ID B5XB14_SALSA Unreviewed; 230 AA.
AC B5XB14;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 5 {ECO:0000256|PIRNR:PIRNR017888};
GN Name=CPSF5 {ECO:0000313|EMBL:ACI68034.1};
GN Synonyms=LOC106562230 {ECO:0000313|RefSeq:XP_013982434.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|EMBL:ACI68034.1};
RN [1] {ECO:0000313|EMBL:ACI68034.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:ACN12771.1}, and Spleen
RC {ECO:0000313|EMBL:ACI68034.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RA Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA Koop B.F.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACN10406.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Mixed brain {ECO:0000313|EMBL:ACN10406.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RA Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar full-length cDNAs.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ACI68034.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:ACN12771.1}, and Spleen
RC {ECO:0000313|EMBL:ACI68034.1};
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
RN [4] {ECO:0000313|EMBL:ACI68034.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:ACN12771.1}, and Spleen
RC {ECO:0000313|EMBL:ACI68034.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|RefSeq:XP_013982434.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013982434.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|PIRNR:PIRNR017888}.
CC -!- SUBUNIT: Homodimer (via N- and C-terminus); binds RNA as homodimer.
CC Component of the cleavage factor Im (CFIm) complex.
CC {ECO:0000256|PIRNR:PIRNR017888}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR017888}.
CC Cytoplasm {ECO:0000256|PIRNR:PIRNR017888}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. CPSF5 subfamily.
CC {ECO:0000256|PIRNR:PIRNR017888}.
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DR EMBL; BT048233; ACI68034.1; -; mRNA.
DR EMBL; BT058693; ACN10406.1; -; mRNA.
DR EMBL; BT060411; ACN12771.1; -; mRNA.
DR RefSeq; XP_013982434.1; XM_014126959.1.
DR STRING; 8030.ENSSSAP00000025512; -.
DR PaxDb; 8030-ENSSSAP00000025512; -.
DR GeneID; 106562230; -.
DR KEGG; sasa:106562230; -.
DR OMA; QCMREEF; -.
DR OrthoDB; 142507at2759; -.
DR Proteomes; UP000087266; Chromosome ssa11.
DR Bgee; ENSSSAG00000024658; Expressed in testis and 16 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR016706; Cleav_polyA_spec_factor_su5.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR13047:SF0; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 5; 1.
DR PANTHER; PTHR13047; PRE-MRNA CLEAVAGE FACTOR IM, 25KD SUBUNIT; 1.
DR Pfam; PF13869; NUDIX_2; 1.
DR PIRSF; PIRSF017888; CPSF-25; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR017888};
KW mRNA processing {ECO:0000256|PIRNR:PIRNR017888};
KW Nucleus {ECO:0000256|PIRNR:PIRNR017888};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR017888}.
FT DOMAIN 79..204
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 230 AA; 26175 MW; 8970A3912F37AE6A CRC64;
MSSVPAPNRS SAGWPRGVSQ FGGNKYMSAP AKPLSLERTI NLYPLTNYTF GTKEPLYEKD
SSVAARFQRM REEFDKLGMR RAVEGVLIVH EHRLPHVLLL QLGTTFFKLP GGELCPGEDE
VDGLKRLMTE ILGRQDGVKQ DWVIDDSIGN WWRPNFEPPQ YPYIPAHITK PKEHKKLFLV
QLQEKALFAV PKNYKLVAAP LFELYDNAPG YGPIISSLPQ LLSRFNFIYN
//
