IF23A_XENLA
ID IF23A_XENLA Reviewed; 594 AA.
AC O73932; B7ZRK2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Insulin-like growth factor 2 mRNA-binding protein 3-A;
DE Short=IGF2 mRNA-binding protein 3-A;
DE Short=IMP-3-A;
DE AltName: Full=69 kDa RNA-binding protein A;
DE AltName: Full=IGF-II mRNA-binding protein 3-A;
DE AltName: Full=KH domain-containing transcription factor B3-A;
DE AltName: Full=RNA-binding protein Vera-A;
DE AltName: Full=Trans-acting factor B3-A;
DE AltName: Full=VICKZ family member 3-A;
DE AltName: Full=VLE-binding protein A;
DE AltName: Full=Vg1 RNA-binding protein A;
DE Short=Vg1 RBP-A;
DE AltName: Full=Vg1 localization element binding protein A;
DE AltName: Full=VgLE-binding and ER association protein A;
GN Name=igf2bp3-a; Synonyms=vera-a, vickz3-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 [MRNA], PROTEIN SEQUENCE OF 151-164; 210-223; 283-289
RP AND 487-496, FUNCTION, AND RNA-BINDING.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 282-290; 442-453; 486-500
RP AND 506-518, FUNCTION, ASSOCIATION WITH MICROTUBULES, 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 [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 151-181; 210-223; 291-300 AND 320-335.
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 [5]
RP RNA-BINDING.
RX PubMed=1465415; DOI=10.1073/pnas.89.24.11895;
RA Schwartz S.P., Aisenthal L., Elisha Z., Oberman F., Yisraeli J.K.;
RT "A 69-kDa RNA-binding protein from Xenopus oocytes recognizes a common
RT motif in two vegetally localized maternal mRNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11895-11899(1992).
RN [6]
RP ASSOCIATION WITH MICROTUBULES.
RX PubMed=7588639; DOI=10.1002/j.1460-2075.1995.tb00193.x;
RA Elisha Z., Havin L., Ringel I., Yisraeli J.K.;
RT "Vg1 RNA binding protein mediates the association of Vg1 RNA with
RT microtubules in Xenopus oocytes.";
RL EMBO J. 14:5109-5114(1995).
RN [7]
RP FUNCTION, INTERACTION WITH TRAPA, SUBCELLULAR LOCATION, AND RNA-BINDING.
RX PubMed=9148809; DOI=10.1126/science.276.5315.1128;
RA Deshler J.O., Highett M.I., Schnapp B.J.;
RT "Localization of Xenopus Vg1 mRNA by Vera protein and the endoplasmic
RT reticulum.";
RL Science 276:1128-1131(1997).
RN [8]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=10525193; DOI=10.1016/s0925-4773(99)00162-8;
RA Zhang Q., Yaniv K., Oberman F., Wolke U., Git A., Fromer M., Taylor W.L.,
RA Meyer D., Standart N., Raz E., Yisraeli J.K.;
RT "Vg1 RBP intracellular distribution and evolutionarily conserved expression
RT at multiple stages during development.";
RL Mech. Dev. 88:101-106(1999).
RN [9]
RP SUBUNIT, AND RNA-BINDING.
RX PubMed=12403469; DOI=10.1017/s135583820202705x;
RA Git A., Standart N.;
RT "The KH domains of Xenopus Vg1RBP mediate RNA binding and self-
RT association.";
RL RNA 8:1319-1333(2002).
RN [10]
RP FUNCTION, IDENTIFICATION IN A MRNP COMPLEX WITH DAZAP1; STAU AND VGRBP60,
RP INTERACTION WITH VGRBP60, SUBCELLULAR LOCATION, AND RNA-BINDING.
RX PubMed=15096527; DOI=10.1083/jcb.200309145;
RA Kress T.L., Yoon Y.J., Mowry K.L.;
RT "Nuclear RNP complex assembly initiates cytoplasmic RNA localization.";
RL J. Cell Biol. 165:203-211(2004).
RN [11]
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. Binds specifically to the
CC vegetal localization elements (VLE or VgLE) in the 3'-UTR of Vg1 and
CC VegT mRNAs. Binds to the Vg1 and VegT mRNAs in both the nucleus and the
CC cytoplasm. May regulate mRNA translation (By similarity). Acts as a
CC transcription regulator (By similarity). Binds to the 5'-[TA]GGTTACT-3'
CC motif within element 3 of the TFIIIA gene promoter (By similarity).
CC {ECO:0000250|UniProtKB:O00425, ECO:0000250|UniProtKB:O57526,
CC ECO:0000269|PubMed:15096527, ECO:0000269|PubMed:9148809,
CC ECO:0000269|PubMed:9560341, ECO:0000269|PubMed:9620847}.
