NCBP1_YEAST
ID NCBP1_YEAST Reviewed; 861 AA.
AC P34160; D6VZU8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Nuclear cap-binding protein complex subunit 1;
DE AltName: Full=80 kDa nuclear cap-binding protein;
DE Short=CBP80;
DE Short=NCBP 80 kDa subunit;
DE AltName: Full=Glycolysis regulation protein 3;
DE AltName: Full=Protein SUT1;
DE AltName: Full=Suppressor of TOP1 protein;
GN Name=STO1; Synonyms=CBC1, CBP80, GCR3, SUT1; OrderedLocusNames=YMR125W;
GN ORFNames=YM8564.07, YM9553.01;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1512188; DOI=10.1128/jb.174.17.5526-5532.1992;
RA Uemura H., Jigami Y.;
RT "GCR3 encodes an acidic protein that is required for expression of
RT glycolytic genes in Saccharomyces cerevisiae.";
RL J. Bacteriol. 174:5526-5532(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=8846890; DOI=10.1093/genetics/142.4.1095;
RA Uemura H., Pandit S., Jigami Y., Sternglanz R.;
RT "Mutations in GCR3, a gene involved in the expression of glycolytic genes
RT in Saccharomyces cerevisiae, suppress the temperature-sensitive growth of
RT hpr1 mutants.";
RL Genetics 142:1095-1103(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION OF INTRON, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10733586; DOI=10.1128/mcb.20.8.2827-2838.2000;
RA Das B., Guo Z., Russo P., Chartrand P., Sherman F.;
RT "The role of nuclear cap binding protein Cbc1p of yeast in mRNA termination
RT and degradation.";
RL Mol. Cell. Biol. 20:2827-2838(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN THE CBC AND SRP1-CBC COMPLEXES,
RP U SNRNA-BINDING, SUBCELLULAR LOCATION, AND FUNCTION OF THE CBC AND SRP1-CBC
RP COMPLEXES.
RX PubMed=8858145; DOI=10.1016/s0092-8674(00)81319-7;
RA Goerlich D., Kraft R., Kostka S., Vogel F., Hartmann E., Laskey R.A.,
RA Mattaj I.W., Izaurraide E.;
RT "Importin provides a link between nuclear protein import and U snRNA
RT export.";
RL Cell 87:21-32(1996).
RN [7]
RP FUNCTION OF THE CBC COMPLEX.
RX PubMed=8811086; DOI=10.1093/nar/24.17.3332;
RA Lewis J.D., Goerlich D., Mattaj I.W.;
RT "A yeast cap binding protein complex (yCBC) acts at an early step in pre-
RT mRNA splicing.";
RL Nucleic Acids Res. 24:3332-3336(1996).
RN [8]
RP FUNCTION.
RX PubMed=9499403; DOI=10.1101/gad.12.5.679;
RA Shen E.C., Henry M.F., Weiss V.H., Valentini S.R., Silver P.A., Lee M.S.;
RT "Arginine methylation facilitates the nuclear export of hnRNP proteins.";
RL Genes Dev. 12:679-691(1998).
RN [9]
RP INTERACTION WITH PRE-MRNA IN THE COMMITMENT COMPLEX.
RX PubMed=10072386; DOI=10.1101/gad.13.5.581;
RA Zhang D., Rosbash M.;
RT "Identification of eight proteins that cross-link to pre-mRNA in the yeast
RT commitment complex.";
RL Genes Dev. 13:581-592(1999).
RN [10]
RP INTERACTION WITH MUD2 AND SNU56, AND FUNCTION OF THE CBC COMPLEX.
RX PubMed=10490594; DOI=10.1128/mcb.19.10.6543;
RA Fortes P., Kufel J., Fornerod M., Polycarpou-Schwarz M., Lafontaine D.,
RA Tollervey D., Mattaj I.W.;
RT "Genetic and physical interactions involving the yeast nuclear cap-binding
RT complex.";
RL Mol. Cell. Biol. 19:6543-6553(1999).
RN [11]
RP IDENTIFICATION IN THE CBC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP INTERACTION OF THE COMPLEX WITH CAPPED RNA.
