CPSF1_MOUSE
ID CPSF1_MOUSE Reviewed; 1441 AA.
AC Q9EPU4;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 1;
DE AltName: Full=Cleavage and polyadenylation specificity factor 160 kDa subunit;
DE Short=CPSF 160 kDa subunit;
GN Name=Cpsf1; Synonyms=Cpsf160;
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 [MRNA].
RC TISSUE=Testis;
RX PubMed=11369601; DOI=10.1095/biolreprod64.6.1722;
RA Dass B., Attaya E.N., Michelle Wallace A., MacDonald C.C.;
RT "Overexpression of the CstF-64 and CPSF-160 polyadenylation protein
RT messenger RNAs in mouse male germ cells.";
RL Biol. Reprod. 64:1722-1729(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [3]
RP INTERACTION WITH TENT2.
RX PubMed=17927953; DOI=10.1016/j.bbrc.2007.09.096;
RA Nakanishi T., Kumagai S., Kimura M., Watanabe H., Sakurai T., Kimura M.,
RA Kashiwabara S., Baba T.;
RT "Disruption of mouse poly(A) polymerase mGLD-2 does not alter
RT polyadenylation status in oocytes and somatic cells.";
RL Biochem. Biophys. Res. Commun. 364:14-19(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Pancreas, Spleen, and Testis;
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 and polyadenylation specificity
CC factor (CPSF) complex that plays 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. This subunit is involved in the RNA recognition step
CC of the polyadenylation reaction (By similarity). May play a role in eye
CC morphogenesis and the development of retinal ganglion cell projections
CC to the midbrain (By similarity). {ECO:0000250|UniProtKB:A0A0R4IC37,
CC ECO:0000250|UniProtKB:Q10570}.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and
CC FIP1L1. Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts
CC with FIP1L1 and SRRM1. Interacts with TUT1; the interaction is direct
CC and mediates the recruitment of the CPSF complex on the 3'UTR of
CC selected pre-mRNAs (By similarity). Interacts with TENT2/GLD2.
CC {ECO:0000250, ECO:0000269|PubMed:17927953}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CPSF1 family. {ECO:0000305}.
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DR EMBL; AF322193; AAG40326.1; -; mRNA.
DR EMBL; BC056388; AAH56388.1; -; mRNA.
DR CCDS; CCDS27577.1; -.
DR RefSeq; NP_001157645.1; NM_001164173.1.
DR RefSeq; NP_444423.1; NM_053193.2.
DR AlphaFoldDB; Q9EPU4; -.
DR SMR; Q9EPU4; -.
DR BioGRID; 220487; 8.
DR STRING; 10090.ENSMUSP00000071794; -.
DR iPTMnet; Q9EPU4; -.
DR PhosphoSitePlus; Q9EPU4; -.
DR EPD; Q9EPU4; -.
DR MaxQB; Q9EPU4; -.
DR PaxDb; Q9EPU4; -.
DR PeptideAtlas; Q9EPU4; -.
DR PRIDE; Q9EPU4; -.
DR ProteomicsDB; 283620; -.
DR Antibodypedia; 14844; 82 antibodies from 21 providers.
DR DNASU; 94230; -.
DR Ensembl; ENSMUST00000071898; ENSMUSP00000071794; ENSMUSG00000034022.
DR GeneID; 94230; -.
DR KEGG; mmu:94230; -.
DR UCSC; uc007wky.2; mouse.
DR CTD; 29894; -.
DR MGI; MGI:2679722; Cpsf1.
DR VEuPathDB; HostDB:ENSMUSG00000034022; -.
DR eggNOG; KOG1896; Eukaryota.
DR GeneTree; ENSGT00950000183151; -.
DR HOGENOM; CLU_002414_0_0_1; -.
DR InParanoid; Q9EPU4; -.
DR OrthoDB; 360328at2759; -.
DR PhylomeDB; Q9EPU4; -.
DR TreeFam; TF314322; -.
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; 94230; 30 hits in 111 CRISPR screens.
DR ChiTaRS; Cpsf1; mouse.
DR PRO; PR:Q9EPU4; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9EPU4; protein.
