COT2_BOVIN
ID COT2_BOVIN Reviewed; 414 AA.
AC Q9TTR7; Q08DL8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=COUP transcription factor 2;
DE Short=COUP-TF2;
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=TFCOUP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Corpus luteum;
RA Walther N.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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
CC PPARGC1A. Interacts with ZFPM2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ249441; CAB55624.1; -; mRNA.
DR EMBL; BC123677; AAI23678.1; -; mRNA.
DR PIR; JH0787; JH0787.
DR RefSeq; NP_776827.1; NM_174402.3.
DR AlphaFoldDB; Q9TTR7; -.
DR SMR; Q9TTR7; -.
DR STRING; 9913.ENSBTAP00000023969; -.
DR PaxDb; Q9TTR7; -.
DR Ensembl; ENSBTAT00000023969; ENSBTAP00000023969; ENSBTAG00000018007.
DR GeneID; 281945; -.
DR KEGG; bta:281945; -.
DR CTD; 7026; -.
DR VEuPathDB; HostDB:ENSBTAG00000018007; -.
DR VGNC; VGNC:32241; NR2F2.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000157540; -.
DR InParanoid; Q9TTR7; -.
DR OMA; NWPYMST; -.
DR OrthoDB; 666130at2759; -.
DR TreeFam; TF352097; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000018007; Expressed in myometrium and 102 other tissues.
DR ExpressionAtlas; Q9TTR7; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
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: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; IEA:Ensembl.
DR GO; GO:0048514; P:blood vessel morphogenesis; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:1904936; P:interneuron migration; IEA:Ensembl.
DR GO; GO:0060838; P:lymphatic endothelial cell fate commitment; IEA:Ensembl.
DR GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060674; P:placenta blood vessel development; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0009956; P:radial pattern formation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IEA:Ensembl.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 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 Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 2: Evidence at transcript 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_0000053605"
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:0000250"
FT REGION 337..414
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 414 AA; 45557 MW; C24CB023C8A27F57 CRC64;
MAMVVSTWRD PQDEVPGSQG SQASQAPPVP GPPPGAPHTP QTPGQGGPAS TPAQTAAGGQ
GGPGGPGSDK QQQQQHIECV VCGDKSSGKH YGQFTCEGCK SFFKRSVRRN LSYTCRANRN
CPIDQHHRNQ CQYCRLKKCL KVGMRREAVQ RGRMPPTQPS 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
