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Database: UniProt
Entry: A0A384CUR0_URSMA
LinkDB: A0A384CUR0_URSMA
Original site: A0A384CUR0_URSMA 
ID   A0A384CUR0_URSMA        Unreviewed;      1441 AA.
AC   A0A384CUR0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   03-AUG-2022, sequence version 2.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Nuclear receptor coactivator {ECO:0000256|PIRNR:PIRNR038181};
GN   Name=NCOA1 {ECO:0000313|RefSeq:XP_008698592.2,
GN   ECO:0000313|RefSeq:XP_008698593.2};
OS   Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008698592.2};
RN   [1] {ECO:0000313|RefSeq:XP_008698592.2, ECO:0000313|RefSeq:XP_008698593.2}
RP   IDENTIFICATION.
RC   TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008698592.2,
RC   ECO:0000313|RefSeq:XP_008698593.2};
RG   RefSeq;
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}.
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DR   RefSeq; XP_008698592.2; XM_008700370.2.
DR   RefSeq; XP_008698593.2; XM_008700371.2.
DR   STRING; 29073.ENSUMAP00000031319; -.
DR   KEGG; umr:103671686; -.
DR   OrthoDB; 4230728at2759; -.
DR   Proteomes; UP000261680; Unplaced.
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: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:0030374; F:nuclear receptor coactivator activity; IEA:Ensembl.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; IEA:Ensembl.
DR   GO; GO:0060713; P:labyrinthine layer morphogenesis; 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: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   PANTHER; PTHR10684; NUCLEAR RECEPTOR COACTIVATOR; 1.
DR   PANTHER; PTHR10684:SF1; NUCLEAR RECEPTOR COACTIVATOR 1; 1.
DR   Pfam; PF07469; DUF1518; 2.
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; 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, ECO:0000256|PIRNR:PIRNR038181};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR038181};
KW   Receptor {ECO:0000313|RefSeq:XP_008698592.2,
KW   ECO:0000313|RefSeq:XP_008698593.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261680};
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          23..80
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   DOMAIN          109..180
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          661..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          988..1049
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1139..1189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1241..1284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1405..1433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..492
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..578
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..683
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..723
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        990..1013
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1163..1177
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1254..1269
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1270..1284
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1414..1433
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1441 AA;  156882 MW;  610AA4A3D5C3E881 CRC64;
     MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL SANISDIDSL
     SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDEVQKSDIS SSSQGVIEKE SLGPLLLEAL
     DGFFFVVNCE GRIVFVSENV TSYLGYNQEE LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG
     VPWPQEATRR NSHTFNCRML IHPPDEPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ
     SCLICIARRL PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF
     QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ SPDMQPFIMG
     IHIIDREHSG LSPQDDTNSG MSIPRVNPSV NSSISPAHGV ARSSTLPPSS NNMVSPRVNR
     QQSSDLHSSS HSNSSNSQGS FGCSPGNQIV ASVALNQGQA SSQSTNPSLN LNNSPMEGTG
     ISLAQFMSPR RQVSSGLAPR PRMPNNSFPP NIPTLSSPVG MTGTACNNSN XSYSNIPVPS
     LQSMNEGPNN SVGFSSSSPV LRQMSSQNSP SRLNIQPAKA ESKDNKEIAS ILNEMIQSDN
     SSSDGKPLDS GLLHNNDRLS DGDNKYSQTS HKLVQLLTTT AEQQLRHADI DTSCKEVLSC
     SGTSSSASAN SSSGSCPSSH SSLTERHKIL HRLLQEGSPS DITTLSVEPD KKDSASTSVS
     VTGQVQGNSS VKLELEASKK KESKDHQLLR YLLDKDEKDL RSTPNLSLDD VKVKVEKKEQ
     MDPCNTNPTP MTKPAPEEIK LESQSQFTAD LDQFDQLLPT LEKAAQLPGL CEPERMDGAV
     TNVTIKSETL PASLQSTTAR PTSRMNRLPE LELEAIDNQF GQPGTGDQIP WANNTVTAVN
     QNKPEDQCIS SQLDELLCPP TTVEGRNDEK ALLEQLVSFL SGKDETELAE LDRALGIDKL
     VQGGGLDVLS ERFPPQQATP PLMMEERPNL YSQPYSSPSP TANLSSPFQG MVRQKPSLGT
     LPVQVTPPRG AFSPGMGMQP RQTLNRPPAA PNQLRLQLQQ RLQGQQQLIH QNRQAILNQF
     AANAPVGINM RSGMQQQITP QPPLNAQMLA QRQRELYSQQ HRQRQLIQQQ RAMLMRQQSF
     GNNLPPSSGL PVQMGNPRLP QGAPQQFPYP PNYGTNPGTP PASTSPFSQL AANPESTLAN
     RNSMVNRGMT GNMGGQFGTG INPQMQQNVF QYPGSGMVPQ GEANFAPSLS PGSSMVPMPI
     PPPQSSLLQP TPPSSGYQSP DMKAWQQGAM GNNNVFSQAV QNQPTPAQPG VYNNMSITVS
     MAGGNTNVQN MNPMMGQMQM SSLQMPGMNT VCPEQINDPA LRHTGLYCNQ LSSTDLLKTE
     TDGTQQVQQV QVFADVQCTV NLVGGDPYLN QPGPLGTQKP TAGPQTPQAQ QKSLLQQLLT
     E
//
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