CPSF2_MOUSE
ID CPSF2_MOUSE Reviewed; 782 AA.
AC O35218;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 2;
DE AltName: Full=Cleavage and polyadenylation specificity factor 100 kDa subunit;
DE Short=CPSF 100 kDa subunit;
GN Name=Cpsf2; Synonyms=Cpsf100, Mcpsf;
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].
RA Tevelev A., Schatz D.G.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 ZC3H3.
RX PubMed=16115198; DOI=10.1111/j.1365-2443.2005.00887.x;
RA Collart C., Remacle J.E., Barabino S., van Grunsven L.A., Nelles L.,
RA Schellens A., Van de Putte T., Pype S., Huylebroeck D., Verschueren K.;
RT "Smicl is a novel Smad interacting protein and cleavage and polyadenylation
RT specificity factor associated protein.";
RL Genes Cells 10:897-906(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Teratocarcinoma;
RX PubMed=17622165; DOI=10.1021/pr070122r;
RA Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT cells.";
RL J. Proteome Res. 6:3174-3186(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419; SER-420 AND SER-423, AND
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419; SER-420 AND SER-423, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, 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 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. Involved in the histone 3' end pre-mRNA processing
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and
CC FIP1L1. Interacts with CPSF3, CSTF2 and SYMPK (By similarity).
CC Interacts with ZC3H3 (PubMed:16115198). {ECO:0000250|UniProtKB:Q9P2I0,
CC ECO:0000269|PubMed:16115198}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF012822; AAB66830.1; -; mRNA.
DR EMBL; BC013628; AAH13628.1; -; mRNA.
DR EMBL; BC007163; AAH07163.1; -; mRNA.
DR CCDS; CCDS26116.1; -.
DR RefSeq; NP_058552.1; NM_016856.3.
DR RefSeq; XP_006516134.1; XM_006516071.3.
DR AlphaFoldDB; O35218; -.
DR SMR; O35218; -.
DR BioGRID; 206172; 14.
DR IntAct; O35218; 2.
DR MINT; O35218; -.
DR STRING; 10090.ENSMUSP00000047797; -.
DR iPTMnet; O35218; -.
DR PhosphoSitePlus; O35218; -.
DR EPD; O35218; -.
DR jPOST; O35218; -.
DR MaxQB; O35218; -.
DR PaxDb; O35218; -.
DR PeptideAtlas; O35218; -.
DR PRIDE; O35218; -.
DR ProteomicsDB; 284002; -.
DR Antibodypedia; 81; 124 antibodies from 25 providers.
DR DNASU; 51786; -.
DR Ensembl; ENSMUST00000047357; ENSMUSP00000047797; ENSMUSG00000041781.
DR GeneID; 51786; -.
DR KEGG; mmu:51786; -.
DR UCSC; uc007otx.2; mouse.
DR CTD; 53981; -.
DR MGI; MGI:1861601; Cpsf2.
DR VEuPathDB; HostDB:ENSMUSG00000041781; -.
DR eggNOG; KOG1135; Eukaryota.
DR GeneTree; ENSGT00910000144260; -.
DR HOGENOM; CLU_002227_1_1_1; -.
DR InParanoid; O35218; -.
DR OMA; MELVENC; -.
DR OrthoDB; 1314980at2759; -.
DR PhylomeDB; O35218; -.
DR TreeFam; TF106131; -.
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; 51786; 27 hits in 71 CRISPR screens.
DR ChiTaRS; Cpsf2; mouse.
DR PRO; PR:O35218; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; O35218; protein.
DR Bgee; ENSMUSG00000041781; Expressed in ileal epithelium and 246 other tissues.
DR Genevisible; O35218; MM.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; ISS:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
DR CDD; cd16293; CPSF2-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR027075; CPSF2.
DR InterPro; IPR025069; Cpsf2_C.
DR InterPro; IPR035639; CPSF2_MBL.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR PANTHER; PTHR45922; PTHR45922; 1.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF13299; CPSF100_C; 1.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..782
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 2"
FT /id="PRO_0000074394"
FT REGION 407..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:17622165, ECO:0007744|PubMed:21183079"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2I0"
SQ SEQUENCE 782 AA; 88383 MW; 5F60DBB9DEDEBB4B CRC64;
MTSIIKLTTL SGVQEESALC YLLQVDEFRF LLDCGWDEHF SVDIIDSLRK HVHQIDAVLL
SHPDPLHLGA LPFAVGKLGL NCAIYATIPV YKMGQMFMYD LYQSRHNTED FTLFTLDDVD
AAFDKIQQLK FSQIVNLKGK GHGLSITPLP AGHMIGGTIW KIVKDGEEEI VYAVDFNHKR
EIHLNGCSLE MLSRPSLLIT DSFNATYVQP RRKQRDEQLL TNVLETLRGD GNVLIAVDTA
GRVLELAQLL DQIWRTKDAG LGVYSLALLN NVSYNVVEFS KSQVEWMSDK LMRCFEDKRN
NPFQFRHLSL CHGLSDLARV PSPKVVLASQ PDLECGFSRD LFIQWCQDPK NSIILTYRTT
PGTLARFLID NPTEKVTEIE LRKRVKLEGK ELEEYVEKEK LKKEAAKKLE QSKEADIDSS
DESDVEEDVD QPSAHKTKHD LMMKGEGSRK GSFFKQAKKS YPMFPAPEER IKWDEYGEII
KPEDFLVPEL QATEEEKSKL ESGLTNGEEP MDQDLSDVPT KCVSATESIE IKARVTYIDY
EGRSDGDSIK KIINQMKPRQ LIIVHGPPEA SQDLAECCRA FGGKDIKVYM PKLHETVDAT
SETHIYQVRL KDSLVSSLQF CKAKDAELAW IDGVLDMRVS KVDTGVILEE GELKDDGEDS
EMQVDAPSDS SAMAQQKAMK SLFGEDEKEL GEETEIIPTL EPLPPHEVPG HQSVFMNEPR
LSDFKQVLLR EGIQAEFVGG VLVCNNQVAV RRTETGRIGL EGCLCQDFYR IRDLLYEQYA
IV
