COT2_CHICK
ID COT2_CHICK Reviewed; 410 AA.
AC Q90733;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
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 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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8119130; DOI=10.1242/dev.120.1.25;
RA Lutz B., Kuratani S., Cooney A.J., Wawersik W., Tsai S.Y., Eichele G.,
RA Tsai M.;
RT "Developmental regulation of the orphan receptor COUP-TF II gene in spinal
RT motor neurons.";
RL Development 120:25-36(1994).
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) (By
CC similarity). May be involved in motor neuron development.
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds DNA as a homodimer.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Highly expressed in the developing spinal motor
CC neurons.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
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DR EMBL; U00697; AAA17733.1; -; mRNA.
DR PIR; I50689; I50689.
DR RefSeq; NP_989752.1; NM_204421.1.
DR AlphaFoldDB; Q90733; -.
DR SMR; Q90733; -.
DR STRING; 9031.ENSGALP00000011318; -.
DR PaxDb; Q90733; -.
DR Ensembl; ENSGALT00000011332; ENSGALP00000011318; ENSGALG00000007000.
DR GeneID; 386585; -.
DR KEGG; gga:386585; -.
DR CTD; 7026; -.
DR VEuPathDB; HostDB:geneid_386585; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000157540; -.
DR HOGENOM; CLU_007368_20_1_1; -.
DR InParanoid; Q90733; -.
DR OMA; NWPYMST; -.
DR OrthoDB; 666130at2759; -.
DR PhylomeDB; Q90733; -.
DR PRO; PR:Q90733; -.
DR Proteomes; UP000000539; Chromosome 10.
DR Bgee; ENSGALG00000007000; Expressed in kidney and 12 other tissues.
DR ExpressionAtlas; Q90733; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
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:AgBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..410
FT /note="COUP transcription factor 2"
FT /id="PRO_0000053609"
FT DOMAIN 173..399
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 72..147
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 75..95
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 111..135
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..410
FT /note="Important for dimerization"
FT COMPBIAS 21..50
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 45427 MW; 760A996E29082E3D CRC64;
MAMVVGAWRD PQDDVPGAQG TQPAPAPPVQ GPPAGTPHTP QTPGPGGPPS TPAQSNAASQ
QSQGDKQQQQ QHIECVVCGD KSSGKHYGQF TCEGCKSFFK RSVRRNLSYT CRANRNCPID
QHHRNQCQYC RLKKCLKVGM RREAVQRGRM PPTQPTHGQF ALTNGDPLNC HSYLSGYISL
LLRAEPYPTS RFGSQCMQPN NIMGIENICE LAARMLFSAV EWARNIPFFP DLQITDQVAL
LRLTWSELFV LNAAQCSMPL HVAPLLAAAG LHASPMSADR VVAFMDHIRI FQEQVEKLKA
LHVDSAEYSC LKAIVLFTSD ACGLSDVAHV ESLQEKSQCA LEEYVRSQYP NQPTRFGKLL
LRLPSLRTVS SSVIEQLFFV RLVGKTPIET LIRDMLLSGS SFNWPYMSIQ
