ID   CPSF4_RAT               Reviewed;         243 AA.
AC   Q5FVR7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Cleavage and polyadenylation specificity factor subunit 4;
DE   AltName: Full=Cleavage and polyadenylation specificity factor 30 kDa subunit;
DE            Short=CPSF 30 kDa subunit;
GN   Name=Cpsf4;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the cleavage and polyadenylation specificity
CC       factor (CPSF) complex that play 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. CPSF4 binds RNA polymers with a preference for
CC       poly(U).
CC   -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC       factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and
CC       FIP1L1. Interacts with FIP1L1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CPSF4/YTH1 family. {ECO:0000305}.
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DR   EMBL; BC089824; AAH89824.1; -; mRNA.
DR   RefSeq; NP_001012351.1; NM_001012351.2.
DR   AlphaFoldDB; Q5FVR7; -.
DR   SMR; Q5FVR7; -.
DR   STRING; 10116.ENSRNOP00000046991; -.
DR   PhosphoSitePlus; Q5FVR7; -.
DR   jPOST; Q5FVR7; -.
DR   PaxDb; Q5FVR7; -.
DR   Ensembl; ENSRNOT00000042474; ENSRNOP00000046991; ENSRNOG00000000985.
DR   GeneID; 304277; -.
DR   KEGG; rno:304277; -.
DR   CTD; 10898; -.
DR   RGD; 620440; Cpsf4.
DR   eggNOG; KOG1040; Eukaryota.
DR   GeneTree; ENSGT00940000155520; -.
DR   HOGENOM; CLU_024513_0_1_1; -.
DR   InParanoid; Q5FVR7; -.
DR   OMA; NSCKQYV; -.
DR   OrthoDB; 1472764at2759; -.
DR   PhylomeDB; Q5FVR7; -.
DR   TreeFam; TF314871; -.
DR   Reactome; R-RNO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR   Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-RNO-72187; mRNA 3'-end processing.
DR   Reactome; R-RNO-73856; RNA Polymerase II Transcription Termination.
DR   Reactome; R-RNO-77595; Processing of Intronless Pre-mRNAs.
DR   PRO; PR:Q5FVR7; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000000985; Expressed in pancreas and 18 other tissues.
DR   ExpressionAtlas; Q5FVR7; baseline and differential.
DR   Genevisible; Q5FVR7; RN.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
DR   InterPro; IPR045348; CPSF4/Yth1.
DR   InterPro; IPR041686; Znf-CCCH_3.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR23102; PTHR23102; 2.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   Pfam; PF15663; zf-CCCH_3; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SMART; SM00356; ZnF_C3H1; 5.
DR   SUPFAM; SSF57756; SSF57756; 1.
DR   SUPFAM; SSF90229; SSF90229; 2.
DR   PROSITE; PS50103; ZF_C3H1; 5.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; mRNA processing; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT   CHAIN           1..243
FT                   /note="Cleavage and polyadenylation specificity factor
FT                   subunit 4"
FT                   /id="PRO_0000266021"
FT   ZN_FING         35..61
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         62..89
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         90..117
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         118..142
FT                   /note="C3H1-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         143..169
FT                   /note="C3H1-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         217..234
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   MOD_RES         241
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95639"
SQ   SEQUENCE   243 AA;  27419 MW;  3520EB40BD525C8F CRC64;
     MQEIIASVDH IKFDLEIAVE QQLGAQPLPF PGMDKSGAAV CEFFLKAACG KGGMCPFRHI
     SGEKTVVCKH WLRGLCKKGD QCEFLHEYDM TKMPECYFYS KFGECSNKEC PFLHIDPESK
     IKDCPWYDRG FCKHGPLCRH RHTRRVICVN YLVGFCPEGP SCKFMHPRFE LPMGTTEQPP
     LPQQTQPPTK RAPQVIGVMQ SQNSSAGNRG PRPLEQVTCY KCGEKGHYAN RCTKGHLAFL
     SGQ