ID CWC22_PONAB Reviewed; 908 AA.
AC Q5RA93;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Pre-mRNA-splicing factor CWC22 homolog;
DE AltName: Full=Nucampholin homolog;
GN Name=CWC22; Synonyms=NCM;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome. As a component of the minor spliceosome, involved in the
CC splicing of U12-type introns in pre-mRNAs (By similarity). Promotes
CC exon-junction complex (EJC) assembly. Hinders EIF4A3 from non-
CC specifically binding RNA and escorts it to the splicing machinery to
CC promote EJC assembly on mature mRNAs. Through its role in EJC assembly,
CC required for nonsense-mediated mRNA decay.
CC {ECO:0000250|UniProtKB:Q9HCG8}.
CC -!- SUBUNIT: Component of the pre-catalytic spliceosome B and the catalytic
CC spliceosome C complexes. Component of the minor spliceosome, which
CC splices U12-type introns (By similarity). Interacts with EIF4A3 and
CC PRPF19 in an RNA-independent manner. Direct interaction with EIF4A3 is
CC mediated by the MIF4G domain. Full interaction with EIF4A3 occurs only
CC when EIF4A3 is not part of the EJC and prevents EIF4A3 binding to RNA.
CC {ECO:0000250|UniProtKB:Q9HCG8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HCG8}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q9HCG8}. Note=Concentrates around
CC speckles, which are sites of pre-mRNA synthesis and processing, where
CC it colocalizes with EJC core proteins. {ECO:0000250|UniProtKB:Q9HCG8}.
CC -!- SIMILARITY: Belongs to the CWC22 family. {ECO:0000305}.
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DR EMBL; CR859125; CAH91317.1; -; mRNA.
DR RefSeq; NP_001125780.1; NM_001132308.1.
DR AlphaFoldDB; Q5RA93; -.
DR SMR; Q5RA93; -.
DR STRING; 9601.ENSPPYP00000014506; -.
DR GeneID; 100172707; -.
DR KEGG; pon:100172707; -.
DR CTD; 57703; -.
DR eggNOG; KOG2140; Eukaryota.
DR InParanoid; Q5RA93; -.
DR OrthoDB; 1115942at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; ISS:UniProtKB.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR Gene3D; 1.25.40.180; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR PANTHER; PTHR18034; CELL CYCLE CONTROL PROTEIN CWF22-RELATED; 1.
DR PANTHER; PTHR18034:SF3; PRE-MRNA-SPLICING FACTOR CWC22 HOMOLOG; 1.
DR Pfam; PF02847; MA3; 1.
DR Pfam; PF02854; MIF4G; 1.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR PROSITE; PS51366; MI; 1.
PE 2: Evidence at transcript level;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome.
FT CHAIN 1..908
FT /note="Pre-mRNA-splicing factor CWC22 homolog"
FT /id="PRO_0000302007"
FT DOMAIN 163..346
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 454..570
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..437
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCG8"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCG8"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C5N3"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCG8"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCG8"
SQ SEQUENCE 908 AA; 105539 MW; 3E7DBFFCAE031989 CRC64;
MKSGVAQIKP SSGHDRRENL NSYQRNSSPE DRYEEQERSP RDRDYFDYSR SDYEHSRRGH
SYDSSMESRN RDREKRRERE RDTDRKRSRK SPSPGRRNPE TSVTQSSPAQ DEPATKKKKD
ELDPLLTRTG GAYIPPAKLR MMQEQITDKN SLAYQRMSWE ALKKSINGLI NKVNISNISI
IIQELLQENI VRGRGLLSRS VLQAQSASPI FTHVYAALVA IINSKFPQIG ELILKRLILN
FRKGYRRNDK QLCLTASKFV AHLINQNVAH EVLCLEMLTL LLERPTDDSV EVAIGFLKEC
GLKLTQVSPR GINAIFGRLR NILHESEIDK RVQYMIEVMF AVRKDGFKDH PIILEGLDLV
EEDDQFTHML PLEDDYNPED VLNVFKMDPN FMENEEKYKA IKKEILDEGD TDSNTDQDAG
SSEEDEEEEE EEGEEDEEGQ KVTIHDKTEI NLVSFRRTIY LAIQSSLDFE ECAHKLLKME
FPESQTKELC NMILDCCAQQ RTYEKFFGLL AGRFCMLKKE YMESFEGIFK EQYDTIHRLE
TNKLRNVAKM FAHLLYTDSL PWSVLECIKL SEETTTSSSR IFVKIFFQEL CEYMGLPKLN
ARLKDETLQP FFEGLLPRDN PRNTRFAINF FTSIGLGGLT DELREHLKNT PKVIVAQKPD
VEQNKSSPSS SSSASSSSES DSSDSDSDSS DSSSESSSEE SDSSSISSHS SASANDVRKK
GHGKTRSKEV DKLIRNQQTN DRKQKERRQE HGHQETRTER ERRSEKHRDQ NSRDSNWRDP
ITKYTSDKDV PSERNNYSRV ANDRDQEMHI DLENKHGDPK KKRGERRNSF SENEKHTHRN
KDSENFRRKD RSKSREMNRR HSGSRSDEDR YQNGAERRWE KSSRYSEQSR ESKKNQDRRR
EKSPAKQK
//
