IF2B3_MOUSE
ID IF2B3_MOUSE Reviewed; 579 AA.
AC Q9CPN8; Q3UHZ6; Q8C2J9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Insulin-like growth factor 2 mRNA-binding protein 3;
DE Short=IGF2 mRNA-binding protein 3;
DE Short=IMP-3;
DE Short=mIMP-3;
DE AltName: Full=IGF-II mRNA-binding protein 3;
DE AltName: Full=VICKZ family member 3;
GN Name=Igf2bp3; Synonyms=Vickz3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=10525192; DOI=10.1016/s0925-4773(99)00160-4;
RA Mueller-Pillasch F., Pohl B., Wilda M., Lacher U., Beil M., Wallrapp C.,
RA Hameister H., Knoechel W., Adler G., Gress T.M.;
RT "Expression of the highly conserved RNA binding protein KOC in
RT embryogenesis.";
RL Mech. Dev. 88:95-99(1999).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=9891060; DOI=10.1128/mcb.19.2.1262;
RA Nielsen J., Christiansen J., Lykke-Andersen J., Johnsen A.H., Wewer U.M.,
RA Nielsen F.C.;
RT "A family of insulin-like growth factor II mRNA-binding proteins represses
RT translation in late development.";
RL Mol. Cell. Biol. 19:1262-1270(1999).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=10875929; DOI=10.1074/jbc.m001156200;
RA Runge S., Nielsen F.C., Nielsen J., Lykke-Andersen J., Wewer U.M.,
RA Christiansen J.;
RT "H19 RNA binds four molecules of insulin-like growth factor II mRNA-binding
RT protein.";
RL J. Biol. Chem. 275:29562-29569(2000).
RN [6]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND RNA-BINDING.
RX PubMed=11288142; DOI=10.1002/jnr.1060;
RA Mori H., Sakakibara S., Imai T., Nakamura Y., Iijima T., Suzuki A.,
RA Yuasa Y., Takeda M., Okano H.;
RT "Expression of mouse igf2 mRNA-binding protein 3 and its implications for
RT the developing central nervous system.";
RL J. Neurosci. Res. 64:132-143(2001).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=12161597; DOI=10.1136/jmg.39.8.575;
RA Monk D., Bentley L., Beechey C., Hitchins M., Peters J., Preece M.A.,
RA Stanier P., Moore G.E.;
RT "Characterisation of the growth regulating gene IMP3, a candidate for
RT Silver-Russell syndrome.";
RL J. Med. Genet. 39:575-581(2002).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=12921532; DOI=10.1042/bj20030943;
RA Nielsen J., Adolph S.K., Rajpert-De Meyts E., Lykke-Andersen J., Koch G.,
RA Christiansen J., Nielsen F.C.;
RT "Nuclear transit of human zipcode-binding protein IMP1.";
RL Biochem. J. 376:383-391(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [10]
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 [11]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=15753088; DOI=10.1074/jbc.m500270200;
RA Liao B., Hu Y., Herrick D.J., Brewer G.;
RT "The RNA-binding protein IMP-3 is a translational activator of insulin-like
RT growth factor II leader-3 mRNA during proliferation of human K562 leukemia
RT cells.";
RL J. Biol. Chem. 280:18517-18524(2005).
RN [12]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=16049158; DOI=10.1530/rep.1.00664;
RA Hammer N.A., Hansen T.O., Byskov A.G., Rajpert-De Meyts E., Groendahl M.L.,
RA Bredkjaer H.E., Wewer U.M., Christiansen J., Nielsen F.C.;
RT "Expression of IGF-II mRNA-binding proteins (IMPs) in gonads and testicular
RT cancer.";
RL Reproduction 130:203-212(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND THR-528, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). Binds to the 3'-UTR of CD44 mRNA and stabilizes it,
CC hence promotes cell adhesion and invadopodia formation (By similarity).
CC Binds to beta-actin/ACTB and MYC transcripts (By similarity). Increases
CC MYC mRNA stability by binding to the coding region instability
CC determinant (CRD) and binding is enhanced by m6A-modification of the
CC CRD (By similarity). Binds to the 5'-UTR of the insulin-like growth
CC factor 2 (IGF2) mRNAs. {ECO:0000250|UniProtKB:O00425,
CC ECO:0000269|PubMed:15753088}.
CC -!- SUBUNIT: Can form homooligomers and heterooligomers with IGF2BP1 and
CC IGF2BP3 in an RNA-dependent manner. Interacts with IGF2BP1. Interacts
CC with ELAVL1, DHX9, HNRNPU, MATR3 and PABPC1.
CC {ECO:0000250|UniProtKB:O00425}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11288142,
CC ECO:0000269|PubMed:12921532}. Cytoplasm {ECO:0000250}. Cytoplasm, P-
CC body {ECO:0000250|UniProtKB:O00425}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:O00425}. Note=Found in lamellipodia of the
CC leading edge, in the perinuclear region, and beneath the plasma
CC membrane. The subcytoplasmic localization is cell specific and
CC regulated by cell contact and growth. Localized at the connecting piece
CC and the tail of the spermatozoa. In response to cellular stress, such
CC as oxidative stress, recruited to stress granules. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes, spermatogonia and
CC spermatocytes (at protein level). {ECO:0000269|PubMed:10525192,
CC ECO:0000269|PubMed:12161597, ECO:0000269|PubMed:16049158}.
