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Pre-mRNA-splicing factor SLU7 (Synthetic lethal with U2 snRNA protein 17) (Synthetic lethal with U5 snRNA protein 7)

 SLU7_YEAST              Reviewed;         382 AA.
Q02775; D6VS75; P89902; Q6Q5U3;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
22-NOV-2017, entry version 158.
RecName: Full=Pre-mRNA-splicing factor SLU7;
AltName: Full=Synthetic lethal with U2 snRNA protein 17;
AltName: Full=Synthetic lethal with U5 snRNA protein 7;
Name=SLU7; Synonyms=SLT17; OrderedLocusNames=YDR088C; ORFNames=D4483;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=1427075; DOI=10.1101/gad.6.11.2112;
Frank D.N., Guthrie C.;
"An essential splicing factor, SLU7, mediates 3' splice site choice in
yeast.";
Genes Dev. 6:2112-2124(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
FUNCTION.
PubMed=1406691; DOI=10.1128/MCB.12.11.5197;
Frank D.N., Patterson B., Guthrie C.;
"Synthetic lethal mutations suggest interactions between U5 small
nuclear RNA and four proteins required for the second step of
splicing.";
Mol. Cell. Biol. 12:5197-5205(1992).
[6]
FUNCTION.
PubMed=7664739;
Ansari A., Schwer B.;
"SLU7 and a novel activity, SSF1, act during the PRP16-dependent step
of yeast pre-mRNA splicing.";
EMBO J. 14:4001-4009(1995).
[7]
FUNCTION.
PubMed=7568198; DOI=10.1073/pnas.92.21.9687;
Jones M.H., Frank D.N., Guthrie C.;
"Characterization and functional ordering of Slu7p and Prp17p during
the second step of pre-mRNA splicing in yeast.";
Proc. Natl. Acad. Sci. U.S.A. 92:9687-9691(1995).
[8]
INTERACTION WITH THE 3' SPLICE SITE.
PubMed=7489518;
Umen J.G., Guthrie C.;
"Prp16p, Slu7p, and Prp8p interact with the 3' splice site in two
distinct stages during the second catalytic step of pre-mRNA
splicing.";
RNA 1:584-597(1995).
[9]
FUNCTION, AND ASSOCIATION WITH THE SPLICEOSOME.
PubMed=8756413;
Brys A., Schwer B.;
"Requirement for SLU7 in yeast pre-mRNA splicing is dictated by the
distance between the branchpoint and the 3' splice site.";
RNA 2:707-717(1996).
[10]
FUNCTION, AND INTERACTION WITH PRP18.
PubMed=9153314; DOI=10.1093/nar/25.11.2146;
Zhang X., Schwer B.;
"Functional and physical interaction between the yeast splicing
factors Slu7 and Prp18.";
Nucleic Acids Res. 25:2146-2152(1997).
[11]
FUNCTION.
PubMed=9528778; DOI=10.1128/MCB.18.4.2055;
Xu D., Field D.J., Tang S.-J., Moris A., Bobechko B.P., Friesen J.D.;
"Synthetic lethality of yeast slt mutations with U2 small nuclear RNA
mutations suggests functional interactions between U2 and U5 snRNPs
that are important for both steps of pre-mRNA splicing.";
Mol. Cell. Biol. 18:2055-2066(1998).
[12]
INTERACTION WITH PRP18.
PubMed=10737784; DOI=10.1073/pnas.97.7.3022;
Jiang J., Horowitz D.S., Xu R.-M.;
"Crystal structure of the functional domain of the splicing factor
Prp18.";
Proc. Natl. Acad. Sci. U.S.A. 97:3022-3027(2000).
[13]
INTERACTION WITH BRR2; PRP18 AND PRP22.
PubMed=11290703;
van Nues R.W., Beggs J.D.;
"Functional contacts with a range of splicing proteins suggest a
central role for Brr2p in the dynamic control of the order of events
in spliceosomes of Saccharomyces cerevisiae.";
Genetics 157:1451-1467(2001).
[14]
INTERACTION WITH ECM2, AND FUNCTION.
