IF2B1_HUMAN
ID IF2B1_HUMAN Reviewed; 577 AA.
AC Q9NZI8; C9JT33;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Insulin-like growth factor 2 mRNA-binding protein 1;
DE Short=IGF2 mRNA-binding protein 1;
DE Short=IMP-1;
DE Short=IMP1;
DE AltName: Full=Coding region determinant-binding protein;
DE Short=CRD-BP;
DE AltName: Full=IGF-II mRNA-binding protein 1;
DE AltName: Full=VICKZ family member 1;
DE AltName: Full=Zipcode-binding protein 1;
DE Short=ZBP-1;
GN Name=IGF2BP1; Synonyms=CRDBP, VICKZ1, ZBP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Ioannidis P., Trangas T., Dimitriadis E., Samiotaki M.,
RA Panoutsakopoulos G., Kyriazoglou I., Voutzoulias S., Tsiapalis C.M.,
RA Kittas C., Agnantis N., Pandis N.;
RT "Ectopic expression of a KH-domain containing protein, highly homologous to
RT both human IMP-1 and mouse CRD-BP, in benign and malignant mesenchymal
RT tumors.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RA Gong H.Y., Hu M.C., Wu J.L.;
RT "A novel splice variant of the human IGF2 mRNA-binding protein 1 (IMP1/CRD-
RT BP) isolated from human Hep3B hepatoma cells.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP PROTEIN SEQUENCE OF 4-19; 26-35; 309-324 AND 508-525, FUNCTION,
RP RNA-BINDING, ASSOCIATION WITH A MRNP COMPLEX, TISSUE SPECIFICITY, GENE
RP NOMENCLATURE, AND SUBCELLULAR LOCATION.
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 PROTEIN SEQUENCE OF 27-35; 66-75 AND 510-524, FUNCTION, IDENTIFICATION IN A
RP MRNP COMPLEX WITH PABPC1 AND CSDE1, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND RNA-BINDING.
RX PubMed=16356927; DOI=10.1093/nar/gki1014;
RA Patel G.P., Ma S., Bag J.;
RT "The autoregulatory translational control element of poly(A)-binding
RT protein mRNA forms a heteromeric ribonucleoprotein complex.";
RL Nucleic Acids Res. 33:7074-7089(2005).
RN [6]
RP PROTEIN SEQUENCE OF 413-429 AND 510-524, SUBCELLULAR LOCATION, AND
RP RNA-BINDING.
RX PubMed=9801297; DOI=10.1093/nar/26.22.5036;
RA Doyle G.A., Betz N.A., Leeds P.F., Fleisig A.J., Prokipcak R.D., Ross J.;
RT "The c-myc coding region determinant-binding protein: a member of a family
RT of KH domain RNA-binding proteins.";
RL Nucleic Acids Res. 26:5036-5044(1998).
RN [7]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=8132663; DOI=10.1016/s0021-9258(17)37102-8;
RA Prokipcak R.D., Herrick D.J., Ross J.;
RT "Purification and properties of a protein that binds to the C-terminal
RT coding region of human c-myc mRNA.";
RL J. Biol. Chem. 269:9261-9269(1994).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND RNA-BINDING.
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 [9]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 213-LYS-GLU-214; 294-LYS-GLU-295 AND 423-LYS-LYS-424.
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 [10]
RP INTERACTION WITH FMR1, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=15282548; DOI=10.1038/sj.emboj.7600341;
RA Rackham O., Brown C.M.;
RT "Visualization of RNA-protein interactions in living cells: FMRP and IMP1
RT interact on mRNAs.";
RL EMBO J. 23:3346-3355(2004).
RN [11]
RP SUBUNIT, AND RNA-BINDING.
RX PubMed=15314207; DOI=10.1093/nar/gkh754;
RA Nielsen J., Kristensen M.A., Willemoes M., Nielsen F.C., Christiansen J.;
RT "Sequential dimerization of human zipcode-binding protein IMP1 on RNA: a
RT cooperative mechanism providing RNP stability.";
RL Nucleic Acids Res. 32:4368-4376(2004).
