PRP11_YEAST
ID PRP11_YEAST Reviewed; 266 AA.
AC Q07350; D6VRV3; Q05434;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Pre-mRNA-splicing factor PRP11;
GN Name=PRP11; Synonyms=PRP10, RNA11; OrderedLocusNames=YDL043C;
GN ORFNames=D2711;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9046088;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<65::aid-yea50>3.0.co;2-t;
RA Saren A.-M., Laamanen P., Lejarcegui J.B., Paulin L.;
RT "The sequence of a 36.7 kb segment on the left arm of chromosome IV from
RT Saccharomyces cerevisiae reveals 20 non-overlapping open reading frames
RT (ORFs) including SIT4, FAD1, NAM1, RNA11, SIR2, NAT1, PRP9, ACT2 and MPS1
RT and 11 new ORFs.";
RL Yeast 13:65-71(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP FUNCTION, AND INTERACTION WITH CUS2.
RX PubMed=9710584; DOI=10.1128/mcb.18.9.5000;
RA Yan D., Perriman R., Igel H., Howe K.J., Neville M., Ares M. Jr.;
RT "CUS2, a yeast homolog of human Tat-SF1, rescues function of misfolded U2
RT through an unusual RNA recognition motif.";
RL Mol. Cell. Biol. 18:5000-5009(1998).
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 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).
CC -!- FUNCTION: mRNA splicing factors, PRP9, PRP11, and PRP21, are necessary
CC for addition of the U2 snRNP to the pre-mRNA in an early step of
CC spliceosome assembly. {ECO:0000269|PubMed:9710584}.
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 CUS2. {ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:9710584}.
CC -!- INTERACTION:
CC Q07350; P32524: PRP21; NbExp=7; IntAct=EBI-688, EBI-603;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 3460 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SF3A2 family. {ECO:0000305}.
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DR EMBL; Z71781; CAA96446.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z74091; CAA98602.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11813.1; -; Genomic_DNA.
DR PIR; S67576; S67576.
DR RefSeq; NP_010241.1; NM_001180102.1.
DR PDB; 4DGW; X-ray; 3.11 A; C=149-266.
DR PDB; 5GM6; EM; 3.50 A; I=1-266.
DR PDB; 5NRL; EM; 7.20 A; U=1-266.
DR PDB; 5ZWM; EM; 3.40 A; v=1-266.
DR PDB; 5ZWO; EM; 3.90 A; v=1-266.
DR PDB; 6G90; EM; 4.00 A; U=1-266.
DR PDBsum; 4DGW; -.
DR PDBsum; 5GM6; -.
DR PDBsum; 5NRL; -.
DR PDBsum; 5ZWM; -.
DR PDBsum; 5ZWO; -.
DR PDBsum; 6G90; -.
DR AlphaFoldDB; Q07350; -.
DR SMR; Q07350; -.
DR BioGRID; 32016; 317.
DR ComplexPortal; CPX-1648; SF3A complex.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR ComplexPortal; CPX-26; U2 small nuclear ribonucleoprotein complex.
DR DIP; DIP-1001N; -.
DR IntAct; Q07350; 57.
DR MINT; Q07350; -.
DR STRING; 4932.YDL043C; -.
DR iPTMnet; Q07350; -.
DR MaxQB; Q07350; -.
DR PaxDb; Q07350; -.
DR PRIDE; Q07350; -.
DR EnsemblFungi; YDL043C_mRNA; YDL043C; YDL043C.
DR GeneID; 851518; -.
DR KEGG; sce:YDL043C; -.
DR SGD; S000002201; PRP11.
DR VEuPathDB; FungiDB:YDL043C; -.
DR eggNOG; KOG0227; Eukaryota.
DR GeneTree; ENSGT00720000108823; -.
DR HOGENOM; CLU_087074_0_0_1; -.
DR InParanoid; Q07350; -.
DR OMA; DKFWTLW; -.
DR BioCyc; YEAST:G3O-29463-MON; -.
DR PRO; PR:Q07350; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07350; protein.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:ComplexPortal.
DR GO; GO:0000245; P:spliceosomal complex assembly; IDA:SGD.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR031781; SF3A2_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR Pfam; PF16835; SF3A2; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..266
FT /note="Pre-mRNA-splicing factor PRP11"
FT /id="PRO_0000174317"
FT ZN_FING 66..96
FT /note="Matrin-type"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:4DGW"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:4DGW"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:4DGW"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:4DGW"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:4DGW"
FT HELIX 235..239
FT /evidence="ECO:0007829|PDB:4DGW"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:4DGW"
FT TURN 245..248
FT /evidence="ECO:0007829|PDB:4DGW"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:4DGW"
SQ SEQUENCE 266 AA; 29921 MW; D8BA3BB27F36F06F CRC64;
MNYLEGVGSK KGGGGIASES QFNLQRRKEV ESLLSKGENV PYTFQDEKDD QVRSNPYIYK
NHSGKLVCKL CNTMHMSWSS VERHLGGKKH GLNVLRRGIS IEKSSLGREG QTTHDFRQQQ
KIIEAKQSLK NNGTIPVCKI ATVKNPKNGS VGLAIQVNYS SEVKENSVDS DDKAKVPPLI
RIVSGLELSD TKQKGKKFLV IAYEPFENIA IELPPNEILF SENNDMDNNN DGVDELNKKC
TFWDAISKLY YVQFFFKQAE QEQADV