PubMed=11158289; DOI=10.1128/MCB.21.4.1011-1023.2001;
Xu D., Friesen J.D.;
"Splicing factor slt11p and its involvement in formation of U2/U6
helix II in activation of the yeast spliceosome.";
Mol. Cell. Biol. 21:1011-1023(2001).
[15]
IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=11884590; DOI=10.1128/MCB.22.7.2011-2024.2002;
Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
"Proteomics analysis reveals stable multiprotein complexes in both
fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel
pre-mRNA splicing factors, and snRNAs.";
Mol. Cell. Biol. 22:2011-2024(2002).
[16]
FUNCTION, INTERACTION WITH PRP18, AND MUTAGENESIS OF CYS-122; HIS-130;
CYS-135; 215-GLU--GLU-217; GLU-217 AND 221-LEU--TYR-224.
PubMed=12212850; DOI=10.1017/S1355838202022033;
James S.-A., Turner W., Schwer B.;
"How Slu7 and Prp18 cooperate in the second step of yeast pre-mRNA
splicing.";
RNA 8:1068-1077(2002).
[17]
INTERACTION WITH PRP18.
PubMed=12403466; DOI=10.1017/S1355838202023099;
Bacikova D., Horowitz D.S.;
"Mutational analysis identifies two separable roles of the
Saccharomyces cerevisiae splicing factor Prp18.";
RNA 8:1280-1293(2002).
[18]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[19]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND THR-212, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[22]
GLYCOSYLATION [LARGE SCALE ANALYSIS].
PubMed=19756047; DOI=10.1038/msb.2009.64;
Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
"Global analysis of the glycoproteome in Saccharomyces cerevisiae
reveals new roles for protein glycosylation in eukaryotes.";
Mol. Syst. Biol. 5:308-308(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Essential protein involved in the second catalytic step
of pre-mRNA splicing. Involved in the selection of 3'-type splice
sites; this selection could be done via a 3'-splice site-binding
factor, PRP16. {ECO:0000269|PubMed:11158289,
ECO:0000269|PubMed:12212850, ECO:0000269|PubMed:1406691,
ECO:0000269|PubMed:1427075, ECO:0000269|PubMed:7568198,
ECO:0000269|PubMed:7664739, ECO:0000269|PubMed:8756413,
ECO:0000269|PubMed:9153314, ECO:0000269|PubMed:9528778}.
-!- SUBUNIT: Belongs to the CWC complex (or CEF1-associated complex),
a spliceosome sub-complex reminiscent of a late-stage spliceosome
composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31,
BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23,
CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20,
PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1,
SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2,
RSE1 and YJU2. Interacts with BRR2, ECM2, PRP18 and PRP22.
{ECO:0000269|PubMed:10737784, ECO:0000269|PubMed:11158289,
ECO:0000269|PubMed:11290703, ECO:0000269|PubMed:11884590,
ECO:0000269|PubMed:12212850, ECO:0000269|PubMed:12403466,
ECO:0000269|PubMed:7489518, ECO:0000269|PubMed:9153314}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
-!- DOMAIN: The CCHC-type zinc finger probably plays a role in the
ability of SLU7 to bypass the requirement for PRP18.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
-!- MISCELLANEOUS: Present with 1490 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the SLU7 family. {ECO:0000305}.
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EMBL; X67810; CAA48011.1; -; Genomic_DNA.
EMBL; X82086; CAA57617.1; -; Genomic_DNA.
EMBL; Z46796; CAA86810.1; -; Genomic_DNA.
EMBL; Z74384; CAA98908.1; -; Genomic_DNA.
EMBL; Z74385; CAA98909.1; -; Genomic_DNA.
EMBL; AY557701; AAS56027.1; -; Genomic_DNA.
EMBL; BK006938; DAA11935.1; -; Genomic_DNA.
PIR; A46229; A46229.
RefSeq; NP_010373.3; NM_001180396.3.
PDB; 5MPS; EM; 3.85 A; c=1-382.
PDB; 5MQ0; EM; 4.17 A; c=1-382.
PDBsum; 5MPS; -.
PDBsum; 5MQ0; -.
ProteinModelPortal; Q02775; -.
SMR; Q02775; -.
BioGrid; 32144; 467.
DIP; DIP-220N; -.
IntAct; Q02775; 11.
MINT; MINT-394061; -.
