NCBP2_BOVIN
ID NCBP2_BOVIN Reviewed; 156 AA.
AC Q3ZBJ1;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Rumen;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the cap-binding complex (CBC), which binds co-
CC transcriptionally to the 5' cap of pre-mRNAs and is involved in various
CC processes such as pre-mRNA splicing, translation regulation, nonsense-
CC mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs
CC (miRNAs) and mRNA export. The CBC complex is involved in mRNA export
CC from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to
CC the recruitment of the mRNA export machinery to the 5' end of mRNA and
CC to mRNA export in a 5' to 3' direction through the nuclear pore. The
CC CBC complex is also involved in mediating U snRNA and intronless mRNAs
CC export from the nucleus. The CBC complex is essential for a pioneer
CC round of mRNA translation, before steady state translation when the CBC
CC complex is replaced by cytoplasmic cap-binding protein eIF4E. The
CC pioneer round of mRNA translation mediated by the CBC complex plays a
CC central role in nonsense-mediated mRNA decay (NMD), NMD only taking
CC place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs.
CC The CBC complex enhances NMD in mRNAs containing at least one exon-
CC junction complex (EJC) via its interaction with UPF1, promoting the
CC interaction between UPF1 and UPF2. The CBC complex is also involved in
CC 'failsafe' NMD, which is independent of the EJC complex, while it does
CC not participate in Staufen-mediated mRNA decay (SMD). During cell
CC proliferation, the CBC complex is also involved in microRNAs (miRNAs)
CC biogenesis via its interaction with SRRT/ARS2, thereby being required
CC for miRNA-mediated RNA interference. The CBC complex also acts as a
CC negative regulator of PARN, thereby acting as an inhibitor of mRNA
CC deadenylation. In the CBC complex, NCBP2/CBP20 recognizes and binds
CC capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize
CC the movement of its N-terminal loop and lock the CBC into a high
CC affinity cap-binding state with the cap structure. The conventional
CC cap-binding complex with NCBP2 binds both small nuclear RNA (snRNA) and
CC messenger (mRNA) and is involved in their export from the nucleus (By
CC similarity). {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 with
CC m7GpppG-capped RNA. Found in a U snRNA export complex with PHAX/RNUXA,
CC NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA. Interacts with
CC PHAX/RNUXA, EIF4G1, HNRNPF, HNRNPH1 and ALYREF/THOC4/ALY. Interacts
CC with SRRT/ARS2 and KPNA3 (By similarity).
CC {ECO:0000250|UniProtKB:P52298}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P52298}. Cytoplasm
CC {ECO:0000250|UniProtKB:P52298}.
CC -!- SIMILARITY: Belongs to the RRM NCBP2 family. {ECO:0000305}.
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DR EMBL; BC103267; AAI03268.1; -; mRNA.
DR RefSeq; NP_001029568.1; NM_001034396.2.
DR AlphaFoldDB; Q3ZBJ1; -.
DR SMR; Q3ZBJ1; -.
DR STRING; 9913.ENSBTAP00000011684; -.
DR PaxDb; Q3ZBJ1; -.
DR PRIDE; Q3ZBJ1; -.
DR Ensembl; ENSBTAT00000011684; ENSBTAP00000011684; ENSBTAG00000008873.
DR GeneID; 510872; -.
DR KEGG; bta:510872; -.
DR CTD; 22916; -.
DR VEuPathDB; HostDB:ENSBTAG00000008873; -.
DR VGNC; VGNC:31908; NCBP2.
DR eggNOG; KOG0121; Eukaryota.
DR GeneTree; ENSGT00390000003197; -.
DR HOGENOM; CLU_070952_2_0_1; -.
DR InParanoid; Q3ZBJ1; -.
DR OMA; AENCMRY; -.
DR OrthoDB; 1421503at2759; -.
DR TreeFam; TF313897; -.
DR Reactome; R-BTA-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR Reactome; R-BTA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-BTA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-BTA-72086; mRNA Capping.
DR Reactome; R-BTA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-BTA-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR Reactome; R-BTA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-BTA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000008873; Expressed in myometrium and 107 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0005846; C:nuclear cap binding complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISS:UniProtKB.
DR GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR GO; GO:0017069; F:snRNA binding; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0008334; P:histone mRNA metabolic process; IEA:Ensembl.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
DR GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; IEA:Ensembl.
DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IEA:Ensembl.
DR GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
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_sf.
DR InterPro; IPR035979; RBD_domain_sf.
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 Acetylation; Cytoplasm; Methylation; mRNA processing; mRNA splicing;
KW mRNA transport; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW Translation regulation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P52298"
FT CHAIN 2..156
FT /note="Nuclear cap-binding protein subunit 2"
FT /id="PRO_0000232991"
FT DOMAIN 40..118
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 124..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 112..116
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 123..127
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT BINDING 133..134
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P52298"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52298"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52298"
FT MOD_RES 146
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P52298"
SQ SEQUENCE 156 AA; 18001 MW; B6C94F3182A2CC3D CRC64;
MSGGLLKALR SDSYVELSQY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY TTEEQIYELF
SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY INGTRLDDRI IRTDWDAGFK
EGRQYGRGRS GGQVRDEYRQ DYDAGRGGYG KLAQNQ
