CWC22_YEAST
ID CWC22_YEAST Reviewed; 577 AA.
AC P53333; D6VV55;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Pre-mRNA-splicing factor CWC22;
DE AltName: Full=Complexed with CEF1 protein 22;
GN Name=CWC22; OrderedLocusNames=YGR278W;
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 96604 / S288c / FY1679;
RX PubMed=9090054;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<251::aid-yea63>3.0.co;2-r;
RA Volckaert G., Voet M., Robben J.;
RT "Sequence analysis of a near-subtelomeric 35.4 kb DNA segment on the right
RT arm of chromosome VII from Saccharomyces cerevisiae carrying the MAL1 locus
RT reveals 15 complete open reading frames, including ZUO1, BGL2 and BIO2
RT genes and an ABC transporter gene.";
RL Yeast 13:251-259(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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [6]
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: May be involved in pre-mRNA splicing.
CC -!- SUBUNIT: Belongs to the CWC complex (or CEF1-associated complex), a
CC spliceosome subcomplex composed of the U2, U5 and U6 snRNAs and at
CC least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21,
CC CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1,
CC MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46,
CC SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1,
CC SYF2, RSE1 and YJU2. {ECO:0000269|PubMed:11884590}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3260 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CWC22 family. {ECO:0000305}.
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DR EMBL; Z73063; CAA97309.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08366.1; -; Genomic_DNA.
DR PIR; S64613; S64613.
DR RefSeq; NP_011794.3; NM_001181407.3.
DR PDB; 5GM6; EM; 3.50 A; Z=1-577.
DR PDB; 5GMK; EM; 3.40 A; Z=1-577.
DR PDB; 5LQW; EM; 5.80 A; H=1-577.
DR PDB; 5MPS; EM; 3.85 A; H=1-577.
DR PDB; 5MQ0; EM; 4.17 A; H=1-577.
DR PDB; 5WSG; EM; 4.00 A; Z=1-577.
DR PDB; 5YLZ; EM; 3.60 A; S=1-577.
DR PDB; 6BK8; EM; 3.30 A; L=1-577.
DR PDB; 6EXN; EM; 3.70 A; H=1-577.
DR PDB; 6J6G; EM; 3.20 A; Z=1-577.
DR PDB; 6J6H; EM; 3.60 A; Z=1-577.
DR PDB; 6J6N; EM; 3.86 A; Z=1-577.
DR PDB; 6J6Q; EM; 3.70 A; Z=1-577.
DR PDBsum; 5GM6; -.
DR PDBsum; 5GMK; -.
DR PDBsum; 5LQW; -.
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; P53333; -.
DR SMR; P53333; -.
DR BioGRID; 33528; 164.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR DIP; DIP-1869N; -.
DR IntAct; P53333; 20.
DR MINT; P53333; -.
DR STRING; 4932.YGR278W; -.
DR iPTMnet; P53333; -.
DR MaxQB; P53333; -.
DR PaxDb; P53333; -.
DR PRIDE; P53333; -.
DR EnsemblFungi; YGR278W_mRNA; YGR278W; YGR278W.
DR GeneID; 853195; -.
DR KEGG; sce:YGR278W; -.
DR SGD; S000003510; CWC22.
DR VEuPathDB; FungiDB:YGR278W; -.
DR eggNOG; KOG2140; Eukaryota.
DR GeneTree; ENSGT00940000153458; -.
DR HOGENOM; CLU_006308_3_4_1; -.
DR InParanoid; P53333; -.
DR OMA; NIFKFDA; -.
DR BioCyc; YEAST:G3O-30942-MON; -.
DR PRO; PR:P53333; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53333; protein.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:SGD.
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 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 3D-structure; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Spliceosome.
FT CHAIN 1..577
FT /note="Pre-mRNA-splicing factor CWC22"
FT /id="PRO_0000215678"
FT DOMAIN 22..204
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 290..407
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 505..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..577
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 9..30
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 88..108
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 148..165
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 167..183
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 188..203
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 246..249
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 250..261
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 286..301
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 322..334
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 341..351
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 355..371
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 378..393
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 399..404
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 414..431
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 433..443
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 455..468
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 475..484
FT /evidence="ECO:0007829|PDB:6J6G"
SQ SEQUENCE 577 AA; 67294 MW; 773E33C71E4A29D0 CRC64;
MSTATIQDED IKFQRENWEM IRSHVSPIIS NLTMDNLQES HRDLFQVNIL IGRNIICKNV
VDFTLNKQNG RLIPALSALI ALLNSDIPDI GETLAKELML MFVQQFNRKD YVSCGNILQC
LSILFLYDVI HEIVILQILL LLLEKNSLRL VIAVMKICGW KLALVSKKTH DMIWEKLRYI
LQTQELSSTL RESLETLFEI RQKDYKSGSQ GLFILDPTSY TVHTHSYIVS DEDEANKELG
NFEKCENFNE LTMAFDTLRQ KLLINNTSDT NEGSNSQLQI YDMTSTNDVE FKKKIYLVLK
SSLSGDEAAH KLLKLKIANN LKKSVVDIII KSSLQESTFS KFYSILSERM ITFHRSWQTA
YNETFEQNYT QDIEDYETDQ LRILGKFWGH LISYEFLPMD CLKIIKLTEE ESCPQGRIFI
KFLFQELVNE LGLDELQLRL NSSKLDGMFP LEGDAEHIRY SINFFTAIGL GLLTEDMRSR
LTIIQEVEDA EEEEKKLREE EELEKLRKKA RESQPTQGPK IHESRLFLQK DTRENSRSRS
PFTVETRKRA RSRTPPRGSR NHRNRSRTPP ARRQRHR
