NCBP1_CAEEL
ID NCBP1_CAEEL Reviewed; 798 AA.
AC O01763;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Nuclear cap-binding protein subunit 1;
DE AltName: Full=80 kDa nuclear cap-binding protein;
DE Short=CBP80;
DE Short=NCBP 80 kDa subunit;
GN Name=ncbp-1; Synonyms=cbp-80; ORFNames=F37E3.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=16207815; DOI=10.1091/mbc.e05-07-0622;
RA Lall S., Piano F., Davis R.E.;
RT "Caenorhabditis elegans decapping proteins: localization and functional
RT analysis of Dcp1, Dcp2, and DcpS during embryogenesis.";
RL Mol. Biol. Cell 16:5880-5890(2005).
CC -!- FUNCTION: Component of the cap-binding complex (CBC), which binds
CC cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in
CC various processes such as pre-mRNA splicing and RNA-mediated gene
CC silencing (RNAi). The CBC complex is involved in miRNA-mediated RNA
CC interference and is required for primary microRNAs (miRNAs) processing.
CC In the CBC complex, ncbp-1 does not bind directly capped RNAs (m7GpppG-
CC capped RNA) but is required to stabilize the movement of the N-terminal
CC loop of ncbp-2 and lock the CBC into a high affinity cap-binding state
CC with the cap structure (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a
CC heterodimer composed of ncbp-1 and ncbp-1 that interacts with m7GpppG-
CC capped RNA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Lethality in 63% of embryos.
CC {ECO:0000269|PubMed:16207815}.
CC -!- SIMILARITY: Belongs to the NCBP1 family. {ECO:0000305}.
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DR EMBL; FO081318; CCD70767.1; -; Genomic_DNA.
DR PIR; T15197; T15197.
DR RefSeq; NP_491850.2; NM_059449.5.
DR AlphaFoldDB; O01763; -.
DR SMR; O01763; -.
DR BioGRID; 37798; 4.
DR ComplexPortal; CPX-957; Nuclear cap-binding complex.
DR STRING; 6239.F37E3.1; -.
DR EPD; O01763; -.
DR PaxDb; O01763; -.
DR PeptideAtlas; O01763; -.
DR EnsemblMetazoa; F37E3.1.1; F37E3.1.1; WBGene00018156.
DR GeneID; 172345; -.
DR KEGG; cel:CELE_F37E3.1; -.
DR UCSC; F37E3.1; c. elegans.
DR CTD; 172345; -.
DR WormBase; F37E3.1; CE29793; WBGene00018156; ncbp-1.
DR eggNOG; KOG1104; Eukaryota.
DR GeneTree; ENSGT00390000001733; -.
DR HOGENOM; CLU_013207_0_0_1; -.
DR InParanoid; O01763; -.
DR OMA; QPFKIPF; -.
DR OrthoDB; 270650at2759; -.
DR PhylomeDB; O01763; -.
DR Reactome; R-CEL-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR Reactome; R-CEL-113418; Formation of the Early Elongation Complex.
DR Reactome; R-CEL-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-CEL-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-CEL-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-CEL-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-CEL-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-CEL-6803529; FGFR2 alternative splicing.
DR Reactome; R-CEL-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-CEL-72086; mRNA Capping.
DR Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-CEL-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-CEL-72187; mRNA 3'-end processing.
DR Reactome; R-CEL-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-CEL-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR Reactome; R-CEL-77595; Processing of Intronless Pre-mRNAs.
DR Reactome; R-CEL-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-CEL-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:O01763; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00018156; Expressed in embryo and 4 other tissues.
DR GO; GO:0005845; C:mRNA cap binding complex; IBA:GO_Central.
DR GO; GO:0005846; C:nuclear cap binding complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IC:ComplexPortal.
DR GO; GO:0031124; P:mRNA 3'-end processing; IC:ComplexPortal.
DR GO; GO:0006406; P:mRNA export from nucleus; IC:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:ComplexPortal.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IC:ComplexPortal.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IBA:GO_Central.
DR GO; GO:0031053; P:primary miRNA processing; IDA:ComplexPortal.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027159; CBP80.
DR InterPro; IPR015172; MIF4G-like_typ-1.
DR InterPro; IPR015174; MIF4G-like_typ-2.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR PANTHER; PTHR12412; PTHR12412; 1.
DR Pfam; PF02854; MIF4G; 1.
DR Pfam; PF09088; MIF4G_like; 1.
DR Pfam; PF09090; MIF4G_like_2; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
PE 3: Inferred from homology;
KW mRNA capping; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW RNA-mediated gene silencing.
FT CHAIN 1..798
FT /note="Nuclear cap-binding protein subunit 1"
FT /id="PRO_0000385244"
FT DOMAIN 28..241
FT /note="MIF4G"
FT REGION 663..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 798 AA; 92527 MW; BECD4EA1AE8FE63C CRC64;
MSRRRQFDDE DEVQMKRRRG APLIEDVEKK LQGVIGKVGE NTGSSIECNL DKLTAFLHDD
LEKYRASIID IIAGCAIYLP NRVTVYTTLV GLLNSKNFNF GGDVVEKLIS EQQDLLSKQK
YQEAQNLAIF LCDLGNSGVL TAQSIGEYLE SFIAAAFEEN MPQVRNDYYI QTVLRCLPWI
GKELTEKAPE QMENIGEAIG KYLELRNKNH VALLQVWREG STDQKQEDYL ESLSAQIEAL
RNADWVENHI PRHYSGFETT LQDALQHNLP SFQSPEHTSD MIYPYPLVVF RLFQDADCSA
FSSKPLPGDS SIDRFLFEGE IAWIIEKNQF NRKACARELL AFAEENPSVP IGFLIFETIF
GQMLRLPHAP YPAIFHCSLV LELLKLKPDD YPQILVQTVE CIYRRADSMQ PVCIDRMVDW
FSFHLSNFQY RYTWTDWKDC LNKDAFSGSQ IFVREVIEKC RRFGSYEKII AALPQDFVKI
HPCSPEVRYL IDEEDTALVQ RAETFTQMFQ ERQPAEAFLN ELKSNDENDE LPYNINEFGL
FVMVMLKMAS KTYSHNFSAL FRYQTTLKTV CDASELYQEK LLETLYSCWK TNQQMLMILT
DKLLKMQVID CSAVVGWLFD EKMWQEHDRQ WLFEVLNQAL EKLTRQINVV EKDIKELTEK
TENKIKEEDD EESDIKMDED ETKEEKFKQD LEDLENNKEK LERMVTFQKG LFNDFLIAFI
EEIKNAATSN TSEMDGSGDT PGTQTPKFMW LRGRFCHVLL AHAETLLKHS SNIADEVFSE
GTDPSIIECF NQFQSLRL
