CPSF1_CAEEL
ID CPSF1_CAEEL Reviewed; 1454 AA.
AC Q9N4C2;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable 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=cpsf-1; ORFNames=Y76B12C.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP IDENTIFICATION.
RX PubMed=18946043; DOI=10.1073/pnas.0807104105;
RA Cui M., Allen M.A., Larsen A., Macmorris M., Han M., Blumenthal T.;
RT "Genes involved in pre-mRNA 3'-end formation and transcription termination
RT revealed by a lin-15 operon Muv suppressor screen.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:16665-16670(2008).
CC -!- FUNCTION: CPSF plays a key role in pre-mRNA 3'-end formation,
CC recognizing the AAUAAA signal sequence and interacting with
CC poly(A)polymerase and other factors to bring about cleavage and poly(A)
CC addition. This subunit is involved in the RNA recognition step of the
CC polyadenylation reaction (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: CPSF is a heterotetramer composed of four distinct subunits
CC 160 (cpsf-1), 100 (cpsf-2), 70 (cpsf-3), and 30 kDa (cpsf-4).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CPSF1 family. {ECO:0000305}.
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DR EMBL; FO081666; CCD73182.1; -; Genomic_DNA.
DR RefSeq; NP_500157.2; NM_067756.4.
DR AlphaFoldDB; Q9N4C2; -.
DR SMR; Q9N4C2; -.
DR BioGRID; 42157; 6.
DR IntAct; Q9N4C2; 1.
DR MINT; Q9N4C2; -.
DR STRING; 6239.Y76B12C.7a.2; -.
DR EPD; Q9N4C2; -.
DR PaxDb; Q9N4C2; -.
DR PeptideAtlas; Q9N4C2; -.
DR EnsemblMetazoa; Y76B12C.7a.1; Y76B12C.7a.1; WBGene00022301.
DR GeneID; 177003; -.
DR KEGG; cel:CELE_Y76B12C.7; -.
DR CTD; 177003; -.
DR WormBase; Y76B12C.7a; CE29932; WBGene00022301; cpsf-1.
DR eggNOG; KOG1896; Eukaryota.
DR HOGENOM; CLU_002414_0_0_1; -.
DR InParanoid; Q9N4C2; -.
DR OMA; PMTKFKL; -.
DR OrthoDB; 360328at2759; -.
DR PhylomeDB; Q9N4C2; -.
DR Reactome; R-CEL-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-CEL-72187; mRNA 3'-end processing.
DR Reactome; R-CEL-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-CEL-77595; Processing of Intronless Pre-mRNAs.
DR PRO; PR:Q9N4C2; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00022301; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; Q9N4C2; baseline and differential.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 3.
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 3: Inferred from homology;
KW mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..1454
FT /note="Probable cleavage and polyadenylation specificity
FT factor subunit 1"
FT /id="PRO_0000074390"
FT REGION 736..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1454 AA; 162716 MW; DEFEF8BB2EFBD16F CRC64;
MYGYLRETDD STAINFSAYG KFLPGENTGF QLLTIGAKFI RIFRVNPYVL KEPGEDNEEW
QQKTKLECMF SCRLLNKCHS IAVARVPQLP DQDSILMTFD DAKLSIVSIN EKERNMQTIS
LHAFENEYLR DGFINHFQPP LVRSDPSNRC AACLVYGKHI AILPFHENSK RIHSYVIPLK
QIDPRLDNIA DMVFLDGYYE PTILFLYEPI QTTPGRACVR YDTMCIMGVS VNIVDRQFAV
VWQTANLPMD CSQLLPIPKP LGGALVFGSN TVVYLNQAVP PCGLVLNSCY DGFTKFPLKD
LKHLKMTLDC STSVYMEDGR IAVGSRDGDL FLLRLMTSSG GGTVKSLEFS KVYETSIAYS
LTVCAPGHLF VGSRLGDSQL LEYTLLKTTR DCAVKRLKID NKDPAAAEIE LDEDDMELYG
GAIEEQQNDD DEQIDESLQF RELDRLRNVG PVKSMCVGRP NYMSNDLVDA KRRDPVFDLV
TASGHGKNGA LCVHQRSLRP EIITSSLLEG AEQLWAVGRK ENESHKYLIV SRVRSTLILE
LGEELVELEE QLFVTGEPTV AAGELSQGAL AVQVTSTCIA LVTDGQQMQE VHIDSNFPVI
QASIVDPYVA LLTQNGRLLL YELVMEPYVQ LREVDISATS FATWHATAQN LTQLTSISIY
ADASEIMKFA AAEKSMGGGG GGDGEVSTAE NAMMKKEQHE EAILLHGEDD DFLYGDEDET
IMEQNFPVEN GEATIKQSNT RKRKRLGHDA IQSSRGGEQS DAIDPTRTFS SISHWLIVSH
ENGRLSIHSL PEMEVVYQIG RFSNVPELLV DLTVEEEEKE RKAKAQQAAK EASVPTDEAE
QLNTEMKQLC ERVLEAQIVG MGINQAHPIL MAIVDEQVVL YEMFSSSNPI PGHLGISFRK
LPHFICLRTS SHLNSDGKRA PFEMKINNGK RFSLIHPFER VSSVNNGVMI VGAVPTLLVY
GAWGGMQTHQ MTVDGPIKAF TPFNNENVLH GIVYMTQHKS ELRIARMHPD FDYEMPYPVK
KIEVGRTIHH VRYLMNSDVY AVVSSIPKPS NKIWVVMNDD KQEEIHEKDE NFVLPAPPKY
TLNLFSSQDW AAVPNTEISF EDMEAVTACE DVALKSESTI SGLETLLAMG TVNNYGEEVL
VRGRIILCEV IEVVPEPDQP TSNRKIKVLF DKEQKGPVTG LCAINGLLLC GMGQKVFIWQ
FKDNDLMGIS FLDMHYYVYQ LHSLRTIAIA CDARESMSLI RFQEDNKAMS IASRDDRKCA
QPPMASQLVV DGAHVGFLLS DETGNITMFN YAPEAPESNG GERLTVRAAI NIGTNINAFV
RLRGHTSLLQ LNNEDEKEAI EQRMTTVFAS LDGSFGFVRP LTEKSYRRLH FLQTFIGSVT
PQIAGLHIKG SRSAKPSQPI VNGRNARNLI DGDVVEQYLH LSLYDKTDLA RRLGVGRYHI
IDDLMQLRRM AFYY
