CPSF6_XENLA
ID CPSF6_XENLA Reviewed; 548 AA.
AC Q6DDW4;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 6 {ECO:0000250|UniProtKB:Q16630};
GN Name=cpsf6 {ECO:0000250|UniProtKB:Q16630};
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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. Plays a role in mRNA export.
CC {ECO:0000250|UniProtKB:Q16630}.
CC -!- SUBUNIT: Component of the cleavage factor Im (CFIm) complex.
CC {ECO:0000250|UniProtKB:Q16630}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q16630}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q16630}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q16630}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q16630}. Note=Shuttles between the nucleus and
CC the cytoplasm. {ECO:0000250|UniProtKB:Q16630}.
CC -!- SIMILARITY: Belongs to the RRM CPSF6/7 family. {ECO:0000305}.
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DR EMBL; BC077388; AAH77388.1; -; mRNA.
DR RefSeq; NP_001086745.1; NM_001093276.1.
DR AlphaFoldDB; Q6DDW4; -.
DR SMR; Q6DDW4; -.
DR PRIDE; Q6DDW4; -.
DR DNASU; 446580; -.
DR GeneID; 446580; -.
DR KEGG; xla:446580; -.
DR CTD; 446580; -.
DR Xenbase; XB-GENE-961710; cpsf6.S.
DR OrthoDB; 1016696at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 446580; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0035061; C:interchromatin granule; ISS:UniProtKB.
DR GO; GO:0005849; C:mRNA cleavage factor complex; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042382; C:paraspeckles; ISS:UniProtKB.
DR GO; GO:0005726; C:perichromatin fibrils; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:1990120; P:messenger ribonucleoprotein complex assembly; ISS:UniProtKB.
DR GO; GO:0110104; P:mRNA alternative polyadenylation; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034769; CPSF6.
DR InterPro; IPR034772; CPSF6/7.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23204; PTHR23204; 1.
DR PANTHER; PTHR23204:SF3; PTHR23204:SF3; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; mRNA processing; Nucleus; Reference proteome.
FT CHAIN 1..548
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 6"
FT /id="PRO_0000081526"
FT DOMAIN 81..161
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 169..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..358
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 59405 MW; 235EA94BC8D2DA6C CRC64;
MADGVDHIDI YADVGEEFNQ EAEYGAHDQI ELYEDVLSPS ANNGDAPEDR DYMDNLAASV
GDDVVKGSVP NIVYTYTGKR IALYIGNLTW WTTDEDLTDA VHSLGVNDIL EIKFFENRAN
GQSKGFALIC VSSESSSKKL MDLLPKREMH GQKPIVTPCN KQFLSQFEMQ SRKTATQAGQ
MSGEGKAGPP GINARLPFPP GGRGRGRFPT SGPGGDRFPG PAGPGGPPPP FSAGMTPPRP
PMCPPGPPGP PGPPPPGQPL PPPLPGPPNR GERPPPPVMF PGQPYGQPSI VTLPPGPPPP
GYGPPPGPPP PQQGPPPPPG AFPPRPPGPP MALGPPPHLP GPPPGGPPPA PHVNPNFFPP
PGNAGMTSSD SRGPPPSDPY GRPPPYERGD YGPPGRDMDV VRTPLSEAEF EEIMNRNRAI
SSSAISRAVS DASAGDYGSA IETLVTAISL IKQSKVSADD RCKVLISSLQ DCLHGIESKS
YGSGSRRRER SRERDHSRSR EKSRRHKSRS RDRHDDYYRE RSRERERHRD RERDRDRERD
REREYRHR
