IF2B3_DANRE
ID IF2B3_DANRE Reviewed; 582 AA.
AC Q9PW80;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Insulin-like growth factor 2 mRNA-binding protein 3;
DE Short=IGF2 mRNA-binding protein 3;
DE Short=IMP-3;
DE AltName: Full=Decapentaplegic and Vg-related 1 RNA-binding protein;
DE AltName: Full=IGF-II mRNA-binding protein 3;
DE AltName: Full=VICKZ family member 3;
DE AltName: Full=Vg1 RNA-binding protein;
DE Short=Vg1-RBP;
GN Name=igf2bp3; Synonyms=dvr1rbp, vickz3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=14522877; DOI=10.1242/dev.00810;
RA Yaniv K., Fainsod A., Kalcheim C., Yisraeli J.K.;
RT "The RNA-binding protein Vg1 RBP is required for cell migration during
RT early neural development.";
RL Development 130:5649-5661(2003).
RN [4]
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
CC -!- FUNCTION: RNA-binding factor that may recruit target transcripts to
CC cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging'
CC into mRNPs allows mRNA transport and transient storage. It also
CC modulates the rate and location at which target transcripts encounter
CC the translational apparatus and shields them from endonuclease attacks
CC or microRNA-mediated degradation (By similarity). Preferentially binds
CC to N6-methyladenosine (m6A)-containing mRNAs and increases their
CC stability (By similarity). Involved in neuronal crest migration
CC (PubMed:14522877). {ECO:0000250|UniProtKB:O00425,
CC ECO:0000269|PubMed:14522877}.
CC -!- SUBUNIT: Homodimer and multimer. {ECO:0000250|UniProtKB:O00425}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10525193}. Nucleus
CC {ECO:0000250}. Cytoplasm, P-body {ECO:0000250|UniProtKB:O00425}.
CC Cytoplasm, Stress granule {ECO:0000250|UniProtKB:O00425}.
CC Note=Accumulates along the vegetal cortex as oogenesis progresses.
CC Colocalizes to extended processes in migrating neuronal crest cells.
CC -!- DEVELOPMENTAL STAGE: Expressed in oocytes from stages I to III.
CC Expressed in 8-cell embryo. Expressed in brain, eye, branchial arches
CC and neural tube at 24 hours post-fertilization (hpf). Detected
CC predominantly in the CNS, putative neural crest, the sensorial layer of
CC the epidermal ectoderm and their derivatives until the tailbud stage.
CC {ECO:0000269|PubMed:10525193, ECO:0000269|PubMed:14522877}.
CC -!- DOMAIN: All KH domains contribute binding to target mRNA. Domains KH3
CC and KH4 are the major RNA-binding modules, although KH1 and KH2 also
CC contribute. They are also required for RNA-dependent homo- and
CC heterooligomerization. The integrity of KH domains seems not to be
CC required for localization to stress granules.
CC {ECO:0000250|UniProtKB:O00425}.
CC -!- SIMILARITY: Belongs to the RRM IMP/VICKZ family. {ECO:0000305}.
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DR EMBL; AF161270; AAD45610.1; -; mRNA.
DR EMBL; BC045873; AAH45873.1; -; mRNA.
DR RefSeq; NP_571566.1; NM_131491.2.
DR AlphaFoldDB; Q9PW80; -.
DR SMR; Q9PW80; -.
DR STRING; 7955.ENSDARP00000010878; -.
DR iPTMnet; Q9PW80; -.
DR PaxDb; Q9PW80; -.
DR PRIDE; Q9PW80; -.
DR DNASU; 30967; -.
DR Ensembl; ENSDART00000010140; ENSDARP00000010878; ENSDARG00000010266.
DR GeneID; 30967; -.
DR KEGG; dre:30967; -.
DR CTD; 10643; -.
DR ZFIN; ZDB-GENE-000308-1; igf2bp3.
DR eggNOG; KOG2193; Eukaryota.
DR GeneTree; ENSGT00940000154957; -.
DR HOGENOM; CLU_020744_1_0_1; -.
DR InParanoid; Q9PW80; -.
DR PhylomeDB; Q9PW80; -.
DR TreeFam; TF320229; -.
DR PRO; PR:Q9PW80; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000010266; Expressed in somite and 30 other tissues.
DR ExpressionAtlas; Q9PW80; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:ZFIN.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; ISS:UniProtKB.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0051252; P:regulation of RNA metabolic process; IBA:GO_Central.
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; 1.
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; mRNA transport; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Translation regulation; Transport.
FT CHAIN 1..582
FT /note="Insulin-like growth factor 2 mRNA-binding protein 3"
FT /id="PRO_0000282541"
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 194..259
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 275..342
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 408..473
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 490..556
FT /note="KH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 164..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
SQ SEQUENCE 582 AA; 63352 MW; 9DAE63200681B306 CRC64;
MNKLYIGNVS EQASALDLES IFEQWKIPFS APFLVKSGYA FVDCPDEKVA MRAIDTLSGK
VELHGKVLEV EHSVPKRQRS CKLQIRNIPP HMQWEVLDGL LAQYGTVESC EQVNTDTETA
VVNVRYGAKD QAREAMDKLN GFLMENYALK VSYIPDETAA ADAPAVGGRR GFNPRGPPRQ
GSPSLGARPK LQSDVPLRLL VPTQFVGAII GKEGATIRNI TKQTHSKIDI HRKENAGAAE
KPITVHSTPE GCSSACRNIM EIMQKEAIDT KITEEIPLKI LAHNNFVGRL IGKEGRNLKK
IEQDTDTKIT ISPLQDLTLY NPERTITVKG TLDACAKAEE EIMKKVRESY ENDVAAMHLQ
SNLIPGLNLN ALGLFPGAAS GGISPSVVSG PPPGAQAGYQ SFGAQMESET VHLFIPALAV
GAIIGKQGQH IKQLSRFAGA SIKIAPADGI DAKQRMVIIS GPPEAQFKAQ GRIFGKLKEE
NFFGPKEEVK LEAHIKVPSF AAGRVIGKGG KTVNELQNLT SAEVVVPRDQ TPDENDQVVV
KITGHFYASQ LAQRKIQEII SQVRRQQQPK PSAAGPPVAR RK
