GenomeNet

Database: UniProt
Entry: D4A3Q3_RAT
LinkDB: D4A3Q3_RAT
Original site: D4A3Q3_RAT 
ID   D4A3Q3_RAT              Unreviewed;      1417 AA.
AC   D4A3Q3; D4AB68;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 2.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Nuclear receptor coactivator {ECO:0000256|PIRNR:PIRNR038181};
GN   Name=Ncoa1 {ECO:0000313|Ensembl:ENSRNOP00000061906.2,
GN   ECO:0000313|RGD:1309046};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000061906.2, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000061906.2, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000061906.2,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000061906.2}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000061906.2};
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}.
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DR   RefSeq; NP_001101482.1; NM_001108012.1.
DR   AlphaFoldDB; D4A3Q3; -.
DR   SMR; D4A3Q3; -.
DR   STRING; 10116.ENSRNOP00000061906; -.
DR   PaxDb; 10116-ENSRNOP00000061906; -.
DR   Ensembl; ENSRNOT00000068531.3; ENSRNOP00000061906.2; ENSRNOG00000004068.8.
DR   KEGG; rno:313929; -.
DR   AGR; RGD:1309046; -.
DR   CTD; 8648; -.
DR   RGD; 1309046; Ncoa1.
DR   eggNOG; KOG3561; Eukaryota.
DR   GeneTree; ENSGT00950000183021; -.
DR   OrthoDB; 4230728at2759; -.
DR   Reactome; R-RNO-159418; Recycling of bile acids and salts.
DR   Reactome; R-RNO-192105; Synthesis of bile acids and bile salts.
DR   Reactome; R-RNO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR   Reactome; R-RNO-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR   Reactome; R-RNO-211976; Endogenous sterols.
DR   Reactome; R-RNO-3214847; HATs acetylate histones.
DR   Reactome; R-RNO-3899300; SUMOylation of transcription cofactors.
DR   Reactome; R-RNO-400206; Regulation of lipid metabolism by PPARalpha.
DR   Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
DR   Reactome; R-RNO-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR   Reactome; R-RNO-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
DR   Reactome; R-RNO-9707564; Cytoprotection by HMOX1.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000004068; Expressed in Ammon's horn and 19 other cell types or tissues.
DR   ExpressionAtlas; D4A3Q3; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR   GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR   GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:RGD.
DR   GO; GO:0016922; F:nuclear receptor binding; IPI:RGD.
DR   GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:RGD.
DR   GO; GO:0042974; F:nuclear retinoic acid receptor binding; IPI:RGD.
DR   GO; GO:0046965; F:nuclear retinoid X receptor binding; IPI:RGD.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IMP:RGD.
DR   GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; ISO:RGD.
DR   GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR   GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR   GO; GO:0044849; P:estrous cycle; IEP:RGD.
DR   GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR   GO; GO:0021854; P:hypothalamus development; IEP:RGD.
DR   GO; GO:0060713; P:labyrinthine layer morphogenesis; ISO:RGD.
DR   GO; GO:0007595; P:lactation; IEP:RGD.
DR   GO; GO:0008584; P:male gonad development; IEP:RGD.
DR   GO; GO:0060179; P:male mating behavior; IMP:RGD.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0045925; P:positive regulation of female receptivity; IMP:RGD.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD.
DR   GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; ISO:RGD.
DR   GO; GO:0002155; P:regulation of thyroid hormone mediated signaling pathway; ISO:RGD.
DR   GO; GO:0032355; P:response to estradiol; IMP:RGD.
DR   GO; GO:0009725; P:response to hormone; IEP:RGD.
DR   GO; GO:0032570; P:response to progesterone; IMP:RGD.
DR   GO; GO:0032526; P:response to retinoic acid; IMP:RGD.
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; 4.
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   1: Evidence at protein level;
KW   Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|PIRNR:PIRNR038181};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR038181};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
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}.
SQ   SEQUENCE   1417 AA;  153761 MW;  51190E264BC3AE31 CRC64;
     MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL SANISDIDSL
     SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS SSSQGVIEKE SLGPLLLEAL
     DGFFFVVNCE GRIVFVSENV TSYLGYNQEE LMNTSVYSIL HVGDHAEFVK NLLPKSLGTE
     NQEACQRYEV MQCFTVSQPK SIQEDGEGKI ISIDTSSLRA AGRTGWEDLV RKCIYAFFQP
     QGREPSYARQ LFQEVMTRGT ASSPSYRFIL NDGTMLSAHT KCKLCYPQSP DMQPFIMGIH
     IIDREHSGLS PQDDTNSGMS IPRINPSVNP GISPAHGVTR SSTLPPSNNN MVSARANRQQ
     STDLNSGSSH SNSSSSQGSF GCSPGNQIVA SVALSQGQAG SQSSNPSLNL NNSPMEGTGI
     SLAQFMSPRR QANSGLATRA RMSNNSFPPN IPTLSSPVGI TSGACSNNNR SYSNIPVTSL
     QGMNEGPNNS VGFSAGSPVL RQMSSQNSPS RLSMQPAKAE SKDNKEIASI LNEMIQSDNS
     ANEGKPLDSG LLHNNDRLSD GDSKYSQTSH KLVQLLTTTA EQQLRHADID TSCKDVLSCT
     GTSSSASSNP SGGTCPSSHS SLTERHKILH RLLQEGSPSD ITTLSVEPEK KDSASASTAM
     SVSGQAQGSA SIKLELDASK KKESKDHQLL RYLLDKDEKD LRSTPNLSLD DVKVKVEKKE
     QMDPCNTNPA PVTKPAPEEV KLESQSQFSA DLDQFDQLLP TLEKAAQLPG LCETDRMDGA
     VPGVNIKSEI LPASLQPTPA RSAPRLNRLP ELELEAIDNQ FGQPGAGDQI PWANNTVTAI
     NQSKPEDQCI SSQLDELLCP PTTVEGRNDE KALLEQLVSF LSGKDETELA ELDRALGIDK
     LVQGGGLDVL SERFPPQQAT PPLMMEDRPT LYPQPYSSPS PTAGLSGPFQ GMVRQKPSLG
     TMPVQVTPPR GTFSPNMGMQ PRQTLNRPPA APNQLRLQLQ QRLQGQQQLM HQNRQAILNQ
     FAANAPVGMN MRSGMQQQIT PQPPLNAQML AQRQRELYSQ QHRQRQIIQQ QRAMLMRHQS
     FGNNIPPSSG LPVQMGNPRL PQGAPQQFPY PPNYGTNPGT PPASTSPFSQ LAANPEASLA
     TRSSMVNRGM AGNMGGQFGT GISPQMQQNV FQYPGSGLVP QAEANFAPSL SPGSSMVPMP
     IPPQSSLLQQ TPPTSGYQSP DMKAWQQGTM GNNNVFSQAV QSQPAPAQPG VYNNMSITVS
     MAGGNANVQN MNPMMGQMQM SSLQMPGMNT VCSEQMNDPA LRHTGLYCNQ LSSTDLLKTE
     ADGNQDKKTE EFFSVQVQQL QVFADVQCTV NLKGASKPTL VLAVLLQEKA IRTNADEEHG
     LKTSRKKPFP QVLPSASHRP WYKQLHKNSI YSETTGL
//
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