RX PubMed=10504710; DOI=10.1038/13732;
RA Rigaut G., Shevchenko A., Rutz B., Wilm M., Mann M., Seraphin B.;
RT "A generic protein purification method for protein complex characterization
RT and proteome exploration.";
RL Nat. Biotechnol. 17:1030-1032(1999).
RN [12]
RP DOMAIN.
RX PubMed=10958635; DOI=10.1101/gr.10.8.1172;
RA Aravind L., Koonin E.V.;
RT "Eukaryote-specific domains in translation initiation factors: implications
RT for translation regulation and evolution of the translation system.";
RL Genome Res. 10:1172-1184(2000).
RN [13]
RP INTERACTION WITH NPL3, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10823828; DOI=10.1074/jbc.m002312200;
RA Shen E.C., Stage-Zimmermann T., Chui P., Silver P.A.;
RT "7The yeast mRNA-binding protein Npl3p interacts with the cap-binding
RT complex.";
RL J. Biol. Chem. 275:23718-23724(2000).
RN [14]
RP INTERACTION WITH EIF4G.
RX PubMed=10949040; DOI=10.1016/s1097-2765(05)00003-1;
RA Fortes P., Inada T., Preiss T., Hentze M.W., Mattaj I.W., Sachs A.B.;
RT "The yeast nuclear cap binding complex can interact with translation factor
RT eIF4G and mediate translation initiation.";
RL Mol. Cell 6:191-196(2000).
RN [15]
RP FUNCTION.
RX PubMed=12897126; DOI=10.1128/mcb.23.16.5502-5515.2003;
RA Das B., Butler J.S., Sherman F.;
RT "Degradation of normal mRNA in the nucleus of Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 23:5502-5515(2003).
RN [16]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [17]
RP FUNCTION.
RX PubMed=14671320; DOI=10.1073/pnas.2536857100;
RA Kushner D.B., Lindenbach B.D., Grdzelishvili V.Z., Noueiry A.O., Paul S.M.,
RA Ahlquist P.;
RT "Systematic, genome-wide identification of host genes affecting replication
RT of a positive-strand RNA virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15764-15769(2003).
RN [18]
RP FUNCTION OF THE CBC COMPLEX.
RX PubMed=12756324; DOI=10.1261/rna.5100903;
RA Baron-Benhamou J., Fortes P., Inada T., Preiss T., Hentze M.W.;
RT "The interaction of the cap-binding complex (CBC) with eIF4G is dispensable
RT for translation in yeast.";
RL RNA 9:654-662(2003).
RN [19]
RP FUNCTION.
RX PubMed=15753296; DOI=10.1073/pnas.0500684102;
RA Gao Q., Das B., Sherman F., Maquat L.E.;
RT "Cap-binding protein 1-mediated and eukaryotic translation initiation
RT factor 4E-mediated pioneer rounds of translation in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4258-4263(2005).
RN [20]
RP FUNCTION.
RX PubMed=16166263; DOI=10.1073/pnas.0506518102;
RA Kuai L., Das B., Sherman F.;
RT "A nuclear degradation pathway controls the abundance of normal mRNAs in
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13962-13967(2005).
RN [21]
RP IDENTIFICATION IN THE CBC COMPLEX, INTERACTION WITH SRP1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16729021; DOI=10.1038/sj.embor.7400702;
RA Hernandez H., Dziembowski A., Taverner T., Seraphin B., Robinson C.V.;
RT "Subunit architecture of multimeric complexes isolated directly from
RT cells.";
RL EMBO Rep. 7:605-610(2006).
RN [22]
RP IDENTIFICATION IN NRD1 COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16427013; DOI=10.1016/j.molcel.2005.11.028;
RA Vasiljeva L., Buratowski S.;
RT "Nrd1 interacts with the nuclear exosome for 3' processing of RNA
RT polymerase II transcripts.";
RL Mol. Cell 21:239-248(2006).