RN [12]
RP 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-181, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [14]
RP FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=16541107; DOI=10.1038/sj.emboj.7601039;
RA Vikesaa J., Hansen T.V., Joenson L., Borup R., Wewer U.M., Christiansen J.,
RA Nielsen F.C.;
RT "RNA-binding IMPs promote cell adhesion and invadopodia formation.";
RL EMBO J. 25:1456-1468(2006).
RN [15]
RP HOMODIMERIZATION, INTERACTION WITH PABPC1, AND RNA-BINDING.
RX PubMed=17212783; DOI=10.1111/j.1742-4658.2006.05556.x;
RA Patel G.P., Bag J.;
RT "IMP1 interacts with poly(A)-binding protein (PABP) and the autoregulatory
RT translational control element of PABP-mRNA through the KH III-IV domain.";
RL FEBS J. 273:5678-5690(2006).
RN [16]
RP FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=17101699; DOI=10.1083/jcb.200608071;
RA Stoehr N., Lederer M., Reinke C., Meyer S., Hatzfeld M., Singer R.H.,
RA Huettelmaier S.;
RT "ZBP1 regulates mRNA stability during cellular stress.";
RL J. Cell Biol. 175:527-534(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [18]
RP FUNCTION, RNA-BINDING, AND INDUCTION.
RX PubMed=16778892; DOI=10.1038/nature04839;
RA Noubissi F.K., Elcheva I., Bhatia N., Shakoori A., Ougolkov A., Liu J.,
RA Minamoto T., Ross J., Fuchs S.Y., Spiegelman V.S.;
RT "CRD-BP mediates stabilization of betaTrCP1 and c-myc mRNA in response to
RT beta-catenin signaling.";
RL Nature 441:898-901(2006).
RN [19]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17255263; DOI=10.1158/1078-0432.ccr-06-1297;
RA Kato T., Hayama S., Yamabuki T., Ishikawa N., Miyamoto M., Ito T.,
RA Tsuchiya E., Kondo S., Nakamura Y., Daigo Y.;
RT "Increased expression of insulin-like growth factor-II messenger RNA-
RT binding protein 1 is associated with tumor progression in patients with
RT lung cancer.";
RL Clin. Cancer Res. 13:434-442(2007).
RN [20]
RP INTERACTION WITH AGO1 AND AGO2.
RX PubMed=17932509; DOI=10.1038/sj.embor.7401088;
RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
RA Urlaub H., Meister G.;
RT "Proteomic and functional analysis of Argonaute-containing mRNA-protein
RT complexes in human cells.";
RL EMBO Rep. 8:1052-1060(2007).
RN [21]
RP FUNCTION.
RX PubMed=17893325; DOI=10.1128/mcb.00972-07;
RA Pan F., Huettelmaier S., Singer R.H., Gu W.;
RT "ZBP2 facilitates binding of ZBP1 to beta-actin mRNA during
RT transcription.";
RL Mol. Cell. Biol. 27:8340-8351(2007).
RN [22]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH DHX9; ELAVL2;
RP HNRNPA2B1; HNRNPC; HNRNPH1; HNRNPU; IGF2BP2; IGF2BP3; ILF2; PABPC1 AND
RP YBX1, RNA-BINDING, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [23]
RP FUNCTION, INTERACTION WITH HIV-1 GAG, AND SUBCELLULAR LOCATION.
RX PubMed=18385235; DOI=10.1128/jvi.00189-08;
RA Zhou Y., Rong L., Lu J., Pan Q., Liang C.;
RT "Insulin-like growth factor II mRNA binding protein 1 associates with Gag
RT protein of human immunodeficiency virus type 1, and its overexpression
RT affects virus assembly.";
RL J. Virol. 82:5683-5692(2008).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [26]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=19647520; DOI=10.1016/j.molcel.2009.06.007;
RA Elcheva I., Goswami S., Noubissi F.K., Spiegelman V.S.;
RT "CRD-BP protects the coding region of betaTrCP1 mRNA from miR-183-mediated
RT degradation.";
RL Mol. Cell 35:240-246(2009).
RN [27]
RP FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX,
RP IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A.,
RA Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs.";
RL RNA 15:104-115(2009).
