ID   COT2_MOUSE              Reviewed;         414 AA.
AC   P43135;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   24-JAN-2024, entry version 188.
DE   RecName: Full=COUP transcription factor 2;
DE            Short=COUP-TF2;
DE   AltName: Full=Apolipoprotein AI regulatory protein 1;
DE            Short=ARP-1;
DE   AltName: Full=COUP transcription factor II;
DE            Short=COUP-TF II;
DE   AltName: Full=Nuclear receptor subfamily 2 group F member 2;
GN   Name=Nr2f2; Synonyms=Aporp1, Arp-1, Arp1, Tfcoup2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX   PubMed=7947324; DOI=10.1016/0925-4773(94)90098-1;
RA   Jonk L.J.C., de Jonge M.E.J., Pals C.E.G.M., Wissink S., Vervaart J.M.A.,
RA   Schoorlemmer J., Kruijer W.;
RT   "Cloning and expression during development of three murine members of the
RT   COUP family of nuclear orphan receptors.";
RL   Mech. Dev. 47:81-97(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=8183930; DOI=10.1073/pnas.91.10.4451;
RA   Qiu Y., Cooney A.J., Kuratani S., DeMayo F.J., Tsai S.Y., Tsai M.J.;
RT   "Spatiotemporal expression patterns of chicken ovalbumin upstream promoter-
RT   transcription factors in the developing mouse central nervous system:
RT   evidence for a role in segmental patterning of the diencephalon.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:4451-4455(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH ZFPM2, AND MUTAGENESIS OF 363-LEU--LEU-367.
RX   PubMed=11382775; DOI=10.1074/jbc.m103577200;
RA   Huggins G.S., Bacani C.J., Boltax J., Aikawa R., Leiden J.M.;
RT   "Friend of GATA 2 physically interacts with chicken ovalbumin upstream
RT   promoter-TF2 (COUP-TF2) and COUP-TF3 and represses COUP-TF2-dependent
RT   activation of the atrial natriuretic factor promoter.";
RL   J. Biol. Chem. 276:28029-28036(2001).
RN   [5]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=28179430; DOI=10.1161/circresaha.116.308825;
RA   Morooka N., Futaki S., Sato-Nishiuchi R., Nishino M., Totani Y.,
RA   Shimono C., Nakano I., Nakajima H., Mochizuki N., Sekiguchi K.;
RT   "Polydom Is an Extracellular Matrix Protein Involved in Lymphatic Vessel
RT   Remodeling.";
RL   Circ. Res. 120:1276-1288(2017).
CC   -!- FUNCTION: Ligand-activated transcription factor. Activated by high
CC       concentrations of 9-cis-retinoic acid and all-trans-retinoic acid, but
CC       not by dexamethasone, cortisol or progesterone (in vitro). Regulation
CC       of the apolipoprotein A-I gene transcription. Binds to DNA site A. May
CC       be required to establish ovary identity during early gonad development.
CC       {ECO:0000250|UniProtKB:P24468}.
CC   -!- SUBUNIT: Interacts with SQSTM1. Binds DNA as a dimer; homodimer or
CC       heterodimer with NR2F6. Interacts with NCOA1, NCOA2, NCOA3 and PPARGC1A
CC       (By similarity). Interacts with ZFPM2. {ECO:0000250,
CC       ECO:0000269|PubMed:11382775}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7947324}.
CC   -!- DEVELOPMENTAL STAGE: Expression in venous vessels of the heart at 16.5
CC       dpc. {ECO:0000269|PubMed:28179430}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X76653; CAA54096.1; -; mRNA.
DR   EMBL; U07635; AAA19854.1; -; mRNA.
DR   EMBL; BC042484; AAH42484.1; -; mRNA.
DR   CCDS; CCDS21359.1; -.
DR   RefSeq; NP_033827.2; NM_009697.3.
DR   AlphaFoldDB; P43135; -.
DR   SMR; P43135; -.
DR   BioGRID; 198166; 1.
DR   IntAct; P43135; 2.
DR   MINT; P43135; -.
DR   STRING; 10090.ENSMUSP00000032768; -.
DR   GlyGen; P43135; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P43135; -.
DR   PhosphoSitePlus; P43135; -.
DR   PaxDb; 10090-ENSMUSP00000032768; -.
DR   PeptideAtlas; P43135; -.
DR   ProteomicsDB; 283355; -.
DR   Pumba; P43135; -.