CC -!- FUNCTION: Component of the CBC complex, which binds co-
CC transcriptionally to the 5'-cap of pre-mRNAs and is involved in
CC maturation, export and degradation of nuclear mRNAs. The CBC complex is
CC required for efficient pre-mRNA splicing through efficient commitment
CC complex and spliceosome formation. Together with NPL3, the CBC complex
CC is required for export of mRNAs out of the nucleus. The CBC complex is
CC also involved in nuclear mRNA degradation, probably by directing the
CC mRNAs to the sites of degradation. Affects replication of the positive-
CC strand RNA virus BMV. {ECO:0000269|PubMed:10490594,
CC ECO:0000269|PubMed:10733586, ECO:0000269|PubMed:10823828,
CC ECO:0000269|PubMed:12756324, ECO:0000269|PubMed:12897126,
CC ECO:0000269|PubMed:14671320, ECO:0000269|PubMed:1512188,
CC ECO:0000269|PubMed:15753296, ECO:0000269|PubMed:16166263,
CC ECO:0000269|PubMed:8811086, ECO:0000269|PubMed:8846890,
CC ECO:0000269|PubMed:8858145, ECO:0000269|PubMed:9499403}.
CC -!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a
CC heterodimer composed of STO1/CBC1 and CBC2 that interacts with capped
CC RNAs. The complex interacts strongly with the importin subunit alpha
CC SRP1. The SRP1-CBC trimer also binds to capped RNAs, but formation of
CC the importin alpha/beta heterodimer upon binding of KAP95 to SRP1 in
CC the cytoplasm causes dissociation of CBC from the RNA. The CBC complex
CC is part of the commitment complex 1 (CC1), binding to the cap of pre-
CC mRNA and interacting with U1 snRNP subunits MUD2 and SNU56. The CBC
CC complex is part of the NRD1 complex, composed of CBC2, NAB1, NRD1, SEN1
CC and STO1/CBC2. The CBC complex also interacts with NPL3 and eIF4G
CC (TIF4631 and TIF4632). {ECO:0000269|PubMed:10072386,
CC ECO:0000269|PubMed:10490594, ECO:0000269|PubMed:10504710,
CC ECO:0000269|PubMed:10823828, ECO:0000269|PubMed:10949040,
CC ECO:0000269|PubMed:16427013, ECO:0000269|PubMed:16729021,
CC ECO:0000269|PubMed:8858145}.
CC -!- INTERACTION:
CC P34160; Q08920: CBC2; NbExp=5; IntAct=EBI-745, EBI-33556;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10733586,
CC ECO:0000269|PubMed:10823828, ECO:0000269|PubMed:8858145}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:10823828}. Note=Predominantly
CC nuclear, is able to exit the nucleus in an RNA-dependent manner.
CC {ECO:0000269|PubMed:10823828}.
CC -!- MISCELLANEOUS: Present with 11300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: In contrast to metazoans, where the CBC complex is
CC involved in the nuclear export of capped U snRNAs, it is believed that
CC in yeast, U snRNAs are not exported from the nucleus and U snRNPs are
CC assembled in the nucleus from RNAs and imported proteins.
CC -!- SIMILARITY: Belongs to the NCBP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA01076.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=L27744; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D10224; BAA01076.1; ALT_SEQ; Genomic_DNA.
DR EMBL; L07650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L27744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z49273; CAA89274.1; -; Genomic_DNA.
DR EMBL; Z48622; CAA88550.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10022.1; -; Genomic_DNA.
DR PIR; A44919; A44919.
DR RefSeq; NP_013844.2; NM_001182626.1.
DR PDB; 3UKY; X-ray; 2.35 A; C=1-30.
DR PDB; 6N7P; EM; 3.60 A; X=1-861.
DR PDBsum; 3UKY; -.
DR PDBsum; 6N7P; -.
DR AlphaFoldDB; P34160; -.
DR SMR; P34160; -.
DR BioGRID; 35302; 200.
DR ComplexPortal; CPX-1657; Nuclear cap-binding complex.
DR DIP; DIP-4434N; -.
DR IntAct; P34160; 52.
DR MINT; P34160; -.
DR STRING; 4932.YMR125W; -.
DR iPTMnet; P34160; -.
DR MaxQB; P34160; -.
DR PaxDb; P34160; -.
DR PRIDE; P34160; -.
DR EnsemblFungi; YMR125W_mRNA; YMR125W; YMR125W.
