NCBP1_SCHPO
ID NCBP1_SCHPO Reviewed; 780 AA.
AC O14253;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 127.
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=cbc1; ORFNames=SPAC6G10.07;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Component of the CBC complex, which binds cotranscriptionally
CC to the 5'-cap of pre-mRNAs and is involved in maturation, export and
CC degradation of nuclear mRNAs. {ECO:0000250|UniProtKB:P34160}.
CC -!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a
CC heterodimer composed of cbc1 and cbc2 that interacts with capped RNAs.
CC {ECO:0000250|UniProtKB:P34160}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P34160}. Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the NCBP1 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11293.1; -; Genomic_DNA.
DR PIR; T39057; T39057.
DR RefSeq; NP_594104.1; NM_001019528.2.
DR AlphaFoldDB; O14253; -.
DR SMR; O14253; -.
DR BioGRID; 279013; 11.
DR STRING; 4896.SPAC6G10.07.1; -.
DR iPTMnet; O14253; -.
DR MaxQB; O14253; -.
DR PaxDb; O14253; -.
DR PRIDE; O14253; -.
DR EnsemblFungi; SPAC6G10.07.1; SPAC6G10.07.1:pep; SPAC6G10.07.
DR GeneID; 2542556; -.
DR KEGG; spo:SPAC6G10.07; -.
DR PomBase; SPAC6G10.07; cbc1.
DR VEuPathDB; FungiDB:SPAC6G10.07; -.
DR eggNOG; KOG1104; Eukaryota.
DR HOGENOM; CLU_013816_0_0_1; -.
DR InParanoid; O14253; -.
DR OMA; NWFRSAL; -.
DR PhylomeDB; O14253; -.
DR Reactome; R-SPO-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SPO-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-SPO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-SPO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-72086; mRNA Capping.
DR Reactome; R-SPO-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-SPO-72187; mRNA 3'-end processing.
DR Reactome; R-SPO-77595; Processing of Intronless Pre-mRNAs.
DR Reactome; R-SPO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:O14253; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0005845; C:mRNA cap binding complex; IBA:GO_Central.
DR GO; GO:0005846; C:nuclear cap binding complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; ISO:PomBase.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IC:PomBase.
DR GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:PomBase.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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 Cytoplasm; mRNA processing; mRNA splicing; mRNA transport; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Transport.
FT CHAIN 1..780
FT /note="Nuclear cap-binding protein subunit 1"
FT /id="PRO_0000373992"
FT DOMAIN 34..249
FT /note="MIF4G"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 780 AA; 90078 MW; 6AAA6562287F74F7 CRC64;
MSSYRGSTRP RKRTREGENY GFRPHRGNSQ ELLAARIKKD ITFLADPRGN SVAADDINYV
AMSLSREAND PETISTILDC IQTTAFIIPV KIPHLATLII RASLRVPLIL EKAAAYFCLQ
YFTNLNSFLY YEAKVDLRML ICMSFALQPG TLKPLFSLLA DAISKETKPS VWGDNFLRII
LINLPYFIAA NNDLGKKDFA NEILDQCEIY VRHRKSSITL SNPLSIHDNL SEEELDLLYK
QLILSRENDF TFPYISQPWK FFESDFVHIV PVSPSIPEWT FQPTPQQNEL PSFKRFFELF
NNFEIRTTPD ASDVAASIFR DISVDVINHL EFNRVEAAQV LTDLDVYFTY KTFALRGTPV
NELPNLDPSE SRWKAEDIIV EAVLGELLGS QNTTYKPVYY HSLLIECCRI APKILAPTFG
RVIRLMYTMS SDLPLQTLDR FIDWFSHHLS NFNFHWKWNE WIPDVELDDL HPKKVFMRET
ITRELILSYY TRISDSLPEE LRCLLGEQPS GPNFVYENET HPLYQQSSQI IEALRLHKPL
EELDIILQSE EIQNSETSAV RLVMSCAYSL GSRSFSHALN VFEKHLNTLK HFSRKSLDSE
IEVVDELFSF WKLQPFNAVM WLDKMLNYSI ISITSIIEWL IKQDVTIWSR SYTWSLVNTT
FNKLAARLRR SVSNKEDSSL INEANEEKEI VTNLLLSALR ALISENAENI WVSHWLNLML
KYVESNFLSV KKDTIEEANE PVQENTSEEQ EDTKMQPVDA VDEQPSENNQ TAADATNEEK
