CPSF7_RAT
ID CPSF7_RAT Reviewed; 462 AA.
AC Q5XI29;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 7 {ECO:0000305};
GN Name=Cpsf7 {ECO:0000312|RGD:1305441};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-194, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. CPSF7 activates directly the mRNA 3'-processing
CC machinery. Binds to pA signals in RNA substrates.
CC {ECO:0000250|UniProtKB:Q8N684}.
CC -!- SUBUNIT: Component of the cleavage factor Im (CFIm) complex which is a
CC heterotetramer composed of two subunits of NUDT21/CPSF5 and two
CC subunits of CPSF6 or CPSF7 or a heterodimer of CPSF6 and CPSF7. The
CC cleavage factor Im (CFIm) complex associates with the CPSF and CSTF
CC complexes to promote the assembly of the core mRNA 3'-processing
CC machinery. Interacts with NUDT21/CPSF5. Interacts (via Arg/Ser-rich
CC domain) with FIP1L1 (preferentially via unphosphorylated form and
CC Arg/Glu/Asp-rich region); this interaction mediates, at least in part,
CC the interaction between the CFIm and CPSF complexes and may be
CC inhibited by CPSF7 hyper-phosphorylation.
CC {ECO:0000250|UniProtKB:Q8N684}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N684}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8N684}. Note=Shuttles between the nucleus and
CC the cytoplasm in a transcription- and XPO1/CRM1-independent manner,
CC most probably in complex with the cleavage factor Im complex (CFIm).
CC {ECO:0000250|UniProtKB:Q8N684}.
CC -!- DOMAIN: Contains an Arg/Ser-rich domain composed of arginine-serine
CC dipeptide repeats within the C-terminal region that is necessary and
CC sufficient for activating mRNA 3'-processing.
CC {ECO:0000250|UniProtKB:Q8N684}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q8N684}.
CC -!- PTM: Asymmetrically dimethylated on arginine residues by PRMT1.
CC {ECO:0000250|UniProtKB:Q8N684}.
CC -!- SIMILARITY: Belongs to the RRM CPSF6/7 family. {ECO:0000305}.
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DR EMBL; BC083864; AAH83864.1; -; mRNA.
DR RefSeq; NP_001014267.1; NM_001014245.2.
DR RefSeq; XP_008758461.1; XM_008760239.2.
DR AlphaFoldDB; Q5XI29; -.
DR SMR; Q5XI29; -.
DR BioGRID; 265348; 1.
DR IntAct; Q5XI29; 1.
DR STRING; 10116.ENSRNOP00000028074; -.
DR iPTMnet; Q5XI29; -.
DR PhosphoSitePlus; Q5XI29; -.
DR jPOST; Q5XI29; -.
DR PaxDb; Q5XI29; -.
DR PRIDE; Q5XI29; -.
DR GeneID; 365407; -.
DR KEGG; rno:365407; -.
DR UCSC; RGD:1305441; rat.
DR CTD; 79869; -.
DR RGD; 1305441; Cpsf7.
DR VEuPathDB; HostDB:ENSRNOG00000020668; -.
DR eggNOG; KOG4849; Eukaryota.
DR HOGENOM; CLU_025289_1_1_1; -.
DR InParanoid; Q5XI29; -.
DR OMA; YGDERCQ; -.
DR OrthoDB; 1016696at2759; -.
DR PhylomeDB; Q5XI29; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-RNO-72187; mRNA 3'-end processing.
DR Reactome; R-RNO-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-RNO-77595; Processing of Intronless Pre-mRNAs.
DR Reactome; R-RNO-9013422; RHOBTB1 GTPase cycle.
DR PRO; PR:Q5XI29; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020668; Expressed in thymus and 20 other tissues.
DR Genevisible; Q5XI29; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISO:RGD.
DR GO; GO:0005849; C:mRNA cleavage factor complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:1990120; P:messenger ribonucleoprotein complex assembly; ISS:UniProtKB.
DR GO; GO:0031124; P:mRNA 3'-end processing; ISO:RGD.
DR GO; GO:0110104; P:mRNA alternative polyadenylation; ISS:UniProtKB.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; ISS:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; ISO:RGD.
DR CDD; cd12644; RRM_CFIm59; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034772; CPSF6/7.
DR InterPro; IPR034770; CPSF7.
DR InterPro; IPR034773; CPSF7_RRM.
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:SF2; PTHR23204:SF2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..462
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 7"
FT /id="PRO_0000081529"
FT DOMAIN 82..162
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 34..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..460
FT /note="Arg/Ser-rich domain"
FT /evidence="ECO:0000250|UniProtKB:Q8N684"
FT COMPBIAS 174..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 194
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTV2"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N684"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N684"
FT CROSSLNK 345
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N684"
SQ SEQUENCE 462 AA; 51073 MW; 125D10ACC75A23C1 CRC64;
MSEGVDLIDI YADEEFNQDS EFNNTDQIDL YDDVLTAASQ PSDDRSSSTE PPPPVRQEPA
PKPNNKTPAI LYTYSGLRSR RAAVYVGSFS WWTTDQQLIQ VIRSIGVYDV VELKFAENRA
NGQSKGYAEV VVASENSVHK LLELLPGKVL NGEKVDVRPA TRQNLSQFEA QARKRIPPRA
HSRDSSDSAD GRATPSENLV PSSARVDKPP SVLPYFNRPP SALPLMGLPP PPIPPPPPLS
SSFGVPPPPP GIHYQHLMPP PPRLPPHLAV PPPGAIPPAL HLNPAFFPPP NATVGPPPDT
YMKASTPYNH HGSRDSGPLP STVSEAEFEE IMKRNRAISS SAISKAVSGA SAGDYSDAIE
TLLTAIAVIK QSRVANDERC RVLISSLKDC LHGIEAKSYS VGASGSSSRK RHRSRERSPS
RSRESSRRHR DLLHNEDRHD DYFQERNREH ERHRDRERDR HH
