CPSF2_CAEEL
ID CPSF2_CAEEL Reviewed; 843 AA.
AC O17403;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=cpsf-2; ORFNames=F09G2.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=15790806; DOI=10.1126/science.1109267;
RA Kim J.K., Gabel H.W., Kamath R.S., Tewari M., Pasquinelli A., Rual J.F.,
RA Kennedy S., Dybbs M., Bertin N., Kaplan J.M., Vidal M., Ruvkun G.;
RT "Functional genomic analysis of RNA interference in C. elegans.";
RL Science 308:1164-1167(2005).
CC -!- FUNCTION: CPSF plays a key role in pre-mRNA 3'-end formation,
CC recognizing the AAUAAA signal sequence and interacting with
CC poly(A)polymerase and other factors to bring about cleavage and poly(A)
CC addition. {ECO:0000269|PubMed:15790806}.
CC -!- SUBUNIT: CPSF is a heterotetramer composed of four distinct subunits
CC 160, 100, 70 and 30 kDa. {ECO:0000250}.
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; FO080529; CCD64424.1; -; Genomic_DNA.
DR PIR; T32487; T32487.
DR RefSeq; NP_504822.1; NM_072421.4.
DR AlphaFoldDB; O17403; -.
DR SMR; O17403; -.
DR BioGRID; 44148; 5.
DR STRING; 6239.F09G2.4; -.
DR iPTMnet; O17403; -.
DR EPD; O17403; -.
DR PaxDb; O17403; -.
DR PeptideAtlas; O17403; -.
DR EnsemblMetazoa; F09G2.4.1; F09G2.4.1; WBGene00017313.
DR GeneID; 179103; -.
DR KEGG; cel:CELE_F09G2.4; -.
DR CTD; 179103; -.
DR WormBase; F09G2.4; CE09299; WBGene00017313; cpsf-2.
DR eggNOG; KOG1135; Eukaryota.
DR GeneTree; ENSGT00910000144260; -.
DR HOGENOM; CLU_002227_3_0_1; -.
DR InParanoid; O17403; -.
DR OMA; MELVENC; -.
DR OrthoDB; 1314980at2759; -.
DR PhylomeDB; O17403; -.
DR Reactome; R-CEL-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-CEL-72187; mRNA 3'-end processing.
DR Reactome; R-CEL-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-CEL-77595; Processing of Intronless Pre-mRNAs.
DR PRO; PR:O17403; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00017313; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:WormBase.
DR GO; GO:0003723; F:RNA binding; ISS:WormBase.
DR GO; GO:0031124; P:mRNA 3'-end processing; ISS:WormBase.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
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 3: Inferred from homology;
KW mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..843
FT /note="Probable cleavage and polyadenylation specificity
FT factor subunit 2"
FT /id="PRO_0000074396"
FT REGION 414..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 95616 MW; BEFBC3928DEC0976 CRC64;
MTSIIKLKVF SGAKDEGPLC YLLQVDGDYI LLDCGWDERF GLQYFEELKP FIPKISAVLI
SHPDPLHLGG LPYLVSKCGL TAPVYATVPV YKMGQMFIYD MVYSHLDVEE FEHYTLDDVD
TAFEKVEQVK YNQTVVLKGD SGVHFTALPA GHMLGGSIWR ICRVTGEDIV YCVDFNHKKE
RHLNGCSFDN FNRPHLLITG AHHISLPQMR RKDRDEQLVT KILRTVRQKG DCMIVIDTAG
RVLELAHLLD QLWSNADAGL STYNLVMMSH VASSVVQFAK SQLEWMNEKL FKYDSSSARY
NPFTLKHVTL CHSHQELMRV RSPKVVLCSS QDMESGFSRE LFLDWCSDPR NGVILTARPA
SFTLAAKLVN MAERANDGVL KHEDRLISLV VKKRVALEGE ELLEYKRRKA ERDAEETRLR
MERARRQAQA NESDDSDDDD IAAPIVPRHS EKDFRSFDGS ENDAHTFDIM AKWDNQQKAS
FFKTTKKSFP MFPYIEEKVK WDDYGEVIKP EDYTVISKID LRKGQNKDEP VVVKKREEEE
EVYNPNDHVE EMPTKCVEFK NRVEVSCRIE FIEYEGISDG ESTKKLLAGL LPRQIIVVHG
SRDDTRDLVA YFADSGFDTT MLKAPEAGAL VDASVESFIY QVALSDALLA DIQFKEVSEG
NSLAWIDARV MEKEAIDNML AVGTSNLMID DKNREEDVND QEENGATEGE GNAEPMEIGE
NGSQESLAIS ESGKEVENGH TNDSRTKKGT KGKIRGNLIL DPLPKRLIPI HQAVFVNDPK
LSDFKNLLTD KGYKAEFLSG TLLINGGNCS IRRNDTGVFQ MEGAFTKDYY KLRRLFYDQF
AVL
