I2BPL_MACMU
ID I2BPL_MACMU Reviewed; 794 AA.
AC Q2MJS2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 82.
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;
GN Name=IRF2BPL; Synonyms=EAP1;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
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 (By similarity). {ECO:0000250|UniProtKB:Q5EIC4,
CC ECO:0000250|UniProtKB:Q9H1B7}.
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 the control of GNRH1 secretion, such as arcuate nucleus.
CC {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; DQ323548; ABC49849.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2MJS2; -.
DR SMR; Q2MJS2; -.
DR STRING; 9544.ENSMMUP00000012987; -.
DR eggNOG; KOG3579; Eukaryota.
DR InParanoid; Q2MJS2; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006718; 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; IEP:ParkinsonsUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:ParkinsonsUK-UCL.
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 2: Evidence at transcript level;
KW Coiled coil; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..794
FT /note="Probable E3 ubiquitin-protein ligase IRF2BPL"
FT /id="PRO_0000323511"
FT ZN_FING 713..760
FT /note="RING-type; degenerate"
FT REGION 172..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 95..130
FT /evidence="ECO:0000255"
FT COILED 334..369
FT /evidence="ECO:0000255"
FT COMPBIAS 208..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..294
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..606
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..663
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 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1B7"
FT MOD_RES 660
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 794 AA; 82446 MW; 24C820685BD97B43 CRC64;
MSAAQVSSSR RQSCYLCDLP RMPWAMIWDF SEPVCRGCVN YEGADRIEFV IETARQLKRA
HGCFQDGRSP GPPPPVGVKT VALSAKEAAA AAAAAAAAAA AAQQQQQQQQ QQQQQQQQQQ
QQQQQLNHVD GSSKPAVLAA PSGLERYGLS AAAAAAAAAA AAVEQRSRFE YPPPPVSLGS
SSHATRLPNG LGGPNGFPKP TPEEGPPELN RQSPNSSSAA ASVASRRGTH GGLVTGLPNP
GGGGGPQLTV PPNLLPQTLL NGPASAAVLP PPPPHALGSR GPPTPAPPGA PGGPACLGGT
PGVSATSSSA SSSTSSSVAE VGVGAGGKRP GSVSSTDQER ELKEKQRNAE ALAELSESLR
NRAEEWANKP KMVRDTLLTL AGCTPYEVRF KKDHSLLGRV FAFDAVSKPG MDYELKLFIE
YPTGSGNVYS SASGVAKQMY QDCMKDFGRG LSSGFKYLEY EKKHGSGDWR LLGDLLPEAV
RFFKEGVPGA DMLPQPYLDA SCPMLPTALV SLSRAPSAPP GTGTLPPAAP SGRGAAASLR
KRKASPEPPD SAEGALKLGE EQQRQQWMAN QSEALKLTMS AGGFAAPGHA AGGPPPPPPP
LGPHSNRTTP PESAPQNGPS PMAALMSVAD TLGTAHSPKD GSSVHSTTAS ARRNSSSPVS
PASVPGQRRL ASRNGDLNLQ VAPPPPSAHP GMDQVHPQNI PDSPMANSGP LCCTICHERL
EDTHFVQCPS VPSHKFCFPC SRESIKAQGA SGEVYCPSGE KCPLVGSNVP WAFMQGEIAT
ILAGDVKVKK ERDP