RN [28]
RP FUNCTION, RNA-BINDING, AND IDENTIFICATION IN A HCV IRES-MEDIATED
RP TRANSLATION COMPLEX.
RX PubMed=19541769; DOI=10.1261/rna.1578409;
RA Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E.,
RA Ostareck-Lederer A., Ostareck D.H.;
RT "IGF2BP1 enhances HCV IRES-mediated translation initiation via the 3'UTR.";
RL RNA 15:1528-1542(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [31]
RP FUNCTION IN CELL MIGRATION.
RX PubMed=22279049; DOI=10.1101/gad.177642.111;
RA Stohr N., Kohn M., Lederer M., Glass M., Reinke C., Singer R.H.,
RA Huttelmaier S.;
RT "IGF2BP1 promotes cell migration by regulating MK5 and PTEN signaling.";
RL Genes Dev. 26:176-189(2012).
RN [32]
RP INTERACTION WITH ELAVL1; DHX9 AND HNRNPU.
RX PubMed=23640942; DOI=10.1515/hsz-2013-0111;
RA Wachter K., Kohn M., Stohr N., Huttelmaier S.;
RT "Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding
RT proteins) is modulated by distinct RNA-binding domains.";
RL Biol. Chem. 394:1077-1090(2013).
RN [33]
RP REVIEW.
RX PubMed=23069990; DOI=10.1007/s00018-012-1186-z;
RA Bell J.L., Wachter K., Muhleck B., Pazaitis N., Kohn M., Lederer M.,
RA Huttelmaier S.;
RT "Insulin-like growth factor 2 mRNA-binding proteins (IGF2BPs): post-
RT transcriptional drivers of cancer progression?";
RL Cell. Mol. Life Sci. 70:2657-2675(2013).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-73; SER-181 AND
RP THR-528, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [35]
RP FUNCTION, INTERACTION WITH ELAVL1; MATR3 AND PABPC1, SUBCELLULAR LOCATION,
RP ROLE OF KH DOMAINS, MUTAGENESIS OF LYS-213; LYS-294; 423-LYS-LYS-424 AND
RP 505-LYS-GLY-506, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29476152; DOI=10.1038/s41556-018-0045-z;
RA Huang H., Weng H., Sun W., Qin X., Shi H., Wu H., Zhao B.S., Mesquita A.,
RA Liu C., Yuan C.L., Hu Y.C., Huettelmaier S., Skibbe J.R., Su R., Deng X.,
RA Dong L., Sun M., Li C., Nachtergaele S., Wang Y., Hu C., Ferchen K.,
RA Greis K.D., Jiang X., Wei M., Qu L., Guan J.L., He C., Yang J., Chen J.;
RT "Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA
RT stability and translation.";
RL Nat. Cell Biol. 20:285-295(2018).
RN [36]
RP FUNCTION, INTERACTION WITH RBRP; ELAVL1; MATR3 AND PABPC1, AND MUTAGENESIS
RP OF 423-LYS-LYS-424 AND 505-LYS-GLY-506.
RX PubMed=32245947; DOI=10.1038/s41467-020-15403-9;
RA Zhu S., Wang J.Z., Chen D., He Y.T., Meng N., Chen M., Lu R.X., Chen X.H.,
RA Zhang X.L., Yan G.R.;
RT "An oncopeptide regulates m6A recognition by the m6A reader IGF2BP1 and
RT tumorigenesis.";
RL Nat. Commun. 11:1685-1685(2020).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 404-566, FUNCTION, RNA-BINDING,
RP AND DOMAIN.
RX PubMed=20080952; DOI=10.1101/gad.1862910;
RA Chao J.A., Patskovsky Y., Patel V., Levy M., Almo S.C., Singer R.H.;
RT "ZBP1 recognition of beta-actin zipcode induces RNA looping.";
RL Genes Dev. 24:148-158(2010).
