CWC22_DANRE
ID CWC22_DANRE Reviewed; 985 AA.
AC Q08C72;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Pre-mRNA-splicing factor CWC22 homolog;
DE AltName: Full=Nucampholin homolog;
GN Name=cwc22; Synonyms=ncm; ORFNames=zgc:153452;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome. Promotes exon-junction complex (EJC) assembly.
CC {ECO:0000250|UniProtKB:Q9HCG8}.
CC -!- SUBUNIT: Component of the pre-catalytic spliceosome B and the catalytic
CC spliceosome C complexes. {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; BC124357; AAI24358.1; -; mRNA.
DR AlphaFoldDB; Q08C72; -.
DR SMR; Q08C72; -.
DR STRING; 7955.ENSDARP00000013971; -.
DR PaxDb; Q08C72; -.
DR PRIDE; Q08C72; -.
DR ZFIN; ZDB-GENE-060929-452; cwc22.
DR eggNOG; KOG2140; Eukaryota.
DR InParanoid; Q08C72; -.
DR PhylomeDB; Q08C72; -.
DR Reactome; R-DRE-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q08C72; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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: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 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; Spliceosome.
FT CHAIN 1..985
FT /note="Pre-mRNA-splicing factor CWC22 homolog"
FT /id="PRO_0000302009"
FT DOMAIN 257..440
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 548..664
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 1..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..157
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..530
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..978
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 985 AA; 113350 MW; BBC2C03B70597930 CRC64;
MAAESNDSQK AMNLGPTLRD EPPSTEEIEQ RQRKASTSSS EDGEHEDNDR RRVVGSPGSR
DGSPRVGSPV ARASPRAKRD QKSSDSDSDS SDSDDGVMRK IRSSVMHIRR TSDEETKNRE
RSSSPDRHEK KSKSRSRSRS RSRSRSRSRS PRERYRRARR SRERERDRYG DRERYERRSS
RERDWEHRRR GRSASPDKND KPPTEEPPVK KRKETLDPIL TRTGGAYIPP AKLRMMQAQI
TDKSSLEYQR MSWEALKKSI NGLINKVNVS NIANIIQELL QENIVRGRGL LARSILQAQA
ASPIFTHVYS AVVAIINSKF PQIGELILKR LILNFRKGYR RNDKQQCLTA SKFVGHLINQ
NVAHEVLCLE MLTLLLERPT DDSVEVAISF LKECGLKLTE VSPRGINAIF ERLRNILHES
EIDKRVQYMI EVMFAIRKDG FKDHPIIPEG LDLVEEEDQF THMLPLEDEY NTEDILNVFK
LDPNFLENEE KYKTIKREIL DEGSSDSGDD AGGSGDDEDD DEEDEEAAAG EEQEKVTIFD
QTEVNLVAFR RTIYLAIQSS LDFEECAHKL IKMDFPESQT KELCNMILDC CAQQRTYEKF
FGLLAGRFCL LKKEYMESFE AIFQEQYETI HRLETNKLRN VARIFAHLLY TDSVPWSVLE
CVRMSEDTTT SSSRIFVKIL FQELCAYMGL PKLNERLKDT TLQPFFEGLF PRDNPRNTRF
AINFFTSIGL GGLTDELREH LKNAPKMIMT QNQEVESSDS SSSSSSSSDS SSSSGSSSES
DSSESDSDSS SDSDSSSSSG SSSDSDSRRK KASGKKKDKS KSKKSSKAAN QRSPLEERPT
KRHENRRQDA SKEDRRGSDK HNRDPQRRGQ QDESPPARPR GEPERIRGQK EPHRHAQDHQ
DRPTDSGRHK DDGKNSRVNK DKDRRRSREK EPLRRSRDRS KSRERSRKEM DSRDSYGNGL
ERADKENRHS DRYKESRRKD DRRHR
