CPSF5_DICDI
ID CPSF5_DICDI Reviewed; 200 AA.
AC Q55E68;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 5 {ECO:0000250|UniProtKB:O43809};
GN Name=nudt21 {ECO:0000250|UniProtKB:O43809};
GN Synonyms=cpsf5 {ECO:0000250|UniProtKB:O43809}; ORFNames=DDB_G0269370;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Component of the cleavage factor Im (CFIm) complex that
CC functions as an activator of the pre-mRNA 3'-end cleavage and
CC polyadenylation processing required for the maturation of pre-mRNA into
CC functional mRNAs. CFIm contributes to the recruitment of multiprotein
CC complexes on specific sequences on the pre-mRNA 3'-end, so called
CC cleavage and polyadenylation signals (pA signals). Most pre-mRNAs
CC contain multiple pA signals, resulting in alternative cleavage and
CC polyadenylation (APA) producing mRNAs with variable 3'-end formation.
CC The CFIm complex acts as a key regulator of cleavage and
CC polyadenylation site choice during APA through its binding to 5'-UGUA-
CC 3' elements localized in the 3'-untranslated region (UTR) for a huge
CC number of pre-mRNAs. Binds to 5'-UGUA-3' elements localized upstream of
CC pA signals that act as enhancers of pre-mRNA 3'-end processing. The
CC homodimer mediates simultaneous sequence-specific recognition of two
CC 5'-UGUA-3' elements within the pre-mRNA. Plays a role in somatic cell
CC fate transitions and pluripotency by regulating widespread changes in
CC gene expression through an APA-dependent function. Binds to chromatin.
CC {ECO:0000250|UniProtKB:O43809, ECO:0000250|UniProtKB:Q9CQF3}.
CC -!- SUBUNIT: Homodimer (via N- and C-terminus); binds RNA as homodimer.
CC Component of the cleavage factor Im (CFIm) complex.
CC {ECO:0000250|UniProtKB:O43809}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43809}. Cytoplasm
CC {ECO:0000250|UniProtKB:O43809}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. CPSF5 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved metal-binding residues in the NUDIX motif
CC and is not expected to have hydrolase activity. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72035.1; -; Genomic_DNA.
DR RefSeq; XP_645913.1; XM_640821.1.
DR AlphaFoldDB; Q55E68; -.
DR SMR; Q55E68; -.
DR STRING; 44689.DDB0233564; -.
DR PaxDb; Q55E68; -.
DR PRIDE; Q55E68; -.
DR EnsemblProtists; EAL72035; EAL72035; DDB_G0269370.
DR GeneID; 8616854; -.
DR KEGG; ddi:DDB_G0269370; -.
DR dictyBase; DDB_G0269370; -.
DR eggNOG; KOG1689; Eukaryota.
DR HOGENOM; CLU_068704_1_1_1; -.
DR InParanoid; Q55E68; -.
DR OMA; EHYEQYG; -.
DR PhylomeDB; Q55E68; -.
DR Reactome; R-DDI-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q55E68; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005849; C:mRNA cleavage factor complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:1990120; P:messenger ribonucleoprotein complex assembly; ISS:UniProtKB.
DR GO; GO:0110104; P:mRNA alternative polyadenylation; ISS:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; ISS:dictyBase.
DR GO; GO:0031439; P:positive regulation of mRNA cleavage; ISS:UniProtKB.
DR GO; GO:1900365; P:positive regulation of mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR InterPro; IPR016706; Cleav_polyA_spec_factor_su5.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR13047; PTHR13047; 1.
DR Pfam; PF13869; NUDIX_2; 1.
DR PIRSF; PIRSF017888; CPSF-25; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Differentiation; mRNA processing; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..200
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 5"
FT /id="PRO_0000327445"
FT DOMAIN 45..170
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 70..72
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:O43809"
FT MOTIF 77..98
FT /note="Nudix box"
FT SITE 24
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:O43809"
SQ SEQUENCE 200 AA; 22786 MW; 63F632661E8A255E CRC64;
MSIKTLTLYN FNTSYSFGKE EKKEKEQSLT SKLARLKDSY EKEGLRKAVE GIIIIHDHGH
PHILLLQDNN YFKLPGGKLK PGENEIDGLI RKLTKKLSPT GTPVSDAPWE IGDHVSTWWR
PNFEPSLFPY IPSHITKPKE CKKLFVVTLP EKCKFAVSNN LSLIAVSLYE IYNNSQRYGA
VISSIPALIS RYTFVYLNVD
