NR4A1_BOVIN
ID NR4A1_BOVIN Reviewed; 598 AA.
AC Q0V8F0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Nuclear receptor subfamily 4 group A member 1;
GN Name=NR4A1;
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 [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Orphan nuclear receptor. May act concomitantly with NURR1 in
CC regulating the expression of delayed-early genes during liver
CC regeneration. Binds the NGFI-B response element (NBRE) 5'-AAAAGGTCA-3'.
CC May inhibit NF-kappa-B transactivation of IL2. Participates in energy
CC homeostasis by sequestrating the kinase STK11 in the nucleus, thereby
CC attenuating cytoplasmic AMPK activation (By similarity). Plays a role
CC in the vascular response to injury (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P12813}.
CC -!- SUBUNIT: Binds DNA as a monomer (By similarity). Interacts with
CC GADD45GIP1 (By similarity). Interacts with STK11 (By similarity).
CC Interacts with IFI27 (By similarity). Heterodimer (via DNA-binding
CC domain) with RXRA (via C-terminus); DNA-binding of the heterodimer is
CC enhanced by 9-cis retinoic acid (By similarity). Competes for the RXRA
CC interaction with EP300 and thereby attenuates EP300 mediated
CC acetylation of RXRA (By similarity). {ECO:0000250|UniProtKB:P22736,
CC ECO:0000250|UniProtKB:P22829}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P22736}. Cytoplasm
CC {ECO:0000250|UniProtKB:P22736}. Mitochondrion
CC {ECO:0000250|UniProtKB:P22736}. Note=Nuclear export to the cytoplasm is
CC XPO1-mediated and positively regulated by IFI27. Translocation to the
CC mitochondrion upon interaction with RXRA and upon the presence of 9-cis
CC retinoic acid (By similarity). {ECO:0000250|UniProtKB:P22736}.
CC -!- PTM: Phosphorylated at Ser-351 by RPS6KA1 and RPS6KA3 in response to
CC mitogenic or stress stimuli. {ECO:0000250}.
CC -!- PTM: Acetylated by p300/CBP, acetylation increases stability.
CC Deacetylated by HDAC1 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR4
CC subfamily. {ECO:0000305}.
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DR EMBL; BT026269; ABG67108.1; -; mRNA.
DR RefSeq; NP_001069379.1; NM_001075911.1.
DR RefSeq; XP_005206276.1; XM_005206219.3.
DR RefSeq; XP_005206277.1; XM_005206220.3.
DR RefSeq; XP_005206278.1; XM_005206221.1.
DR RefSeq; XP_010803210.1; XM_010804908.2.
DR AlphaFoldDB; Q0V8F0; -.
DR SMR; Q0V8F0; -.
DR STRING; 9913.ENSBTAP00000000648; -.
DR PaxDb; Q0V8F0; -.
DR PRIDE; Q0V8F0; -.
DR Ensembl; ENSBTAT00000000648; ENSBTAP00000000648; ENSBTAG00000000507.
DR Ensembl; ENSBTAT00000076548; ENSBTAP00000057165; ENSBTAG00000000507.
DR Ensembl; ENSBTAT00000082220; ENSBTAP00000064607; ENSBTAG00000000507.
DR GeneID; 528390; -.
DR KEGG; bta:528390; -.
DR CTD; 3164; -.
DR VEuPathDB; HostDB:ENSBTAG00000000507; -.
DR VGNC; VGNC:32245; NR4A1.
DR eggNOG; KOG4217; Eukaryota.
DR GeneTree; ENSGT00950000183038; -.
DR HOGENOM; CLU_007368_14_2_1; -.
DR InParanoid; Q0V8F0; -.
DR OMA; HASCQHY; -.
DR OrthoDB; 454476at2759; -.
DR TreeFam; TF315430; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000000507; Expressed in adenohypophysis and 104 other tissues.
DR ExpressionAtlas; Q0V8F0; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IBA:GO_Central.
DR GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; 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:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0071376; P:cellular response to corticotropin-releasing hormone stimulus; ISS:UniProtKB.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IEA:Ensembl.
DR GO; GO:0035767; P:endothelial cell chemotaxis; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0061469; P:regulation of type B pancreatic cell proliferation; ISS:UniProtKB.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; 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; IPR003071; Nuc_orp_HMR_rcpt.
DR InterPro; IPR003070; Nuc_orph_rcpt.
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; PR01285; HMRNUCRECPTR.
DR PRINTS; PR01284; NUCLEARECPTR.
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 Acetylation; Cytoplasm; DNA-binding; Metal-binding; Mitochondrion; Nucleus;
KW Phosphoprotein; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..598
FT /note="Nuclear receptor subfamily 4 group A member 1"
FT /id="PRO_0000274208"
FT DOMAIN 360..595
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 264..339
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 267..287
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 303..327
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..466
FT /note="Required for nuclear import"
FT /evidence="ECO:0000250|UniProtKB:P22736"
FT REGION 299..361
FT /note="Required for the interaction with RXRA"
FT /evidence="ECO:0000250|UniProtKB:P22736"
FT REGION 341..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 341
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P22829"
FT MOD_RES 351
FT /note="Phosphoserine; by PKA, RPS6KA1 and RPS6KA3"
FT /evidence="ECO:0000250|UniProtKB:P22829"
SQ SEQUENCE 598 AA; 64437 MW; D8936BD9C5AB661C CRC64;
MPCIQAQYGT PAPSPGPRDH LAGDLLTPEL SKPTMDLASP EAAPAVPTAL PSFSTFMDGY
TGEFDTFLYQ LSGTAQPCSS ASSSASSTSS SSATSPASAS FKFEDFQVYG CYPGTLSGPL
DETLSSSGSD YYGSPCSAPS PSTPSFQPPQ LSPWDGSFGP FSPSQTYEGL RAWTEQLPKA
SGPPQPPAFF SFSPPPGPSP SLAPSPLKLF PSQAAHQLGE GESYSMQTAF PGLVPTSPHL
DGSGRLDAPV TSAKARSGAP GGSEGRCAVC GDNASCQHYG VRTCEGCKGF FKRTVQKNAK
YICLANKDCP VDKRRRNRCQ FCRFQKCLAV GMVKEVVRTD SLKGRRGRLP SKPKQPPETS
PAHLLTSLVR AHLDSGPSTS KLDYSKFQEL ALPHFGKEDA GDVQQFYDLL SGSLEVIRKW
AEKIPGFAEL SPGDQDLLLE SAFLELFILR LAYRSKPAEG KLIFCSGLVL HRLQCARGFG
DWIDSILAFS RSLHSLVVDI PAFACLSALV LITDRHGLQE PRRVEELQNR IASCLKEHVS
AEAGEPQPAS CLSRLLGKLP ELRTLCTQGL QRIFYLKLED LVPPPPIVDK IFMDTLPF
