I2BLA_XENLA
ID I2BLA_XENLA Reviewed; 690 AA.
AC Q66IY8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Interferon regulatory factor 2-binding protein-like A;
DE AltName: Full=Enhanced at puberty protein 1 homolog A;
GN Name=irf2bpl-a; Synonyms=eap1-a;
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=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IRF2BP family. {ECO:0000305}.
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DR EMBL; BC081137; AAH81137.1; -; mRNA.
DR RefSeq; NP_001087721.1; NM_001094252.1.
DR AlphaFoldDB; Q66IY8; -.
DR SMR; Q66IY8; -.
DR DNASU; 447545; -.
DR GeneID; 447545; -.
DR KEGG; xla:447545; -.
DR CTD; 447545; -.
DR OMA; WASKPKM; -.
DR OrthoDB; 1156771at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 447545; 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 Coiled coil; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..690
FT /note="Interferon regulatory factor 2-binding protein-like
FT A"
FT /id="PRO_0000328732"
FT ZN_FING 609..656
FT /note="RING-type; degenerate"
FT REGION 59..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 231..263
FT /evidence="ECO:0000255"
FT COMPBIAS 63..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..505
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 690 AA; 72642 MW; 4FAAD1E7A9FC17AC CRC64;
MSAAQVSSSR RQSCYLCDLP RMPWAMIWDF TEPVCRGCVN YEGADRIEFV IDTARQLKRS
HSFQDGRSPG PQGPGSGASN KQHPAVQAAL TAKDTAQLNH LDGATKAAAA SGLERYGLTT
DRGRFEYTLA ARLPNGLNGF PKPGEDGPPE LNRQSPNSRG RTGHGLIPQL VPGQLSVPPN
LIPQTLLNGP PPGTPGGAPH VLGRGPASSS GLGVPPTASS SGDPKRPGSV SSTDQERELK
EKQRNSEALS ELTESLRNRA EEWAGKPKAV RDTLLTLTAS TPFDVRFKKD HNLLGRVFAF
DAASKPGLLD YELKLFVEYP SGSLNVFSSA SGVAKQMYQD CMKDFGRGLS SGFKYLEYEK
KHGSGDWRLL GDLLPESVRF FKEMVGADML PQPYLDPGCP MLPSALVNLP RALAAAAAAS
SSAGSSGQAR SGVRKRKASP EPDSADGQMW LTGQPDGIKQ LSMAPAGGTP SSSSAAYGVP
SAPPPPLGPG HPQRTTPPES APPNGPSPMA ALQSVTDTLG TAHSPKDGQA GGLPPVHSTT
SSARRNSSSP VSPASVTGQR RLNSRNGAGS AELSLQVAPT GGAPHPGMDQ VHPQNIPDSP
MANSGPLCCT ICHERLEDTH FVQCPSVPSH KFCFPCSRDS IKAQGATGEV YCPSGEKCPL
VGSNVPWAFM QGEIATILAG DVKVKKERDP