IF23B_XENLA
ID IF23B_XENLA Reviewed; 593 AA.
AC O57526;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Insulin-like growth factor 2 mRNA-binding protein 3-B;
DE Short=IGF2 mRNA-binding protein 3-B;
DE Short=IMP-3-B;
DE AltName: Full=69 kDa RNA-binding protein B;
DE AltName: Full=B3.65 protein B;
DE AltName: Full=IGF-II mRNA-binding protein 3-B;
DE AltName: Full=KH domain-containing transcription factor B3-B;
DE AltName: Full=RNA-binding protein Vera-B;
DE AltName: Full=Trans-acting factor B3-B;
DE AltName: Full=VICKZ family member 3-B;
DE AltName: Full=VLE-binding protein B;
DE AltName: Full=Vg1 RNA-binding protein B;
DE Short=Vg1 RBP-B;
DE AltName: Full=Vg1 localization element binding protein B;
DE AltName: Full=VgLE-binding and ER association protein B;
GN Name=igf2bp3-b; Synonyms=vickz3-b;
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 [MRNA], AND DNA-BINDING.
RC TISSUE=Oocyte;
RX PubMed=1577195; DOI=10.1016/0012-1606(92)90235-9;
RA Pfaff S.L., Taylor W.L.;
RT "Characterization of a Xenopus oocyte factor that binds to a
RT developmentally regulated cis-element in the TFIIIA gene.";
RL Dev. Biol. 151:306-316(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 281-289; 441-452; 485-499
RP AND 505-517, AND RNA-BINDING.
RC TISSUE=Oocyte;
RX PubMed=9620847; DOI=10.1101/gad.12.11.1593;
RA Havin L., Git A., Elisha Z., Oberman F., Yaniv K., Schwartz S.P.,
RA Standart N., Yisraeli J.K.;
RT "RNA-binding protein conserved in both microtubule- and microfilament-based
RT RNA localization.";
RL Genes Dev. 12:1593-1598(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 151-180; 209-222; 290-299
RP AND 319-334, IDENTIFICATION IN A B3 ACTIVATOR COMPLEX, TISSUE SPECIFICITY,
RP AND DNA-BINDING.
RC TISSUE=Oocyte;
RX PubMed=12957389; DOI=10.1016/s0378-1119(03)00678-4;
RA Griffin D., Penberthy W.T., Lum H., Stein R.W., Taylor W.L.;
RT "Isolation of the B3 transcription factor of the Xenopus TFIIIA gene.";
RL Gene 313:179-188(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 151-164; 209-222; 282-288 AND 486-495.
RC TISSUE=Oocyte;
RX PubMed=9560341; DOI=10.1016/s0960-9822(98)70200-3;
RA Deshler J.O., Highett M.I., Abramson T., Schnapp B.J.;
RT "A highly conserved RNA-binding protein for cytoplasmic mRNA localization
RT in vertebrates.";
RL Curr. Biol. 8:489-496(1998).
RN [6]
RP REVIEW.
RX PubMed=15601260; DOI=10.1042/bc20040151;
RA Yisraeli J.K.;
RT "VICKZ proteins: a multi-talented family of regulatory RNA-binding
RT proteins.";
RL Biol. Cell 97:87-96(2005).
CC -!- FUNCTION: RNA-binding protein that acts as a regulator of mRNA
CC transport and localization. Binds to the RNA sequence motif 5'-UUCAC-
CC 3'. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs
CC and increases their stability (By similarity). Mediates the specific
CC association of Vg1 RNA to microtubules. May regulate mRNA translation
CC (By similarity). Binds specifically to the vegetal localization
CC elements (VLE or VgLE) in the 3'-UTR of Vg1 and VegT mRNAs. Binds to
CC the Vg1 and VegT mRNAs in both the nucleus and the cytoplasm. May
CC regulate mRNA translation (By similarity). Acts as a transcription
CC regulator (PubMed:1577195, PubMed:12957389). Binds to the 5'-
CC [TA]GGTTACT-3' motif within element 3 of the TFIIIA gene promoter
CC (PubMed:1577195, PubMed:12957389). {ECO:0000250|UniProtKB:O00425,
CC ECO:0000250|UniProtKB:O73932, ECO:0000269|PubMed:12957389,
CC ECO:0000269|PubMed:1577195}.
CC -!- SUBUNIT: Homodimer and multimer (By similarity). Associates with
CC microtubules (By similarity). Interaction with a translocation
CC machinery protein TRAPA of the endoplasmic reticulum (By similarity).