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 (PubMed:29476152, PubMed:32245947). Plays a direct role in the
CC transport and translation of transcripts required for axonal
CC regeneration in adult sensory neurons (By similarity). Regulates
CC localized beta-actin/ACTB mRNA translation, a crucial process for cell
CC polarity, cell migration and neurite outgrowth. Co-transcriptionally
CC associates with the ACTB mRNA in the nucleus. This binding involves a
CC conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the
CC 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a
CC motor protein and is transported along the cytoskeleton to the cell
CC periphery. During transport, prevents ACTB mRNA from being translated
CC into protein. When the RNP complex reaches its destination near the
CC plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA,
CC allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB
CC protein synthesis. Monomeric ACTB then assembles into the subcortical
CC actin cytoskeleton (By similarity). During neuronal development, key
CC regulator of neurite outgrowth, growth cone guidance and neuronal cell
CC migration, presumably through the spatiotemporal fine tuning of protein
CC synthesis, such as that of ACTB (By similarity). May regulate mRNA
CC transport to activated synapses (By similarity). Binds to and
CC stabilizes ABCB1/MDR-1 mRNA (By similarity). During interstinal wound
CC repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA
CC stabilization may be crucial for colonic mucosal wound healing (By
CC similarity). Binds to the 3'-UTR of IGF2 mRNA by a mechanism of
CC cooperative and sequential dimerization and regulates IGF2 mRNA
CC subcellular localization and translation. Binds to MYC mRNA, in the
CC coding region instability determinant (CRD) of the open reading frame
CC (ORF), hence preventing MYC cleavage by endonucleases and possibly
CC microRNA targeting to MYC-CRD (PubMed:29476152). Binding to MYC mRNA is
CC enhanced by m6A-modification of the CRD (PubMed:29476152). Binds to the
CC 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and
CC invadopodia formation in cancer cells. Binds to the oncofetal H19
CC transcript and to the neuron-specific TAU mRNA and regulates their
CC localizations. Binds to and stabilizes BTRC/FBW1A mRNA. Binds to the
CC adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and
CC represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1
CC protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-
CC dependent interaction with AGO2. Promotes the directed movement of
CC tumor-derived cells by fine-tuning intracellular signaling networks.
CC Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN
CC transcript open reading frame (ORF) and prevents mRNA decay. This
CC combined action on MAPK4 (down-regulation) and PTEN (up-regulation)
CC antagonizes HSPB1 phosphorylation, consequently it prevents G-actin
CC sequestration by phosphorylated HSPB1, allowing F-actin polymerization.
CC Hence enhances the velocity of cell migration and stimulates directed
CC cell migration by PTEN-modulated polarization. Interacts with Hepatitis
CC C virus (HCV) 5'-UTR and 3'-UTR and specifically enhances translation
CC at the HCV IRES, but not 5'-cap-dependent translation, possibly by
CC recruiting eIF3. Interacts with HIV-1 GAG protein and blocks the
CC formation of infectious HIV-1 particles. Reduces HIV-1 assembly by
CC inhibiting viral RNA packaging, as well as assembly and processing of
CC GAG protein on cellular membranes. During cellular stress, such as
CC oxidative stress or heat shock, stabilizes target mRNAs that are
CC recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN,
CC RAPGEF2 and RPS6KA5 transcripts. {ECO:0000250,
CC ECO:0000269|PubMed:10875929, ECO:0000269|PubMed:16356927,
CC ECO:0000269|PubMed:16541107, ECO:0000269|PubMed:16778892,
CC ECO:0000269|PubMed:17101699, ECO:0000269|PubMed:17255263,
CC ECO:0000269|PubMed:17893325, ECO:0000269|PubMed:18385235,
CC ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19541769,
CC ECO:0000269|PubMed:19647520, ECO:0000269|PubMed:20080952,
CC ECO:0000269|PubMed:22279049, ECO:0000269|PubMed:29476152,
CC ECO:0000269|PubMed:32245947, ECO:0000269|PubMed:8132663,
CC ECO:0000269|PubMed:9891060}.
CC -!- SUBUNIT: Can form homodimers and heterodimers with IGF2BP1 and IGF2BP3.
