ARI5A_BOVIN
ID ARI5A_BOVIN Reviewed; 592 AA.
AC Q3SWY1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=AT-rich interactive domain-containing protein 5A;
DE Short=ARID domain-containing protein 5A;
GN Name=ARID5A;
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].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-binding protein that may regulate transcription and act
CC as a repressor by binding to AT-rich stretches in the promoter region
CC of target genes. May act as repressor and down-regulate enhancer-
CC dependent gene expressison. May positively regulate chondrocyte-
CC specific transcription such as of COL2A1 in collaboration with SOX9 and
CC positively regulate histone H3 acetylation at chondrocyte-specific
CC genes. May stimulate early-stage chondrocyte differentiation and
CC inhibit later stage differention. Can repress ESR1-mediated
CC transcriptional activation; proposed to act as corepressor for
CC selective nuclear hormone receptors. As RNA-binding protein involved in
CC the regulation of inflammatory response by stabilizing selective
CC inflammation-related mRNAs, such as IL6, STAT3 and TBX21. Binds to stem
CC loop structures located in the 3'UTRs of IL6, STAT3 and TBX21 mRNAs; at
CC least for STAT3 prevents binding of ZC3H12A to the mRNA stem loop
CC structure thus inhibiting its degradation activity. Contributes to
CC elevated IL6 levels possibly implicated in autoimmunity processes. IL6-
CC dependent stabilization of STAT3 mRNA may promote differentiation of
CC naive CD4+ T-cells into T-helper Th17 cells. In CD4+ T-cells may also
CC inhibit RORC-induced Th17 cell differentiation independently of IL6
CC signaling. Stabilization of TBX21 mRNA contributes to elevated
CC interferon-gamma secretion in Th1 cells possibly implicated in the
CC establishment of septic shock. Stabilizes TNFRSF4/OX40 mRNA by binding
CC to the conserved stem loop structure in its 3'UTR; thereby competing
CC with the mRNA-destabilizing functions of RC3H1 and endoribonuclease
CC ZC3H12A (By similarity). {ECO:0000250|UniProtKB:Q3U108}.
CC -!- SUBUNIT: Interacts with SOX9. Interacts with ESR1. Interacts with RORC.
CC {ECO:0000250|UniProtKB:Q03989, ECO:0000250|UniProtKB:Q3U108}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03989,
CC ECO:0000250|UniProtKB:Q3U108, ECO:0000255|PROSITE-ProRule:PRU00355}.
CC -!- PTM: Phosphorylated by MAPK14 on serine residues involving a TLR4
CC signaling pathway upon lipopolysaccharide (LPS) stimulation leading to
CC its ubiquitination and proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q3U108}.
CC -!- PTM: Ubiquitinated leading to proteasomal degradation; involving WWP1
CC linked to MAPK14-mediated phosphorylation upon LPS stimulation.
CC {ECO:0000250|UniProtKB:Q3U108}.
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DR EMBL; BC104604; AAI04605.1; -; mRNA.
DR RefSeq; NP_001030426.1; NM_001035349.1.
DR AlphaFoldDB; Q3SWY1; -.
DR SMR; Q3SWY1; -.
DR STRING; 9913.ENSBTAP00000054489; -.
DR PaxDb; Q3SWY1; -.
DR PRIDE; Q3SWY1; -.
DR Ensembl; ENSBTAT00000026200; ENSBTAP00000026200; ENSBTAG00000014090.
DR GeneID; 524118; -.
DR KEGG; bta:524118; -.
DR CTD; 10865; -.
DR VEuPathDB; HostDB:ENSBTAG00000014090; -.
DR VGNC; VGNC:26131; ARID5A.
DR eggNOG; KOG2744; Eukaryota.
DR GeneTree; ENSGT00940000161253; -.
DR HOGENOM; CLU_032275_0_0_1; -.
DR InParanoid; Q3SWY1; -.
DR OrthoDB; 368297at2759; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000014090; Expressed in intramuscular adipose tissue and 104 other tissues.
DR ExpressionAtlas; Q3SWY1; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR Pfam; PF01388; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR PROSITE; PS51011; ARID; 1.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Immunity; Innate immunity; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; RNA-binding;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..592
FT /note="AT-rich interactive domain-containing protein 5A"
FT /id="PRO_0000288929"
FT DOMAIN 52..144
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT REGION 1..299
FT /note="Interaction with SOX9"
FT /evidence="ECO:0000250|UniProtKB:Q3U108"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U108"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U108"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U108"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U108"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q3U108"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q3U108"
SQ SEQUENCE 592 AA; 64136 MW; 00E06E8066B4AF8A CRC64;
MAPPVKGKRK QSEEGEPLDP PVSPQPDGEP RSRSPVRLEE PPEAGREREE EQEEEQAFLV
SLYKFMKERH TPIERVPHLG FKQINLWKIY KAVEKLGAYE LVTGRRLWKN VYDELGGSPG
STSAATCTRR HYERLVLPYV RHLKGEDDKP LPPSKPRKQY KMAKEPRGDD GATERPKKVK
EEKRVDQLMP AKTKTDAPDP ARLPSQETPR DGMEQRGPAA GPSLPFLGAS GCPEAYKRLL
SSFYCRGTHG IMSPLAKKKL LAQVSKAEAL QCQEEGCRHG AGGEPQAPPA APPLESPQSP
GGPAEDSRHR LTPLEGRQAP GGGLWGETQA GPRPSAPVVT GCFHAYPSEV LKPISQRPRD
LFPSLKDRVL LGPPAKEEGL PAKEPPLVWG GDAGRPSAFH KGSSRKGSLY PKPKACWVSP
MTKVPAESPV PLPTFPSSPG LGHKRSLAED SSVHGSKKLR AVSPFLKEAN AQECGTKPRG
PDLAVSCLLG PALPEAYRGT LLRCPLNFAG TLGPLKGQAT LPFSPLVIPA FPAHLLATTA
PSPMTAGLMH LPPASFDSAL CHRLCPASSP WHVPPATAYT APHFSFHLNT KL