DR Bgee; ENSMUSG00000034022; Expressed in dorsal pancreas and 255 other tissues.
DR ExpressionAtlas; Q9EPU4; baseline and differential.
DR Genevisible; Q9EPU4; MM.
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:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISO:MGI.
DR GO; GO:0006378; P:mRNA polyadenylation; ISO:MGI.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF03178; CPSF_A; 1.
DR Pfam; PF10433; MMS1_N; 1.
PE 1: Evidence at protein level;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..1441
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 1"
FT /id="PRO_0000074388"
FT REGION 404..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10570"
SQ SEQUENCE 1441 AA; 160818 MW; 5D927224152AC3B9 CRC64;
MYAVYKQAHP PTGLEFTMYC NFFNNSERNL VVAGTSQLYV YRLNRDAEAL TKNDGSTEGK
AHREKLELVA SFSFFGNVMS MASVQLAGAK RDALLLSFKD AKLSVVEYDP GTHDLKTLSL
HYFEEPELRD GFVQNVHTPR VRVDPDGRCA AMLIYGTRLV VLPFRRESLA EEHEGLMGEG
QRSSFLPSYI IDVRALDEKL LNIIDLQFLH GYYEPTLLIL FEPNQTWPGR VAVRQDTCSI
VAISLNITQK VHPVIWSLTS LPFDCTQALA VPKPIGGVVI FAVNSLLYLN QSVPPYGVAL
NSLTTGTTAF PLRTQEGVRI TLDCAQAAFI SYDKMVISLK GGEIYVLTLI TDGMRSVRAF
HFDKAAASVL TTSMVTMEPG YLFLGSRLGN SLLLKYTEKL QEPPASSVRE AADKEEPPSK
KKRVEPAVGW TGGKTVPQDE VDEIEVYGSE AQSGTQLATY SFEVCDSMLN IGPCANAAVG
EPAFLSEEFQ NSPEPDLEIV VCSGYGKNGA LSVLQKSIRP QVVTTFELPG CYDMWTVIAP
VRKEEEETPK AESTEQEPSA PKAEEDGRRH GFLILSREDS TMILQTGQEI MELDTSGFAT
QGPTVFAGNI GDNRYIVQVS PLGIRLLEGV NQLHFIPVDL GAPIVQCAVA DPYVVIMSAE
GHVTMFLLKS DSYGGRHHRL ALHKPPLHHQ SKVIALCLYR DVSGMFTTES RLGGARDELG
GRSGSEAEGL GSETSPTVDD EEEMLYGDSS ALFSPSKEEA RRSSQPPADR DPAPFKADPT
HWCLLVRENG TMEIYQLPDW RLVFLVKNFP VGQRVLVDSS FGQPTTQGEV RKEEATRQGE
LPLVKEVLLV ALGSRQSRPY LLVHVDQELL IYEAFPHDSQ LGQGNLKVRF KKVPHNINFR
EKKPKPSKKK AEGCSTEEGS GGRGRVARFR YFEDIYGYSG VFICGPSPHW LLVTGRGALR
LHPMGIDGPI DSFAPFHNVN CPRGFLYFNR QGELRISVLP AYLSYDAPWP VRKIPLRCTA
HYVAYHVESK VYAVATSTNT PCTRIPRMTG EEKEFEAIER DDRYIHPQQE AFSIQLISPV
SWEAIPNARI ELEEWEHVTC MKTVSLRSEE TVSGLKGYVA AGTCLMQGEE VTCRGRILIM
DVIEVVPEPG QPLTKNKFKV LYEKEQKGPV TALCHCNGHL VSAIGQKIFL WSLRASELTG
MAFIDTQLYI HQMISVKNFI LAADVMKSIS LLRYQEESKT LSLVSRDAKP LEVYSVDFMV
DNAQLGFLVS DRDRNLMVYM YLPEAKESFG GMRLLRRADF HVGAHVNTFW RTPCRGAAEG
PSKKSVVWEN KHITWFATLD GGIGLLLPMQ EKTYRRLLML QNALTTMLPH HAGLNPRAFR
MLHVDRRILQ NAVRNVLDGE LLNRYLYLST MERSELAKKI GTTPDIILDD LLETDRVTAH
F
