CWC22_MOUSE
ID CWC22_MOUSE Reviewed; 908 AA.
AC Q8C5N3; Q3UEH0; Q3V267; Q8BR58; Q99KV6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Pre-mRNA-splicing factor CWC22 homolog;
DE AltName: Full=Nucampholin homolog;
GN Name=Cwc22; Synonyms=Ncm;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Liver, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome. Promotes exon-junction complex (EJC) assembly. Hinders
CC EIF4A3 from non-specifically binding RNA and escorts it to the splicing
CC machinery to promote EJC assembly on mature mRNAs. Through its role in
CC EJC assembly, 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. Interacts with EIF4A3 and PRPF19 in an RNA-
CC independent manner. Direct interaction with EIF4A3 is mediated by the
CC MIF4G domain. Full interaction with EIF4A3 occurs only when EIF4A3 is
CC 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C5N3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C5N3-2; Sequence=VSP_027905;
CC -!- SIMILARITY: Belongs to the CWC22 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH03993.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK045589; BAC32427.1; -; mRNA.
DR EMBL; AK132001; BAE20931.1; -; mRNA.
DR EMBL; AK077961; BAC37085.1; -; mRNA.
DR EMBL; AK149528; BAE28941.1; -; mRNA.
DR EMBL; BC003993; AAH03993.1; ALT_INIT; mRNA.
DR CCDS; CCDS16165.1; -. [Q8C5N3-1]
DR CCDS; CCDS57178.1; -. [Q8C5N3-2]
DR RefSeq; NP_001277669.1; NM_001290740.1.
DR RefSeq; NP_085037.2; NM_030560.5. [Q8C5N3-1]
DR RefSeq; NP_766255.1; NM_172667.2. [Q8C5N3-2]
DR RefSeq; XP_006500499.1; XM_006500436.3.
DR RefSeq; XP_011238158.1; XM_011239856.1.
DR AlphaFoldDB; Q8C5N3; -.
DR SMR; Q8C5N3; -.
DR BioGRID; 219805; 37.
DR STRING; 10090.ENSMUSP00000064947; -.
DR iPTMnet; Q8C5N3; -.
DR PhosphoSitePlus; Q8C5N3; -.
DR EPD; Q8C5N3; -.
DR jPOST; Q8C5N3; -.
DR MaxQB; Q8C5N3; -.
DR PaxDb; Q8C5N3; -.
DR PRIDE; Q8C5N3; -.
DR ProteomicsDB; 279236; -. [Q8C5N3-1]
DR ProteomicsDB; 279237; -. [Q8C5N3-2]
DR DNASU; 80744; -.
DR Ensembl; ENSMUST00000065889; ENSMUSP00000064947; ENSMUSG00000027014. [Q8C5N3-1]
DR Ensembl; ENSMUST00000111818; ENSMUSP00000107449; ENSMUSG00000027014. [Q8C5N3-2]
DR Ensembl; ENSMUST00000111821; ENSMUSP00000107452; ENSMUSG00000027014. [Q8C5N3-1]
DR GeneID; 80744; -.
DR KEGG; mmu:80744; -.
DR UCSC; uc008kgc.3; mouse. [Q8C5N3-1]
DR UCSC; uc008kgd.3; mouse. [Q8C5N3-2]
DR CTD; 57703; -.
DR MGI; MGI:2136773; Cwc22.
DR VEuPathDB; HostDB:ENSMUSG00000027014; -.
DR eggNOG; KOG2140; Eukaryota.
DR GeneTree; ENSGT00940000153458; -.
DR HOGENOM; CLU_006308_1_0_1; -.
DR InParanoid; Q8C5N3; -.
DR OMA; VIEGCCE; -.
DR OrthoDB; 996017at2759; -.
DR PhylomeDB; Q8C5N3; -.
DR TreeFam; TF300510; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 80744; 13 hits in 72 CRISPR screens.
