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NCBP2_ORYSJ
ID   NCBP2_ORYSJ             Reviewed;         243 AA.
AC   Q84L14; A0A0P0VLM0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 124.
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=CBP20; OrderedLocusNames=Os02g0612300, LOC_Os02g39890;
GN   ORFNames=OJ1004_A05.24;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Nipponbare;
RA   Kmieciak M., Rogowski A., Jarmolowski A.;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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 and RNA-mediated gene silencing
CC       (RNAi) by microRNAs (miRNAs). The CBC complex is involved in miRNA-
CC       mediated RNA interference and is required for primary miRNA processing.
CC       In the CBC complex, CBP20 recognizes and binds capped RNAs (m7GpppG-
CC       capped RNA) but requires ABH1/CBP80 to stabilize the movement of its N-
CC       terminal loop and lock the CBC into a high affinity cap-binding state
CC       with the cap structure. CBP20 also plays a role in stabilization of
CC       ABH1/CBP80 and ABH1/CBP80 localization to the nucleus (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a
CC       heterodimer composed of ABH1/CBP80 and CBP20 that interacts with
CC       m7GpppG-capped RNA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Predominantly nuclear. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RRM NCBP2 family. {ECO:0000305}.
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DR   EMBL; AY278997; AAP33448.1; -; mRNA.
DR   EMBL; AP005286; BAD19690.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF09326.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS79728.1; -; Genomic_DNA.
DR   EMBL; AK101546; BAG95116.1; -; mRNA.
DR   RefSeq; XP_015625308.1; XM_015769822.1.
DR   AlphaFoldDB; Q84L14; -.
DR   SMR; Q84L14; -.
DR   STRING; 4530.OS02T0612300-01; -.
DR   iPTMnet; Q84L14; -.
DR   PaxDb; Q84L14; -.
DR   PRIDE; Q84L14; -.
DR   EnsemblPlants; Os02t0612300-01; Os02t0612300-01; Os02g0612300.
DR   GeneID; 4329963; -.
DR   Gramene; Os02t0612300-01; Os02t0612300-01; Os02g0612300.
DR   KEGG; osa:4329963; -.
DR   eggNOG; KOG0121; Eukaryota.
DR   HOGENOM; CLU_070952_0_0_1; -.
DR   InParanoid; Q84L14; -.
DR   OMA; APPQYDR; -.
DR   OrthoDB; 1421503at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q84L14; OS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005845; C:mRNA cap binding complex; IEA:EnsemblPlants.
DR   GO; GO:0005846; C:nuclear cap binding complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR   GO; GO:1901527; P:abscisic acid-activated signaling pathway involved in stomatal movement; IEA:EnsemblPlants.
DR   GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IEA:EnsemblPlants.
DR   GO; GO:0051607; P:defense response to virus; IEA:EnsemblPlants.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0031053; P:primary miRNA processing; IEA:EnsemblPlants.
DR   GO; GO:0000394; P:RNA splicing, via endonucleolytic cleavage and ligation; IEA:EnsemblPlants.
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   Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   RNA-binding; RNA-mediated gene silencing.
FT   CHAIN           1..243
FT                   /note="Nuclear cap-binding protein subunit 2"
FT                   /id="PRO_0000385278"
FT   DOMAIN          34..112
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          120..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         14
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="mRNA cap"
FT                   /evidence="ECO:0000250"
FT   BINDING         37
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="mRNA cap"
FT                   /evidence="ECO:0000250"
FT   BINDING         106..110
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="mRNA cap"
FT                   /evidence="ECO:0000250"
FT   BINDING         117..121
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="mRNA cap"
FT                   /evidence="ECO:0000250"
FT   BINDING         127..128
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="mRNA cap"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   243 AA;  28573 MW;  97FEC73CCA94139F CRC64;
     MASLFKDPTK LSAYRDRRFT GTQEEYEAAL QASVTVYVGN MSFYTTEEQA YELFSRAGEI
     RKIIMGLDKN SKTPCGFCFI LYYSREDAED AVKYISGTML DDRPIRVDFD WGFEEGRQWG
     RGRSGGQVRD EYRTDYDPGR GGYGKMVQKE LEAQRELVDY GGAFQPNAPP QYDRGDRKRG
     YGDSYRNDRD YQRKRYRNDE RSSQRAPDSE FKRDAIDSEK NPRFREKGDS DEEDDDYDKR
     RRR
 
 
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