ID   Q9QYU6_RAT              Unreviewed;       229 AA.
AC   Q9QYU6;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Cleavage and polyadenylation specificity factor subunit 4 {ECO:0000256|RuleBase:RU369008};
DE            Short=CPSF 30 kDa subunit {ECO:0000256|RuleBase:RU369008};
DE   AltName: Full=Cleavage and polyadenylation specificity factor 30 kDa subunit {ECO:0000256|RuleBase:RU369008};
DE   Flags: Fragment;
GN   Name=Cpsf4 {ECO:0000313|RGD:620440};
GN   Synonyms=CDK106 {ECO:0000313|EMBL:CAB56623.1};
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 {ECO:0000313|EMBL:CAB56623.1};
RN   [1] {ECO:0000313|EMBL:CAB56623.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GK {ECO:0000313|EMBL:CAB56623.1};
RA   Zaidi Q.J.;
RL   Submitted (MAY-1998) 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). {ECO:0000256|RuleBase:RU369008}.
CC   -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC       factor (CPSF) complex. {ECO:0000256|RuleBase:RU369008}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU369008}.
CC   -!- SIMILARITY: Belongs to the CPSF4/YTH1 family.
CC       {ECO:0000256|RuleBase:RU369008}.
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DR   EMBL; Y17326; CAB56623.1; -; mRNA.
DR   AlphaFoldDB; Q9QYU6; -.
DR   RGD; 620440; Cpsf4.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0031124; P:mRNA 3'-end processing; IEA:UniProtKB-UniRule.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 2.
DR   InterPro; IPR045348; CPSF4/Yth1.
DR   InterPro; IPR041686; Znf-CCCH_3.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR23102:SF18; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 4; 1.
DR   PANTHER; PTHR23102; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 4-RELATED; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   Pfam; PF15663; zf-CCCH_3; 1.
DR   SMART; SM00356; ZnF_C3H1; 5.
DR   SUPFAM; SSF90229; CCCH zinc finger; 2.
DR   PROSITE; PS50103; ZF_C3H1; 4.
PE   2: Evidence at transcript level;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; mRNA processing {ECO:0000256|RuleBase:RU369008};
KW   Nucleus {ECO:0000256|RuleBase:RU369008};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU369008};
KW   RNA-binding {ECO:0000256|RuleBase:RU369008};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          34..58
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          61..88
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          89..116
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          141..167
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         34..58
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         61..88
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         89..116
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         141..167
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          171..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAB56623.1"
SQ   SEQUENCE   229 AA;  25930 MW;  676B6F337A8B64D0 CRC64;
     GTRIASVDHI KFDLEIAVEQ QLGAQPLPFP GMDKSGAAVC EFFLKAACGK GGMCPFRHIS
     GEKTVVCKHW LRGLCKKGDQ CEFLHEYDMT KMPECYFYSK FGECSNKECP FLHIDPESKI
     KDCPWYDRGF CKHGPLQHRH TRRVICVNYL VGFCPEGTSC KFMHPRFELP MGTTEQPPLP
     QQNSSNKPKP PRSLGPAKSN TMQATGTPAP EQFLATICEK EDMCFRWFP
//