NR4A1_CANLF
ID NR4A1_CANLF Reviewed; 598 AA.
AC P51666;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Nuclear receptor subfamily 4 group A member 1;
DE AltName: Full=Orphan nuclear receptor HMR;
DE AltName: Full=Orphan nuclear receptor NGFI-B;
GN Name=NR4A1; Synonyms=HMR;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8895335; DOI=10.1210/endo.137.11.8895335;
RA Pichon B., Jimenez-Cervantes C., Pirson I., Maenhaut C., Christophe D.;
RT "Induction of nerve growth factor-induced gene-B (NGFI-B) as an early event
RT in the cyclic adenosine monophosphate response of dog thyrocytes in primary
RT culture.";
RL Endocrinology 137:4691-4698(1996).
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). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GADD45GIP1. Interacts with STK11. Binds DNA as
CC a monomer (By similarity). Heterodimer (via DNA-binding domain) with
CC RXRA (via C-terminus); DNA-binding of the heterodimer is enhanced by 9-
CC cis retinoic acid (By similarity). Competes for the RXRA interaction
CC with EP300 and thereby attenuates EP300 mediated acetylation of RXRA
CC (By similarity). {ECO:0000250|UniProtKB:P22736,
CC ECO:0000250|UniProtKB:P22829}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P22736}. Nucleus
CC {ECO:0000250|UniProtKB:P22736}. Mitochondrion
CC {ECO:0000250|UniProtKB:P22736}. Note=Translocation to the mitochondrion
CC upon interaction with RXRA and upon the presence of 9-cis retinoic
CC acid. {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; X97226; CAA65863.1; -; mRNA.
DR RefSeq; NP_001003227.1; NM_001003227.1.
DR RefSeq; XP_005636733.1; XM_005636676.2.
DR RefSeq; XP_013963720.1; XM_014108245.1.
DR RefSeq; XP_013963721.1; XM_014108246.1.
DR AlphaFoldDB; P51666; -.
DR SMR; P51666; -.
DR STRING; 9612.ENSCAFP00000010883; -.
DR Ensembl; ENSCAFT00845047929; ENSCAFP00845037598; ENSCAFG00845026982.
DR GeneID; 403897; -.
DR KEGG; cfa:403897; -.
DR CTD; 3164; -.
DR VEuPathDB; HostDB:ENSCAFG00845026982; -.
DR eggNOG; KOG4217; Eukaryota.
DR GeneTree; ENSGT00950000183038; -.
DR InParanoid; P51666; -.
DR OrthoDB; 454476at2759; -.
DR Reactome; R-CFA-198693; AKT phosphorylates targets in the nucleus.
DR Reactome; R-CFA-383280; Nuclear Receptor transcription pathway.
DR Proteomes; UP000002254; Chromosome 27.
DR Bgee; ENSCAFG00000007338; Expressed in tongue and 48 other tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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: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:0071376; P:cellular response to corticotropin-releasing hormone stimulus; ISS:UniProtKB.
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: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 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_0000053714"
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..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..159
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 COMPBIAS 120..140
FT /note="Polar residues"
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; 64424 MW; 773563A8EC48F906 CRC64;
MPCIQAQYGT PAPSPGPRDH LASDPLTPEL SKPTMDLASP EAAPTAPTAL PSFSTFMDGY
TGEFDTFLYQ LPGTAQPCSS ASSSASSTSS SSATSPASAS FKFEDFQVYG CYPGPLSGPL
DETLSSSGSD YYGSPCSAPS PSTPSFQPPQ LSPWDGSFGP FSPSQTYEGL RAWTEQLPKA
SGHPQPPAFF SFSPPTGPSP SLAQSPLKLF PSQATCQLGE RESYSISTAF PGLAPTSPHL
DGPGMLDAPV PSAKARSGAP SGSEGRCAVC GDNASCQHYG VRTCEGCKGF FKRTVQKNAK
YICLANKDCP VDKRRRNRCQ FCRFQKCLAV GMVKEVVRTD SLKGRRGRLP SKPKQPPDAS
PANLLTSLVR AHLDSGPSTA KLDYSKFQEL VLPHFGKEDA GDVQQFYDLL SGSLEVIRKW
AEKIPGFAEL SPGDQDLLLE SAFLELFILR LAYRSKPAEG KLIFCSGLVL HRLQCARGFG
DWIDSILAFS RSLHGLVVDV PAFACLSALV LITDRHGLQE PRRVEELQNR IASCLKEHVS
AVAGEPQPAS CLSRLLGKLP ELRTLCTQGL QRIFYLKLED LVPPPPIVDK IFMDTLPF