DR ChiTaRS; Cwc22; mouse.
DR PRO; PR:Q8C5N3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8C5N3; protein.
DR Bgee; ENSMUSG00000027014; Expressed in epiblast (generic) and 129 other tissues.
DR ExpressionAtlas; Q8C5N3; baseline and differential.
DR Genevisible; Q8C5N3; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome.
FT CHAIN 1..908
FT /note="Pre-mRNA-splicing factor CWC22 homolog"
FT /id="PRO_0000302006"
FT DOMAIN 161..344
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 453..569
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..436
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCG8"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCG8"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCG8"
FT VAR_SEQ 713..718
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_027905"
FT CONFLICT 9
FT /note="K -> KQ (in Ref. 2; AAH03993)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="L -> P (in Ref. 2; AAH03993)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="T -> I (in Ref. 2; AAH03993)"
FT /evidence="ECO:0000305"
FT CONFLICT 706
FT /note="S -> SS (in Ref. 2; AAH03993)"
FT /evidence="ECO:0000305"
FT CONFLICT 749
FT /note="R -> Q (in Ref. 2; AAH03993)"
FT /evidence="ECO:0000305"
FT CONFLICT 847
FT /note="R -> K (in Ref. 1; BAE20931)"
FT /evidence="ECO:0000305"
FT CONFLICT 874
FT /note="S -> G (in Ref. 2; AAH03993)"
FT /evidence="ECO:0000305"
FT CONFLICT 896
FT /note="Q -> R (in Ref. 1; BAE28941)"
FT /evidence="ECO:0000305"
FT CONFLICT 898
FT /note="R -> G (in Ref. 1; BAC32427)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 908 AA; 104773 MW; 722C782B3D74643B CRC64;
MKSSVAHMKS SGHNRRETHS SYRRSSSPED RYTEQERSPR DRGYSDYSRS DYERSRRGYS
YDDSMESRSR DREKRRERER DADHRKRSRK SPSPDRSPAR GGGQSSPQEE PTWKKKKDEL
DPLLTRTGGA YIPPAKLRMM QEQITDKSSL AYQRMSWEAL KKSINGLINK VNISNISIII
QELLQENIVR GRGLLSRSVL QAQSASPIFT HVYAALVAII NSKFPQIGEL ILKRLILNFR
KGYRRNDKQL CLTASKFVAH LINQNVAHEV LCLEMLTLLL ERPTDDSVEV AIGFLKECGL
KLTQVSPRGI NAIFERLRNI LHESEIDKRV QYMIEVMFAV RKDGFKDHPV ILEGLDLVEE
DDQFTHMLPL EDDYNPEDVL NVFKMDPNFM ENEEKYKAIK KEILDEGDSD SNTDQGAGSS
EDEEEEDEEE EGEDEEGGQK VTIHDKTEIN LVSFRRTIYL AIQSSLDFEE CAHKLLKMEF
AESQTKELCN MILDCCAQQR TYEKFFGLLA GRFCMLKKEY MESFESIFKE QYDTIHRLET
NKLRNVAKMF AHLLYTDSLP WSVLECIKLS EETTTSSSRI FVKIFFQELC EYMGLPKLNA
RLKDETLQPF FEGLLPRDNP RNTRFAINFF TSIGLGGLTD ELREHLKNTP KVIVAQKPEA
EQKKPALTSS SSESSSASDS SDSESDSSES SSESSSDASD SSSSSSTQSS TSGITAHSAK
GTRKKRQGKA RGEEVDKLAR GHQALERRRE GGREDQRHQE GRTERARSER RRAQNSRDAD
WRDPLAKHID DRSHENSHSR VGNGREQGSH REPEDRHGEP KKRRERRDSF SENEKQRSRN
QDSDNVRRKD RSKSRERSRR HSGHKGDDAR CQNSAERRWE KPGRRPEQSR ESKRSQDRRR
EKSPTTQK
