IF2B1_DANRE
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 03-AUG-2022, entry version 86.
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; Q08CK7; -.
DR PRIDE; Q08CK7; -.
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 Proteomes; UP000814640; Unplaced.
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: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:0003407; P:neural retina development; IMP:ZFIN.
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; cd12625; RRM1_IGF2BP1; 1.
DR CDD; cd12628; RRM2_IGF2BP1; 1.
DR Gene3D; 3.30.1370.10; -; 2.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034837; IGF2BP1_RRM1.
DR InterPro; IPR034842; IGF2BP1_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 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
