CPSF1_DROME
ID CPSF1_DROME Reviewed; 1455 AA.
AC Q9V726; Q7KR84; Q960R9; Q9GV83; Q9GV84; Q9GV85;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 1;
DE AltName: Full=Cleavage and polyadenylation specificity factor 160 kDa subunit;
DE Short=CPSF 160 kDa subunit;
DE Short=dCPSF 160;
GN Name=Cpsf160; Synonyms=cpsf; ORFNames=CG10110;
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 [MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo, and Eye imaginal disk;
RX PubMed=9604891; DOI=10.1007/s004380050696;
RA Salinas C.A., Sinclair D.A., O'Hare K., Brock H.W.;
RT "Characterization of a Drosophila homologue of the 160-kDa subunit of the
RT cleavage and polyadenylation specificity factor CPSF.";
RL Mol. Gen. Genet. 257:672-680(1998).
RN [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 [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [5]
RP IDENTIFICATION IN THE CPSF COMPLEX.
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. This subunit is involved in the RNA recognition step
CC of the polyadenylation reaction (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex, composed of at least Clp, Cpsf73, Cpsf100 and
CC Cpsf160. {ECO:0000269|PubMed:19450530}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9V726-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9V726-2; Sequence=VSP_001216;
CC -!- SIMILARITY: Belongs to the CPSF1 family. {ECO:0000305}.
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DR EMBL; AF241364; AAF98386.1; -; mRNA.
DR EMBL; AF241365; AAF98387.1; -; mRNA.
DR EMBL; AF241366; AAF98388.1; -; mRNA.
DR EMBL; AE013599; AAF58240.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68553.1; -; Genomic_DNA.
DR EMBL; AY051896; AAK93320.1; -; mRNA.
DR RefSeq; NP_725397.1; NM_166056.3. [Q9V726-2]
DR RefSeq; NP_995833.1; NM_206111.3. [Q9V726-1]
DR AlphaFoldDB; Q9V726; -.
DR SMR; Q9V726; -.
DR BioGRID; 68918; 4.
DR IntAct; Q9V726; 5.
DR STRING; 7227.FBpp0089163; -.
DR PaxDb; Q9V726; -.
DR PRIDE; Q9V726; -.
DR DNASU; 44250; -.
DR EnsemblMetazoa; FBtr0089257; FBpp0088317; FBgn0024698. [Q9V726-2]
DR EnsemblMetazoa; FBtr0089258; FBpp0089163; FBgn0024698. [Q9V726-1]
DR GeneID; 44250; -.
DR KEGG; dme:Dmel_CG10110; -.
DR CTD; 44250; -.
DR FlyBase; FBgn0024698; Cpsf160.
DR VEuPathDB; VectorBase:FBgn0024698; -.
DR eggNOG; KOG1896; Eukaryota.
DR GeneTree; ENSGT00950000183151; -.
DR HOGENOM; CLU_002414_0_0_1; -.
DR InParanoid; Q9V726; -.
DR OMA; PMTKFKL; -.
DR PhylomeDB; Q9V726; -.
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; Q9V726; -.
DR BioGRID-ORCS; 44250; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 44250; -.
DR PRO; PR:Q9V726; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0024698; Expressed in egg cell and 25 other tissues.
DR Genevisible; Q9V726; DM.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:FlyBase.
DR GO; GO:0017022; F:myosin binding; IPI:FlyBase.
DR GO; GO:0006378; P:mRNA polyadenylation; ISS:FlyBase.
DR GO; GO:0010508; P:positive regulation of autophagy; IGI:FlyBase.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; ISS:FlyBase.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF03178; CPSF_A; 1.
