I2BPL_RAT
ID I2BPL_RAT Reviewed; 783 AA.
AC Q5EIC4; Q4G048;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Probable E3 ubiquitin-protein ligase IRF2BPL {ECO:0000250|UniProtKB:Q9H1B7};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9H1B7};
DE AltName: Full=Enhanced at puberty protein 1;
DE AltName: Full=Interferon regulatory factor 2-binding protein-like;
DE AltName: Full=Polyglutamine-containing protein;
GN Name=Irf2bpl; Synonyms=Eap1, Pqcp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RX PubMed=17627301; DOI=10.1172/jci31752;
RA Heger S., Mastronardi C., Dissen G.A., Lomniczi A., Cabrera R., Roth C.L.,
RA Jung H., Galimi F., Sippell W., Ojeda S.R.;
RT "Enhanced at puberty 1 (EAP1) is a new transcriptional regulator of the
RT female neuroendocrine reproductive axis.";
RL J. Clin. Invest. 117:2145-2154(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 434-783.
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-534, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Probable E3 ubiquitin protein ligase involved in the
CC proteasome-mediated ubiquitin-dependent degradation of target proteins.
CC Through the degradation of CTNNB1, functions downstream of FOXF2 to
CC negatively regulate the Wnt signaling pathway. Probably plays a role in
CC the development of the central nervous system and in neuronal
CC maintenance (By similarity). Also acts as a transcriptional regulator
CC of genes controlling female reproductive function. May play a role in
CC gene transcription by transactivating GNRH1 promoter and repressing
CC PENK promoter. {ECO:0000250|UniProtKB:Q9H1B7,
CC ECO:0000269|PubMed:17627301}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9H1B7};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9H1B7}.
CC -!- SUBUNIT: Interacts with CTNNB1. {ECO:0000250|UniProtKB:Q9H1B7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17627301}.
CC -!- TISSUE SPECIFICITY: Expressed in the regions of the hypothalamus
CC involved in reproductive control, such as medial preoptic area, arcuate
CC nucleus and ventromedial nucleus. {ECO:0000269|PubMed:17627301}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during puberty in the hypothalamus,
CC but not in the cerebral cortex. {ECO:0000269|PubMed:17627301}.
CC -!- SIMILARITY: Belongs to the IRF2BP family. {ECO:0000305}.
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DR EMBL; AY879229; AAW72780.1; -; Genomic_DNA.
DR EMBL; BC098759; AAH98759.1; -; mRNA.
DR RefSeq; NP_001012488.1; NM_001012470.1.
DR AlphaFoldDB; Q5EIC4; -.
DR SMR; Q5EIC4; -.
DR STRING; 10116.ENSRNOP00000064525; -.
DR iPTMnet; Q5EIC4; -.
DR PhosphoSitePlus; Q5EIC4; -.
DR jPOST; Q5EIC4; -.
DR PaxDb; Q5EIC4; -.
DR GeneID; 314329; -.
DR KEGG; rno:314329; -.
DR UCSC; RGD:1310994; rat.
DR CTD; 64207; -.
DR RGD; 1310994; Irf2bpl.
DR eggNOG; KOG3579; Eukaryota.
DR InParanoid; Q5EIC4; -.
DR OrthoDB; 1156771at2759; -.
DR PhylomeDB; Q5EIC4; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5EIC4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0046543; P:development of secondary female sexual characteristics; IMP:ParkinsonsUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:ParkinsonsUK-UCL.
DR GO; GO:0007399; P:nervous system development; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:ParkinsonsUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.1580; -; 1.
DR InterPro; IPR044882; I2BP1/2_C3HC4-RING_sf.
DR InterPro; IPR022750; Interferon_reg_fac2-bd1_2_Znf.
DR Pfam; PF11261; IRF-2BP1_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..783
FT /note="Probable E3 ubiquitin-protein ligase IRF2BPL"
FT /id="PRO_0000323512"
FT ZN_FING 702..749
FT /note="RING-type; degenerate"
FT REGION 94..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 85..112
FT /evidence="ECO:0000255"
FT COILED 323..358
FT /evidence="ECO:0000255"
FT COMPBIAS 94..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..284
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..595
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT CROSSLNK 79
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
SQ SEQUENCE 783 AA; 81496 MW; 27BB8D21D8EA85FE CRC64;
MSAAQVSSSR RQSCYLCDLP RMPWAMIWDF SEPVCRGCVN YEGADRIEFV IETARQLKRA
HGCFQDGRSP GPPPPVGVKT VALSAKEAAA AAAAAQQQQQ QQQQQQQQQQ QQPQQLNHVD
GSTKPAVLPA PSGLERYGLS AAAAAAAAAA AAVEQRSRFE YPPPPVSLGS SSHAARLPNG
LGGPNGFPKP APEEGPPELN RQSPNSSSAA TSVASRRGTH SGLVTGLPNP GGGGGPQLTV
PPNLLPQTLL NGPASAAVLP PPHGLGGSRG PPTPAPPGAP GGPACLGGPP GVSATVSSAP
SSTSSTVAEV GVGAAGKRPG SVSSTDQERE LKEKQRNAEA LAELSESLRN RAEEWANKPK
MVRDTLLTLA GCTPYEVRFK KDHSLLGRVF AFDAVSKPGM DYELKLFIEY PTGSGNVYSS
ASGVAKQMYQ DCMKDFGRGL SSGFKYLEYE KKHGSGDWRL LGDLLPEAVR FFKEGVPGAD
MLPQPYLDAS CPMLPTALVS LSRAPSAPPG TGALPPAAPT GRGAAASLRK RKASPEPPDS
AESALKLGEE QQRQQWMANQ SEALKLTMSA GGFAAPGHAA GGPPPPPPPL GPHSNRTTPP
ESAPQNGPSP MAALMSVADT LGTAHSPKDG SSVHSTTASA RRNSSSPVSP ASVPGQRRLA
SRNGDLNLQV APPPPSAHPG MDQVHPQNIP DSPMANSGPL CCTICHERLE DTHFVQCPSV
PSHKFCFPCS RESIKAQGAT GEVYCPSGEK CPLVGSNVPW AFMQGEIATI LAGDVKVKKE
RDP
