH
     IIDRDHGMLS PQENTNSAMA LPRVSPSLNP NISPGQGMAL PPSIPPSNGS MLATPGNQQP
     GAGLHSSNSS TSQTSFGCSP GNQIGANVAL SQGQAGPPNS NHNLNLSSSP MNSPGITPPQ
     FMSPRHRVSP GLVPRPRGPS NPFSPTMPTM HSPVGMANSG GGGNGGGGGG GSRSFPTAPI
     NSLQGLSEGA STPVGYSTPP PVLRQLGSQS SPGRLGMQPM KAESKDSKEI ASILSEMIQS
     DGSAGDGKPL DSGVLHASER LTEGESKCSQ ATSHKLVQLL ASTAEQQLRH ADADTSCKDS
     LACAGTTGTL GASNPPSSTC PSSHSSLTER HKILHRLLQE GSPSDITTLA MEHDKKDNVP
     NPATTPTAPS QLPGTQDIKL ESDAMKKKDV KDHQLLRYLL DKDEKELAAA PALSLDDVKV
     KVEKTEQMEP CNTTPVPLAK PPAAEEVKLE SQGQFAAELE QLDQLLPSLE KAAQLPGLCG
     PERSESGVAV KSEMLAAPLQ PSTAPRAPTG LNPLSSGQGM QAARAPFEFC DPLEPAQLRP
     VAFPTTNGSS PRPRAPAEQG RGTVPGPNPF PPDTGMSELE MGVPDHQFGQ PGMGEQMPWT
     DNSMAPMNRG TLSKPEDPCI TSQLDELLCP PTTPEGRNDE KALLEQLVSF LSGKDETELA
     ELDRALGIDK LVQGGGLEAL TERFQPQQAT PPLMMEQKPG MYPQPYSSAS PTTNLPAAFP
     GMVRQKPSFG PMPVQVPPPR GAFPTTMAMQ PRQALSRPPT APNQLRLQLQ QRLQGQQQLI
     HQNRQAILNQ FAANSPVGIN MRAGMQQQMT PQPPLNAQML AQRQRELYSQ QHRQRQLMQQ
     RAILMRQQSF GNNLPPSAGL PVQMGAARLP QAPPQQFPYP PNYGTSPGNP PTSTSPFSQL
     ASSPEAALAN RGGMVTRGMM GSVGGQFGTG MTPQMQQNIF QYSGSGMGQQ NEPTFAPSLS
     PSSPLMSPQL PPSQSPMLQP APPAPGYQSP DMKTWQQGAM GNSNVFSQTG QTQPAPAQQG
     MYNNMSITVS MAGGNTNVQN MNPMAGQMQM NSLQMPGMNS MCSEQVNDPA LRPTGLYCNQ
     LSSTDLLKTE ADGAQQVQQV QVFADVQCTV NLVGDPYLNP PAPLGAPKAA AVPPTPQGQQ
     KSLLQQLLTE
//
DBGET integrated database retrieval system