CC Component of the coding region determinant (CRD)-mediated complex,
CC composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. During HCV
CC infection, identified in a HCV IRES-mediated translation complex, at
CC least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon. Interacts
CC (via the KH domains) with HIV-1 GAG (via the second zinc finger motif
CC of NC). Associates (via the RRM domains and KH domains) with HIV-1
CC particles. Identified in a mRNP complex, composed of at least DHX9,
CC DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1,
CC STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule
CC complex containing untranslated mRNAs. Interacts with DHX9, ELAVL2,
CC HNRNPA2B1, HNRNPC, HNRNPH1, HNRNPU, IGF2BP2, ILF2, and YBX1. Interacts
CC with FMR1. Component of a multisubunit autoregulatory RNP complex
CC (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1/UNR. Directly
CC interacts with PABPC1 (PubMed:17212783, PubMed:29476152,
CC PubMed:32245947). Component of a TAU mRNP complex, at least composed of
CC IGF2BP1, ELAVL4 and G3BP. Interacts with ELAVL4 in an RNA-dependent
CC manner. Associates with microtubules and polysomes. Interacts with AGO1
CC and AGO2. Interacts with ELAVL1 and MATR3 (PubMed:29476152,
CC PubMed:32245947). Interacts (via KH3 and KH4 domains) with SEPIN14P20
CC peptide RBRP; the interaction results in increased binding of IGF2BP1
CC to N6-methyladenosine (m6A)-containing mRNAs (PubMed:32245947).
CC {ECO:0000269|PubMed:15282548, ECO:0000269|PubMed:15314207,
CC ECO:0000269|PubMed:16356927, ECO:0000269|PubMed:17212783,
CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17932509,
CC ECO:0000269|PubMed:18385235, ECO:0000269|PubMed:19029303,
CC ECO:0000269|PubMed:19541769, ECO:0000269|PubMed:23640942,
CC ECO:0000269|PubMed:29476152, ECO:0000269|PubMed:32245947}.
CC -!- INTERACTION:
CC Q9NZI8; O95793: STAU1; NbExp=6; IntAct=EBI-1053892, EBI-358174;
CC Q9NZI8; Q8VDS3: Cbx7; Xeno; NbExp=2; IntAct=EBI-1053892, EBI-1216533;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, perinuclear
CC region. Cytoplasm, P-body {ECO:0000269|PubMed:29476152}. Cytoplasm,
CC Stress granule {ECO:0000269|PubMed:29476152}. Cell projection,
CC lamellipodium. Cell projection, dendrite {ECO:0000250}. Cell
CC projection, dendritic spine {ECO:0000250}. Cell projection, growth
CC cone. Cell projection, filopodium {ECO:0000250}. Cell projection, axon
CC {ECO:0000250}. Note=In the nucleus, located in discrete foci,
CC coinciding with the sites of ACTB transcription (By similarity). In the
CC cytoplasm, localizes in cytoplasmic mRNP granules. Colocalizes with
CC microtubules in growth cone filopodia and along neurites in neuronal
CC cells (By similarity). Cytoplasmic colocalization with ACTB mRNA is
CC partially lost at the cell periphery, suggesting release of the
CC transcript. In neuronal processes, exhibits fast retrograde and
CC anterograde movements, when associated with ACTB mRNA; this motility is
CC lost when the association is inhibited (By similarity). In hippocampal
CC neurons, predominantly located within dendrites, particularly at
CC dendritic branching points in young cells, compared to axons (By
CC similarity). In axons, predominantly found in axonal branches and their
CC growth cones (By similarity). In motile cells, such as migrating
CC fibroblasts, localizes to leading edges where it colocalizes with
CC microtubules and microfilaments and to retracting tails (By
CC similarity). Dendritic levels are regulated by neuronal activity and
CC glutaminergic signals: they are increased by KCl-induced
CC depolarization, which induces rapid efflux from the cell body into
CC dendrites, and decreased by the NMDA receptor agonist (By similarity).
CC In motile cells, transported towards the leading edge into the cortical
CC region of the lamellipodia where it is connected to microfilaments (By
CC similarity). In response to cellular stress, such as oxidative stress
CC or heat shock, recruited to stress granules, but not to processing
CC bodies. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NZI8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZI8-2; Sequence=VSP_045366;
CC -!- TISSUE SPECIFICITY: Mainly expressed in the embryo, including in fetal
CC liver, fetal lung, fetal kidney, fetal thymus (at protein level). Also
CC expressed follicles of ovary, as well as in gonocytes of testis,
CC spermatogonia, semen, oocytes and placenta (at protein level).
