ID SP382_YEAST Reviewed; 708 AA.
AC Q06411; D6VZ60;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 167.
DE RecName: Full=Pre-mRNA-splicing factor SPP382;
DE AltName: Full=CLF1 complex factor 8;
DE AltName: Full=Nineteen complex-related protein 1;
DE Short=NTC-related protein 1;
DE AltName: Full=Suppressor of PRP38 protein 2;
GN Name=SPP382; Synonyms=CCF8, NTR1; OrderedLocusNames=YLR424W;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 INTERACTION WITH CLF1.
RX PubMed=12509417; DOI=10.1074/jbc.m210839200;
RA Wang Q., Hobbs K., Lynn B., Rymond B.C.;
RT "The Clf1p splicing factor promotes spliceosome assembly through N-terminal
RT tetratricopeptide repeat contacts.";
RL J. Biol. Chem. 278:7875-7883(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH PRP43 AND PRP45.
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 [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, IDENTIFICATION IN THE NTC-RELATED COMPLEX, AND INTERACTION WITH
RP CLF1; NTR2 AND PRP43.
RX PubMed=16357217; DOI=10.1101/gad.1377405;
RA Tsai R.-T., Fu R.-H., Yeh F.-L., Tseng C.-K., Lin Y.-C., Huang Y.-H.,
RA Cheng S.-C.;
RT "Spliceosome disassembly catalyzed by Prp43 and its associated components
RT Ntr1 and Ntr2.";
RL Genes Dev. 19:2991-3003(2005).
RN [8]
RP FUNCTION, AND INTERACTION WITH NTR2 AND PRP43.
RX PubMed=16880513; DOI=10.1128/mcb.02347-05;
RA Boon K.-L., Auchynnikava T., Edwalds-Gilbert G., Barrass J.D., Droop A.P.,
RA Dez C., Beggs J.D.;
RT "Yeast ntr1/spp382 mediates prp43 function in postspliceosomes.";
RL Mol. Cell. Biol. 26:6016-6023(2006).
CC -!- FUNCTION: Involved in pre-mRNA splicing and spliceosome disassembly.
CC Promotes release of excised lariat intron from the spliceosome by
CC acting as a receptor for PRP43. This targeting of PRP43 leads to
CC disassembly of the spliceosome with the separation of the U2, U5, U6
CC snRNPs and the NTC complex. {ECO:0000269|PubMed:16357217,
CC ECO:0000269|PubMed:16880513}.
CC -!- SUBUNIT: Component of the NTR complex (NTC-related complex), composed
CC of NTR1, NTR2 and PRP43. Interacts with CLF1 and NTR2. Interacts with
CC PRP43 and PRP45. {ECO:0000269|PubMed:12509417,
CC ECO:0000269|PubMed:14690591, ECO:0000269|PubMed:16357217,
CC ECO:0000269|PubMed:16880513}.
CC -!- INTERACTION:
CC Q06411; Q03654: CEF1; NbExp=3; IntAct=EBI-576, EBI-476;
CC Q06411; P52868: CWC23; NbExp=6; IntAct=EBI-576, EBI-560;
CC Q06411; P36118: NTR2; NbExp=10; IntAct=EBI-576, EBI-26362;
CC Q06411; P53131: PRP43; NbExp=11; IntAct=EBI-576, EBI-505;
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}.
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DR EMBL; U20939; AAB67507.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09726.1; -; Genomic_DNA.
DR PIR; S53411; S53411.
DR RefSeq; NP_013528.1; NM_001182312.1.
DR PDB; 5Y88; EM; 3.70 A; U=1-708.
DR PDBsum; 5Y88; -.
DR AlphaFoldDB; Q06411; -.
DR EMDB; EMD-6817; -.
DR SMR; Q06411; -.
DR BioGRID; 31683; 150.
DR ComplexPortal; CPX-1886; Post-mRNA release spliceosomal complex.
