ID   CPSF4_XENLA             Reviewed;         269 AA.
AC   Q6DJP7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Cleavage and polyadenylation specificity factor subunit 4;
GN   Name=cpsf4;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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) (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC       factor (CPSF) complex, composed of cpsf1, cpsf2, cpsf3, cpsf4 and
CC       fip1l1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CPSF4/YTH1 family. {ECO:0000305}.
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DR   EMBL; BC075128; AAH75128.1; -; mRNA.
DR   RefSeq; NP_001086337.1; NM_001092868.1.
DR   AlphaFoldDB; Q6DJP7; -.
DR   SMR; Q6DJP7; -.
DR   DNASU; 444766; -.
DR   GeneID; 444766; -.
DR   KEGG; xla:444766; -.
DR   CTD; 444766; -.
DR   Xenbase; XB-GENE-948308; cpsf4.S.
DR   OMA; RAVCRKN; -.
DR   OrthoDB; 1472764at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 444766; Expressed in egg cell and 19 other tissues.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IEA:InterPro.
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; 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; Reference proteome; Repeat;
KW   RNA-binding; Zinc; Zinc-finger.
FT   CHAIN           1..269
FT                   /note="Cleavage and polyadenylation specificity factor
FT                   subunit 4"
FT                   /id="PRO_0000317364"
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..145
FT                   /note="C3H1-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         146..169
FT                   /note="C3H1-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         243..260
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          173..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   269 AA;  30492 MW;  54D42C17A41AFE28 CRC64;
     MQELIACVDH LRFDLELAVE QQLGAQPLPF PGMDKSGAAV CEFFLKSACG KGGMCPFRHI
     SGEKTVVCKH WLRGLCKKGD QCEFLHEYDM TKMPECYFYS KFGECSNKEC PFLHIDPESK
     IKDCPWYDRG FCKHGPLCRH RHTRRVICVN YLVGFCIEGP NCKFMHPRFE LPMGTAEQPP
     LPQQTQNQQK QNNNQVLQRS SSLIQLTSQN SPVSQQRSPQ TIGVMQLQSG TQGNRGPRPL
     DQVTCYKCGE KGHYANRCTK GHLAFLSGQ