CC Expressed in various cancers, including testis and lung cancers (at
CC protein level), as well as kidney, prostate and trachea cancers.
CC {ECO:0000269|PubMed:12921532, ECO:0000269|PubMed:16049158,
CC ECO:0000269|PubMed:17255263, ECO:0000269|PubMed:9891060}.
CC -!- INDUCTION: May be up-regulated in response to CTNNB1/beta-catenin
CC activation. {ECO:0000269|PubMed:16778892}.
CC -!- DOMAIN: Domains KH3 and KH4 are the major RNA-binding modules, although
CC KH1 and KH2 may also contribute (PubMed:29476152). 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 RNA-dependent homo- and
CC heterooligomerization and for localization to stress granules. KH3 and
CC KH4 mediate association with the cytoskeleton. Two nuclear export
CC signals (NES) have been identified in KH2 and KH4 domains,
CC respectively. Only KH2 NES is XPO1-dependent. Both NES may be
CC redundant, since individual in vitro mutations do not affect
CC subcellular location of the full-length protein. The 4 KH domains are
CC important to suppress HIV-1 infectivity. {ECO:0000269|PubMed:20080952,
CC ECO:0000269|PubMed:29476152}.
CC -!- PTM: Phosphorylated. Phosphorylation may impair association with ACTB
CC mRNA and hence abolishes translational repression (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM IMP/VICKZ family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/IGF2BP1ID40969ch17q21.html";
CC ---------------------------------------------------------------------------
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DR EMBL; AF198254; AAF37203.1; -; mRNA.
DR EMBL; DQ227344; ABB46294.1; -; mRNA.
DR EMBL; AC091133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS11543.1; -. [Q9NZI8-1]
DR CCDS; CCDS54138.1; -. [Q9NZI8-2]
DR RefSeq; NP_001153895.1; NM_001160423.1. [Q9NZI8-2]
DR RefSeq; NP_006537.3; NM_006546.3. [Q9NZI8-1]
DR PDB; 3KRM; X-ray; 2.75 A; A/B/C=404-566.
DR PDB; 6QEY; X-ray; 2.20 A; A=194-369.
DR PDBsum; 3KRM; -.
DR PDBsum; 6QEY; -.
DR AlphaFoldDB; Q9NZI8; -.
DR SMR; Q9NZI8; -.
DR BioGRID; 115886; 393.
DR ComplexPortal; CPX-1080; CRD-mediated mRNA stability complex.
DR CORUM; Q9NZI8; -.
DR DIP; DIP-38139N; -.
DR IntAct; Q9NZI8; 104.
DR MINT; Q9NZI8; -.
DR STRING; 9606.ENSP00000290341; -.
DR GlyGen; Q9NZI8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NZI8; -.
DR PhosphoSitePlus; Q9NZI8; -.
DR SwissPalm; Q9NZI8; -.
DR BioMuta; IGF2BP1; -.
DR DMDM; 296434536; -.
DR EPD; Q9NZI8; -.
DR jPOST; Q9NZI8; -.
DR MassIVE; Q9NZI8; -.
DR MaxQB; Q9NZI8; -.
DR PaxDb; Q9NZI8; -.
DR PeptideAtlas; Q9NZI8; -.
DR PRIDE; Q9NZI8; -.
DR ProteomicsDB; 11549; -.
DR ProteomicsDB; 83410; -. [Q9NZI8-1]
DR TopDownProteomics; Q9NZI8-1; -. [Q9NZI8-1]
DR Antibodypedia; 17915; 333 antibodies from 37 providers.
DR DNASU; 10642; -.
DR Ensembl; ENST00000290341.8; ENSP00000290341.3; ENSG00000159217.10. [Q9NZI8-1]
DR Ensembl; ENST00000431824.2; ENSP00000389135.2; ENSG00000159217.10. [Q9NZI8-2]
DR GeneID; 10642; -.
DR KEGG; hsa:10642; -.
DR MANE-Select; ENST00000290341.8; ENSP00000290341.3; NM_006546.4; NP_006537.3.
