IF2B3_CHICK
ID IF2B3_CHICK Reviewed; 584 AA.
AC Q5ZLP8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=IGF-II mRNA-binding protein 3;
DE AltName: Full=VICKZ family member 3;
GN Name=IGF2BP3; Synonyms=VICKZ3; ORFNames=RCJMB04_5e15;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
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 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. Preferentially binds to N6-
CC methyladenosine (m6A)-containing mRNAs and increases their stability.
CC {ECO:0000250|UniProtKB:O00425}.
CC -!- SUBUNIT: Homodimer and multimer. {ECO:0000250|UniProtKB:O00425}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cytoplasm, P-body {ECO:0000250|UniProtKB:O00425}. Cytoplasm, Stress
CC granule {ECO:0000250|UniProtKB:O00425}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ719686; CAG31345.1; -; mRNA.
DR RefSeq; NP_001006359.1; NM_001006359.1.
DR RefSeq; XP_015136930.1; XM_015281444.1.
DR AlphaFoldDB; Q5ZLP8; -.
DR SMR; Q5ZLP8; -.
DR BioGRID; 681555; 1.
DR STRING; 9031.ENSGALP00000043342; -.
DR PaxDb; Q5ZLP8; -.
DR Ensembl; ENSGALT00000017840; ENSGALP00000017819; ENSGALG00000010961.
DR Ensembl; ENSGALT00000045214; ENSGALP00000043342; ENSGALG00000010961.
DR GeneID; 420617; -.
DR KEGG; gga:420617; -.
DR CTD; 10643; -.
DR VEuPathDB; HostDB:geneid_420617; -.
DR eggNOG; KOG2193; Eukaryota.
DR GeneTree; ENSGT00940000154957; -.
DR HOGENOM; CLU_020744_1_0_1; -.
DR InParanoid; Q5ZLP8; -.
DR OrthoDB; 394765at2759; -.
DR PhylomeDB; Q5ZLP8; -.
DR TreeFam; TF320229; -.
DR PRO; PR:Q5ZLP8; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000010961; Expressed in granulocyte and 12 other tissues.
DR ExpressionAtlas; Q5ZLP8; 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; ISS:UniProtKB.
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; 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 2: Evidence at transcript level;
KW Cytoplasm; mRNA transport; Nucleus; Reference proteome; Repeat;
KW RNA-binding; Translation regulation; Transport.
FT CHAIN 1..584
FT /note="Insulin-like growth factor 2 mRNA-binding protein 3"
FT /id="PRO_0000282540"
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 196..261
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 277..344
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 409..474
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 491..557
FT /note="KH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 160..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 64373 MW; 54CBB457D0596123 CRC64;
MNKLYIGNLG ENVSPLDLES LFKDSKIPFS GQFLVKTGYA FVDCPDESWA MKAIEALSGK
VELHGKLIEV EHSVPKRQRS RKLQIRNIPP HLQWEVLDSL LAQYGTVENC EQVNTDTETA
VVNVTYGNKD QARQAIEKLN GFQLENYSLK VAYIPDEMAA QQPPQQHPQG RRGFGQRGPP
RQGSPSATTR QKPQSDVPLR MLVPTQFVGA IIGKEGATIR NITKQTQSKI DIHRKENAGA
AEKPITIHST PEGCSTACKI IMEIMQKEAQ DTKFTEEIPL KILAHNNFVG RLIGKEGRNL
KKIEQDTDTK ITISPLQDLT LYNPERTITV KGSIETCAKA EEEIMKKIRE SYENDIAAMN
LQAHLIPGLN LNALGLFPPS SSGIPPPAVS VASAAAAASY PPFGQQPESE TVHLFIPALA
VGAIIGKQGQ HIKQLSRFAG ASIKIAPAEG PDAKLRMVII TGPPEAQFKA QGRIYGKLKE
ENFFGPKEEV KLEAHIKVPS YAAGRVIGKG GKTVNELQNL TSAEVVVPRD QTPDENDQVV
VKITGHFYAC QLAQRKIQEI LAQVRRQQQQ QKTLQSGQPQ PRRK
