NCBP1_DICDI
ID NCBP1_DICDI Reviewed; 772 AA.
AC Q55D17;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=ncbp1; Synonyms=cbp80; ORFNames=DDB_G0269814;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(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, ncbp1 does not bind directly capped RNAs (m7GpppG-
CC capped RNA) but is required to stabilize the movement of the N-terminal
CC loop of ncbp2 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 ncbp1 and ncbp2 that interacts with m7GpppG-
CC capped RNA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NCBP1 family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72257.1; -; Genomic_DNA.
DR RefSeq; XP_646314.1; XM_641222.1.
DR AlphaFoldDB; Q55D17; -.
DR SMR; Q55D17; -.
DR STRING; 44689.DDB0233457; -.
DR PaxDb; Q55D17; -.
DR EnsemblProtists; EAL72257; EAL72257; DDB_G0269814.
DR GeneID; 8617269; -.
DR KEGG; ddi:DDB_G0269814; -.
DR dictyBase; DDB_G0269814; ncbp1.
DR eggNOG; KOG1104; Eukaryota.
DR HOGENOM; CLU_013207_0_0_1; -.
DR InParanoid; Q55D17; -.
DR OMA; NWFRSAL; -.
DR PhylomeDB; Q55D17; -.
DR Reactome; R-DDI-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR Reactome; R-DDI-113418; Formation of the Early Elongation Complex.
DR Reactome; R-DDI-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DDI-6803529; FGFR2 alternative splicing.
DR Reactome; R-DDI-72086; mRNA Capping.
DR Reactome; R-DDI-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DDI-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-DDI-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-DDI-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR Reactome; R-DDI-77595; Processing of Intronless Pre-mRNAs.
DR Reactome; R-DDI-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-DDI-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:Q55D17; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005845; C:mRNA cap binding complex; IBA:GO_Central.
DR GO; GO:0005846; C:nuclear cap binding complex; ISS:dictyBase.
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:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:dictyBase.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IBA:GO_Central.
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..772
FT /note="Nuclear cap-binding protein subunit 1"
FT /id="PRO_0000385245"
FT DOMAIN 37..249
FT /note="MIF4G"
FT REGION 1..31
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 772 AA; 88630 MW; 6F7E722B50FD35FA CRC64;
MAYQNNGGNF RGPRHSFNGQ PSGRGNFQRH DPEEDFKSKL TSLIVRIGDK ATSSLESNID
ALANALLADI PKQSSLIQDI LFKCVSSLTY KTPIYATLVG LINVKNSEFG KEVVCRLVDE
IFSAMEKKKF HNAKLLIRFI PELVNANVLT INAIFELYET LLSVLNTSDY TPNKADYFVF
LVLSTIPWIG EHLSHNHSGQ LDAVIEECES YIQSRSTGDK KFYQAYNNGY TDDRLESMLK
QIKSLRDCDQ PWIVNGILRP YKHFNETLTS SSSQQHILPT IHFPEDEKLE YPNNLNKPLF
RVLSNDNNNS VERYIVEDYI IDILSFFNSD HKECSKFIYS LPVENEIDDI VVETILGEMF
MLPEPTFKPI YYSVLFVDFF KSQPSVIPVF AYAINLLFEN IHKLDFEVMD RFALAFAHHL
SNFDYKWIWS DWAQSLVPPT AAAAAAAATT TVEGSTSNEN KEDSTATTTA IIEDENQIRN
RELRIIYIKR VLSSLCRLSY LEKIKQNLPS EYHQYLPPSP APTFKFLNAD NPEEESKELI
AESHKLLLSF KTKEPLENII SHVANIPSHI NIVELLTKCI LQIGSTSFSH LTYAIERYIT
LFKTVLKSQD DRQECIRSIF EFWKLSHQHI VIVVDKFVTF KIIYPIDTVT WFMKPENIDR
FITEPFTWEC LHNSIQKTII IIQTLTLDLE ENQSQEKEFK LNTSISEQQL LLAELVKGLG
SILSSEKYQL GASSKLLISG QLKSIIRKYF NQMKPVIQSQ PQLSNIINQY TQ