STRING; 4932.YDR088C; -.
iPTMnet; Q02775; -.
MaxQB; Q02775; -.
PRIDE; Q02775; -.
EnsemblFungi; YDR088C; YDR088C; YDR088C.
GeneID; 851661; -.
KEGG; sce:YDR088C; -.
EuPathDB; FungiDB:YDR088C; -.
SGD; S000002495; SLU7.
HOGENOM; HOG000154339; -.
InParanoid; Q02775; -.
KO; K12819; -.
OMA; MYSCEAF; -.
OrthoDB; EOG092C2PD6; -.
BioCyc; YEAST:G3O-29693-MONOMER; -.
PRO; PR:Q02775; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005681; C:spliceosomal complex; IDA:SGD.
GO; GO:0071021; C:U2-type post-spliceosomal complex; IDA:SGD.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IDA:SGD.
Gene3D; 4.10.60.10; -; 1.
InterPro; IPR021715; Slu7.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF11708; Slu7; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Glycoprotein; Metal-binding;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
Reference proteome; Spliceosome; Zinc; Zinc-finger.
CHAIN 1 382 Pre-mRNA-splicing factor SLU7.
/FTId=PRO_0000218554.
ZN_FING 120 137 CCHC-type. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
REGION 200 224 Interaction with PRP8.
MOD_RES 120 120 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 212 212 Phosphothreonine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MUTAGEN 122 122 C->A: Affects the ability to associate
with the spliceosome. Loss of growth and
in vitro splicing activity; when
associated with 215-AAA-217. Cryo- and
thermosensitivity; when associated with
A-217. {ECO:0000269|PubMed:12212850}.
MUTAGEN 130 130 H->A: Affects the ability to associate
with the spliceosome. Loss of growth and
in vitro splicing activity; when
associated with 215-AAA-217. Cryo- and
thermosensitivity; when associated with
A-217. {ECO:0000269|PubMed:12212850}.
MUTAGEN 135 135 C->A: Affects the ability to associate
with the spliceosome. Loss of growth,
spliceosome binding, and in vitro
splicing activity; when associated with
215-AAA-217. Cryo- and thermosensitivity;
when associated with A-217.
{ECO:0000269|PubMed:12212850}.
MUTAGEN 215 217 EIE->AAA: Abolishes the interaction with
PRP18, and temperature sensitive growth
defect. Loss of growth and in vitro
splicing activity; when associated with
A-122 or A-130 or A-135.
{ECO:0000269|PubMed:12212850}.
MUTAGEN 217 217 E->A: Abolishes the interaction with
PRP18. Cryo- and thermosensitivity; when
associated with A-122 or A-130 or A-135.
{ECO:0000269|PubMed:12212850}.
MUTAGEN 217 217 E->K: Abolishes the interaction with
PRP18, and temperature sensitive growth
defect. {ECO:0000269|PubMed:12212850}.
MUTAGEN 221 224 LELY->AAAA: Abolishes the interaction
with PRP18, and temperature sensitive
growth defect.
{ECO:0000269|PubMed:12212850}.
CONFLICT 235 235 D -> G (in Ref. 4; AAS56027).
{ECO:0000305}.
SEQUENCE 382 AA; 44637 MW; 6405458FC367A7D3 CRC64;
MNNNSRNNEN RSTINRNKRQ LQQAKEKNEN IHIPRYIRNQ PWYYKDTPKE QEGKKPGNDD
TSTAEGGEKS DYLVHHRQKA KGGALDIDNN SEPKIGMGIK DEFKLIRPQK MSVRDSHSLS
FCRNCGEAGH KEKDCMEKPR KMQKLVPDLN SQKNNGTVLV RATDDDWDSR KDRWYGYSGK
EYNELISKWE RDKRNKIKGK DKSQTDETLW DTDEEIELMK LELYKDSVGS LKKDDADNSQ
LYRTSTRLRE DKAAYLNDIN STESNYDPKS RLYKTETLGA VDEKSKMFRR HLTGEGLKLN
ELNQFARSHA KEMGIRDEIE DKEKVQHVLV ANPTKYEYLK KKREQEETKQ PKIVSIGDLE
ARKVDGTKQS EEQRNHLKDL YG


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