DR GeneID; 855155; -.
DR KEGG; sce:YMR125W; -.
DR SGD; S000004732; STO1.
DR VEuPathDB; FungiDB:YMR125W; -.
DR eggNOG; KOG1104; Eukaryota.
DR GeneTree; ENSGT00390000001733; -.
DR HOGENOM; CLU_011380_0_0_1; -.
DR InParanoid; P34160; -.
DR OMA; QPFKIPF; -.
DR BioCyc; YEAST:G3O-32818-MON; -.
DR Reactome; R-SCE-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-72086; mRNA Capping.
DR Reactome; R-SCE-77595; Processing of Intronless Pre-mRNAs.
DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P34160; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P34160; protein.
DR GO; GO:0000243; C:commitment complex; IPI:SGD.
DR GO; GO:0005845; C:mRNA cap binding complex; IPI:ComplexPortal.
DR GO; GO:0005846; C:nuclear cap binding complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IPI:SGD.
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:0031124; P:mRNA 3'-end processing; IMP:ComplexPortal.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:ComplexPortal.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IMP:ComplexPortal.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:ComplexPortal.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:SGD.
DR GO; GO:0031053; P:primary miRNA processing; IC:ComplexPortal.
DR GO; GO:0006970; P:response to osmotic stress; IDA:ComplexPortal.
DR IDEAL; IID50172; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; mRNA capping;
KW mRNA processing; mRNA splicing; mRNA transport;
KW Nonsense-mediated mRNA decay; Nucleus; Reference proteome; RNA-binding;
KW Transport.
FT CHAIN 1..861
FT /note="Nuclear cap-binding protein complex subunit 1"
FT /id="PRO_0000087447"
FT DOMAIN 36..264
FT /note="MIF4G"
FT MOTIF 22..30
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT CONFLICT 164
FT /note="D -> V (in Ref. 3; L27744)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="R -> I (in Ref. 3; L27744)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="A -> R (in Ref. 3; L27744)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 861 AA; 100018 MW; EDD04907BDC9207D CRC64;
MFNRKRRGDF DEDENYRDFR PRMPKRQRIP PVVQLCKEMM PDIRTIGESV KAFEDDIKFL
SEAIMNEYGH EDYFNNALLS TLNAVVVEQP QKQAAIALLT MVVNSKNNVA GKSIINYFFE
ELQKWCKQTY NDEFKSTSNE TGPWNKIKLI LRFLSILSPM FLVDELINIY KSLFELSIEL
NNLDPGNRVP LSEAIYTNTL LNIPYLFFFN RNNDGLRTKV EELLAYVEQN YLVKTTDINL
LREYNGEPPY EMVELVRVVL PNVKKALINN LEQLNELFPD WNHLLTPQTG DEGFNDALTL
PSVDDLKSFV RLNKNFGSVD SMWKTPRYAF HVYLPNSAGN FETVVPISTY AGQLFNDIII
DLVESLEFNR KEVARQVITL DLFFKAGIFT EPGESIAQLI ATYEENPLAP TFKIEDLAIE
TILGLIFKLP SVSQPFAYFY TLLVDICQNS PKAIAPVFGR AFRFFYSHLD SLDFELKLRY
LDWFSIQMSN FNFSWKWNEW EDDSIKFGKY FYNPKVNFAK NLIQKELRLT SNFSEVEDSL
PQEFTKYLDT SYIPRDQLIN YYQSLFTGYT VEEDSVRKND LYFRQEGVPM ENTVRKILDY
THKANNSREV TELESILGEL KNEYGSIISD FNRFVIILLV QAVTDSGSRS LSHANKYIND
LKEDLKTIFA KIELDIETKE YIIIEAVLTF WNANPQTGFL VADAFKYAGL LTSRTIFTFI
FNETGLKNNG LIEATAIEAV FRNLSQQISE ENESGNNFEF VFERLCTIAN STIDLLDVNA
DEDIEIPKVN GEMDIDDIED DKLDLKWKYF TVIGFIKSIL RRYSHEYREL ADKFIANIDN
AIPHESTRRT ISNWIQETKE V