CC Component of a mRNP complex, at least composed of DAZAP1, IGF2BP3, STAU
CC and VgRBP60 (By similarity). The mRNP complex with DAZAP1, IGF2BP3,
CC STAU and VgRBP60 is only found in the cytoplasm (By similarity).
CC Interacts with a hnRNP 1 related RNA transport protein VgRBP60 both in
CC the nucleus (in an RNA-independent manner) and the cytoplasm (in an
CC RNA-dependent manner) (By similarity). Found in a B3 activator complex.
CC {ECO:0000250|UniProtKB:O73932, ECO:0000269|PubMed:12957389}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Endoplasmic reticulum.
CC Note=Accumulates along the vegetal cortex in oocytes as oogenesis
CC progresses ('late pathway' for RNA localization). Colocalizes with Vg1
CC RNA along the vegetal cortex (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes, kidney and pancreas (at
CC protein level). Expressed in oocytes, kidney and pancreas.
CC {ECO:0000269|PubMed:12957389}.
CC -!- DOMAIN: The third and fourth KH domains are involved in RNA binding and
CC self-association. Stable self-association requires RNA (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM IMP/VICKZ family. {ECO:0000305}.
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DR EMBL; AF042353; AAB97457.1; -; mRNA.
DR EMBL; AF064633; AAC18597.1; -; mRNA.
DR EMBL; BC057700; AAH57700.1; -; mRNA.
DR RefSeq; NP_001079932.1; NM_001086463.1.
DR AlphaFoldDB; O57526; -.
DR SMR; O57526; -.
DR BioGRID; 97866; 1.
DR DNASU; 379623; -.
DR GeneID; 379623; -.
DR KEGG; xla:379623; -.
DR CTD; 379623; -.
DR Xenbase; XB-GENE-6255198; igf2bp3.S.
DR OrthoDB; 394765at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 379623; Expressed in embryo and 1 other tissue.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd12630; RRM2_IGF2BP3; 1.
DR Gene3D; 3.30.1370.10; -; 2.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034844; IGF2BP3_RRM2.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00013; KH_1; 4.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00322; KH; 4.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54791; SSF54791; 4.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50084; KH_TYPE_1; 4.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Direct protein sequencing; DNA-binding;
KW Endoplasmic reticulum; mRNA transport; Nucleus; Reference proteome; Repeat;
KW RNA-binding; Transcription; Transcription regulation;
KW Translation regulation; Transport.
FT CHAIN 1..593
FT /note="Insulin-like growth factor 2 mRNA-binding protein 3-
FT B"
FT /id="PRO_0000282543"
FT DOMAIN 2..75
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 81..156
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 204..269
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 285..352
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 417..482
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 499..565
FT /note="KH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 159..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 160
FT /note="T -> A (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="S -> A (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="L -> M (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="G -> T (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="L -> V (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="L -> I (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 593 AA; 65386 MW; 5A5AB4B4A1D55DF7 CRC64;
MNKLYIGNLS ENVSPPDLES LFKESKIPFT GQFLVKSGYA FVDCPDETWA MKAIDTLSGK
VELHGKVIEV EHSVPKRQRS RKLQIRNIPP HLQWEVLDSL LAQYGTVENC EQVNTDSETA
VVNVTYANKE HARQGLEKLN GYQLENYSLK VTYIPDEMAT PQSPSQQLQQ PQQQHPQGRR
GFGQRGPARQ GSPGAAARPK PQSEVPLRML VPTQFVGAII GKEGATIRNI TKQTQSKIDI
HRKENAGAAE KPITIHSTPE GCSAACKIIM EIMQKEAQDT KFTEEIPLKI LAHNNFVGRL
IGKEGRNLKK IEQDTDTKIT ISPLQDLTLY NPERTITVKG SIETCAKAEE EVMKKIRESY
ENDIAAMNLQ AHLIPGLNLN ALGLFPPSSS GMPPPSAGVS SPTTSASYPP FGQQPESETV
HLFIPALAVG AIIGKQGQHI KQLSRFAGAS IKIAPAEGPD AKLRMVIITG PPEAQFKAQG
RIYGKLKEEN FFGPKEEVKL EAHIKVPSYA AGRVIGKGGK TVNELQNLTS AEVVVPRDQT
PDENDQVVVK ITGHFYASQL AQRKIQEILA QVRRQQQQQQ KTAQSGQPQP RRK
