CWC22_CAEBR
ID CWC22_CAEBR Reviewed; 935 AA.
AC A8WT19;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Pre-mRNA-splicing factor CWC22 homolog;
DE AltName: Full=Lethal protein 858 {ECO:0000250|UniProtKB:Q17336, ECO:0000312|EMBL:CAP23630.2};
DE AltName: Full=Nucampholin {ECO:0000250|UniProtKB:Q17336};
GN Name=let-858 {ECO:0000312|EMBL:CAP23630.2}; ORFNames=CBG02984;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP23630.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP23630.2};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Required for early embryogenesis and tissue differentiation.
CC Required for pre-mRNA splicing and for exon-junction complex (EJC)
CC assembly. Hinders EIF4A3 from non-specifically binding RNA and escorts
CC it to the splicing machinery to promote EJC assembly on mature mRNAs.
CC Through its role in EJC assembly, required for nonsense-mediated mRNA
CC decay (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q17336}. Nucleus
CC speckle {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CWC22 family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE601438; CAP23630.2; -; Genomic_DNA.
DR AlphaFoldDB; A8WT19; -.
DR SMR; A8WT19; -.
DR STRING; 6238.CBG02984; -.
DR EnsemblMetazoa; CBG02984a.1; CBG02984a.1; WBGene00025938.
DR WormBase; CBG02984a; CBP27846; WBGene00025938; Cbr-let-858.
DR eggNOG; KOG2140; Eukaryota.
DR HOGENOM; CLU_006308_1_2_1; -.
DR InParanoid; A8WT19; -.
DR OMA; VIEGCCE; -.
DR OrthoDB; 996017at2759; -.
DR Proteomes; UP000008549; Chromosome II.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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 3: Inferred from homology;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome.
FT CHAIN 1..935
FT /note="Pre-mRNA-splicing factor CWC22 homolog"
FT /id="PRO_0000367032"
FT DOMAIN 212..400
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 502..633
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 1..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..146
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..482
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..935
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 935 AA; 109059 MW; 42A32B47D1B91CAA CRC64;
MSRSPSPDSP PAVRDDEEKD AREQSDSPTS NTDDPKSPSE SPKSNRSQES SRKDSRESGK
RRDSHEDEKM PLTPPNRSSE ASPQHRRHRE SRSPSRSRSR SHRSHSRSQY RRSRSRSRDR
RSRSRSRDRR SHSRSRDRRS PARRRSPVRA KSPAQAVKPT EEPEKKKNDP KDLLRTRTGG
AYIPPAKLRL MQQQITDKSS EQYQRMNWER MKKKIHGLVN RVNAKNLVQI VRELLQENVI
RSKGLLCRDI IQAQAFSPGF SNVYAALAAV INSKFPHIGE LLLRRLIVQF KRSFRRNDRG
VTVNVIKFIA HLINQQVAHE VLALEIMILM LEEPTDDSVE VAIAFLKECG AKLMEIAPAA
LNSVYDRLRA ILMETERSEN ALDRRIQYMI ETAMQIRKDK FAAYPAVVED LDLIEEEDQI
IHTLNLEDAV DPENGLNVFK LDPEFEKNEN VYEEIRKEII GDADISSDEE EEVEDDDEES
EAEEAPRKTT EIIDNTDQNL TAFRREVYLT LQSSLDYQEA AHKLLKMKIP DNLQVNVILK
FIQKKSEFQN ELCAMLVDCC AQQRTYERFY GMLIERFCRL RLEYQQCFEK LCQDTYATVH
RIDITKLRNL ARLVAHLLST DAIEWKILAD VKMTEEDTTS AGRIYIKFIF MELVEAMGMV
KLHTRVTDPT LAHCFVGMFP RTDPQDARFA INFFTMIGLG GLTLELREWL NRGLKKKKGI
IDELKAAQSS SDSSSDSSDS SDSSDSSGSS DSSDDSSSSS SSDSSKEPPK KKKKSGTVLK
KKETDTNDHK EARGDSRAER RNDEEKLKRR SDEGRRDRSA ENREPRRGRD RRDSGDDRHD
RGRRDRSKEK EDRGDKRSQR HDSREEDRRE RKDRDRRDRS EERDNRRDRK ERSRSRDRRD
HRDRSRSRER NEKRRHDDDR RREEKVGSDD RRRRH