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Insulin-like growth factor 2 mRNA-binding protein 1 (IGF2 mRNA-binding protein 1) (IMP-1) (IGF-II mRNA-binding protein 1) (VICKZ family member 1) (Zip-code binding polypeptide) (Zipcode-binding protein 1) (ZBP-1)

 IF2B1_CHICK             Reviewed;         576 AA.
O42254;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
23-MAY-2018, entry version 120.
RecName: Full=Insulin-like growth factor 2 mRNA-binding protein 1;
Short=IGF2 mRNA-binding protein 1;
Short=IMP-1;
AltName: Full=IGF-II mRNA-binding protein 1;
AltName: Full=VICKZ family member 1;
AltName: Full=Zip-code binding polypeptide;
AltName: Full=Zipcode-binding protein 1;
Short=ZBP-1;
Name=IGF2BP1; Synonyms=VICKZ1, ZBP1;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, RNA-BINDING, AND TISSUE
SPECIFICITY.
TISSUE=Embryonic fibroblast;
PubMed=9121465; DOI=10.1128/MCB.17.4.2158;
Ross A.F., Oleynikov Y., Kislauskis E.H., Taneja K.L., Singer R.H.;
"Characterization of a beta-actin mRNA zipcode-binding protein.";
Mol. Cell. Biol. 17:2158-2165(1997).
[2]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11502257; DOI=10.1016/S0896-6273(01)00357-9;
Zhang H.L., Eom T., Oleynikov Y., Shenoy S.M., Liebelt D.A.,
Dictenberg J.B., Singer R.H., Bassell G.J.;
"Neurotrophin-induced transport of a beta-actin mRNP complex increases
beta-actin levels and stimulates growth cone motility.";
Neuron 31:261-275(2001).
[3]
FUNCTION, RNA-BINDING, ASSOCIATION WITH CYTOSKELETON, AND SUBCELLULAR
LOCATION.
PubMed=12573215; DOI=10.1016/S0960-9822(03)00044-7;
Oleynikov Y., Singer R.H.;
"Real-time visualization of ZBP1 association with beta-actin mRNA
during transcription and localization.";
Curr. Biol. 13:199-207(2003).
[4]
FUNCTION, RNA-BINDING, ASSOCIATION WITH CYTOSKELETON, SUBCELLULAR
LOCATION, AND DOMAIN.
PubMed=12507992; DOI=10.1083/jcb.200206003;
Farina K.L., Huttelmaier S., Musunuru K., Darnell R., Singer R.H.;
"Two ZBP1 KH domains facilitate beta-actin mRNA localization, granule
formation, and cytoskeletal attachment.";
J. Cell Biol. 160:77-87(2003).
[5]
SUBCELLULAR LOCATION.
PubMed=17101699; DOI=10.1083/jcb.200608071;
Stoehr N., Lederer M., Reinke C., Meyer S., Hatzfeld M., Singer R.H.,
Huettelmaier S.;
"ZBP1 regulates mRNA stability during cellular stress.";
J. Cell Biol. 175:527-534(2006).
[6]
FUNCTION, PHOSPHORYLATION AT TYR-396, MUTAGENESIS OF TYR-396, AND
SUBCELLULAR LOCATION.
PubMed=16306994; DOI=10.1038/nature04115;
Huttelmaier S., Zenklusen D., Lederer M., Dictenberg J., Lorenz M.,
Meng X., Bassell G.J., Condeelis J., Singer R.H.;
"Spatial regulation of beta-actin translation by Src-dependent
phosphorylation of ZBP1.";
Nature 438:512-515(2005).
[7]
FUNCTION IN CELL MIGRATION.
PubMed=22279049; DOI=10.1101/gad.177642.111;
Stohr N., Kohn M., Lederer M., Glass M., Reinke C., Singer R.H.,
Huttelmaier S.;
"IGF2BP1 promotes cell migration by regulating MK5 and PTEN
signaling.";
Genes Dev. 26:176-189(2012).
[8]
FUNCTION, RNA-BINDING, OLIGOMERIZATION, INTERACTION WITH ELAVL1; DHX9
AND HNRNPU, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF LYS-213;
LYS-294; 423-LYS-LYS-424 AND 505-LYS-GLY-506.
PubMed=23640942; DOI=10.1515/hsz-2013-0111;
Wachter K., Kohn M., Stohr N., Huttelmaier S.;
"Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-
binding proteins) is modulated by distinct RNA-binding domains.";
Biol. Chem. 394:1077-1090(2013).
[9]
REVIEW.