DR UCSC; uc002iom.4; human. [Q9NZI8-1]
DR CTD; 10642; -.
DR DisGeNET; 10642; -.
DR GeneCards; IGF2BP1; -.
DR HGNC; HGNC:28866; IGF2BP1.
DR HPA; ENSG00000159217; Tissue enhanced (placenta, testis).
DR MIM; 608288; gene.
DR neXtProt; NX_Q9NZI8; -.
DR OpenTargets; ENSG00000159217; -.
DR PharmGKB; PA143485501; -.
DR VEuPathDB; HostDB:ENSG00000159217; -.
DR eggNOG; KOG2193; Eukaryota.
DR GeneTree; ENSGT00940000160427; -.
DR HOGENOM; CLU_020744_1_0_1; -.
DR InParanoid; Q9NZI8; -.
DR OMA; XAIMKLN; -.
DR OrthoDB; 286875at2759; -.
DR PhylomeDB; Q9NZI8; -.
DR TreeFam; TF320229; -.
DR PathwayCommons; Q9NZI8; -.
DR Reactome; R-HSA-428359; Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RNA.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR SignaLink; Q9NZI8; -.
DR SIGNOR; Q9NZI8; -.
DR BioGRID-ORCS; 10642; 29 hits in 1089 CRISPR screens.
DR ChiTaRS; IGF2BP1; human.
DR EvolutionaryTrace; Q9NZI8; -.
DR GeneWiki; IGF2BP1; -.
DR GenomeRNAi; 10642; -.
DR Pharos; Q9NZI8; Tbio.
DR PRO; PR:Q9NZI8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9NZI8; protein.
DR Bgee; ENSG00000159217; Expressed in ganglionic eminence and 126 other tissues.
DR Genevisible; Q9NZI8; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
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:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:BHF-UCL.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0045182; F:translation regulator activity; IDA:BHF-UCL.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IDA:UniProtKB.
DR GO; GO:0140059; P:dendrite arborization; IEA:Ensembl.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:ComplexPortal.
DR GO; GO:0017148; P:negative regulation of translation; IDA:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0022013; P:pallium cell proliferation in forebrain; IEA:Ensembl.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IDA:ComplexPortal.
DR GO; GO:0001817; P:regulation of cytokine production; IC:BHF-UCL.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0010610; P:regulation of mRNA stability involved in response to stress; IMP:UniProtKB.
DR GO; GO:0051252; P:regulation of RNA metabolic process; IBA:GO_Central.
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; 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Cytoplasm;
KW Direct protein sequencing; mRNA transport; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Synapse; Translation regulation;
KW Transport.
FT CHAIN 1..577
FT /note="Insulin-like growth factor 2 mRNA-binding protein 1"
FT /id="PRO_0000282533"
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 160..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..570
FT /note="Necessary for interaction with ELAVL4 and binding to
FT TAU mRNA"
FT /evidence="ECO:0000250"
FT REGION 310..324
FT /note="Sufficient for nuclear export"
FT REGION 485..495
FT /note="Sufficient for nuclear export"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 528
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 135..273
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_045366"
FT MUTAGEN 213..214
FT /note="KE->EL: 50-fold decrease in RNA-binding affinity,
FT decreased location in cytoplasmic RNP, increased nuclear
FT location; when associated with 294-E-L-295 and 423-E-L-
FT 424."
FT /evidence="ECO:0000269|PubMed:12921532"
FT MUTAGEN 213
FT /note="K->E: Partial reduction in interaction with m6A-
FT modified mRNA; when associated with E-294."
FT /evidence="ECO:0000269|PubMed:29476152"
FT MUTAGEN 294..295
FT /note="KE->EL: 50-fold decrease in RNA-binding affinity,
FT decreased location in cytoplasmic RNP, increased nuclear
FT location; when associated with 213-E-L-214 and 423-E-L-
FT 424."
FT /evidence="ECO:0000269|PubMed:12921532"
FT MUTAGEN 294
FT /note="K->E: Partial reduction in interaction with m6A-
FT modified mRNA; when associated with E-213."
FT /evidence="ECO:0000269|PubMed:29476152"
FT MUTAGEN 423..424
FT /note="KK->EE: Loss of binding to RBPR and loss of
FT interaction with m6A-modified mRNA; when associated with
FT 505-E-E-506."
