CPSF3_DROME
ID CPSF3_DROME Reviewed; 684 AA.
AC Q9VE51;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Cleavage and polyadenylation specificity factor 73 {ECO:0000312|EMBL:AAF55578.2};
DE EC=3.1.27.- {ECO:0000250|UniProtKB:Q9UKF6};
GN Name=Cpsf73; ORFNames=CG7698;
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] {ECO:0000312|EMBL:AAF55578.2}
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] {ECO:0000312|EMBL:AAF55578.2}
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] {ECO:0000312|EMBL:AAM50988.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM50988.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=18042462; DOI=10.1016/j.molcel.2007.10.009;
RA Wagner E.J., Burch B.D., Godfrey A.C., Salzler H.R., Duronio R.J.,
RA Marzluff W.F.;
RT "A genome-wide RNA interference screen reveals that variant histones are
RT necessary for replication-dependent histone pre-mRNA processing.";
RL Mol. Cell 28:692-699(2007).
RN [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE CPSF COMPLEX, AND INTERACTION WITH SYM;
RP CPSF100; 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).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=19854135; DOI=10.1016/j.molcel.2009.08.016;
RA Yang X.C., Burch B.D., Yan Y., Marzluff W.F., Dominski Z.;
RT "FLASH, a proapoptotic protein involved in activation of caspase-8, is
RT essential for 3' end processing of histone pre-mRNAs.";
RL Mol. Cell 36:267-278(2009).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=21078872; DOI=10.1128/mcb.00943-10;
RA Ezzeddine N., Chen J., Waltenspiel B., Burch B., Albrecht T., Zhuo M.,
RA Warren W.D., Marzluff W.F., Wagner E.J.;
RT "A subset of Drosophila integrator proteins is essential for efficient U7
RT snRNA and spliceosomal snRNA 3'-end formation.";
RL Mol. Cell. Biol. 31:328-341(2011).
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. Has endonuclease activity and functions as mRNA 3'-
CC end-processing endonuclease. Required for the cotranscriptional
CC processing of 3'-ends of polyadenylated and histone pre-mRNA.
CC {ECO:0000250|UniProtKB:Q9UKF6, ECO:0000269|PubMed:18042462,
CC ECO:0000269|PubMed:19450530, ECO:0000269|PubMed:19854135,
CC ECO:0000269|PubMed:21078872}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9UKF6};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9UKF6};
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 Cpsf100 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|PubMed:19450530}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. CPSF3 subfamily.
CC {ECO:0000255}.
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DR EMBL; AE014297; AAF55578.2; -; Genomic_DNA.
DR EMBL; AY119128; AAM50988.1; -; mRNA.
DR RefSeq; NP_650738.1; NM_142481.3.
DR AlphaFoldDB; Q9VE51; -.
DR SMR; Q9VE51; -.
DR BioGRID; 67248; 11.
DR IntAct; Q9VE51; 3.
DR STRING; 7227.FBpp0083105; -.
DR PaxDb; Q9VE51; -.
DR PRIDE; Q9VE51; -.
DR DNASU; 42240; -.
DR EnsemblMetazoa; FBtr0083690; FBpp0083105; FBgn0261065.
DR GeneID; 42240; -.
DR KEGG; dme:Dmel_CG7698; -.
DR UCSC; CG7698-RA; d. melanogaster.
DR CTD; 42240; -.
DR FlyBase; FBgn0261065; Cpsf73.
DR VEuPathDB; VectorBase:FBgn0261065; -.
DR eggNOG; KOG1137; Eukaryota.
DR GeneTree; ENSGT00940000155699; -.
DR HOGENOM; CLU_009673_2_3_1; -.
DR InParanoid; Q9VE51; -.
DR OMA; VMIPRRC; -.
DR OrthoDB; 218195at2759; -.
DR PhylomeDB; Q9VE51; -.
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 BioGRID-ORCS; 42240; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Cpsf73; fly.
DR GenomeRNAi; 42240; -.
DR PRO; PR:Q9VE51; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0261065; Expressed in eye disc (Drosophila) and 55 other tissues.
DR Genevisible; Q9VE51; DM.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:FlyBase.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR021718; CPSF73-100_C.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF11718; CPSF73-100_C; 1.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM01098; CPSF73-100_C; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Metal-binding; mRNA processing; Nuclease; Nucleus;
KW Reference proteome; RNA-binding; Zinc.
FT CHAIN 1..684
FT /note="Cleavage and polyadenylation specificity factor 73"
FT /id="PRO_0000422157"
FT ACT_SITE 402
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6, ECO:0000255"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
SQ SEQUENCE 684 AA; 76826 MW; F059330C06BFEC53 CRC64;
MTQATGDARM PDEESDLLQI KPLGAGQEVG RSCIMLEFKG KKIMLDCGIH PGLSGMDALP
YVDLIEADEI DLLFISHFHL DHCGALPWFL MKTSFKGRCF MTHATKAIYR WMLSDYIKIS
NISTEQMLYT EADLEASMEK IETINFHEER DVMGVRFCAY IAGHVLGAAM FMIEIAGIKI
LYTGDFSRQE DRHLMAAEVP PMKPDVLITE STYGTHIHEK REDRENRFTS LVQKIVQQGG
RCLIPVFALG RAQELLLILD EFWSQNPDLH EIPIYYASSL AKKCMAVYQT YINAMNDRIR
RQIAVNNPFV FRHISNLKGI DHFEDIGPCV IMASPGMMQS GLSRELFESW CTDPKNGVII
AGYCVEGTLA KAVLSEPEEI TTLSGQKLPL NMSVDYISFS AHTDYQQTSE FIRLLKPTHV
VLVHGEQNEM SRLKLALQRE YEADASTDIK FYNPRNTHAV DLYFRGEKTA KVMGSLAAKN
SEVGSKLSGV LVKRDFKYHL LAPSDLGKYT DMSMSVVTQR QSIPWGSSLS TLELLLDRIG
AGCVEVLEAE RKLRVFGCIE LTVEQKIIVM EWQATHVNDV YADAVLACIM QSELGGTNLK
GATKQTKSED SRFRECLIET LQDTFGDNCV PKMFEGDLLP VTVSGKRAEI NLETLAISCA
EDDVLRQMLN TTVQKLHQTL VSAL
