CPSF4_MOUSE
ID CPSF4_MOUSE Reviewed; 211 AA.
AC Q8BQZ5; O54930;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 4;
DE AltName: Full=Cleavage and polyadenylation specificity factor 30 kDa subunit;
DE Short=CPSF 30 kDa subunit;
DE AltName: Full=Clipper homolog;
DE AltName: Full=Clipper/CPSF 30K;
GN Name=Cpsf4; Synonyms=Cpsf30;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
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 [MRNA] OF 17-211 (ISOFORM 2), AND FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=9512528; DOI=10.1093/nar/26.7.1597;
RA Bai C., Tolias P.P.;
RT "Drosophila clipper/CPSF 30K is a post-transcriptionally regulated nuclear
RT protein that binds RNA containing GC clusters.";
RL Nucleic Acids Res. 26:1597-1604(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-211 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
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) (By similarity). {ECO:0000250, ECO:0000269|PubMed:9512528}.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and
CC FIP1L1. Interacts with FIP1L1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BQZ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BQZ5-2; Sequence=VSP_008603, VSP_008604, VSP_008606,
CC VSP_008608;
CC Name=3;
CC IsoId=Q8BQZ5-3; Sequence=VSP_008603, VSP_008605, VSP_008607;
CC -!- SIMILARITY: Belongs to the CPSF4/YTH1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC53567.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH57067.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK046064; BAC32587.1; -; mRNA.
DR EMBL; AF033201; AAC53567.1; ALT_INIT; mRNA.
DR EMBL; BC057067; AAH57067.1; ALT_INIT; mRNA.
DR CCDS; CCDS19859.1; -. [Q8BQZ5-1]
DR RefSeq; NP_001278177.1; NM_001291248.1.
DR RefSeq; NP_001278178.1; NM_001291249.1.
DR RefSeq; NP_848671.1; NM_178576.3. [Q8BQZ5-1]
DR AlphaFoldDB; Q8BQZ5; -.
DR SMR; Q8BQZ5; -.
DR BioGRID; 207591; 2.
DR STRING; 10090.ENSMUSP00000069243; -.
DR iPTMnet; Q8BQZ5; -.
DR PhosphoSitePlus; Q8BQZ5; -.
DR EPD; Q8BQZ5; -.
DR MaxQB; Q8BQZ5; -.
DR PaxDb; Q8BQZ5; -.
DR PeptideAtlas; Q8BQZ5; -.
DR PRIDE; Q8BQZ5; -.
DR ProteomicsDB; 283940; -. [Q8BQZ5-1]
DR ProteomicsDB; 283941; -. [Q8BQZ5-2]
DR ProteomicsDB; 283942; -. [Q8BQZ5-3]
DR Antibodypedia; 16165; 227 antibodies from 30 providers.
DR DNASU; 54188; -.
DR Ensembl; ENSMUST00000070487; ENSMUSP00000069243; ENSMUSG00000029625. [Q8BQZ5-1]
DR GeneID; 54188; -.
DR KEGG; mmu:54188; -.
DR UCSC; uc009amj.2; mouse. [Q8BQZ5-1]
DR CTD; 10898; -.
DR MGI; MGI:1861602; Cpsf4.
DR VEuPathDB; HostDB:ENSMUSG00000029625; -.
DR eggNOG; KOG1040; Eukaryota.
DR GeneTree; ENSGT00940000155520; -.
DR InParanoid; Q8BQZ5; -.
DR PhylomeDB; Q8BQZ5; -.
DR TreeFam; TF314871; -.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
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 BioGRID-ORCS; 54188; 27 hits in 75 CRISPR screens.
DR ChiTaRS; Cpsf4; mouse.
DR PRO; PR:Q8BQZ5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BQZ5; protein.
DR Bgee; ENSMUSG00000029625; Expressed in floor plate of midbrain and 274 other tissues.
DR ExpressionAtlas; Q8BQZ5; baseline and differential.
DR Genevisible; Q8BQZ5; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
DR InterPro; IPR045348; CPSF4/Yth1.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR23102; PTHR23102; 3.
DR Pfam; PF00642; zf-CCCH; 2.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SMART; SM00356; ZnF_C3H1; 4.
DR SUPFAM; SSF57756; SSF57756; 1.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 3.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Metal-binding; mRNA processing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..211
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 4"
FT /id="PRO_0000074403"
FT ZN_FING 35..61
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 62..89
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 111..137
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 185..202
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95639"
FT VAR_SEQ 103
FT /note="G -> GECSNKECPFLHIDPESKIKDCPWYDRGFCKHG (in isoform 2
FT and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9512528"
FT /id="VSP_008603"
FT VAR_SEQ 158
FT /note="K -> KQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9512528"
FT /id="VSP_008604"
FT VAR_SEQ 159..180
FT /note="RAPQVIGVMQSQNSSAGNRGPR -> VLYPAASLATLACRDGLITHSV (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008605"
FT VAR_SEQ 174..188
FT /note="AGNRGPRPLEQVTCY -> DSSSSSSSWNHCGAA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9512528"
FT /id="VSP_008606"
FT VAR_SEQ 181..211
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008607"
FT VAR_SEQ 189..211
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9512528"
FT /id="VSP_008608"
SQ SEQUENCE 211 AA; 23653 MW; F5656741519E0E26 CRC64;
MQEIIASVDH IKFDLEIAVE QQLGAQPLPF PGMDKSGAAV CEFFLKAACG KGGMCPFRHI
SGEKTVVCKH WLRGLCKKGD QCEFLHEYDM TKMPECYFYS KFGPLCRHRH TRRVICVNYL
VGFCPEGPSC KFMHPRFELP MGTTEQPPLP QQTQPPTKRA PQVIGVMQSQ NSSAGNRGPR
PLEQVTCYKC GEKGHYANRC TKGHLAFLSG Q
