ID   CWC15_RAT               Reviewed;         229 AA.
AC   Q5BJP2;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Spliceosome-associated protein CWC15 homolog;
GN   Name=Cwc15;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110 AND SER-121, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Involved in pre-mRNA splicing as component of the
CC       spliceosome. Component of the PRP19-CDC5L complex that forms an
CC       integral part of the spliceosome and is required for activating pre-
CC       mRNA splicing. {ECO:0000250|UniProtKB:Q9P013}.
CC   -!- SUBUNIT: Identified in the spliceosome C complex. Component of the
CC       PRP19-CDC5L splicing complex composed of a core complex comprising a
CC       homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less
CC       stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts directly
CC       with CTNNBL1 in the complex. {ECO:0000250|UniProtKB:Q9P013}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9P013}.
CC   -!- SIMILARITY: Belongs to the CWC15 family. {ECO:0000305}.
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DR   EMBL; BC091396; AAH91396.1; -; mRNA.
DR   RefSeq; NP_001020158.1; NM_001024987.1.
DR   RefSeq; XP_006242582.1; XM_006242520.3.
DR   AlphaFoldDB; Q5BJP2; -.
DR   STRING; 10116.ENSRNOP00000011856; -.
DR   iPTMnet; Q5BJP2; -.
DR   PhosphoSitePlus; Q5BJP2; -.
DR   PaxDb; Q5BJP2; -.
DR   PRIDE; Q5BJP2; -.
DR   Ensembl; ENSRNOT00000011855; ENSRNOP00000011856; ENSRNOG00000008490.
DR   GeneID; 300361; -.
DR   KEGG; rno:300361; -.
DR   UCSC; RGD:1310669; rat.
DR   CTD; 51503; -.
DR   RGD; 1310669; Cwc15.
DR   eggNOG; KOG3228; Eukaryota.
DR   GeneTree; ENSGT00390000012084; -.
DR   HOGENOM; CLU_068312_0_1_1; -.
DR   InParanoid; Q5BJP2; -.
DR   OMA; NCARSEP; -.
DR   OrthoDB; 1576404at2759; -.
DR   PhylomeDB; Q5BJP2; -.
DR   TreeFam; TF321323; -.
DR   Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR   PRO; PR:Q5BJP2; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000008490; Expressed in heart and 19 other tissues.
DR   Genevisible; Q5BJP2; RN.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000974; C:Prp19 complex; ISO:RGD.
DR   GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   InterPro; IPR006973; Cwf_Cwc_15.
DR   PANTHER; PTHR12718; PTHR12718; 1.
DR   Pfam; PF04889; Cwf_Cwc_15; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Reference proteome; Spliceosome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P013"
FT   CHAIN           2..229
FT                   /note="Spliceosome-associated protein CWC15 homolog"
FT                   /id="PRO_0000291546"
FT   REGION          1..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          123..165
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        35..89
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..127
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P013"
FT   MOD_RES         18
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHS9"
FT   MOD_RES         47
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P013"
FT   MOD_RES         110
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   229 AA;  26638 MW;  B21E6EEF5835AD7C CRC64;
     MTTAARPTFE PARGGRGKGE GDLSQLSKQY SSRDLPSHTK IKYRQTTQDA PEEVRNRDFR
     RELEERERAA AREKNRDRPT REHTTSSSVS KKPRLDQIPA ANLDADDPLT DEEDEDFEEE
     SDDDDTAALL AELEKIKKER AEEQARKEQE QKAEEERIRM ENILSGNPLL NLTGPSQPQA
     NFKVKRRWDD DVVFKNCAKG IDDQKKDKRF VNDTLRSEFH KKFMEKYIK