CNOT1_CAEEL
ID CNOT1_CAEEL Reviewed; 2641 AA.
AC Q20937; A0A1D3PCL8; A0A1D3PCL9; A0A1D3PCM5; S5ZDJ9;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=CCR4-NOT transcription complex subunit let-711 {ECO:0000305};
DE AltName: Full=CCR4-associated factor let-711 {ECO:0000305};
DE AltName: Full=Lethal protein 711 {ECO:0000312|WormBase:F57B9.2a};
DE AltName: Full=Negative regulator of transcription subunit 1 homolog {ECO:0000250|UniProtKB:A5YKK6};
DE Short=NOT1 {ECO:0000250|UniProtKB:A5YKK6};
GN Name=let-711 {ECO:0000303|PubMed:23843623, ECO:0000312|WormBase:F57B9.2a};
GN Synonyms=ntl-1 {ECO:0000312|WormBase:F57B9.2a},
GN spn-3 {ECO:0000312|WormBase:F57B9.2a};
GN ORFNames=F57B9.2 {ECO:0000312|WormBase:F57B9.2a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AGT18674.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN THE CCR4-NOT
RP COMPLEX, INTERACTION WITH CCF-1 AND CCR-4, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=23843623; DOI=10.1242/jcs.132936;
RA Nousch M., Techritz N., Hampel D., Millonigg S., Eckmann C.R.;
RT "The Ccr4-Not deadenylase complex constitutes the main poly(A) removal
RT activity in C. elegans.";
RL J. Cell Sci. 126:4274-4285(2013).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16971515; DOI=10.1091/mbc.e06-02-0107;
RA DeBella L.R., Hayashi A., Rose L.S.;
RT "LET-711, the Caenorhabditis elegans NOT1 ortholog, is required for spindle
RT positioning and regulation of microtubule length in embryos.";
RL Mol. Biol. Cell 17:4911-4924(2006).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18692039; DOI=10.1016/j.ydbio.2008.07.008;
RA Gallo C.M., Munro E., Rasoloson D., Merritt C., Seydoux G.;
RT "Processing bodies and germ granules are distinct RNA granules that
RT interact in C. elegans embryos.";
RL Dev. Biol. 323:76-87(2008).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=28204614; DOI=10.1093/nar/gkw872;
RA Wu E., Vashisht A.A., Chapat C., Flamand M.N., Cohen E., Sarov M.,
RA Tabach Y., Sonenberg N., Wohlschlegel J., Duchaine T.F.;
RT "A continuum of mRNP complexes in embryonic microRNA-mediated silencing.";
RL Nucleic Acids Res. 45:2081-2098(2017).
CC -!- FUNCTION: Scaffolding component of the CCR4-NOT complex which is one of
CC the major cellular mRNA deadenylases and is linked to various cellular
CC processes including bulk mRNA degradation, miRNA-mediated repression,
CC translational repression during translational initiation and general
CC transcription regulation (PubMed:23843623, PubMed:28204614). Positively
CC regulates the accumulation of the CCR4-NOT complex component ccr-1
CC (PubMed:23843623). Within the complex promotes germ cell development
CC and fertility in hermaphrodites (PubMed:23843623). Additional complex
CC functions may be a consequence of its influence on mRNA expression (By
CC similarity). Its scaffolding function implies its interaction with the
CC catalytic complex module and diverse RNA-binding proteins mediating the
CC complex recruitment to selected mRNA 3'UTRs (By similarity). Mediates
CC the recruitment of the CCR4-NOT complex to miRNA targets and to the
CC RISC complex (Probable). Acts as a transcriptional repressor (By
CC similarity). Represses the ligand-dependent transcriptional activation
CC by nuclear receptors (By similarity). In embryos, plays a role in
CC female pronucleus and mitotic spindle positioning during the first
CC cleavage divisions after fertilization (PubMed:16971515). This may
CC partly be through negatively regulating the accumulation of zyg-9 at
CC the centrosome (PubMed:16971515). Negatively regulates the formation of
CC long astral microtubules in developing embryos (PubMed:16971515).
CC Required for the stabilization and degradation of maternal mRNAs such
CC as nos-2 in somatic blastomeres (PubMed:18692039).
CC {ECO:0000250|UniProtKB:A5YKK6, ECO:0000269|PubMed:16971515,
CC ECO:0000269|PubMed:18692039, ECO:0000269|PubMed:23843623,
CC ECO:0000269|PubMed:28204614, ECO:0000305|PubMed:28204614}.
CC -!- SUBUNIT: Component of the CCR4-NOT complex at least composed of ccf-1,
CC ccr-4 and let-711, which is required for germ cell development in
CC hermaphrodites (PubMed:23843623). Within the complex interacts with
CC ccf-1 and ccr-4; the interactions are direct (PubMed:23843623).
