SPP2_YEAST
ID SPP2_YEAST Reviewed; 185 AA.
AC Q02521; D6W2K5; Q12353;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Pre-mRNA-splicing factor SPP2;
DE AltName: Full=Spliceosome maturation protein SPP2;
DE AltName: Full=Suppressor of PRP protein 2;
GN Name=SPP2; OrderedLocusNames=YOR148C;
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 [GENOMIC DNA], FUNCTION, AND INTERACTION WITH PRP2.
RX PubMed=7493316;
RA Roy J., Kim K., Maddock J.R., Anthony J.G., Woolford J.L. Jr.;
RT "The final stages of spliceosome maturation require Spp2p that can interact
RT with the DEAH box protein Prp2p and promote step 1 of splicing.";
RL RNA 1:375-390(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1678;
RX PubMed=9046089;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<73::aid-yea52>3.0.co;2-m;
RA Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A., Winsor B.,
RA Martin R.P.;
RT "Analysis of a 35.6 kb region on the right arm of Saccharomyces cerevisiae
RT chromosome XV.";
RL Yeast 13:73-83(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
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 [5]
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 [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 INTERACTION WITH PRP2, AND MUTAGENESIS OF LEU-109.
RX PubMed=15542821; DOI=10.1128/mcb.24.23.10101-10110.2004;
RA Silverman E.J., Maeda A., Wei J., Smith P., Beggs J.D., Lin R.-J.;
RT "Interaction between a G-patch protein and a spliceosomal DEXD/H-box ATPase
RT that is critical for splicing.";
RL Mol. Cell. Biol. 24:10101-10110(2004).
RN [9]
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 [10]
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; specifically in the final
CC stages of spliceosome maturation. Promotes the first step of splicing.
CC {ECO:0000269|PubMed:7493316}.
CC -!- SUBUNIT: Belongs to the CWC complex (or CEF1-associated complex), a
CC spliceosome sub-complex reminiscent of a late-stage spliceosome
CC composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2,
CC CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24,
CC CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9,
CC PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3,
CC SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts
CC with PRP2. {ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:15542821,
CC ECO:0000269|PubMed:7493316}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 752 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SPP2 family. {ECO:0000305}.
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DR EMBL; U20613; AAA62318.1; -; Genomic_DNA.
DR EMBL; U55020; AAC49634.1; -; Genomic_DNA.
DR EMBL; Z75056; CAA99354.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10921.1; -; Genomic_DNA.
DR PIR; S67036; S67036.
DR RefSeq; NP_014791.1; NM_001183567.1.
DR PDB; 7DCO; EM; 2.50 A; y=1-185.
DR PDB; 7DCP; EM; 3.15 A; y=1-185.
DR PDB; 7DCR; EM; 3.15 A; y=1-185.
DR PDB; 7DD3; EM; 3.20 A; y=1-185.
DR PDBsum; 7DCO; -.
DR PDBsum; 7DCP; -.
DR PDBsum; 7DCR; -.
DR PDBsum; 7DD3; -.
DR AlphaFoldDB; Q02521; -.
DR SMR; Q02521; -.
DR BioGRID; 34544; 16.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR DIP; DIP-4140N; -.
DR IntAct; Q02521; 4.
DR MINT; Q02521; -.
DR STRING; 4932.YOR148C; -.
DR iPTMnet; Q02521; -.
DR MaxQB; Q02521; -.
DR PaxDb; Q02521; -.
DR PRIDE; Q02521; -.
DR EnsemblFungi; YOR148C_mRNA; YOR148C; YOR148C.
DR GeneID; 854319; -.
DR KEGG; sce:YOR148C; -.
DR SGD; S000005674; SPP2.
DR VEuPathDB; FungiDB:YOR148C; -.
DR eggNOG; ENOG502S8BR; Eukaryota.
DR GeneTree; ENSGT00390000015154; -.
DR HOGENOM; CLU_110336_0_0_1; -.
DR InParanoid; Q02521; -.
DR OMA; KIRITHI; -.
DR BioCyc; YEAST:G3O-33666-MON; -.
DR PRO; PR:Q02521; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q02521; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; IDA:SGD.
DR GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:SGD.
DR DisProt; DP02917; -.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR045166; Spp2-like.
DR InterPro; IPR026822; Spp2/MOS2_G-patch.
DR PANTHER; PTHR15818; PTHR15818; 1.
DR Pfam; PF12656; G-patch_2; 1.
DR SMART; SM00443; 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..185
FT /note="Pre-mRNA-splicing factor SPP2"
FT /id="PRO_0000218529"
FT DOMAIN 100..149
FT /note="G-patch"
FT REGION 112..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 109
FT /note="L->E,R: Loss of the interaction with PRP2."
FT /evidence="ECO:0000269|PubMed:15542821"
FT MUTAGEN 109
FT /note="L->V: Restores interactions with PRP2 mutants."
FT /evidence="ECO:0000269|PubMed:15542821"
FT CONFLICT 68..69
FT /note="KK -> GG (in Ref. 1; AAA62318)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="P -> L (in Ref. 1; AAA62318)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="G -> V (in Ref. 1; AAA62318)"
FT /evidence="ECO:0000305"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:7DD3"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:7DCP"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:7DCP"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:7DCR"
SQ SEQUENCE 185 AA; 20648 MW; 3120C3234D178FCD CRC64;
MSKFSLKLGS KTLKKNISKK TKKKNSLQKA NLFDWDDAET ASLSHKPQSK IKIQSIDKFD
LDEESSSKKK LVIKLSENAD TKKNDAPLVE YVTEKEYNEV PVEEFGDALL RGMGWESDSE
QDSKGDKTQS RNKDVSNVSQ IHPDGLGIGA KLNKAINVEE ASFMPVVKID KITGTKVDDD
KKNKS
