CPSF2_DROME
ID CPSF2_DROME Reviewed; 756 AA.
AC Q9V3D6; Q8IML7;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Probable cleavage and polyadenylation specificity factor subunit 2;
DE AltName: Full=Cleavage and polyadenylation specificity factor 100 kDa subunit;
DE Short=CPSF 100 kDa subunit;
GN Name=Cpsf100; ORFNames=CG1957;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221 AND THR-226, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE CPSF COMPLEX, AND INTERACTION WITH SYM;
RP CPSF73; SLBP AND LSM11.
RX PubMed=19450530; DOI=10.1016/j.molcel.2009.04.024;
RA Sullivan K.D., Steiniger M., Marzluff W.F.;
RT "A core complex of CPSF73, CPSF100, and Symplekin may form two different
RT cleavage factors for processing of poly(A) and histone mRNAs.";
RL Mol. Cell 34:322-332(2009).
CC -!- FUNCTION: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex that plays a key role in pre-mRNA 3'-end
CC formation, recognizing the AAUAAA signal sequence and interacting with
CC poly(A) polymerase and other factors to bring about cleavage and
CC poly(A) addition. Required for the cotranscriptional processing of 3'-
CC ends of polyadenylated and histone pre-mRNA.
CC {ECO:0000269|PubMed:19450530}.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex, composed of at least Clp, Cpsf73, Cpsf100 and
CC Cpsf160. Interacts with Sym and Cpsf73 forming a core cleavage factor
CC required for both polyadenylated and histone mRNA processing. Interacts
CC with Slbp and Lsm11. {ECO:0000269|PubMed:19450530}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE014297; AAF56844.1; -; Genomic_DNA.
DR EMBL; AF160933; AAD46873.1; -; mRNA.
DR RefSeq; NP_651658.1; NM_143401.3.
DR AlphaFoldDB; Q9V3D6; -.
DR SMR; Q9V3D6; -.
DR BioGRID; 68297; 11.
DR IntAct; Q9V3D6; 4.
DR MINT; Q9V3D6; -.
DR STRING; 7227.FBpp0084726; -.
DR iPTMnet; Q9V3D6; -.
DR PaxDb; Q9V3D6; -.
DR PRIDE; Q9V3D6; -.
DR DNASU; 43426; -.
DR EnsemblMetazoa; FBtr0085357; FBpp0084726; FBgn0027873.
DR GeneID; 43426; -.
DR KEGG; dme:Dmel_CG1957; -.
DR UCSC; CG1957-RA; d. melanogaster.
DR CTD; 43426; -.
DR FlyBase; FBgn0027873; Cpsf100.
DR VEuPathDB; VectorBase:FBgn0027873; -.
DR eggNOG; KOG1135; Eukaryota.
DR GeneTree; ENSGT00910000144260; -.
DR HOGENOM; CLU_002227_1_1_1; -.
DR InParanoid; Q9V3D6; -.
DR OMA; MELVENC; -.
DR OrthoDB; 1314980at2759; -.
DR PhylomeDB; Q9V3D6; -.
DR Reactome; R-DME-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DME-72187; mRNA 3'-end processing.
DR Reactome; R-DME-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-DME-77595; Processing of Intronless Pre-mRNAs.
DR SignaLink; Q9V3D6; -.
DR BioGRID-ORCS; 43426; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43426; -.
DR PRO; PR:Q9V3D6; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0027873; Expressed in embryonic/larval hemocyte (Drosophila) and 39 other tissues.
DR Genevisible; Q9V3D6; DM.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IMP:FlyBase.
DR GO; GO:0006378; P:mRNA polyadenylation; IMP:FlyBase.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
DR CDD; cd16293; CPSF2-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR027075; CPSF2.
DR InterPro; IPR025069; Cpsf2_C.
DR InterPro; IPR035639; CPSF2_MBL.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR PANTHER; PTHR45922; PTHR45922; 1.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF13299; CPSF100_C; 1.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..756
FT /note="Probable cleavage and polyadenylation specificity
FT factor subunit 2"
FT /id="PRO_0000074397"
FT MOD_RES 221
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 226
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 756 AA; 85418 MW; E391D61CFA1DD821 CRC64;
MTSIIKLHTI SGAMDESPPC YILQIDDVRI LLDCGWDEKF DANFIKELKR QVHTLDAVLL
SHPDAYHLGA LPYLVGKLGL NCPIYATIPV FKMGQMFMYD LYMSHFNMGD FDLFSLDDVD
TAFEKITQLK YNQTVSLKDK GYGISITPLN AGHMIGGTIW KIVKVGEEDI VYATDFNHKK
ERHLSGCELD RLQRPSLLIT DAYNAQYQQA RRRARDEKLM TNILQTVRNN GNVLIAVDTA
GRVLELAHML DQLWKNKESG LMAYSLALLN NVSYNVIEFA KSQIEWMSDK LTKAFEGARN
NPFQFKHIQL CHSLADVYKL PAGPKVVLAS TPDLESGFTR DLFVQWASNA NNSIILTTRT
SPGTLAMELV ENCAPGKQIE LDVRRRVDLE GAELEEYLRT QGEKLNPLIV KPDVEEESSS
ESEDDIEMSV ITGKHDIVVR PEGRHHSGFF KSNKRHHVMF PYHEEKVKCD EYGEIINLDD
YRIADATGYE FVPMEEQNKE NVKKEEPGIG AEQQANGGIV DNDVQLLEKP TKLISQRKTI
EVNAQVQRID FEGRSDGESM LKILSQLRPR RVIVIHGTAE GTQVVARHCE QNVGARVFTP
QKGEIIDVTS EIHIYQVRLT EGLVSQLQFQ KGKDAEVAWV DGRLGMRVKA IEAPMDVTVE
QDASVQEGKT LTLETLADDE IPIHNSVLIN ELKLSDFKQT LMRNNINSEF SGGVLWCSNG
TLALRRVDAG KVAMEGCLSE EYYKIRELLY EQYAIV