CC {ECO:0000269|PubMed:23843623}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A5YKK6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=a {ECO:0000312|WormBase:F57B9.2a}; Synonyms=NTL-1a
CC {ECO:0000303|PubMed:23843623};
CC IsoId=Q20937-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F57B9.2b};
CC IsoId=Q20937-2; Sequence=VSP_061213;
CC Name=c {ECO:0000312|WormBase:F57B9.2c};
CC IsoId=Q20937-3; Sequence=VSP_061212;
CC Name=d {ECO:0000312|WormBase:F57B9.2d}; Synonyms=NTL-1b
CC {ECO:0000303|PubMed:23843623};
CC IsoId=Q20937-4; Sequence=VSP_061211;
CC Name=e {ECO:0000312|WormBase:F57B9.2e};
CC IsoId=Q20937-5; Sequence=VSP_061210;
CC -!- TISSUE SPECIFICITY: Highly expressed in the germline of hermaphrodites.
CC {ECO:0000269|PubMed:23843623}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in embryos.
CC {ECO:0000269|PubMed:23843623}.
CC -!- DOMAIN: Contains Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, a motif known to
CC be important for the association with nuclear receptors.
CC {ECO:0000250|UniProtKB:A5YKK6}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in sterility and
CC the production of inviable embryos which are osmotically sensitive,
CC exhibit nuclear rotation defects and irregular positioning of the
CC mitotic spindle which is located towards the posterior or lateral
CC cortex during anaphase (PubMed:23843623, PubMed:16971515). RNAi-
CC mediated knockdown may also result in a reduced brood size and larval
CC lethality (PubMed:23843623). RNAi-mediated knockdown disrupts the
CC arrangement and differentiation of oocytes in the proximal region and
CC as a result small oocyte-like cells arrange in several rows in the
CC germline (PubMed:23843623). RNAi-mediated knockdown reduces the levels
CC of ccf-1, but does not alter ccr-4 levels (PubMed:23843623). RNAi-
CC mediated knockdown results in reduced global poly(A) tail deadenylation
CC (PubMed:23843623). RNAi-mediated knockdown results in reduces
CC degradation of nos-2 mRNA, impairs the recruitment of lsm-1 and
CC decreases the number of patr-1-positive granules in somatic blastomeres
CC (PubMed:18692039). {ECO:0000269|PubMed:16971515,
CC ECO:0000269|PubMed:18692039, ECO:0000269|PubMed:23843623}.
CC -!- SIMILARITY: Belongs to the CNOT1 family. {ECO:0000305}.
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DR EMBL; KC964869; AGT18674.1; -; mRNA.
DR EMBL; KC964870; AGT18675.1; -; mRNA.
DR EMBL; BX284603; CCD70321.2; -; Genomic_DNA.
DR EMBL; BX284603; SCN13882.1; -; Genomic_DNA.
DR EMBL; BX284603; SCN13883.1; -; Genomic_DNA.
DR EMBL; BX284603; SCN13884.1; -; Genomic_DNA.
DR EMBL; BX284603; SCN13885.1; -; Genomic_DNA.
DR RefSeq; NP_001333556.1; NM_001346614.1.
DR RefSeq; NP_001333557.1; NM_001346615.1. [Q20937-3]
DR RefSeq; NP_001333558.1; NM_001346616.1. [Q20937-4]
DR RefSeq; NP_001333559.1; NM_001346617.1. [Q20937-5]
DR RefSeq; NP_498516.3; NM_066115.5. [Q20937-1]
DR AlphaFoldDB; Q20937; -.
DR SMR; Q20937; -.
DR ComplexPortal; CPX-634; Ccr4-Not complex.
DR IntAct; Q20937; 3.
DR STRING; 6239.F57B9.2; -.
DR EPD; Q20937; -.
DR PaxDb; Q20937; -.
DR PeptideAtlas; Q20937; -.
DR EnsemblMetazoa; F57B9.2a.1; F57B9.2a.1; WBGene00002845. [Q20937-1]
DR EnsemblMetazoa; F57B9.2b.1; F57B9.2b.1; WBGene00002845. [Q20937-2]
DR EnsemblMetazoa; F57B9.2c.1; F57B9.2c.1; WBGene00002845. [Q20937-3]
DR EnsemblMetazoa; F57B9.2d.1; F57B9.2d.1; WBGene00002845. [Q20937-4]
DR EnsemblMetazoa; F57B9.2e.1; F57B9.2e.1; WBGene00002845. [Q20937-5]
DR GeneID; 175971; -.
DR KEGG; cel:CELE_F57B9.2; -.
DR UCSC; F57B9.2; c. elegans. [Q20937-1]
DR CTD; 175971; -.