DR   Antibodypedia; 16260; 381 antibodies from 34 providers.
DR   DNASU; 11819; -.
DR   Ensembl; ENSMUST00000032768.15; ENSMUSP00000032768.8; ENSMUSG00000030551.15.
DR   GeneID; 11819; -.
DR   KEGG; mmu:11819; -.
DR   UCSC; uc009hni.1; mouse.
DR   AGR; MGI:1352452; -.
DR   CTD; 7026; -.
DR   MGI; MGI:1352452; Nr2f2.
DR   VEuPathDB; HostDB:ENSMUSG00000030551; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   GeneTree; ENSGT00940000157540; -.
DR   InParanoid; P43135; -.
DR   OMA; FQGFQAK; -.
DR   OrthoDB; 5400963at2759; -.
DR   PhylomeDB; P43135; -.
DR   TreeFam; TF352097; -.
DR   BioGRID-ORCS; 11819; 8 hits in 81 CRISPR screens.
DR   ChiTaRS; Nr2f2; mouse.
DR   PRO; PR:P43135; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P43135; Protein.
DR   Bgee; ENSMUSG00000030551; Expressed in gonadal ridge and 319 other cell types or tissues.
DR   ExpressionAtlas; P43135; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR   GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0001972; F:retinoic acid binding; ISS:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR   GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0008585; P:female gonad development; ISS:UniProtKB.
DR   GO; GO:0009566; P:fertilization; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IDA:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:1904936; P:interneuron migration; IDA:MGI.
DR   GO; GO:0001945; P:lymph vessel development; IEP:BHF-UCL.
DR   GO; GO:0060838; P:lymphatic endothelial cell fate commitment; ISO:MGI.
DR   GO; GO:0001893; P:maternal placenta development; IMP:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:MGI.
DR   GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0001764; P:neuron migration; IDA:MGI.
DR   GO; GO:0060674; P:placenta blood vessel development; IMP:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0009956; P:radial pattern formation; IMP:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR   GO; GO:0060707; P:trophoblast giant cell differentiation; IMP:MGI.
DR   CDD; cd06958; NR_DBD_COUP_TF; 1.
DR   CDD; cd06948; NR_LBD_COUP-TF; 1.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR   Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR24083:SF45; COUP TRANSCRIPTION FACTOR 2; 1.
DR   PANTHER; PTHR24083; NUCLEAR HORMONE RECEPTOR; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR01282; COUPTNFACTOR.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR   PROSITE; PS51843; NR_LBD; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR   Genevisible; P43135; MM.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Receptor;
KW   Reference proteome; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..414
FT                   /note="COUP transcription factor 2"
FT                   /id="PRO_0000053607"
FT   DOMAIN          177..403
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        76..151
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         79..99
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         115..139
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..414
FT                   /note="Interaction with ZFPM2"
FT                   /evidence="ECO:0000269|PubMed:11382775"
FT   REGION          337..414
FT                   /note="Important for dimerization"
FT   COMPBIAS        26..41
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         51
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P24468"
FT   MUTAGEN         363..367
FT                   /note="LLLRL->RSLRF: Abolishes interaction with ZFPM2."
FT                   /evidence="ECO:0000269|PubMed:11382775"
FT   CONFLICT        36
FT                   /note="A -> P (in Ref. 1; CAA54096)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   414 AA;  45571 MW;  C24CB2E8C8A27E8C CRC64;
     MAMVVSTWRD PQDEVPGSQG SQASQAPPVP GPPPGAPHTP QTPGQGGPAS TPAQTAAGGQ
     GGPGGPGSDK QQQQQHIECV VCGDKSSGKH YGQFTCEGCK SFFKRSVRRN LSYTCRANRN
     CPIDQHHRNQ CQYCRLKKCL KVGMRREAVQ RGRMPPTQPT HGQFALTNGD PLNCHSYLSG
     YISLLLRAEP YPTSRFGSQC MQPNNIMGIE NICELAARML FSAVEWARNI PFFPDLQITD
     QVALLRLTWS ELFVLNAAQC SMPLHVAPLL AAAGLHASPM SADRVVAFMD HIRIFQEQVE
     KLKALHVDSA EYSCLKAIVL FTSDACGLSD VAHVESLQEK SQCALEEYVR SQYPNQPTRF
     GKLLLRLPSL RTVSSSVIEQ LFFVRLVGKT PIETLIRDML LSGSSFNWPY MAIQ
//