I2BP2_XENLA
ID I2BP2_XENLA Reviewed; 537 AA.
AC Q7ZXS3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Interferon regulatory factor 2-binding protein 2;
DE Short=IRF-2-binding protein 2;
DE Short=IRF-2BP2;
GN Name=irf2bp2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a transcriptional repressor. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IRF2BP family. {ECO:0000305}.
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DR EMBL; BC044275; AAH44275.1; -; mRNA.
DR RefSeq; NP_001080568.1; NM_001087099.1.
DR AlphaFoldDB; Q7ZXS3; -.
DR SMR; Q7ZXS3; -.
DR DNASU; 380260; -.
DR GeneID; 380260; -.
DR KEGG; xla:380260; -.
DR CTD; 380260; -.
DR OMA; KAEHMSP; -.
DR OrthoDB; 1156771at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 380260; Expressed in blastula and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Metal-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..537
FT /note="Interferon regulatory factor 2-binding protein 2"
FT /id="PRO_0000328737"
FT ZN_FING 456..503
FT /note="RING-type; degenerate"
FT REGION 60..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..503
FT /note="Cys-rich"
FT COMPBIAS 68..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 57244 MW; DFE8611B462AF728 CRC64;
MSSATVAASR RQSCYLCDLP RMPWAMIWDF TEPVCRGCVN YEGADRIEFV IETARHLKRA
HGFQEGRSPG PSPSSSSSSS SSSSVKPQLS AKEMAQIGHT MGGPEGVTRT SQQPPPPQCL
DRYSLERPPP PRLGSEYGLG RQVNGILLPN GFPKPEEPPE LNRQSPNPRR TSTVPQSLGA
LMNGTPMGSA RATIGLSGAS LVAAAAATTS ADLSGKRPGS VSSSEHDGKE KHRADSYSEL
GENHKSRAEE WISKPKTVRD TLMAMQHSHS PFDSKFKKDT GPGRVLSFEA NNPVSKSGAR
GGRKRKTSPE PEGEGGSVKI NGEGQPWLPA TESLKISTMA SPSFISPPST VSPHSNRTTP
PEAAQNGQSP MAALILVADN AGGNHASKDA NQVHSTTRRN SSSPPSPSSM NQRRMAPRDV
PSQLPSGGTS SHAGMEQGLP QSIPDSSIPN SIPLCCTLCH ERLEDTHFVQ CPSVPSHKFC
FPCSRQSIKQ QGSSGEVYCP SGEKCPLVGS NVPWAFMQGE IATILAGDVK VKKERDS