CPSF3_BOVIN
ID CPSF3_BOVIN Reviewed; 684 AA.
AC P79101; Q3MHX7;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 3;
DE EC=3.1.27.- {ECO:0000250|UniProtKB:Q9QXK7};
DE AltName: Full=Cleavage and polyadenylation specificity factor 73 kDa subunit;
DE Short=CPSF 73 kDa subunit;
DE AltName: Full=mRNA 3'-end-processing endonuclease CPSF-73;
GN Name=CPSF3; Synonyms=CPSF73;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8929409; DOI=10.1126/science.274.5292.1514;
RA Jenny A., Minvielle-Sebastia L., Preker P.J., Keller W.;
RT "Sequence similarity between the 73-kilodalton protein of mammalian CPSF
RT and a subunit of yeast polyadenylation factor I.";
RL Science 274:1514-1517(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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. Also involved in the histone 3'-end pre-
CC mRNA processing. U7 snRNP-dependent protein that induces both the 3'-
CC endoribonucleolytic cleavage of histone pre-mRNAs and acts as a 5' to
CC 3' exonuclease for degrading the subsequent downstream cleavage product
CC (DCP) of mature histone mRNAs. Cleavage occurs after the 5'-ACCCA-3'
CC sequence in the histone pre-mRNA leaving a 3'hydroxyl group on the
CC upstream fragment containing the stem loop (SL) and 5' phosphate on the
CC downstream cleavage product (DCP) starting with CU nucleotides. The U7-
CC dependent 5' to 3' exonuclease activity is processive and degrades the
CC DCP RNA substrate even after complete removal of the U7-binding site.
CC Binds to the downstream cleavage product (DCP) of histone pre-mRNAs and
CC the cleaved DCP RNA substrate in a U7 snRNP dependent manner. Required
CC for entering/progressing through S-phase of the cell cycle (By
CC similarity). Required for the selective processing of microRNAs
CC (miRNAs) during embryonic stem cell differentiation via its interaction
CC with ISY1 (By similarity). Required for the biogenesis of all miRNAs
CC from the pri-miR-17-92 primary transcript except miR-92a (By
CC similarity). Only required for the biogenesis of miR-290 and miR-96
CC from the pri-miR-290-295 and pri-miR-96-183 primary transcripts,
CC respectively (By similarity). {ECO:0000250|UniProtKB:Q9QXK7,
CC ECO:0000250|UniProtKB:Q9UKF6}.
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 CPSF1, CPSF2, CPSF3, CPSF4 and
CC FIP1L1. Interacts with CPSF2, CSTF2 and SYMPK. Interacts with TUT1; the
CC interaction is direct and mediates the recruitment of the CPSF complex
CC on the 3'UTR of pre-mRNAs. Interacts with WDR33. Interacts with ZC3H3.
CC {ECO:0000250|UniProtKB:Q9QXK7, ECO:0000250|UniProtKB:Q9UKF6}.
CC -!- INTERACTION:
CC P79101; P03120: E2; Xeno; NbExp=2; IntAct=EBI-7894416, EBI-1779322;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UKF6}.
CC -!- PTM: Sumoylated on Lys-462, Lys-465 and Lys-545, preferentially by
CC SUMO3. {ECO:0000250|UniProtKB:Q9UKF6}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. CPSF3 subfamily.
CC {ECO:0000305}.
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DR EMBL; X95906; CAA65151.1; -; mRNA.
DR EMBL; BC104553; AAI04554.1; -; mRNA.
DR RefSeq; NP_776709.1; NM_174284.2.
DR AlphaFoldDB; P79101; -.
DR SMR; P79101; -.
DR IntAct; P79101; 1.
DR MINT; P79101; -.
DR STRING; 9913.ENSBTAP00000026303; -.
DR PaxDb; P79101; -.
DR PRIDE; P79101; -.
DR Ensembl; ENSBTAT00000026303; ENSBTAP00000026303; ENSBTAG00000019735.
DR GeneID; 281712; -.
DR KEGG; bta:281712; -.
DR CTD; 51692; -.
DR VEuPathDB; HostDB:ENSBTAG00000019735; -.
DR VGNC; VGNC:27672; CPSF3.
DR eggNOG; KOG1137; Eukaryota.
DR GeneTree; ENSGT00940000155699; -.
DR HOGENOM; CLU_009673_2_3_1; -.
DR InParanoid; P79101; -.
DR OMA; TRSVECE; -.
DR OrthoDB; 218195at2759; -.
DR TreeFam; TF105643; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000019735; Expressed in semen and 109 other tissues.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:UniProtKB.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IBA:GO_Central.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0031124; P:mRNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; ISS:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
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; PF00753; Lactamase_B; 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 Acetylation; Endonuclease; Hydrolase; Isopeptide bond; Metal-binding;
KW mRNA processing; Nuclease; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Ubl conjugation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT CHAIN 2..684
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 3"
FT /id="PRO_0000074399"
FT ACT_SITE 396
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXK7"
FT MOD_RES 681
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT CROSSLNK 462
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT CROSSLNK 465
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
FT CROSSLNK 545
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKF6"
SQ SEQUENCE 684 AA; 77488 MW; 17A0C4FED2B8172E CRC64;
MSAIPAEESD QLLIRPLGAG QEVGRSCIIL EFKGRKIMLD CGIHPGLEGM DALPYIDLID
PAEIDLLLIS HFHLDHCGAL PWFLQKTSFK GRTFMTHATK AIYRWLLSDY VKVSNISADD
MLYTETDLEE SMDKIETINF HEVKEVAGIK FWCYHAGHVL GAAMFMIEIA GVKLLYTGDF
SRQEDRHLMA AEIPNIKPDI LIIESTYGTH IHEKREEREA RFCNTVHDIV NRGGRGLIPV
FALGRAQELL LILDEYWQNH PELHDIPIYY ASSLAKKCMA VYQTYVNAMN DKIRKQININ
NPFVFKHISN LKSMDHFDDI GPSVVMASPG MMQSGLSREL FESWCTDKRN GVIIAGYCVE
GTLAKHIMSE PEEITTMSGQ KLPLKMSVDY ISFSAHTDYQ QTSEFIRALK PPHVILVHGE
QNEMARLKAA LIREYEDNDE VHIEVHNPRN TEAVTLNFRG EKLAKVMGFL ADKKPEQGQR
VSGILVKRNF NYHILSPCDL SNYTDLAMST VKQTQAIPYT GPFNLLYYQL QKLTGDVEEL
EIQEKPALKV FKNITVIQEP GMVVLEWLAN PSNDMYADTV TTVILEVQSN PKIRKGAVQK
VSKKLEMHVY SKRLEIMLQD IFGEDCVSVK DGSILSVTVD GKTANINLET RTVECEEGSE
DDESLREMVE LAAQRLYEAL TPVH
