ID NCBP2_SALSA Reviewed; 155 AA. AC C0H859; B5DGH3; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 1. DT 15-FEB-2017, entry version 25. DE RecName: Full=Nuclear cap-binding protein subunit 2; DE AltName: Full=20 kDa nuclear cap-binding protein; DE AltName: Full=NCBP 20 kDa subunit; DE Short=CBP20; GN Name=ncbp2; Synonyms=cbp20; OS Salmo salar (Atlantic salmon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; OC Salmoniformes; Salmonidae; Salmoninae; Salmo. OX NCBI_TaxID=8030; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=White muscle; RA Andreassen R., Hoyheim B.; RT "Characterization of full-length sequenced inserts (FLIcs) from a RT salmo salar white muscle specific cDNA library."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=20433749; DOI=10.1186/1471-2164-11-279; RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., RA Messmer A.M., Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., RA Davidson W.S., Koop B.F.; RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes RT in evolutionary pressures on a post-tetraploidization genome."; RL BMC Genomics 11:279-279(2010). CC -!- FUNCTION: Component of the cap-binding complex (CBC), which binds CC co-transcriptionally to the 5' cap of pre-mRNAs and is involved in CC various processes such as pre-mRNA splicing, translation CC regulation, nonsense-mediated mRNA decay, RNA-mediated gene CC silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC CC complex is involved in mRNA export from the nucleus, leading to CC the recruitment of the mRNA export machinery to the 5' end of mRNA CC and to mRNA export in a 5' to 3' direction through the nuclear CC pore. The CBC complex is also involved in mediating U snRNA and CC intronless mRNAs export from the nucleus. The CBC complex is CC essential for a pioneer round of mRNA translation, before steady CC state translation when the CBC complex is replaced by cytoplasmic CC cap-binding protein eIF4E. The pioneer round of mRNA translation CC mediated by the CBC complex plays a central role in nonsense- CC mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to CC the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex CC enhances NMD in mRNAs containing at least one exon-junction CC complex (EJC), promoting the interaction between upf1 and upf2. CC The CBC complex is also involved in 'failsafe' NMD, which is CC independent of the EJC complex, while it does not participate in CC Staufen-mediated mRNA decay (SMD). During cell proliferation, the CC CBC complex is also involved in microRNAs (miRNAs) biogenesis via CC its interaction with srrt/ars2, thereby being required for miRNA- CC mediated RNA interference. The CBC complex also acts as a negative CC regulator of parn, thereby acting as an inhibitor of mRNA CC deadenylation. In the CBC complex, ncbp2/cbp20 recognizes and CC binds capped RNAs (m7GpppG-capped RNA) but requires ncbp1/cbp80 to CC stabilize the movement of its N-terminal loop and lock the CBC CC into a high affinity cap-binding state with the cap structure. The CC conventional cap-binding complex with NCBP2 binds both small CC nuclear RNA (snRNA) and messenger (mRNA) and is involved in their CC export from the nucleus (By similarity). CC {ECO:0000250|UniProtKB:P52298}. CC -!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a CC heterodimer composed of ncbp1/cbp80 and ncbp2/cbp20 that interacts CC with m7GpppG-capped RNA. {ECO:0000250|UniProtKB:P52298}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P52298}. CC Cytoplasm {ECO:0000250|UniProtKB:P52298}. CC -!- SIMILARITY: Belongs to the RRM NCBP2 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BT043732; ACH70847.1; -; mRNA. DR EMBL; BT058515; ACN10228.1; -; mRNA. DR EMBL; BT060223; ACN12583.1; -; mRNA. DR RefSeq; XP_013979037.1; XM_014123562.1. DR UniGene; Ssa.8109; -. DR ProteinModelPortal; C0H859; -. DR GeneID; 100196301; -. DR CTD; 22916; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005846; C:nuclear cap binding complex; IEA:InterPro. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISS:UniProtKB. DR GO; GO:0017069; F:snRNA binding; ISS:UniProtKB. DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW. DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW. DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:UniProtKB. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW. DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0008380; P:RNA splicing; ISS:UniProtKB. DR GO; GO:0006408; P:snRNA export from nucleus; ISS:UniProtKB. DR CDD; cd12240; RRM_NCBP2; 1. DR Gene3D; 3.30.70.330; -; 1. DR InterPro; IPR027157; NCBP2. DR InterPro; IPR034148; NCBP2_RRM. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR18847; PTHR18847; 1. DR Pfam; PF00076; RRM_1; 1. DR SMART; SM00360; RRM; 1. DR SUPFAM; SSF54928; SSF54928; 1. DR PROSITE; PS50102; RRM; 1. PE 2: Evidence at transcript level; KW Cytoplasm; mRNA processing; mRNA splicing; mRNA transport; KW Nonsense-mediated mRNA decay; Nucleus; RNA-binding; KW RNA-mediated gene silencing; Translation regulation; Transport. FT CHAIN 1 155 Nuclear cap-binding protein subunit 2. FT /FTId=PRO_0000385253. FT DOMAIN 39 117 RRM. {ECO:0000255|PROSITE- FT ProRule:PRU00176}. FT REGION 111 115 mRNA cap-binding. {ECO:0000250}. FT REGION 122 126 mRNA cap-binding. {ECO:0000250}. FT REGION 132 133 mRNA cap-binding. {ECO:0000250}. FT BINDING 19 19 mRNA cap. {ECO:0000250}. FT BINDING 42 42 mRNA cap. {ECO:0000250}. FT CONFLICT 3 3 S -> I (in Ref. 1; ACH70847). FT {ECO:0000305}. SQ SEQUENCE 155 AA; 17940 MW; 37E447A35C516D7B CRC64; MSSKLNALFS DSYVDVSQYR DQHFKGNRYE QEKLLKQANT LYVGNLSFYT TEEQVYELFS KSGDVKRIII GLDKVKKTAC GFCFVEYYTR TDAENAMRFV NGTRLDDRII RTDWDAGFKE GRQYGRGKSG GQVRDEYRQD YDPARGGYGK VVSRP //