ARI5B_CHICK
ID ARI5B_CHICK Reviewed; 1185 AA.
AC Q5ZJ69;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=AT-rich interactive domain-containing protein 5B;
DE Short=ARID domain-containing protein 5B;
GN Name=ARID5B; ORFNames=RCJMB04_20e24;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Transcription coactivator that binds to the 5'-AATA[CT]-3'
CC core sequence and plays a key role in adipogenesis and liver
CC development. Required for adipogenesis: regulates triglyceride
CC metabolism in adipocytes by regulating expression of adipogenic genes
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}.
CC -!- DOMAIN: The ARID domain mediates the interaction with DNA.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ARID5B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ720565; CAG32224.1; -; mRNA.
DR RefSeq; NP_001026391.1; NM_001031220.1.
DR AlphaFoldDB; Q5ZJ69; -.
DR BMRB; Q5ZJ69; -.
DR SMR; Q5ZJ69; -.
DR STRING; 9031.ENSGALP00000004725; -.
DR PaxDb; Q5ZJ69; -.
DR GeneID; 423661; -.
DR KEGG; gga:423661; -.
DR CTD; 84159; -.
DR VEuPathDB; HostDB:geneid_423661; -.
DR eggNOG; KOG2744; Eukaryota.
DR InParanoid; Q5ZJ69; -.
DR OrthoDB; 368297at2759; -.
DR PhylomeDB; Q5ZJ69; -.
DR PRO; PR:Q5ZJ69; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0060612; P:adipose tissue development; ISS:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.150.60; -; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR InterPro; IPR030408; ARID5B.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR043151; BAH_sf.
DR PANTHER; PTHR13964:SF37; PTHR13964:SF37; 1.
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; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1185
FT /note="AT-rich interactive domain-containing protein 5B"
FT /id="PRO_0000288932"
FT DOMAIN 321..413
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT REGION 248..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1053
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1185 AA; 132723 MW; 1A1B4D771B43DCB1 CRC64;
MERSALQWVG APCGSHGPYV FYRAFRFQRR GGGRARVLSL GDFFFVRCRA EEPACIAELQ
LLWEERTSRQ LLSSAKLYFL PEDTPQGRTS DHGEDEVIAV SEKVTVKLED LAKWAQSDFS
KWKCGFRAEP VKPMDVGKNG QKEALMRYRQ STLNSGLNFK DILKEKADLG EDDEDSNLLI
LSYPQYCRYR SMLKRIQDKP SSILTDQFVL ALGGIAVTSK NPQIFYCRDT FDHPTLIENE
SICDEFAPNL KGRPRKKKPC PQRRDSLNGI KDSNNNSESK AVAKVKCEAK SALPKPKSNN
SNCKKGSSED KSKIAVGEEC RADEQAFLVA LYKYMKERKT PIERIPYLGF KQINLWTMFQ
AAQKLGGYET ITARRQWKHI YDELGGNPGS TSAATCTRRH YERLILPYER FIKGEEDKPL
PPVKPRKQDN SSQEGEAKTK VSGTKRIKNE NQKSKKEKDN AQKPQDASEV SSEQEKDQES
ADQKNFTEHP TAGETKQPNQ GPPPLLPEAA RPLPMEKIDV TENSSSSEKA KEEVPHLSSF
PSLSMPPDED TVLDATVTKR LHSSADTQED TKPERRIHKA FTESLENEPP EMPFSTFPVQ
LPTQSDMEDD KLPEMADYIA NCTVKVDQLG NEDIHNALKQ TPKVLVVQNF DMFKEKELPG
SMSDDSTFGY TPLLYSKGNP GIMSPLAKKK LLSQVSGAAL SCSYPYGSPP PLISKKKLNS
RDELSSSLSQ GPHVPNSDPI AINRPSVIQH VQSFKSKEER KSINDVFKHD MLSKVDPQRC
DFSQHCLSSL AESYVPKTDI QDCKDKMTEK RALQHSRVPT FLADFYSSPH LHNLFRHTEH
HLNNEQTSKY LPRDMFRESE NISTFTQHKH QEKLNLNYHP SLHQQEKKAT VEASSDDQPT
DLSLPKSIHK QTAKAPGPGL SHSSMAQQEG KGVSLFQAAS SQAVSLDCNP KACRVSPMAM
TAPKKHSELL HRSGKQQAQR LENLRKMEGM VHPIISRRMS PQNIGAARPL KRGLEELDKV
ISEKKVRAVS PLHLPKETSV KEKVPDAEGE GSKSLHGLHS GSVLESHKFP LSAPIFPGLY
PGTLCTGLNN RLPPGYSHPL QYLKNQTVLS PLMQPLALHS LMVQRQFLTS PANSQQLYRH
LATATPVGSS YGDLLHNSIY PLAAINPQAA FPPSQLSSVH PSTKL