DR WormBase; F57B9.2a; CE47929; WBGene00002845; let-711. [Q20937-1]
DR WormBase; F57B9.2b; CE51783; WBGene00002845; let-711. [Q20937-2]
DR WormBase; F57B9.2c; CE51773; WBGene00002845; let-711. [Q20937-3]
DR WormBase; F57B9.2d; CE51776; WBGene00002845; let-711. [Q20937-4]
DR WormBase; F57B9.2e; CE51767; WBGene00002845; let-711. [Q20937-5]
DR eggNOG; KOG1831; Eukaryota.
DR GeneTree; ENSGT00390000014869; -.
DR HOGENOM; CLU_000286_2_0_1; -.
DR InParanoid; Q20937; -.
DR OMA; AIRRYHK; -.
DR OrthoDB; 42530at2759; -.
DR PhylomeDB; Q20937; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00002845; Expressed in pharyngeal muscle cell (C elegans) and 5 other tissues.
DR ExpressionAtlas; Q20937; baseline and differential.
DR GO; GO:0030014; C:CCR4-NOT complex; IDA:WormBase.
DR GO; GO:0030015; C:CCR4-NOT core complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0030953; P:astral microtubule organization; IMP:WormBase.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:WormBase.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:WormBase.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IBA:GO_Central.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IMP:WormBase.
DR GO; GO:0048477; P:oogenesis; IMP:WormBase.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0010468; P:regulation of gene expression; IMP:WormBase.
DR Gene3D; 1.25.40.840; -; 1.
DR InterPro; IPR007196; CCR4-Not_Not1_C.
DR InterPro; IPR032191; CNOT1_CAF1_bind.
DR InterPro; IPR024557; CNOT1_dom_4.
DR InterPro; IPR032194; CNOT1_HEAT.
DR InterPro; IPR032193; CNOT1_TTP_bind.
DR InterPro; IPR038535; CNOT1_TTP_bind_sf.
DR InterPro; IPR040398; Not1.
DR PANTHER; PTHR13162; PTHR13162; 1.
DR Pfam; PF16415; CNOT1_CAF1_bind; 1.
DR Pfam; PF16418; CNOT1_HEAT; 1.
DR Pfam; PF16417; CNOT1_TTP_bind; 1.
DR Pfam; PF12842; DUF3819; 1.
DR Pfam; PF04054; Not1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome; Repressor;
KW RNA-mediated gene silencing; Transcription; Transcription regulation;
KW Translation regulation.
FT CHAIN 1..2641
FT /note="CCR4-NOT transcription complex subunit let-711"
FT /id="PRO_0000453922"
FT REGION 771..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1518..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2034..2054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2609..2641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 660..664
FT /note="LXXLL"
FT /evidence="ECO:0000305"
FT MOTIF 2341..2345
FT /note="LXXLL"
FT /evidence="ECO:0000305"
FT COMPBIAS 771..850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1519..1533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2627..2641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..2384
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_061210"
FT VAR_SEQ 1..766
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_061211"
FT VAR_SEQ 1..307
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_061212"
FT VAR_SEQ 1..17
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_061213"