FT /evidence="ECO:0000269|PubMed:29476152,
FT ECO:0000269|PubMed:32245947"
FT MUTAGEN 423..424
FT /note="KK->EL: 50-fold decrease in RNA-binding affinity,
FT decreased location in cytoplasmic RNP, increased nuclear
FT location; when associated with 213-E-L-214 and 294-E-L-
FT 295."
FT /evidence="ECO:0000269|PubMed:12921532"
FT MUTAGEN 505..506
FT /note="KG->EE: Loss of binding to RBPR and loss of
FT interaction with m6A-modified mRNA; when associated with
FT 423-E-E-424."
FT /evidence="ECO:0000269|PubMed:29476152,
FT ECO:0000269|PubMed:32245947"
FT CONFLICT 10
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="I -> T (in Ref. 1; AAF37203)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="I -> T (in Ref. 1; AAF37203)"
FT /evidence="ECO:0000305"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:6QEY"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:6QEY"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:6QEY"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:6QEY"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:6QEY"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:6QEY"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:6QEY"
FT HELIX 250..270
FT /evidence="ECO:0007829|PDB:6QEY"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:6QEY"
FT HELIX 285..292
FT /evidence="ECO:0007829|PDB:6QEY"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:6QEY"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:6QEY"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:6QEY"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:6QEY"
FT STRAND 324..331
FT /evidence="ECO:0007829|PDB:6QEY"
FT HELIX 333..361
FT /evidence="ECO:0007829|PDB:6QEY"
FT STRAND 406..413
FT /evidence="ECO:0007829|PDB:3KRM"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:3KRM"
FT HELIX 417..421
FT /evidence="ECO:0007829|PDB:3KRM"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:3KRM"
FT HELIX 426..435
FT /evidence="ECO:0007829|PDB:3KRM"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:3KRM"
FT STRAND 450..458
FT /evidence="ECO:0007829|PDB:3KRM"
FT HELIX 460..476
FT /evidence="ECO:0007829|PDB:3KRM"
FT STRAND 488..495
FT /evidence="ECO:0007829|PDB:3KRM"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:3KRM"
FT HELIX 499..503
FT /evidence="ECO:0007829|PDB:3KRM"
FT HELIX 505..507
FT /evidence="ECO:0007829|PDB:3KRM"
FT HELIX 508..517
FT /evidence="ECO:0007829|PDB:3KRM"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:3KRM"
FT STRAND 533..541
FT /evidence="ECO:0007829|PDB:3KRM"
FT HELIX 543..560
FT /evidence="ECO:0007829|PDB:3KRM"
SQ SEQUENCE 577 AA; 63481 MW; 1D036AE5388D05FA CRC64;
MNKLYIGNLN ESVTPADLEK VFAEHKISYS GQFLVKSGYA FVDCPDEHWA MKAIETFSGK
VELQGKRLEI EHSVPKKQRS RKIQIRNIPP QLRWEVLDSL LAQYGTVENC EQVNTESETA
VVNVTYSNRE QTRQAIMKLN GHQLENHALK VSYIPDEQIA QGPENGRRGG FGSRGQPRQG
SPVAAGAPAK QQQVDIPLRL LVPTQYVGAI IGKEGATIRN ITKQTQSKID VHRKENAGAA
EKAISVHSTP EGCSSACKMI LEIMHKEAKD TKTADEVPLK ILAHNNFVGR LIGKEGRNLK
KVEQDTETKI TISSLQDLTL YNPERTITVK GAIENCCRAE QEIMKKVREA YENDVAAMSL
QSHLIPGLNL AAVGLFPASS SAVPPPPSSV TGAAPYSSFM QAPEQEMVQV FIPAQAVGAI
IGKKGQHIKQ LSRFASASIK IAPPETPDSK VRMVIITGPP EAQFKAQGRI YGKLKEENFF
GPKEEVKLET HIRVPASAAG RVIGKGGKTV NELQNLTAAE VVVPRDQTPD ENDQVIVKII
GHFYASQMAQ RKIRDILAQV KQQHQKGQSN QAQARRK
