ID   IF2B1_DANRE             Reviewed;         598 AA.
AC   Q08CK7;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Insulin-like growth factor 2 mRNA-binding protein 1;
DE            Short=IGF2 mRNA-binding protein 1;
DE            Short=IMP-1;
DE   AltName: Full=IGF-II mRNA-binding protein 1;
DE   AltName: Full=VICKZ family member 1;
GN   Name=igf2bp1; Synonyms=vickz1; ORFNames=zgc:152963;
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 [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185; THR-573; THR-583 AND
RP   SER-587, AND IDENTIFICATION BY 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 recruits 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       (By similarity). Plays a direct role in the transport and translation
CC       of transcripts required for axonal regeneration in adult sensory
CC       neurons (By similarity). Regulates localized beta-actin/ACTB mRNA
CC       translation in polarized cells, a crucial process for cell migration
CC       and neurite outgrowth. Promotes the directed movement of cells by fine-
CC       tuning intracellular signaling networks and enhances the velocity of
CC       cell migration (By similarity). {ECO:0000250|UniProtKB:Q9NZI8}.
CC   -!- SUBUNIT: Component of the CRD-mediated complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, P-body
CC       {ECO:0000250|UniProtKB:Q9NZI8}. Cytoplasm, Stress granule
CC       {ECO:0000250|UniProtKB:Q9NZI8}. Cell projection, growth cone
CC       {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell
CC       projection, lamellipodium {ECO:0000250}.
CC   -!- DOMAIN: Domains KH3 and KH4 are the major RNA-binding modules, although
CC       KH1 and KH2 may also contribute to transcript binding. KH1 and KH2, and
CC       possibly KH3 and KH4, promote the formation of higher ordered protein-
CC       RNA complexes, which may be essential for IGF2BP1 cytoplasmic
CC       retention. KH domains are required for localization to stress granules.
CC       KH3 and KH4 mediate association with the cytoskeleton. Two nuclear
CC       export signals (NES) have been identified in KH2 and KH4 domains,
CC       respectively. Only KH2 NES is XPO1-dependent. Both NES may be
CC       redundant. {ECO:0000250|UniProtKB:Q9NZI8}.
CC   -!- SIMILARITY: Belongs to the RRM IMP/VICKZ family. {ECO:0000305}.
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DR   EMBL; BC124196; AAI24197.1; -; mRNA.
DR   AlphaFoldDB; Q08CK7; -.
DR   SMR; Q08CK7; -.
DR   STRING; 7955.ENSDARP00000082159; -.
DR   iPTMnet; Q08CK7; -.
DR   PaxDb; 7955-ENSDARP00000082159; -.
DR   AGR; ZFIN:ZDB-GENE-060929-1258; -.
DR   ZFIN; ZDB-GENE-060929-1258; igf2bp1.
DR   eggNOG; KOG2193; Eukaryota.
DR   InParanoid; Q08CK7; -.
DR   PhylomeDB; Q08CK7; -.
DR   PRO; PR:Q08CK7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISS:UniProtKB.
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:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR   GO; GO:1990247; F:N6-methyladenosine-containing RNA reader activity; 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:0003407; P:neural retina development; IMP:ZFIN.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:2000345; P:regulation of hepatocyte proliferation; IMP:ZFIN.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   CDD; cd22490; KH-I_IGF2BP1_rpt1; 1.
DR   CDD; cd22493; KH-I_IGF2BP1_rpt2; 1.
DR   CDD; cd22496; KH-I_IGF2BP1_rpt3; 1.
DR   CDD; cd22499; KH-I_IGF2BP1_rpt4; 1.
DR   CDD; cd12625; RRM1_IGF2BP1; 1.
DR   CDD; cd12630; RRM2_IGF2BP3; 1.
DR   Gene3D; 3.30.310.210; -; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 2.
DR   InterPro; IPR034837; IGF2BP1_RRM1.
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   PANTHER; PTHR10288:SF92; INSULIN-LIKE GROWTH FACTOR 2 MRNA-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR10288; KH DOMAIN CONTAINING RNA BINDING PROTEIN; 1.
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; Eukaryotic type KH-domain (KH-domain type I); 4.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 4.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   Cell projection; Cytoplasm; mRNA transport; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; RNA-binding; Translation regulation; Transport.
FT   CHAIN           1..598
FT                   /note="Insulin-like growth factor 2 mRNA-binding protein 1"
FT                   /id="PRO_0000282537"
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          198..263
FT                   /note="KH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          279..346
FT                   /note="KH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          407..472
FT                   /note="KH 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          489..555
FT                   /note="KH 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   REGION          155..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
FT   MOD_RES         399
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         573
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
FT   MOD_RES         583
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
FT   MOD_RES         587
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
SQ   SEQUENCE   598 AA;  65530 MW;  CED67F6C29CA2AAD CRC64;
     MNKLYIGNLN EKVTAEDLVK TFEDYKIPYS GQFLMKTGYA SVDCPDDQWA MKAIETFSGK
     VELHGKRIEV EHSVPKKQRT RKLQIRNIPP HLQWEVLDGL LAQYGTVENC EQVNTDSETA
     VVNVTYGTRE QARQAIQKLN GYQFDNNALR VSYIPDENSE VDSQRGPDNG RRPGYGPRGT
     SRQMSPGSGI PSKHQHADIP LRLLVPTQYV GAIIGKEGAT IRNITKQTQS KIDVHRKENA
     GAAEKPISIH STPEGCSAAC RMILEIMNQE AKDTKTADEV PLKVLAHNNF VGRLIGKEGR
     NLKKVEQDTD TKITISPLQD LTLYNPERTI TVKGSIEACC LAEQEIMKKV REAYDNDIAA
     MNQQTHLIPG LNLGAIGLFP PSSAMPPPAL GNSVPGPPYG PMGASEQETV HVYIPAQAVG
     ALIGKKGQHI KQLSRFAGAS IKIAPAEAPD SKMRMVIVTG PPEAQFKAQG RIYGKLKEEN
     FFGPKEEVKL ETHIKVAAAA AGRVIGKGGK TVNELQNLTA AEVVVPREQT PDEHDQVIVK
     IIGHFYASQL AQRKIRDILT QVKQQQKGGG MGTPQGPHPQ GMTELGSPQG LAQEPRRK
//