CC -!- DEVELOPMENTAL STAGE: Expressed in zygotes and blastocysts (at protein
CC level). Expressed in gonads at 12.5 and 14.5 dpc (at protein level).
CC Expressed in germ cells at 16.5 dpc (at protein level). Expressed in
CC brain at 10.5 dpc and declining towards birth (at protein level).
CC Expressed during fetal development at 7, 9.5, 10.5, 12.5, 14.5 and 17.5
CC dpc and declining towards birth. {ECO:0000269|PubMed:10875929,
CC ECO:0000269|PubMed:11288142, ECO:0000269|PubMed:16049158,
CC ECO:0000269|PubMed:9891060}.
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. The KH domains are also required for RNA-dependent
CC homo- and heterooligomerization. The integrity of KH domains seems not
CC to be 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; AK088465; BAC40370.1; -; mRNA.
DR EMBL; AK011689; BAB27779.1; -; mRNA.
DR EMBL; AK147140; BAE27710.1; -; mRNA.
DR EMBL; BC045138; AAH45138.1; -; mRNA.
DR EMBL; BC049082; AAH49082.1; -; mRNA.
DR CCDS; CCDS39485.1; -.
DR RefSeq; NP_076159.3; NM_023670.3.
DR AlphaFoldDB; Q9CPN8; -.
DR SMR; Q9CPN8; -.
DR BioGRID; 228262; 6.
DR IntAct; Q9CPN8; 2.
DR MINT; Q9CPN8; -.
DR STRING; 10090.ENSMUSP00000031838; -.
DR iPTMnet; Q9CPN8; -.
DR PhosphoSitePlus; Q9CPN8; -.
DR EPD; Q9CPN8; -.
DR jPOST; Q9CPN8; -.
DR MaxQB; Q9CPN8; -.
DR PaxDb; Q9CPN8; -.
DR PeptideAtlas; Q9CPN8; -.
DR PRIDE; Q9CPN8; -.
DR ProteomicsDB; 267095; -.
DR Antibodypedia; 1056; 423 antibodies from 39 providers.
DR DNASU; 140488; -.
DR Ensembl; ENSMUST00000031838; ENSMUSP00000031838; ENSMUSG00000029814.
DR GeneID; 140488; -.
DR KEGG; mmu:140488; -.
DR UCSC; uc009bwi.2; mouse.
DR CTD; 10643; -.
DR MGI; MGI:1890359; Igf2bp3.
DR VEuPathDB; HostDB:ENSMUSG00000029814; -.
DR eggNOG; KOG2193; Eukaryota.
DR GeneTree; ENSGT00940000154957; -.
DR HOGENOM; CLU_020744_1_0_1; -.
DR InParanoid; Q9CPN8; -.
DR OMA; CPDEGWA; -.
DR OrthoDB; 394765at2759; -.
DR PhylomeDB; Q9CPN8; -.
DR TreeFam; TF320229; -.
DR BioGRID-ORCS; 140488; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Igf2bp3; mouse.
DR PRO; PR:Q9CPN8; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9CPN8; protein.
DR Bgee; ENSMUSG00000029814; Expressed in primitive streak and 165 other tissues.
DR Genevisible; Q9CPN8; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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:0048027; F:mRNA 5'-UTR binding; ISO:MGI.
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; Isopeptide bond; mRNA transport; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Translation regulation; Transport;
KW Ubl conjugation.
FT CHAIN 1..579
FT /note="Insulin-like growth factor 2 mRNA-binding protein 3"
FT /id="PRO_0000282539"
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 195..260
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 276..343
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 405..470
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 487..553
FT /note="KH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 158..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00425"
FT MOD_RES 528
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 450
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00425"
FT CROSSLNK 475
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00425"
FT CONFLICT 161
FT /note="Q -> R (in Ref. 1; BAE27710)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="H -> N (in Ref. 1; BAC40370)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="P -> H (in Ref. 1; BAE27710)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 63575 MW; CABD9A4355B392B7 CRC64;
MNKLYIGNLS DHAGPADLES VFKDAKIPVA GPFLVKTGYA FVDCPDEGWA LKAIEALSGK
MELHGKPMEV EHSVPKRQRI RKLQIRNIPP HLQWEVLDSL LVQYGVVESC EQVNTDSETA
VVNVTYSSKD QARQALDKLN GFQLENFTLK VAYIPDETAA QQNPSPQLRG RRGPGQRGSS
RQASPGSVSK QKPCDLPLRL LVPTQFVGAI IGKEGATIRN ITKQTQSKID VHRKENTGAA
EKSITILSTP EGTSAACKSI LEIMHKEAQD IKFTEEIPLK ILAHNNFVGR LIGKEGRNLK
KIEQDTDTKI TISPLQELTL YNPERTITVK GSVETCAKAE EEIMKKIRES YENDIASMNL
QAHLIPGLNL NALGLFPPTS GMPPPTSGPP STLTPPYPQF EQSETETVHL FIPALSVGAI
IGKQGQHIKQ LSRFAGASIK IAPAEAPDAK VRMVIITGPP EAQFKAQGRI YGKIKEENFV
SPKEEVKLEA HIRVPSFAAG RVIGKGGKTV NELQSLSSAE VVVPRDQTPD ENDQVVVKIT
GHFYACQVAQ RKIQEILTQV KQHQQQKALQ SGPPQSRRK
