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Database: UniProt
Entry: A0A2K5ESG2_AOTNA
LinkDB: A0A2K5ESG2_AOTNA
Original site: A0A2K5ESG2_AOTNA 
ID   A0A2K5ESG2_AOTNA        Unreviewed;       456 AA.
AC   A0A2K5ESG2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Retinoic acid receptor gamma {ECO:0000313|Ensembl:ENSANAP00000036156.1};
GN   Name=RARG {ECO:0000313|Ensembl:ENSANAP00000036156.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000036156.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000036156.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU004334}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000256|ARBA:ARBA00008092}.
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DR   AlphaFoldDB; A0A2K5ESG2; -.
DR   STRING; 37293.ENSANAP00000036156; -.
DR   Ensembl; ENSANAT00000054227.1; ENSANAP00000036156.1; ENSANAG00000035586.1.
DR   GeneTree; ENSGT00940000156458; -.
DR   OMA; MQYTCHK; -.
DR   Proteomes; UP000233020; Unplaced.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR   GO; GO:0046965; F:nuclear retinoid X receptor binding; IEA:Ensembl.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR   GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR   GO; GO:0031076; P:embryonic camera-type eye development; IEA:Ensembl.
DR   GO; GO:0048048; P:embryonic eye morphogenesis; IEA:Ensembl.
DR   GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
DR   GO; GO:0060324; P:face development; IEA:Ensembl.
DR   GO; GO:0002068; P:glandular epithelial cell development; IEA:Ensembl.
DR   GO; GO:0003430; P:growth plate cartilage chondrocyte growth; IEA:Ensembl.
DR   GO; GO:0070384; P:Harderian gland development; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0060740; P:prostate gland epithelium morphogenesis; IEA:Ensembl.
DR   GO; GO:0045637; P:regulation of myeloid cell differentiation; IEA:Ensembl.
DR   GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR   GO; GO:0048384; P:retinoic acid receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR   GO; GO:0060534; P:trachea cartilage development; IEA:Ensembl.
DR   CDD; cd06964; NR_DBD_RAR; 1.
DR   CDD; cd06937; NR_LBD_RAR; 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; IPR047159; NR_DBD_RAR.
DR   InterPro; IPR047158; NR_LBD_RAR.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR003078; Retinoic_acid_rcpt.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR24085; NUCLEAR HORMONE RECEPTOR; 1.
DR   PANTHER; PTHR24085:SF7; RETINOIC ACID RECEPTOR GAMMA; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR01292; RETNOICACIDR.
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.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004334};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004334};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004334};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004334};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004334};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU004334};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004334};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU004334}.
FT   DOMAIN          87..162
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000259|PROSITE:PS51030"
FT   DOMAIN          185..419
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51843"
FT   REGION          58..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   456 AA;  50675 MW;  6429E344F9E4E762 CRC64;
     MATNKERLFA AGALGPGSGY PGAGFPFAFP GALRGSPPFE MLSPSFRGLG QPDLPKEMAS
     LSVETQSTSS EEMVPSSPSP PPPPRVYKPC FVCNDKSSGY HYGVSSCEGC KGFFRRSIQK
     NMVYTCHRDK NCIINKVTRN RCQYCRLQKC FEVGMSKEAV RNDRNKKKKE VKEEGSPDSY
     ELSPQLEELI TKVSKAHQET FPSLCQLGKY TTNSSADHRV QLDLGLWDKF SELATKCIIK
     IVEFAKRLPG FTGLSIADQI TLLKAACLDI LMLRICTRYT PEQDTMTFSD GLTLNRTQMH
     NAGFGPLTDL VFAFAGQLLP LEMDDTETGL LSAICLICGD RMDLEEPEKV DKLQEPLLEA
     LRLYARRRRP SQPYMFPRML MKITDLRGIS TKGAERAITL KMEIPGPMPP LIREMLENPE
     MFEDDSSQPG PHPNASSEDE VPGGQGPALP SPHPFQ
//
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