CPSF6_DANRE
ID CPSF6_DANRE Reviewed; 545 AA.
AC Q6NWC6; Q6TH26;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 6 {ECO:0000250|UniProtKB:Q16630};
GN Name=cpsf6 {ECO:0000250|UniProtKB:Q16630};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NWC6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NWC6-2; Sequence=VSP_017193;
CC -!- SIMILARITY: Belongs to the RRM CPSF6/7 family. {ECO:0000305}.
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DR EMBL; AY398330; AAQ97763.1; -; mRNA.
DR EMBL; BC067642; AAH67642.1; -; mRNA.
DR RefSeq; NP_001017993.1; NM_001017993.1. [Q6NWC6-2]
DR RefSeq; XP_005164510.1; XM_005164453.3. [Q6NWC6-1]
DR AlphaFoldDB; Q6NWC6; -.
DR SMR; Q6NWC6; -.
DR STRING; 7955.ENSDARP00000076726; -.
DR PaxDb; Q6NWC6; -.
DR PRIDE; Q6NWC6; -.
DR Ensembl; ENSDART00000082289; ENSDARP00000076726; ENSDARG00000018618. [Q6NWC6-2]
DR Ensembl; ENSDART00000129521; ENSDARP00000110285; ENSDARG00000018618. [Q6NWC6-1]
DR GeneID; 327069; -.
DR KEGG; dre:327069; -.
DR CTD; 11052; -.
DR ZFIN; ZDB-GENE-030131-5277; cpsf6.
DR eggNOG; KOG4849; Eukaryota.
DR GeneTree; ENSGT00730000110905; -.
DR HOGENOM; CLU_025289_1_0_1; -.
DR InParanoid; Q6NWC6; -.
DR OMA; MFQGGPM; -.
DR OrthoDB; 1016696at2759; -.
DR PhylomeDB; Q6NWC6; -.
DR TreeFam; TF316430; -.
DR Reactome; R-DRE-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DRE-72187; mRNA 3'-end processing.
DR Reactome; R-DRE-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-DRE-77595; Processing of Intronless Pre-mRNAs.
DR PRO; PR:Q6NWC6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000018618; Expressed in early embryo and 34 other tissues.
DR ExpressionAtlas; Q6NWC6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0035061; C:interchromatin granule; ISS:UniProtKB.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
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:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
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 Alternative splicing; Cytoplasm; mRNA processing; Nucleus;
KW Reference proteome.
FT CHAIN 1..545
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 6"
FT /id="PRO_0000081525"
FT DOMAIN 81..161
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 37..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..385
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 174
FT /note="S -> SERRGFDNSHYHKG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15520368"
FT /id="VSP_017193"
SQ SEQUENCE 545 AA; 58775 MW; C67AF81A90BAAADF CRC64;
MADGVDHIDI YADVEEEFNQ ESDYPVHDQI DLYDDVISPS ANNGDAPEDR DYLDSLPAPG
GNEGSKGAPA NVVYTYNGKR IALYIGNLTW WTTDEDLTDA IRSIGINDVL EIKFFENRAN
GQSKGFALVC VGSDSSSRKL MDLLSKRELH GQNPIVTPCN KQSLSQFEMQ SRKSTQSGQM
SGEGKAGPPG SGSRGGGFPP GKGQRRFPGP PGQGDRFPGP VGPGGPPPHF PGMQGPPRLP
SGPPGPLGPP GPPPPGQGLP PPLGGPPNRG DRPPPPVLFP GQFGQPPMGP MPPGPPPPGY
GPPPGPPPPQ QGPPPPGPFP PRPPGPLGPP LGLAPPPHMQ GPPPGGPPPA PHVNPAFFPP
PGNNMPSSDG RGPPPGDPYG RPPPYDRDFP GGRDMDASRT PLSEAEFEEI MNRNRAISSS
AISRAVSDAS AADYGSAIET LVTAISLIKQ SKVSADDRCK VLISSLQDCL HGIESKSYGS
VAGRRERSRE RDHSRSREKS RRHKSRSRDR HEDYYRERSR ERDRHRERDR DRERDRERER
EYRHR
