ID A0A2K6QCV6_RHIRO Unreviewed; 179 AA.
AC A0A2K6QCV6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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};
GN Name=CPSF4L {ECO:0000313|Ensembl:ENSRROP00000026609.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000026609.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000026609.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 RefSeq; XP_010358645.1; XM_010360343.1.
DR AlphaFoldDB; A0A2K6QCV6; -.
DR STRING; 61622.ENSRROP00000026609; -.
DR Ensembl; ENSRROT00000050864.1; ENSRROP00000026609.1; ENSRROG00000037051.1.
DR GeneID; 104660084; -.
DR KEGG; rro:104660084; -.
DR CTD; 642843; -.
DR GeneTree; ENSGT00940000162882; -.
DR OMA; CKKNEKC; -.
DR OrthoDB; 33612at2759; -.
DR Proteomes; UP000233200; Unplaced.
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:SF19; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 4-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR23102; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 4-RELATED; 1.
DR Pfam; PF14608; zf-CCCH_2; 2.
DR Pfam; PF15663; zf-CCCH_3; 1.
DR SMART; SM00356; ZnF_C3H1; 4.
DR SUPFAM; SSF90229; CCCH zinc finger; 2.
DR PROSITE; PS50103; ZF_C3H1; 5.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000233200};
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 35..61
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 62..89
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 90..117
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 118..145
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 147..169
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 35..61
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 62..89
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 90..117
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 118..145
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 147..169
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
SQ SEQUENCE 179 AA; 20890 MW; 4F82C3503600148A CRC64;
MQEVIAGLER FTFAFEEDVE MQKGAGLLPF PGMDKSASAV CNFFAKGLCE KGKLCPFRHD
RREKMVVCKH WLRGLCKKGD HCKFLHQYDI TRMPECYFYS KFGDCSNKEC PFLHVKPAFK
SQDCPWYDQG FCKDRPLCKY RHVPRIMCLN YLVGFCPEGP KCRFSQKIRE FKLLPGSKI
//