DR DIP; DIP-1491N; -.
DR IntAct; Q06411; 134.
DR MINT; Q06411; -.
DR STRING; 4932.YLR424W; -.
DR iPTMnet; Q06411; -.
DR MaxQB; Q06411; -.
DR PaxDb; 4932-YLR424W; -.
DR PeptideAtlas; Q06411; -.
DR EnsemblFungi; YLR424W_mRNA; YLR424W; YLR424W.
DR GeneID; 851143; -.
DR KEGG; sce:YLR424W; -.
DR AGR; SGD:S000004416; -.
DR SGD; S000004416; SPP382.
DR VEuPathDB; FungiDB:YLR424W; -.
DR eggNOG; KOG2184; Eukaryota.
DR HOGENOM; CLU_434104_0_0_1; -.
DR InParanoid; Q06411; -.
DR OMA; NKILYQW; -.
DR OrthoDB; 3060898at2759; -.
DR BioCyc; YEAST:G3O-32484-MONOMER; -.
DR BioGRID-ORCS; 851143; 3 hits in 10 CRISPR screens.
DR PRO; PR:Q06411; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06411; Protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0071008; C:U2-type post-mRNA release spliceosomal complex; IDA:SGD.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IMP:SGD.
DR GO; GO:1904876; P:negative regulation of DNA ligase activity; IMP:BHF-UCL.
DR GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; IMP:BHF-UCL.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:BHF-UCL.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:BHF-UCL.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IDA:SGD.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR045211; TFP11/STIP/Ntr1.
DR PANTHER; PTHR23329:SF1; TUFTELIN-INTERACTING PROTEIN 11; 1.
DR PANTHER; PTHR23329; TUFTELIN-INTERACTING PROTEIN 11-RELATED; 1.
DR Pfam; PF01585; G-patch; 1.
DR SMART; SM00443; G_patch; 1.
DR PROSITE; PS50174; G_PATCH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Spliceosome.
FT CHAIN 1..708
FT /note="Pre-mRNA-splicing factor SPP382"
FT /id="PRO_0000270560"
FT DOMAIN 61..108
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
SQ SEQUENCE 708 AA; 83049 MW; 9986B547B9582338 CRC64;
MEDSDSNTDK KFFFKKRRID SYNYSDEEDN NSSMNSDMTY TNDALKTSSG NAPTISKLTK
TYGIGAKLLS SMGYVAGKGL GKDGSGITTP IETQSRPMHN AGLGMFSNTN SSNYHSENED
YLSSEDEVVE GIEQVKFNKT STEVLGEALL NDSGDMTIVR TLRELRLAGV QLPESILKEL
DPLNAVPKPK KDVVVEILQE LLGIEKSLEA IRQRTSPLEV QVKEYYGQER LLSELEVTLR
DESKHVSLYD KIGAILKLSD DELIDRLTSC LLRKELLIEF DLDHLEKPND ILDELTQIIE
LLAYRMDTTS KFLNRTQTTI FKVIYPKLKK FWEGFDMTKS KIDSAITLLL DFQQVLSFIG
CKEHIMEEFV YPKLLQELDN WELHDEVDHV SPRIWVLDFM VLIDDKIKDT IVDKIEAKFF
AYCKNWYHRE SFCITNSDII FIKELICERR YYKILCKEFL PKFLDELWER HNDPIYELED
WKEKQEWKEK DSGFFYFMKK LRSYTHYFHP KQYELMMRGT FNNINKILYQ WHLYSTVEDL
HKSKWWLNWL MNTVFEHSLP TEIELSEIRK SYNIFAMSHR YHLDKSTLDE DFDLRQGLRN
LMETQVIDDI SQSEQEPTYT VQNIPLGKVS SSFKDVVEDY CLEKGYLISK IPNRYTQLPY
GRDQDCIVPL FEIRNGKKKM EVALKHDILW VEDSSGTFKP IYLWALDL
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