CPSF7_MOUSE
ID CPSF7_MOUSE Reviewed; 471 AA.
AC Q8BTV2; Q3TNF1; Q8BKE7; Q8CFS8;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 7 {ECO:0000312|MGI:MGI:1917826};
GN Name=Cpsf7 {ECO:0000312|MGI:MGI:1917826};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye, Spleen, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND SER-205, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BTV2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BTV2-2; Sequence=VSP_017196;
CC Name=3;
CC IsoId=Q8BTV2-3; Sequence=VSP_017195;
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; AK053375; BAC35368.1; -; mRNA.
DR EMBL; AK165330; BAE38138.1; -; mRNA.
DR EMBL; AK088603; BAC40447.1; -; mRNA.
DR EMBL; BC038812; AAH38812.1; -; mRNA.
DR CCDS; CCDS29579.1; -. [Q8BTV2-1]
DR RefSeq; NP_001157744.1; NM_001164272.1. [Q8BTV2-2]
DR RefSeq; NP_758506.3; NM_172302.3. [Q8BTV2-1]
DR RefSeq; XP_006527179.1; XM_006527116.3. [Q8BTV2-1]
DR RefSeq; XP_006527186.1; XM_006527123.2.
DR AlphaFoldDB; Q8BTV2; -.
DR SMR; Q8BTV2; -.
DR BioGRID; 234601; 6.
DR STRING; 10090.ENSMUSP00000038958; -.
DR iPTMnet; Q8BTV2; -.
DR PhosphoSitePlus; Q8BTV2; -.
DR EPD; Q8BTV2; -.
DR jPOST; Q8BTV2; -.
DR MaxQB; Q8BTV2; -.
DR PaxDb; Q8BTV2; -.
DR PeptideAtlas; Q8BTV2; -.
DR PRIDE; Q8BTV2; -.
DR ProteomicsDB; 283943; -. [Q8BTV2-1]
DR ProteomicsDB; 283944; -. [Q8BTV2-2]
DR ProteomicsDB; 283945; -. [Q8BTV2-3]
DR Antibodypedia; 14651; 138 antibodies from 24 providers.
DR Ensembl; ENSMUST00000038379; ENSMUSP00000038958; ENSMUSG00000034820. [Q8BTV2-1]
DR Ensembl; ENSMUST00000237321; ENSMUSP00000157834; ENSMUSG00000034820. [Q8BTV2-1]
DR GeneID; 269061; -.
DR KEGG; mmu:269061; -.
DR UCSC; uc008gpw.2; mouse. [Q8BTV2-1]
DR UCSC; uc008gqa.2; mouse. [Q8BTV2-2]
DR CTD; 79869; -.
DR MGI; MGI:1917826; Cpsf7.
DR VEuPathDB; HostDB:ENSMUSG00000034820; -.
DR eggNOG; KOG4849; Eukaryota.
DR GeneTree; ENSGT00730000110905; -.
DR HOGENOM; CLU_025289_1_1_1; -.
DR InParanoid; Q8BTV2; -.
DR OMA; YGDERCQ; -.
DR OrthoDB; 1016696at2759; -.
DR PhylomeDB; Q8BTV2; -.
DR TreeFam; TF316430; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-MMU-77595; Processing of Intronless Pre-mRNAs.
DR Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle.
DR BioGRID-ORCS; 269061; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Cpsf7; mouse.
DR PRO; PR:Q8BTV2; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8BTV2; protein.
DR Bgee; ENSMUSG00000034820; Expressed in retinal neural layer and 268 other tissues.
DR ExpressionAtlas; Q8BTV2; baseline and differential.
DR Genevisible; Q8BTV2; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISO:MGI.
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:MGI.
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:MGI.
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 Alternative splicing; Cytoplasm; Isopeptide bond; mRNA processing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..471
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 7"
FT /id="PRO_0000081528"
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 176..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..469
FT /note="Arg/Ser-rich domain"
FT /evidence="ECO:0000250|UniProtKB:Q8N684"
FT COMPBIAS 427..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N684"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N684"
FT CROSSLNK 354
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N684"
FT VAR_SEQ 1..234
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017195"
FT VAR_SEQ 176..184
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017196"
FT CONFLICT 262
FT /note="H -> Q (in Ref. 1; BAC40447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 52011 MW; 3ACC0F1FF7224109 CRC64;
MSEGVDLIDI YADEEFNQDS EFNNTDQIDL YDDVLTAASQ PSDDRSSSTE PPPPVRQEPA
PKPNNKTPAI LYTYSGLRSR RAAVYVGSFS WWTTDQQLIQ VIRSIGVYDV VELKFAENRA
NGQSKGYAEV VVASENSVHK LLELLPGKVL NGEKVDVRPA TRQNLSQFEA QARKRECVRV
PRGGIPPRAH SRDSSDSADG RATPSENLVP SSARVDKPPS VLPYFNRPPS ALPLMGLPPP
PIPPPPPLSS SFGVPPPPPG IHYQHLMPPP PRLPPHLAVP PPGAIPPALH LNPAFFPPPN
ATVGPPPDTY MKASTPYNHH GSRDSGPPPS TVSEAEFEEI MKRNRAISSS AISKAVSGAS
AGDYSDAIET LLTAIAVIKQ SRVANDERCR VLISSLKDCL HGIEAKSYSV GASGSSSRKR
HRSRERSPSR SRESSRRHRD LLHNEDRHDD YFQERNREHE RHRDRERDRH H