PubMed=23069990; DOI=10.1007/s00018-012-1186-z;
Bell J.L., Wachter K., Muhleck B., Pazaitis N., Kohn M., Lederer M.,
Huttelmaier S.;
"Insulin-like growth factor 2 mRNA-binding proteins (IGF2BPs): post-
transcriptional drivers of cancer progression?";
Cell. Mol. Life Sci. 70:2657-2675(2013).
-!- FUNCTION: RNA-binding factor that recruits target transcripts to
cytoplasmic protein-RNA complexes (mRNPs). This transcript
'caging' into mRNPs allows mRNA transport and transient storage.
It also modulates the rate and location at which target
transcripts encounter the translational apparatus and shields them
from endonuclease attacks or microRNA-mediated degradation. Plays
a direct role in the transport and translation of transcripts
required for axonal regeneration in adult sensory neurons (By
similarity). Regulates localized beta-actin/ACTB mRNA translation
in polarized cells, a crucial process for cell migration and
neurite outgrowth. Co-transcriptionally associates with the ACTB
mRNA in the nucleus. This binding involves by a conserved 54-
nucleotide element in the ACTB mRNA 3'-UTR, known as the
'zipcode'. The ribonucleoparticle (RNP) thus formed is exported to
the cytoplasm, binds to a motor protein and is transported along
the cytoskeleton to the cell periphery. During transport, IGF2BP1
prevents beta-actin mRNA from being translated into protein. When
the RNP complex reaches its destination near the plasma membrane,
IGF2BP1 is phosphorylated by SRC. This releases the mRNA, allowing
ribosomal 40S and 60S subunits to assemble and initiate ACTB
protein synthesis. The monomeric ACTB protein then assembles into
the subcortical actin cytoskeleton, which pushes the leading edge
onwards. Binds MYC mRNA. Promotes the directed movement of cells
by fine-tuning intracellular signaling networks. Binds to MAPK4
3'-UTR and inhibits its translation. Interacts with PTEN
transcript open reading frame (ORF) and prevents mRNA decay. This
combined action on MAPK4 (down-regulation) and PTEN (up-
regulation) antagonizes HSPB1 phosphorylation, consequently it
prevents G-actin sequestration by phosphorylated HSPB1, allowing
F-actin polymerization. Hence enhances the velocity of cell
migration and stimulates directed cell migration by PTEN-modulated
polarization. {ECO:0000250, ECO:0000269|PubMed:11502257,
ECO:0000269|PubMed:12507992, ECO:0000269|PubMed:12573215,
ECO:0000269|PubMed:16306994, ECO:0000269|PubMed:22279049,
ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:9121465}.
-!- SUBUNIT: Can form homooligomers and heterooligomers with IGF2BP1
and IGF2BP3 in an RNA-dependent manner. Associates with the
cytoskeleton, predominantly with actin filament bundles and
occasionally with microtubules. In a heterologous system,
interacts with ELAVL1, DHX9 and HNRNPU.
{ECO:0000269|PubMed:23640942}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, perinuclear
region. Cell projection, growth cone. Cell projection, filopodium.
Cell projection, lamellipodium. Note=In the nucleus, located in
discrete foci, coinciding with the sites of ACTB transcription.
Export from the nucleus is mediated by XPO1. In the cytoplasm,
colocalizes with ACTB mRNA at the leading edge, in growth cone
filopodia and along neurites. In these locations, also colocalizes
with microtubules. Colocalization with ACTB mRNA is partially lost
at the cell periphery, suggesting release of the transcript. In
neuronal processes, exhibits fast retrograde and anterograde
movements, when associated with ACTB mRNA; this motility is lost
when the association is inhibited. In migrating fibroblasts,
localizes not only to leading edges, but also to retracting tails.
In response to cellular stress, such as oxidative stress or heat
shock, recruited to stress granules.
-!- TISSUE SPECIFICITY: Expressed in neurons and embryonic fibroblasts
(at protein level). {ECO:0000269|PubMed:11502257,
ECO:0000269|PubMed:9121465}.
-!- DOMAIN: Domain KH3 and KH4 are the major RNA-binding modules,
although KH1 and KH2 may also contribute to transcript binding.
The contribution to RNA-binding of individual KH domains may be
target-specific. KH1 and KH2, and possibly KH3 and KH4, promote
the formation of higher ordered protein-RNA complexes, which may
be essential for IGF2BP1 cytoplasmic retention. KH domains are
required for RNA-dependent homo- and heterooligomerization and for
localization to stress granules. KH3 and KH4 mediate association
with the cytoskeleton. Two nuclear export signals (NES) have been
identified in KH2 and KH4 domains, respectively. Only KH2 NES is
XPO1-dependent. Both NES may be redundant, since individual in
vitro mutations do not affect subcellular location of the full
length protein (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated by SRC at Tyr-396. This residue is involved in
ACTB mRNA binding, its phosphorylation impairs association with
ACTB mRNA and hence abolishes translational repression.
