CWC21_YEAST
ID CWC21_YEAST Reviewed; 135 AA.
AC Q03375; D6VTA5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Pre-mRNA-splicing factor CWC21;
DE AltName: Full=Complexed with CEF1 protein 21;
GN Name=CWC21; OrderedLocusNames=YDR482C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT "Proteomics analysis reveals stable multiprotein complexes in both fission
RT and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT splicing factors, and snRNAs.";
RL Mol. Cell. Biol. 22:2011-2024(2002).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH PRP8 AND SNU114.
RX PubMed=19854871; DOI=10.1261/rna.1908309;
RA Grainger R.J., Barrass J.D., Jacquier A., Rain J.-C., Beggs J.D.;
RT "Physical and genetic interactions of yeast Cwc21p, an ortholog of human
RT SRm300/SRRM2, suggest a role at the catalytic center of the spliceosome.";
RL RNA 15:2161-2173(2009).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN SPLICEOSOME.
RX PubMed=19789211; DOI=10.1261/rna.1790509;
RA Khanna M., Van Bakel H., Tang X., Calarco J.A., Babak T., Guo G., Emili A.,
RA Greenblatt J.F., Hughes T.R., Krogan N.J., Blencowe B.J.;
RT "A systematic characterization of Cwc21, the yeast ortholog of the human
RT spliceosomal protein SRm300.";
RL RNA 15:2174-2185(2009).
CC -!- FUNCTION: Involved in pre-mRNA splicing. May function at or prior to
CC the first catalytic step of splicing at the catalytic center of the
CC spliceosome, together with ISY1. May do so by stabilizing the catalytic
CC center or the position of the RNA substrate.
CC {ECO:0000269|PubMed:19789211, ECO:0000269|PubMed:19854871}.
CC -!- SUBUNIT: Associates with the NTC complex (or PRP19-associated complex),
CC composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, and
CC PRP19. The NTC complex associates with the spliceosome after the
CC release of the U1 and U4 snRNAs and forms the CWC spliceosome
CC subcomplex (or CEF1-associated complex) reminiscent of a late-stage
CC spliceosome composed also of the U2, U5 and U6 snRNAs and at least
CC BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23,
CC CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11,
CC PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3,
CC SNU114, SPP2, RSE1 and YJU2. Interacts directly with PRP8 (via SCwid
CC domain). Interacts directly with SNU114 (via C-terminus).
CC {ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:19789211,
CC ECO:0000269|PubMed:19854871}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 556 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CWC21 family. {ECO:0000305}.
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DR EMBL; U33050; AAB64929.1; -; Genomic_DNA.
DR EMBL; AY557800; AAS56126.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12315.1; -; Genomic_DNA.
DR PIR; S69649; S69649.
DR RefSeq; NP_010770.3; NM_001180790.3.
DR PDB; 5GM6; EM; 3.50 A; X=1-135.
DR PDB; 5GMK; EM; 3.40 A; J=1-135.
DR PDB; 5LJ3; EM; 3.80 A; R=1-135.
DR PDB; 5LJ5; EM; 3.80 A; R=1-135.
DR PDB; 5MPS; EM; 3.85 A; R=1-135.
DR PDB; 5MQ0; EM; 4.17 A; R=1-135.
DR PDB; 5WSG; EM; 4.00 A; J=1-135.
DR PDB; 5YLZ; EM; 3.60 A; R=1-135.
DR PDB; 6BK8; EM; 3.30 A; K=1-135.
DR PDB; 6EXN; EM; 3.70 A; R=1-135.
DR PDB; 6J6G; EM; 3.20 A; J=1-135.
DR PDB; 6J6H; EM; 3.60 A; J=1-135.
DR PDB; 6J6N; EM; 3.86 A; J=1-135.
DR PDB; 6J6Q; EM; 3.70 A; J=1-135.
DR PDBsum; 5GM6; -.
DR PDBsum; 5GMK; -.
DR PDBsum; 5LJ3; -.
DR PDBsum; 5LJ5; -.
DR PDBsum; 5MPS; -.
DR PDBsum; 5MQ0; -.
DR PDBsum; 5WSG; -.
DR PDBsum; 5YLZ; -.
DR PDBsum; 6BK8; -.
DR PDBsum; 6EXN; -.
DR PDBsum; 6J6G; -.
DR PDBsum; 6J6H; -.
DR PDBsum; 6J6N; -.
DR PDBsum; 6J6Q; -.
DR AlphaFoldDB; Q03375; -.
DR SMR; Q03375; -.
DR BioGRID; 32534; 167.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR DIP; DIP-1847N; -.
DR IntAct; Q03375; 10.
DR MINT; Q03375; -.
DR STRING; 4932.YDR482C; -.
DR PaxDb; Q03375; -.
DR PRIDE; Q03375; -.
DR TopDownProteomics; Q03375; -.
DR EnsemblFungi; YDR482C_mRNA; YDR482C; YDR482C.
DR GeneID; 852093; -.
DR KEGG; sce:YDR482C; -.
DR SGD; S000002890; CWC21.
DR VEuPathDB; FungiDB:YDR482C; -.
DR eggNOG; KOG1869; Eukaryota.
DR HOGENOM; CLU_067891_3_1_1; -.
DR InParanoid; Q03375; -.
DR OMA; ISKPGHY; -.
DR BioCyc; YEAST:G3O-30007-MON; -.
DR PRO; PR:Q03375; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03375; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IDA:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR InterPro; IPR013170; mRNA_splic_Cwf21_dom.
DR Pfam; PF08312; cwf21; 1.
DR SMART; SM01115; cwf21; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Spliceosome.
FT CHAIN 1..135
FT /note="Pre-mRNA-splicing factor CWC21"
FT /id="PRO_0000123505"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..97
FT /note="Interaction with PRP8"
FT /evidence="ECO:0000269|PubMed:19854871"
FT REGION 110..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 65..102
FT /evidence="ECO:0000255"
FT COMPBIAS 1..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 59..86
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 92..114
FT /evidence="ECO:0007829|PDB:6BK8"
SQ SEQUENCE 135 AA; 15763 MW; 9723E1C0A393508B CRC64;
MSYNGIGLKS AKGSSTSGHV QRSLASNNRR RPQGSQQQRQ QRQNAIKKAS HDKASRPLAV
QKQIETHMEK REIEVQVSEL RDRLEEEETL SEEQIDKKCE ALRAKLTNEW QEQQRMSSLY
TPRKARLTEE QHRHE
