ID G1MTQ2_MELGA Unreviewed; 164 AA.
AC G1MTQ2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Nuclear cap-binding protein subunit 2 {ECO:0000256|ARBA:ARBA00019878, ECO:0000256|RuleBase:RU364036};
DE AltName: Full=20 kDa nuclear cap-binding protein {ECO:0000256|RuleBase:RU364036};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000001807.2, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000001807.2, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000001807.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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, leading to the recruitment of the mRNA export
CC machinery to the 5' end of mRNA and to mRNA export in a 5' to 3'
CC direction through the nuclear pore. The CBC complex is also involved in
CC mediating U snRNA and intronless mRNAs export from the nucleus. The CBC
CC complex is essential for a pioneer round of mRNA translation, before
CC steady state translation when the CBC complex is replaced by
CC cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA
CC translation mediated by the CBC complex plays a central role in
CC nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs
CC bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex
CC enhances NMD in mRNAs containing at least one exon-junction complex
CC (EJC), promoting the interaction between upf1 and upf2. The CBC complex
CC is also involved in 'failsafe' NMD, which is independent of the EJC
CC complex, while it does not participate in Staufen-mediated mRNA decay
CC (SMD). During cell proliferation, the CBC complex is also involved in
CC microRNAs (miRNAs) biogenesis via its interaction with srrt/ars2,
CC thereby being required for miRNA-mediated RNA interference. The CBC
CC complex also acts as a negative regulator of parn, thereby acting as an
CC inhibitor of mRNA deadenylation. In the CBC complex, ncbp2/cbp20
CC recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires
CC ncbp1/cbp80 to stabilize the movement of its N-terminal loop and lock
CC the CBC into a high affinity cap-binding state with the cap structure.
CC The 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. {ECO:0000256|RuleBase:RU364036}.
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. {ECO:0000256|RuleBase:RU364036}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU364036}.
CC -!- SIMILARITY: Belongs to the RRM NCBP2 family.
CC {ECO:0000256|ARBA:ARBA00010725, ECO:0000256|RuleBase:RU364036}.
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DR AlphaFoldDB; G1MTQ2; -.
DR SMR; G1MTQ2; -.
DR Ensembl; ENSMGAT00000002476.2; ENSMGAP00000001807.2; ENSMGAG00000002257.2.
DR GeneTree; ENSGT00390000003197; -.
DR HOGENOM; CLU_070952_2_0_1; -.
DR InParanoid; G1MTQ2; -.
DR TreeFam; TF313897; -.
DR Proteomes; UP000001645; Chromosome 9.
DR Bgee; ENSMGAG00000002257; Expressed in bursa of Fabricius and 17 other cell types or tissues.
DR GO; GO:0005846; C:nuclear cap binding complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000339; F:RNA cap binding; IEA:InterPro.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
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; 20 KD NUCLEAR CAP BINDING PROTEIN; 1.
DR PANTHER; PTHR18847:SF0; NUCLEAR CAP-BINDING PROTEIN SUBUNIT 2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU364036};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU364036};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364036};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176,
KW ECO:0000256|RuleBase:RU364036};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158}.
FT DOMAIN 39..117
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 164 AA; 18653 MW; 2D24D2F914E92EA5 CRC64;
DSHKPATPRP SSGSSGLCQA QQHQRPPKKL QEKFLKISST LYVGNLSFYT TEEQIQELFS
KCGDVKRIVM GLDKIKKTPC GFCFVEYYTR ADAEHAMRFI NGTRLDDRIV RTDWDAGFKE
GRQYGRGKTG GQVRDEYRTD YDVGRGGFGK IIQMQKANQQ PAVY
//