Phosphorylation occurs in close proximity to filopodia and in the
growth cones of differentiated neuroglioblastoma cells.
{ECO:0000269|PubMed:16306994}.
-!- SIMILARITY: Belongs to the RRM IMP/VICKZ family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF026527; AAB82295.1; -; mRNA.
RefSeq; NP_990402.1; NM_205071.1.
UniGene; Gga.567; -.
PDB; 2N8L; NMR; -; A=387-573.
PDB; 2N8M; NMR; -; A=387-573.
PDBsum; 2N8L; -.
PDBsum; 2N8M; -.
ProteinModelPortal; O42254; -.
SMR; O42254; -.
STRING; 9031.ENSGALP00000001973; -.
iPTMnet; O42254; -.
PaxDb; O42254; -.
PRIDE; O42254; -.
Ensembl; ENSGALT00000052497; ENSGALP00000051506; ENSGALG00000041204.
Ensembl; ENSGALT00000080686; ENSGALP00000053168; ENSGALG00000041204.
GeneID; 395953; -.
KEGG; gga:395953; -.
CTD; 10642; -.
eggNOG; KOG2193; Eukaryota.
eggNOG; ENOG410ZKB4; LUCA.
GeneTree; ENSGT00530000063171; -.
HOGENOM; HOG000000675; -.
HOVERGEN; HBG052725; -.
InParanoid; O42254; -.
KO; K17391; -.
OMA; EKPISIH; -.
OrthoDB; EOG091G17T1; -.
PhylomeDB; O42254; -.
TreeFam; TF320229; -.
PRO; PR:O42254; -.
Proteomes; UP000000539; Chromosome 27.
Bgee; ENSGALG00000001293; -.
GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISS:UniProtKB.
GO; GO:0010494; C:cytoplasmic stress granule; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0030175; C:filopodium; IDA:AgBase.
GO; GO:0030426; C:growth cone; IDA:AgBase.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:AgBase.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
GO; GO:0048027; F:mRNA 5'-UTR binding; IEA:Ensembl.
GO; GO:0003729; F:mRNA binding; IMP:AgBase.
GO; GO:0045182; F:translation regulator activity; IEA:Ensembl.
GO; GO:0070934; P:CRD-mediated mRNA stabilization; IEA:Ensembl.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0017148; P:negative regulation of translation; IDA:AgBase.
GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
GO; GO:0022013; P:pallium cell proliferation in forebrain; IEA:Ensembl.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:AgBase.
GO; GO:0010610; P:regulation of mRNA stability involved in response to stress; IEA:Ensembl.
CDD; cd12625; RRM1_IGF2BP1; 1.
CDD; cd12628; RRM2_IGF2BP1; 1.
Gene3D; 3.30.1370.10; -; 2.
Gene3D; 3.30.70.330; -; 2.
InterPro; IPR034837; IGF2BP1_RRM1.
InterPro; IPR034842; IGF2BP1_RRM2.
InterPro; IPR004087; KH_dom.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00013; KH_1; 4.
Pfam; PF00076; RRM_1; 2.
SMART; SM00322; KH; 4.
SMART; SM00360; RRM; 2.
SUPFAM; SSF54791; SSF54791; 4.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50084; KH_TYPE_1; 4.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
3D-structure; Cell projection; Complete proteome; Cytoplasm;
mRNA transport; Nucleus; Phosphoprotein; Reference proteome; Repeat;
RNA-binding; Translation regulation; Transport.
CHAIN 1 576 Insulin-like growth factor 2 mRNA-binding
protein 1.
/FTId=PRO_0000282536.
DOMAIN 2 75 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 81 156 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 195 260 KH 1. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 276 343 KH 2. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 404 469 KH 3. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 486 552 KH 4. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
MOD_RES 396 396 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:16306994}.
MUTAGEN 213 213 K->E: Decrease in Y RNA binding. Only
small decrease in affinity for binding to
ACTB and MYC transcripts, some
accumulation in the nucleus, and complete
loss of formation of higher ordered
protein-RNA complexes; when associated
with E-294. Loss of homo- and
heterooligomerization with IGF2BP1 and
IGF2BP2, almost complete loss of ACTB and
MYC transcript binding, almost complete
loss of ELAVL1-, DHX9- and HNRNPU-binding
and perturbed subcellular location,
including accumulation in the nucleus and
loss of localization to stress granules;
when associated with E-294, 422-E-E-423
and 505-E-E-506.
{ECO:0000269|PubMed:23640942}.
