NR4A2_PONAB
ID NR4A2_PONAB Reviewed; 598 AA.
AC Q5R5Y4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Nuclear receptor subfamily 4 group A member 2;
GN Name=NR4A2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional regulator which is important for the
CC differentiation and maintenance of meso-diencephalic dopaminergic
CC (mdDA) neurons during development. It is crucial for expression of a
CC set of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential
CC for development of mdDA neurons (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SFPQ, NCOR2, SIN3A and HADC1. The interaction
CC with NCOR2 increases in the absence of PITX3. Interacts with PER2 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00407}. Note=Mostly nuclear; oxidative
CC stress promotes cytoplasmic localization. {ECO:0000250}.
CC -!- DOMAIN: the ligand-binding domain (LBD) contains no cavity as a result
CC of the tight packing of side chains from several bulky hydrophobic
CC residues in the region normally occupied by ligands. NR4A2 lacks a
CC 'classical' binding site for coactivators (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family.
CC {ECO:0000305}.
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DR EMBL; CR860717; CAH92832.1; -; mRNA.
DR AlphaFoldDB; Q5R5Y4; -.
DR BMRB; Q5R5Y4; -.
DR SMR; Q5R5Y4; -.
DR STRING; 9601.ENSPPYP00000014352; -.
DR eggNOG; KOG4217; Eukaryota.
DR InParanoid; Q5R5Y4; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071376; P:cellular response to corticotropin-releasing hormone stimulus; ISS:UniProtKB.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; ISS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; ISS:UniProtKB.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR003070; Nuc_orph_rcpt.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR003073; NURR_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; PR01284; NUCLEARECPTR.
DR PRINTS; PR01287; NURRNUCRCPTR.
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 Cytoplasm; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..598
FT /note="Nuclear receptor subfamily 4 group A member 2"
FT /id="PRO_0000326152"
FT DOMAIN 360..595
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 260..335
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 263..283
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 299..318
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 287..314
FT /note="Bipartite nuclear localization signal (NLS1)"
FT /evidence="ECO:0000250"
FT MOTIF 338..350
FT /note="Nuclear localization signal (NLS1)"
FT /evidence="ECO:0000250"
FT MOTIF 443..452
FT /note="nuclear export sequence (NES1)"
FT /evidence="ECO:0000250"
FT MOTIF 568..577
FT /note="nuclear export sequence (NES2)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 598 AA; 66690 MW; 9CC06E60E1541844 CRC64;
MPCVQAQYGS SPQGASPASQ GYSYHSSGEY SSDFLTPEFV KFSMDLTNTE ITATTSLPSF
STFMDNYSTG YDVKPPCLYQ MPLSGQQSSI KVEDIQMHNY QQHSHLPPQS EEMMPHSGSV
YYKPSSPPTP TTPGFQVQHS PMWDDPGSLH NFHQNYVATT HMIEQRKTPV SRLSLFSFKQ
SPPGTPVSSC QMRFDGPLHV PMNPEPAGSH HVVDGQTFAV PNPIRKPASM GFPGLQIGHA
SQLLDTQVPS PPSRGSPSNE GLCAVCGDNA ACQHYGVRTC EGCKGFFKRT VQKNAKYVCL
ANKNCPVDKR RRNRCQYCRF QKCLAVGMVK EVVRTDSLKG RRGRLPSKPK SPQEPSPPSP
PVSLISALVR AHVDSNPAMT SLDYSRFQAN PDYQMSGDDT QHIQQFYDLL TGSMEIIRGW
AEKIPGFADL PKADQDLLFE SAFLELFVLR LAYRSNPVEG KLIFCNGVVL HRLQCVRGFG
EWIDSIVEFS SNLQNMNIDI SAFSCIAALA MVTERHWLKE PKRVEELQNK IVNCLKDHVT
FNNGGLNRPN YLSKLLGKLP ELRTLCTQGL QRIFYLKLED LVPPPAIIDK LFLDTLPF