DR Pfam; PF10433; MMS1_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; mRNA processing; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..1455
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 1"
FT /id="PRO_0000074389"
FT VAR_SEQ 244..278
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_001216"
FT CONFLICT 907
FT /note="M -> L (in Ref. 1; AAF98388)"
FT /evidence="ECO:0000305"
FT CONFLICT 921
FT /note="D -> E (in Ref. 1; AAF98388)"
FT /evidence="ECO:0000305"
FT CONFLICT 1076
FT /note="G -> D (in Ref. 1; AAF98388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1455 AA; 164681 MW; B939D522310F479F CRC64;
MFSMCKQTHS ATAVEFSIAC RFFNNLDENL VVAGANVLKV YRIAPNVEAS QRQKLNPSEM
RLAPKMRLEC LATYTLYGNV MSLQCVSLAG AMRDALLISF KDAKLSVLQH DPDTFALKTL
SLHYFEEDDI RGGWTGRYFV PTVRVDPDSR CAVMLVYGKR LVVLPFRKDN SLDEIELADV
KPIKKAPTAM VSRTPIMASY LIALRDLDEK IDNVLDIQFL HGYYEPTLLI LYEPVRTCPG
RIKVRSDTCV LVAISLNIQQ RVHPIIWTVN SLPFDCLQVY PIQKPIGGCL VMTVNAVIYL
NQSVPPYGVS LNSSADNSTA FPLKPQDGVR ISLDCANFAF IDVDKLVISL RTGDLYVLTL
CVDSMRTVRN FHFHKAAASV LTSCICVLHS EYIFLGSRLG NSLLLHFTEE DQSTVITLDE
VEQQSEQQQR NLQDEDQNLE EIFDVDQLEM APTQAKSRRI EDEELEVYGS GAKASVLQLR
KFIFEVCDSL MNVAPINYMC AGERVEFEED GVTLRPHAES LQDLKIELVA ATGHSKNGAL
SVFVNCINPQ IITSFELDGC LDVWTVFDDA TKKSSRNDQH DFMLLSQRNS TLVLQTGQEI
NEIENTGFTV NQPTIFVGNL GQQRFIVQVT TRHVRLLQGT RLIQNVPIDV GSPVVQVSIA
DPYVCLRVLN GQVITLALRE TRGTPRLAIN KHTISSSPAV VAISAYKDLS GLFTVKGDDI
NLTGSSNSAF GHSFGGYMKA EPNMKVEDEE DLLYGDAGSA FKMNSMADLA KQSKQKNSDW
WRRLLVQAKP SYWLVVARQS GTLEIYSMPD MKLVYLVNDV GNGSMVLTDA MEFVPISLTT
QENSKAGIVQ ACMPQHANSP LPLELSVIGL GLNGERPLLL VRTRVELLIY QVFRYPKGHL
KIRFRKMDQL NLLDQQPTHI DLDENDEQEE IESYQMQPKY VQKLRPFANV GGLSGVMVCG
VNPCFVFLTF RGELRIHRLL GNGDVRSFAA FNNVNIPNGF LYFDTTYELK ISVLPSYLSY
DSVWPVRKVP LRCTPRQLVY HRENRVYCLI TQTEEPMTKY YRFNGEDKEL SEESRGERFI
YPIGSQFEMV LISPETWEIV PDASITFEPW EHVTAFKIVK LSYEGTRSGL KEYLCIGTNF
NYSEDITSRG NIHIYDIIEV VPEPGKPMTK FKIKEIFKKE QKGPVSAISD VLGFLVTGLG
QKIYIWQLRD GDLIGVAFID TNIYVHQIIT VKSLIFIADV YKSISLLRFQ EEYRTLSLAS
RDFNPLEVYG IEFMVDNSNL GFLVTDAERN IIVYMYQPEA RESLGGQKLL RKADYHLGQV
VNTMFRVQCH QKGLHQRQPF LYENKHFVVY GTLDGALGYC LPLPEKVYRR FLMLQNVLLS
YQEHLCGLNP KEYRTLKSSK KQGINPSRCI IDGDLIWSYR LMANSERNEV AKKIGTRTEE
ILGDLLEIER LASVF