SQ SEQUENCE 2641 AA; 295080 MW; F7A359E893C846F8 CRC64;
MHSTSGLAPV FRVEENHMIR NRENLERPIS KKGTITLLSK MPMGFVLNSC SCAYIDNLLA
HSSIHRVKPH SFMIQRLVVI CGRSSPSLPN HAANIILSAF NFCQIEAPAK KFLEEDAALS
LFHTILSYST VTQINRSGIE ILGAQRLTSA LCDLIYAYTK TMDDMVASKT LTHLCKKLAG
LFDPLVVLPF ISKLAKSRRL RHYLQPLFLG HCEYTSDTWG VSPEGAEIYN QIARGNFTTQ
TLIEIVQTFL EKEVKEVIIS STTDPIKLVQ YLISCSNPDN TEIVQALAFL LYSNTKLLPA
GSGGTIDMDV QAADTITTAR LGDTKFTQPV KDALLDSGRE ALLRRMEIYG VSLLSSVENF
VTELKQAPIQ KKMVTNNSVA NAILYMLQYN FDMSRDIENG RQDNSPFWGG SNFVIGITRF
VEEQQAAVRD MEGFSDWYPD INWVEVIKEF DSEEFAICRQ TIIMFADIFP IMFQPQNFPV
SFFLTPWRYY DHQLRLFEFM IEYADVWNIS QYPHTKVLTP DLNLKTIPDD STSVVQLWNC
QEFSNCLLTI ANSQPSLYNA IKQFYNVGSM QAGDVSMLAL ILSPTQWTTG RQDLIRHFLP
SFILKSPNVT PVLNLVWNDT SLSKHMRQHV IYCLTSMHAA DSSQLAKILD VAHDIKPTGL
SELLNQAPKH LAFMVDLACL ASKRDYLNLE KWIEDKEKAH GEAMTVAVLQ FIQKKYQHAQ
LVAAIAPKTQ ATTPGAPSEP LQVLIPFVSK RARKPLRQQF PLVFQVMKEN SGRSSSVSSG
GHVQQSSGSQ PQQQQFGGGS GLPPSGVVPV QQQPQQPPSL QQQHSQQSLP TPPTTSQQQI
HVQQSVPGPI QRPAQFAPQP MFPPQAQAQH QHQHMMGQPP PSSQNAQPGM NLLMNMSPFA
SGNNRDLLKV VQPAPPPPSS MSPSTQMMRS LIPPLTQRQN SNSGWHAAPA PQRPSGPPTP
QQQMDFRGQI QEFAPQGPHQ LQRSGSVTGR SMGIVGQKTS SNFSVGAPIP GSAAATAAAA
ANVQQPMNED FQSMTFAEDI QEEANSYFEK IYSVNNAMSV ENLIDLLKRF RVSNDRRERL
VLACVVKNLF EEYRFFHEYP ERELRTTAAV YGGIIREDII SNVQFATAVR KVIESLSADP
NTMLWTFGIV ALQHCRSKLC AYPKVCQMIV SSENFARFPQ LLKDYVIAGV KGELPPEGGR
HTPVGSAQAG SASSTPTPAA APTNWGAVAR AASVDPKNSL PANRTGNVLS YTNVDTLVMA
TNKDGAEIAQ PAEAIVDKIS FLFNNLSQSN LIQKKDEVVE MISDHGDAFT LWLAQYIVMK
RVSIEQNFQP LYNQFVNAIE NPYLDQCIKR ETFRNIRILL RTDKRTTVAS NYSDRQLLKN
LGSWLGAITI ARNKPILLND LDLKSLLLEA YYKGQAELLY VVPFISKILT ACSKTSLFTP
TCAWIRSILK VLAELHNEPD LKINLKFEIE VLCKELNVDL NQLQMDGILK DTEKLVRVPQ
QLCDVKLLTR PEAASPVQSK IHMSGSAEQL SGMSPAIPDQ VKPATPQPTE AELQSGTGGG
GSQGAEAQVV PNVTHFAYHD INVLTYDGLI PHVKIVSHLP LFQLHPHAKH LVRPAMIHAI
KELIGPVTER ALKIAMTVTE SLVRKDFALD PEEQNLRAAS FHMMRAMTAG MAMITCRDPL
ASSMHSNLAN AFSSSLRSTA ANPEMKQMIE DAAATITQDN VELSTNFIVK TACEKATQDI
EKRLEADYQK RIAAKAEMSF YRDEIAAAIH AQLPKAIATV PGPTDKALMG IYDQFSSRIC
GFKANSGEDP VSAEPGSGAI TPVQTQSKEM ELVCQQLQVI IKEVDQTTQA QPHLSNSAFQ
TVCLMRELMQ NVISTKDANH LMILVTRSTE HLLHAYRLEG TPPKNLLDVE WARRLRDLFI
GLMRLLQNYF PLVELSRRIT TAIMQIRSDY KWNMEGIEIL FKQNLLQSVL WDQHLAGSMD
NGGNMEAVLF AQKFVRSIGG GDMSRIQFLK ERFPLTCEQL TKLHQLQSAT RTEGMNNAMN
NGAGNAAHHH AGLQQQPPVA LPMEAAPMPQ ASADAMAQRG YDDQEMTAKV EIIMREWIGL
CYSPTGQRSP QESLAQMIQL MHEHGVLATD DKITQFFRLC VENCVDISVR VMKSEQLANG
LPTTLIRHRC YYTLDAFVKL MALMIRHSDN GQSQNKINLL KKLLNIIVGV LHMDHEVRKQ
DFNAMPYHRI LISLFNEITG PDPLKLLEPI AWSILEAFGQ TFFALQPRRM PGFAFAWLDI
VGHRNVIGRL LANTGIAETV DAVKTAATYT QLIISHLKFL APFLRNIQLP KSIAILYKGT
LRVLLVILHD FPELLCEFHY VICDTIPPNC VQLRNLILSA YPRQMRLPDP FALNFKQVDT
IPEMAVEPKS NLNMATIIPD NIRIPLDEYL ANRISVDFLP NLPTLLQTQN QAGTKYNTTV
MNALVLYVGI RAIEHLHLRR QRISTLNIAH TSYMDIFQNL AIQLDTEGRY LLFNGIANQL
RYPNAHTHYF SCVFLYLFKN STNDTIQEQI TRILFERLVA LRPHPWGLLI TFIELIKNPT
YNFWRYEFTS CAPEIQRLFQ NVANTCVPAQ GSQPQAQPDG APGPLGNNTG AANQQQNPNT
N