MUTAGEN 294 294 K->E: Decrease in Y RNA binding. Only
small decrease in affinity for binding to
ACTB and MYC transcripts, some
accumulation in the nucleus, and complete
loss of formation of higher ordered
protein-RNA complexes; when associated
with E-213. Loss of homo- and
heterooligomerization with IGF2BP1 and
IGF2BP2, almost complete loss of ACTB and
MYC transcript binding, almost complete
loss of ELAVL1-, DHX9- and HNRNPU-binding
and accumulation in the nucleus; when
associated with E-213, 422-E-E-423 and
505-E-E-506.
{ECO:0000269|PubMed:23640942}.
MUTAGEN 396 396 Y->F: Increases the interaction with ACTB
mRNA and its translational repression.
{ECO:0000269|PubMed:16306994}.
MUTAGEN 396 396 Y->Q: Impairs the interaction with beta-
actin mRNA and its translation
repression.
{ECO:0000269|PubMed:16306994}.
MUTAGEN 422 423 KK->EE: Almost complete loss of Y RNA
binding. About 80-fold decrease in
affinity for binding to ACTB transcript,
but almost no effect on MYC transcript
binding; when associated with 505-E-E-
506. Loss of homo- and
heterooligomerization with IGF2BP1 and
IGF2BP2, almost complete loss of ACTB and
MYC transcript binding, almost complete
loss of ELAVL1-, DHX9- and HNRNPU-binding
and accumulation in the nucleus; when
associated with E-213, E-294 and 505-E-E-
506.
MUTAGEN 504 505 KG->EE: Decrease in Y RNA binding. About
80-fold decrease in affinity for binding
to ACTB transcript, but almost no effect
on MYC transcript binding; when
associated with 422-E-E-423. Loss of
homo- and heterooligomerization with
IGF2BP1 and IGF2BP2, almost complete loss
of ACTB and MYC transcript binding,
almost complete loss of ELAVL1-,
DHX9- and HNRNPU-binding and accumulation
in the nucleus; when associated with E-
213, E-294 and 422-E-E-423.
STRAND 404 412 {ECO:0000244|PDB:2N8L}.
HELIX 413 420 {ECO:0000244|PDB:2N8L}.
HELIX 422 424 {ECO:0000244|PDB:2N8L}.
HELIX 426 434 {ECO:0000244|PDB:2N8L}.
STRAND 436 440 {ECO:0000244|PDB:2N8L}.
STRAND 449 457 {ECO:0000244|PDB:2N8L}.
HELIX 459 476 {ECO:0000244|PDB:2N8L}.
STRAND 481 483 {ECO:0000244|PDB:2N8L}.
STRAND 489 494 {ECO:0000244|PDB:2N8L}.
HELIX 495 501 {ECO:0000244|PDB:2N8L}.
STRAND 504 506 {ECO:0000244|PDB:2N8L}.
HELIX 508 516 {ECO:0000244|PDB:2N8L}.
STRAND 518 521 {ECO:0000244|PDB:2N8L}.
HELIX 529 531 {ECO:0000244|PDB:2N8L}.
STRAND 533 540 {ECO:0000244|PDB:2N8L}.
HELIX 542 560 {ECO:0000244|PDB:2N8L}.
HELIX 561 563 {ECO:0000244|PDB:2N8L}.
TURN 565 569 {ECO:0000244|PDB:2N8M}.
SEQUENCE 576 AA; 63271 MW; 01AAF2D1D81C8811 CRC64;
MNKLYIGNLN ESVTPADLEK VFNDHKISFS GQFLVKSGYA FVDCPDEQWA MKAIETFSGK
VELHGKQLEI EHSVPKKQRS RKIQIRNIPP QLRWEVLDGL LAQYGTVENC EQVNTDSETA
VVNVTYTNRE QTRQAIMKLN GHQLENHVLK VSYIPDEQSV QGPENGRRGG FGARGAPRQG
SPVTAGAPVK QQPVDIPLRL LVPTQYVGAI IGKEGATIRN ITKQTQSKID VHRKENAGAA
EKAISIHSTP EGCSAACKMI LEIMQKEAKD TKTADEVPLK ILAHNNFVGR LIGKEGRNLK
KVEQDTETKI TISSLQDLTL YNPERTITVK GSIENCCKAE QEIMKKVREA YENDVAAMSL
QSHLIPGLNL AAVGLFPASS NAVPPPPSSV SGAAPYSSFM PPEQETVHVF IPAQAVGAII
GKKGQHIKQL SRFASASIKI APPETPDSKV RMVVITGPPE AQFKAQGRIY GKLKEENFFG
PKEEVKLETH IRVPASAAGR VIGKGGKTVN ELQNLTAAEV VVPRDQTPDE NEQVIVKIIG
HFYASQMAQR KIRDILAQVK QQHQKGQSGQ LQARRK


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