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Database: UniProt
Entry: G5BV66_HETGA
LinkDB: G5BV66_HETGA
Original site: G5BV66_HETGA 
ID   G5BV66_HETGA            Unreviewed;       227 AA.
AC   G5BV66;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Cleavage and polyadenylation specificity factor subunit 5 {ECO:0000256|PIRNR:PIRNR017888};
GN   ORFNames=GW7_04702 {ECO:0000313|EMBL:EHB13177.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB13177.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB13177.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
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; JH172081; EHB13177.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5BV66; -.
DR   STRING; 10181.G5BV66; -.
DR   InParanoid; G5BV66; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
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   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.
PE   3: Inferred from homology;
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:UP000006813};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR017888}.
SQ   SEQUENCE   227 AA;  26269 MW;  9B4AFEEAD1C9DC23 CRC64;
     MSVVPPNRSK MGWPQGVTQF SNKYIQQTKP LTLERTINLY PLTNYTFGTK EPLYEKSSSV
     AARFQHMREE FDKIGIRRTI EGVLIVHEHR LPRVLLLQLG TTFFKLPGGE LNPREDEVEG
     LKCLMTEILG RQDGVLQDWV IDDCIGNWWR SNFEPLQYPY IPAHITKPKE HKKLFLVQLQ
     EKALFAVPKN YKLVAAPLFE LYDNASGYGP IISSLPKLLS RFNFIYN
//
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