CWC22_CAEEL
ID CWC22_CAEEL Reviewed; 897 AA.
AC Q17336;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Pre-mRNA-splicing factor CWC22 homolog;
DE AltName: Full=Lethal protein 858;
DE AltName: Full=Nucampholin;
GN Name=let-858 {ECO:0000312|WormBase:F33A8.1};
GN ORFNames=F33A8.1 {ECO:0000312|WormBase:F33A8.1};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=9136012; DOI=10.1093/genetics/146.1.227;
RA Kelly W.G., Xu S., Montgomery M.K., Fire A.;
RT "Distinct requirements for somatic and germline expression of a generally
RT expressed Caernorhabditis elegans gene.";
RL Genetics 146:227-238(1997).
RN [2]
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=12724425; DOI=10.1128/mcb.23.10.3681-3691.2003;
RA Jedrusik M.A., Schulze E.;
RT "Telomeric position effect variegation in Saccharomyces cerevisiae by
RT Caenorhabditis elegans linker histones suggests a mechanistic connection
RT between germ line and telomeric silencing.";
RL Mol. Cell. Biol. 23:3681-3691(2003).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23149939; DOI=10.1128/mcb.01298-12;
RA Shiimori M., Inoue K., Sakamoto H.;
RT "A specific set of exon junction complex subunits is required for the
RT nuclear retention of unspliced RNAs in Caenorhabditis elegans.";
RL Mol. Cell. Biol. 33:444-456(2013).
CC -!- FUNCTION: Required for pre-mRNA splicing and for exon-junction complex
CC (EJC) assembly. Hinders EIF4A3 from non-specifically binding RNA and
CC escorts it to the splicing machinery to promote EJC assembly on mature
CC mRNAs. Through its role in EJC assembly, required for nonsense-mediated
CC mRNA decay (By similarity). Plays a role in the nuclear retention of
CC unspliced mRNAs (PubMed:23149939). Plays a role in sex determination
CC (PubMed:23149939). Required for early embryogenesis and tissue
CC differentiation. {ECO:0000250, ECO:0000269|PubMed:23149939,
CC ECO:0000269|PubMed:9136012}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9136012}. Nucleus
CC speckle {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in germ cells, oocytes, and sperm cells.
CC {ECO:0000269|PubMed:12724425}.
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously throughout development.
CC {ECO:0000269|PubMed:9136012}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in germline
CC masculinization and the accumulation of unspliced mRNAs in the
CC cytoplasm. {ECO:0000269|PubMed:23149939}.
CC -!- SIMILARITY: Belongs to the CWC22 family. {ECO:0000305}.
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DR EMBL; U19615; AAB51351.1; -; mRNA.
DR EMBL; BX284602; CAB04256.1; -; Genomic_DNA.
DR PIR; T21688; T21688.
DR RefSeq; NP_496363.1; NM_063962.6.
DR AlphaFoldDB; Q17336; -.
DR SMR; Q17336; -.
DR BioGRID; 39999; 2.
DR DIP; DIP-26173N; -.
DR IntAct; Q17336; 1.
DR STRING; 6239.F33A8.1; -.
DR iPTMnet; Q17336; -.
DR EPD; Q17336; -.
DR PaxDb; Q17336; -.
DR PeptideAtlas; Q17336; -.
DR PRIDE; Q17336; -.
DR EnsemblMetazoa; F33A8.1.1; F33A8.1.1; WBGene00002957.
DR GeneID; 174689; -.
DR KEGG; cel:CELE_F33A8.1; -.
DR UCSC; F33A8.1.1; c. elegans.
DR CTD; 174689; -.
DR WormBase; F33A8.1; CE17753; WBGene00002957; let-858.
DR eggNOG; KOG2140; Eukaryota.
DR GeneTree; ENSGT00940000153458; -.
DR HOGENOM; CLU_006308_1_2_1; -.
DR InParanoid; Q17336; -.
DR OMA; VIEGCCE; -.
DR OrthoDB; 996017at2759; -.
DR PhylomeDB; Q17336; -.
DR Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q17336; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002957; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0000785; C:chromatin; IDA:WormBase.
DR GO; GO:0043073; C:germ cell nucleus; IDA:WormBase.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IMP:WormBase.
DR GO; GO:0007369; P:gastrulation; IMP:WormBase.
DR GO; GO:0042078; P:germ-line stem cell division; IMP:WormBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR Pfam; PF02847; MA3; 1.
DR Pfam; PF02854; MIF4G; 1.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51366; MI; 1.
PE 2: Evidence at transcript level;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome.
FT CHAIN 1..897
FT /note="Pre-mRNA-splicing factor CWC22 homolog"
FT /id="PRO_0000302012"
FT DOMAIN 194..382
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 485..601
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 1..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..464
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 104269 MW; ADB068467BF7C434 CRC64;
MSSSRSQSPE TPKAASEERE EEEKESSEQP DTPKTSSEKS ASRSQSPRES REVSQETETS
ENQEKIKEKD DGDDQPGTPN SYRSRETSPA PKRSKETRES ESPEKSPVRS RSPRRSSARS
PSRSPRRRRE RSSERKQSEE PAPLPEKKKK EPLDILRTRT GGAYIPPAKL RLMQQQISDK
QSEQYQRMNW ERMKKKIHGL VNRVNAKNLV QIVRELLQEN VIRSKGLLCR DIIQAQAFSP
GFSNVYAALA AVINSKFPHV GELLLRRLIV QFKRSFRRND RGVTVNVIKF IAHLINQQVA
HEVLALEIMI LMLEEPTDDS VEVAIAFLKE CGAKLLEIAP AALNSVYDRL RAILMETERS
ENALDRRIQY MIETAMQIRK DKFAAYPAVI EDLDLIEEED QIIHTLNLED AVDPENGLNV
FKLDPEFEKN EEVYEEIRKE IIGNADISDE DGGDELDDEE EGSDVEEAPK KTTEIIDNTD
QNLTAFRREV YLTMQSSLDY QEAAHKLLKM KIPDSMQNEL CAMLVDCCAQ QRTYERFYGM
LIERFCRLRL EYQQYFEKLC QDTYSTIHRI DITKLRNLAR LIAHLLSTDA IDWKILADMK
MTEEDTTSSG RIYIKYIFNE LVEAMGMVKL HSRVTDPTLA HCFVGLFPRT NPNSARFSIN
FFTMIGLGGL TLELREWLAK GLKKKKGMLD QLKAESSSDS SSSSDSSDSS DSSDSDDSSD
SSSDSSSSSE SEPEPPKKKK KKNSEESSKK KEKENIGRRD RGDKRAERHR DQSVENKDKD
RRRRQDSDEN RRPERGDDRK DRSKDRRRQD SDDEDRKGRE RREDSGERRR GDRDRRDRNK
DQEDHREDRR DRSKDREDRR DRRRHDSDDD RKTRRDRSEE RGGRRREVES DDRRRRR
