IF2B2_PONAB
ID IF2B2_PONAB Reviewed; 556 AA.
AC Q5RB68;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Insulin-like growth factor 2 mRNA-binding protein 2;
DE Short=IGF2 mRNA-binding protein 2;
DE Short=IMP-2;
DE AltName: Full=IGF-II mRNA-binding protein 2;
DE AltName: Full=VICKZ family member 2;
GN Name=IGF2BP2; Synonyms=VICKZ2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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).
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 (By similarity). Preferentially binds
CC to N6-methyladenosine (m6A)-containing mRNAs and increases their
CC stability (By similarity). Binds to the 5'-UTR of the insulin-like
CC growth factor 2 (IGF2) mRNAs. Binding is isoform-specific. Binds to
CC beta-actin/ACTB and MYC transcripts (By similarity). Increases MYC mRNA
CC stability by binding to the coding region instability determinant (CRD)
CC and binding is enhanced by m6A-modification of the CRD (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y6M1}.
CC -!- SUBUNIT: Can form homooligomers and heterooligomers with IGF2BP1 and
CC IGF2BP3 in an RNA-dependent manner. Interacts with HNRPD. Interacts
CC with IGF2BP1. Interacts with ELAVL1, DHX9, HNRNPU, MATR3 and PABPC1.
CC {ECO:0000250|UniProtKB:Q9Y6M1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9Y6M1}. Cytoplasm, Stress
CC granule {ECO:0000250|UniProtKB:Q9Y6M1}. Note=Localized in cytoplasmic
CC mRNP granules containing untranslated mRNAs. Localizes at the
CC connecting piece and the tail of the spermatozoa. In response to
CC cellular stress, such as oxidative stress, recruited to stress granules
CC (By similarity). {ECO:0000250}.
CC -!- DOMAIN: Domain KH3 and KH4 are the major RNA-binding modules, although
CC KH1 and KH2 may also contribute. The contribution to RNA-binding of
CC individual KH domains may be target-specific. KH1 and KH2, and possibly
CC KH3 and KH4, promote the formation of higher ordered protein-RNA
CC complexes, which may be essential for IGF2BP1 cytoplasmic retention. KH
CC domains are required for RNA-dependent homo- and heterooligomerization
CC and for localization to stress granules.
CC {ECO:0000250|UniProtKB:Q9Y6M1}.
CC -!- SIMILARITY: Belongs to the RRM IMP/VICKZ family. {ECO:0000305}.
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DR EMBL; CR858786; CAH90992.1; -; mRNA.
DR RefSeq; NP_001125573.1; NM_001132101.1.
DR AlphaFoldDB; Q5RB68; -.
DR SMR; Q5RB68; -.
DR PRIDE; Q5RB68; -.
DR GeneID; 100172487; -.
DR KEGG; pon:100172487; -.
DR CTD; 10644; -.
DR InParanoid; Q5RB68; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; ISS:UniProtKB.
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:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd12626; RRM1_IGF2BP2; 1.
DR Gene3D; 3.30.1370.10; -; 2.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR028743; IGF2BP2.
DR InterPro; IPR034843; IGF2BP2_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:SF93; PTHR10288:SF93; 2.
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 2: Evidence at transcript level;
KW Cytoplasm; mRNA transport; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Translation regulation; Transport.
FT CHAIN 1..556
FT /note="Insulin-like growth factor 2 mRNA-binding protein 2"
FT /id="PRO_0000244498"
FT DOMAIN 3..76
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 82..157
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 193..258
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 274..341
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 384..449
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 466..532
FT /note="KH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 156..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6M1"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6M1"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6M1"
FT MOD_RES 507
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5SF07"
SQ SEQUENCE 556 AA; 61785 MW; B76336B97B1D07E8 CRC64;
MMNKLYIGNL SPAVTVDDLR QLFGDRKLPL AGQVLLKSGY AFVDYPDQNW AIRAIETLSG
KVELHGKIME VDYSVSKKLR SRKIQIRNIP PHLQWEVLDG LLAQYGTVEN VEQVNTDTET
AVVNVTYATR EEAKIAVEKL SGHQFENYSF KISYIPDEEV SSPSPPQRAQ RGDHSSREQG
HAPGGTSQAR QIDFPLRILV PTQFVGAIIG KEGLTIKNIT KQTQSRVDIH RKENSGAAEK
PVTIHATPEG TSEACRMILE IMQKEADETK LAEEIPLKIL AHNGLVGRLI GKEGRNLKKI
EHETGTKITI SSLQDLSIYN PERTITVKGT VEACASAEIE IMKKLREAFE NDMLAVNTHS
GYFSSLYPHH QFGPFPHHHS YPEQEIVNLF IPTQAVGAII GKKGAHIKQL ARFAGASIKI
APAEGPDVSE RMVIITGPPE AQFKAQGRIF GKLKEENFFN PKEEVKLEAH IRVPSSTAGR
VIGKGGKTVN ELQNLTSAEV IVPRDQTPDE NEEVIVRIIG HFFASQTAQR KIREIVQQVK
QQEQKYPQGV ASQCSK