CC -!- SUBUNIT: Homodimer and multimer (PubMed:12403469). Associates with
CC microtubules (PubMed:9620847, PubMed:7588639). Interaction with a
CC translocation machinery protein TRAPA of the endoplasmic reticulum
CC (PubMed:9148809). Component of a mRNP complex, at least composed of
CC DAZAP1, IGF2BP3, STAU and VgRBP60 (PubMed:15096527). The mRNP complex
CC with DAZAP1, IGF2BP3, STAU and VgRBP60 is only found in the cytoplasm
CC (PubMed:15096527). Interacts with a hnRNP 1 related RNA transport
CC protein VgRBP60 both in the nucleus (in a RNA-independent manner) and
CC the cytoplasm (in a RNA-dependent manner) (PubMed:15096527). Found in a
CC B3 activator complex (By similarity). {ECO:0000250|UniProtKB:O57526,
CC ECO:0000269|PubMed:12403469, ECO:0000269|PubMed:15096527,
CC ECO:0000269|PubMed:7588639, ECO:0000269|PubMed:9148809,
CC ECO:0000269|PubMed:9620847}.
CC -!- INTERACTION:
CC O73932; Q98SP8: epabp-a; NbExp=2; IntAct=EBI-619004, EBI-7191347;
CC O73932; P45441: ybx2-b; NbExp=2; IntAct=EBI-619004, EBI-8486848;
CC O73932; P17506; NbExp=4; IntAct=EBI-619004, EBI-8486828;
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.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the oocyte development from
CC stages I to VI (at protein level). Levels begin to increase in the
CC developing nervous system at stage 12 (at protein level). At the neural
CC tube stage, expression is detected throughout the developing neural
CC epithelium and in the cells migrating out of the mesencephalon and
CC rhombencephalon, eye, neural tube, otic vesicle, pronephros, branchial
CC arches and blood islands (at protein level). Detected in low levels
CC throughout early embryogenesis. {ECO:0000269|PubMed:10525193}.
CC -!- DOMAIN: The third and fourth KH domains are involved in RNA binding and
CC self-association. Stable self-association requires RNA.
CC -!- SIMILARITY: Belongs to the RRM IMP/VICKZ family. {ECO:0000305}.
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DR EMBL; AF055923; AAC41285.1; -; mRNA.
DR EMBL; AF064634; AAC18598.1; -; mRNA.
DR EMBL; BC170196; AAI70196.1; -; mRNA.
DR EMBL; BC170224; AAI70224.1; -; mRNA.
DR EMBL; BC170477; AAI70477.1; -; mRNA.
DR EMBL; BC170479; AAI70479.1; -; mRNA.
DR RefSeq; NP_001081752.1; NM_001088283.1.
DR AlphaFoldDB; O73932; -.
DR SMR; O73932; -.
DR BioGRID; 98895; 3.
DR IntAct; O73932; 11.
DR MINT; O73932; -.
DR GeneID; 394293; -.
DR KEGG; xla:394293; -.
DR CTD; 394293; -.
DR Xenbase; XB-GENE-864935; igf2bp3.L.
DR OMA; CPDEGWA; -.
DR OrthoDB; 394765at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 394293; Expressed in gastrula and 12 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IPI:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA: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..594
FT /note="Insulin-like growth factor 2 mRNA-binding protein 3-
FT A"
FT /id="PRO_0000282542"
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 205..270
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 286..353
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 418..483
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 500..566
FT /note="KH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 161..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 160
FT /note="T -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="L -> M (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="G -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="L -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="L -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 594 AA; 65643 MW; 54CEA7BFF0856DD6 CRC64;
MNKLYIGNLS ENVSPTDLES LFKESKIPFT GQFLVKSGYA FVDCPDETWA MKAIDTLSGK
VELHGKVIEV EHSVPKRQRS RKLQIRNIPP HLQWEVLDSL LAQYGTVENC EQVNTESETA
VVNVTYANKE HARQGLEKLN GYQLENYSLK VTYIPDEMAT PQAPSQQLQQ QPQQQHPQGR
RGFGQRGPAR QGSPGAAARP KPQTEVPLRM LVPTQFVGAI IGKEGATIRN ITKQTQSKID
IHRKENAGAA EKPITIHSTP EGCSAACKII MEIMQKEAQD TKFTEEIPLK ILAHNNFVGR
LIGKEGRNLK KIEQDTDTKI TISPLQDLTL YNPERTITVK GSIEPCAKAE EEIMKKIRES
YENDIAAMNL QAHLIPGLNL NALGLFPSSS SGMPPPSVGV PSPTSSTSYP PFGQQPESET
VHLFIPALAV GAIIGKQGQH IKQLSRFAGA SIKIAPAEGP DAKLRMVIIT GPPEAQFKAQ
GRIYGKLKEE NFFGPKEEVK LETHIKVPSY AAGRVIGKGG KTVNELQNLT SAEVVVPRDQ
TPDENDEVVV KITGHFYASQ LAQRKIQEIL AQVRRQQQQQ QKTVQSGQPQ PRRK
