NTR2_YEAST
ID NTR2_YEAST Reviewed; 322 AA.
AC P36118; D6VX87;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Pre-mRNA-splicing factor NTR2;
DE AltName: Full=Nineteen complex-related protein 2;
DE Short=NTC-related protein 2;
GN Name=NTR2; OrderedLocusNames=YKR022C;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 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 [4]
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 [5]
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 [6]
RP FUNCTION, IDENTIFICATION IN THE NTC-RELATED COMPLEX, AND INTERACTION WITH
RP CLF1; NTR1 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 [7]
RP FUNCTION, AND INTERACTION WITH NTR1 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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-153, AND
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-197, AND
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: 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, NTR1 and PRP43.
CC {ECO:0000269|PubMed:16357217, ECO:0000269|PubMed:16880513}.
CC -!- INTERACTION:
CC P36118; Q06411: SPP382; NbExp=10; IntAct=EBI-26362, EBI-576;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 892 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z28247; CAA82094.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09177.1; -; Genomic_DNA.
DR PIR; S38091; S38091.
DR RefSeq; NP_012947.1; NM_001179812.1.
DR PDB; 5Y88; EM; 3.70 A; V=1-322.
DR PDBsum; 5Y88; -.
DR AlphaFoldDB; P36118; -.
DR SMR; P36118; -.
DR BioGRID; 34154; 167.
DR ComplexPortal; CPX-1886; Post-mRNA release spliceosomal complex.
DR DIP; DIP-1924N; -.
DR IntAct; P36118; 20.
DR MINT; P36118; -.
DR STRING; 4932.YKR022C; -.
DR iPTMnet; P36118; -.
DR MaxQB; P36118; -.
DR PaxDb; P36118; -.
DR PRIDE; P36118; -.
DR EnsemblFungi; YKR022C_mRNA; YKR022C; YKR022C.
DR GeneID; 853892; -.
DR KEGG; sce:YKR022C; -.
DR SGD; S000001730; NTR2.
DR VEuPathDB; FungiDB:YKR022C; -.
DR eggNOG; ENOG502SA8V; Eukaryota.
DR HOGENOM; CLU_074884_0_0_1; -.
DR InParanoid; P36118; -.
DR OMA; QISERAY; -.
DR BioCyc; YEAST:G3O-31998-MON; -.
DR PRO; PR:P36118; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36118; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005681; C:spliceosomal complex; IDA:SGD.
DR GO; GO:0071008; C:U2-type post-mRNA release spliceosomal complex; IDA:SGD.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IDA:SGD.
DR DisProt; DP01471; -.
DR InterPro; IPR028211; Ntr2.
DR Pfam; PF15458; NTR2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome.
FT CHAIN 1..322
FT /note="Pre-mRNA-splicing factor NTR2"
FT /id="PRO_0000203201"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 322 AA; 36647 MW; D7A601A46839244C CRC64;
MAIKKRNKIR LPSGSPEEVG IDGSAHKPMQ QIKPLVSNDS EDDDNDICVL QPIKFKKVPK
RDITFDGEQA IKEDNSHYED LYHSKKNTNA STRNKDDLLI LNMEDLMEGN HHLLSDSSEA
GSSSEGEHIS SIPTRGEIAK LKAQKSLSRR KISESDVTTE RDYVKLLDSE DKREIMETIR
LNGGLKRNNE KEITNFSDDE MQGFQDEMLA LTDNQIAIQK DSKRKIIEKA INEVPYRTNE
EWETQLLSKG NINKSNEKII TPLPVLFPDD DESGNSIERI NEMVSKICLQ RKKVEMRLQA
LEKTKIDLEK SKASLINKLI GN
