ID   SF3B1_YEAST             Reviewed;         971 AA.
AC   P49955; D6W0B5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=U2 snRNP component HSH155;
GN   Name=HSH155; OrderedLocusNames=YMR288W; ORFNames=YM8021.14;
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=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(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   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   [4]
RP   INTERACTION WITH RDS3.
RX   PubMed=14517302; DOI=10.1128/mcb.23.20.7339-7349.2003;
RA   Wang Q., Rymond B.C.;
RT   "Rds3p is required for stable U2 snRNP recruitment to the splicing
RT   apparatus.";
RL   Mol. Cell. Biol. 23:7339-7349(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).
CC   -!- FUNCTION: Contacts pre-mRNA on both sides of the branch site early in
CC       spliceosome assembly. {ECO:0000250}.
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 RDS3. {ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:14517302}.
CC   -!- INTERACTION:
CC       P49955; Q04693: RSE1; NbExp=3; IntAct=EBI-664, EBI-519;
CC       P49955; P0C074: YSF3; NbExp=3; IntAct=EBI-664, EBI-970846;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SF3B1 family. {ECO:0000305}.
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DR   EMBL; Z49704; CAA89786.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10189.1; -; Genomic_DNA.
DR   PIR; S54595; S54595.
DR   RefSeq; NP_014015.1; NM_001182795.1.
DR   PDB; 5GM6; EM; 3.50 A; G=1-971.
DR   PDB; 5LQW; EM; 5.80 A; Q=1-971.
DR   PDB; 5NRL; EM; 7.20 A; O=1-971.
DR   PDB; 5ZWM; EM; 3.40 A; 1=1-971.
DR   PDB; 5ZWO; EM; 3.90 A; 1=1-971.
DR   PDB; 6G90; EM; 4.00 A; O=1-971.
DR   PDB; 7OQB; EM; 9.00 A; O=1-971.
DR   PDB; 7OQE; EM; 5.90 A; O=1-971.
DR   PDBsum; 5GM6; -.
DR   PDBsum; 5LQW; -.
DR   PDBsum; 5NRL; -.
DR   PDBsum; 5ZWM; -.
DR   PDBsum; 5ZWO; -.
DR   PDBsum; 6G90; -.
DR   PDBsum; 7OQB; -.
DR   PDBsum; 7OQE; -.
DR   AlphaFoldDB; P49955; -.
DR   EMDB; EMD-13028; -.
DR   EMDB; EMD-13033; -.
DR   EMDB; EMD-3683; -.
DR   EMDB; EMD-4364; -.
DR   EMDB; EMD-6972; -.
DR   EMDB; EMD-6974; -.
DR   EMDB; EMD-9524; -.
DR   SMR; P49955; -.
DR   BioGRID; 35468; 282.
DR   ComplexPortal; CPX-1647; SF3B complex.
DR   ComplexPortal; CPX-1651; PRP19-associated complex.
DR   ComplexPortal; CPX-26; U2 small nuclear ribonucleoprotein complex.
DR   DIP; DIP-2628N; -.
DR   IntAct; P49955; 30.
DR   MINT; P49955; -.
DR   STRING; 4932.YMR288W; -.
DR   iPTMnet; P49955; -.
DR   MaxQB; P49955; -.
DR   PaxDb; 4932-YMR288W; -.
DR   PeptideAtlas; P49955; -.
DR   EnsemblFungi; YMR288W_mRNA; YMR288W; YMR288W.
DR   GeneID; 855332; -.
DR   KEGG; sce:YMR288W; -.
DR   AGR; SGD:S000004901; -.
DR   SGD; S000004901; HSH155.
DR   VEuPathDB; FungiDB:YMR288W; -.
DR   eggNOG; KOG0213; Eukaryota.
DR   GeneTree; ENSGT00390000018393; -.
DR   HOGENOM; CLU_002242_0_1_1; -.
DR   InParanoid; P49955; -.
DR   OMA; LWHPARK; -.
DR   OrthoDB; 226540at2759; -.
DR   BioCyc; YEAST:G3O-32958-MONOMER; -.
DR   BioGRID-ORCS; 855332; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P49955; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P49955; Protein.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR   GO; GO:0005681; C:spliceosomal complex; NAS:ComplexPortal.
DR   GO; GO:0005686; C:U2 snRNP; IDA:SGD.
DR   GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR   GO; GO:0005684; C:U2-type spliceosomal complex; IPI:ComplexPortal.
DR   GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IPI:SGD.
DR   GO; GO:0000245; P:spliceosomal complex assembly; IPI:SGD.
DR   GO; GO:1903241; P:U2-type prespliceosome assembly; NAS:ComplexPortal.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 3.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR038737; SF3b_su1-like.
DR   PANTHER; PTHR12097:SF0; SPLICING FACTOR 3B SUBUNIT 1; 1.
DR   PANTHER; PTHR12097; SPLICING FACTOR 3B, SUBUNIT 1-RELATED; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   1: Evidence at protein level;
KW   3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   Repeat; Spliceosome.
FT   CHAIN           1..971
FT                   /note="U2 snRNP component HSH155"
FT                   /id="PRO_0000174327"
FT   REPEAT          199..237
FT                   /note="HEAT 1"
FT   REPEAT          273..310
FT                   /note="HEAT 2"
FT   REPEAT          350..387
FT                   /note="HEAT 3"
FT   REPEAT          513..550
FT                   /note="HEAT 4"
FT   REPEAT          596..633
FT                   /note="HEAT 5"
FT   REPEAT          680..717
FT                   /note="HEAT 6"
FT   REPEAT          722..759
FT                   /note="HEAT 7"
FT   REPEAT          792..829
FT                   /note="HEAT 8"
FT   REPEAT          832..870
FT                   /note="HEAT 9"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   971 AA;  110028 MW;  27D26E4252A788E2 CRC64;
     MSHPIQFVNA NNSDKSHQLG GQYSIPQDLR ENLQKEAARI GENEKDVLQE KMETRTVQNR
     EDSYHKRRFD MKFEPDSDTQ TVTSSENTQD AVVPRKRKSR WDVKGYEPPD ESSTAVKENS
     DSALVNVEGI HDLMFFKPSD HKYFADVISK KPIDELNKDE KKERTLSMLL LKIKNGNTAS
     RRTSMRILTD KAVTFGPEMI FNRLLPILLD RSLEDQERHL MIKTIDRVLY QLGDLTKPYV
     HKILVVAAPL LIDEDPMVRS TGQEIITNLS TVAGLKTILT VMRPDIENED EYVRNVTSRA
     AAVVAKALGV NQLLPFINAA CHSRKSWKAR HTGIKIVQQI GILLGIGVLN HLTGLMSCIK
     DCLMDDHVPV RIVTAHTLST LAENSYPYGI EVFNVVLEPL WKGIRSHRGK VLSSFLKAVG
     SMIPLMDPEY AGYYTTEAMR IIRREFDSPD DEMKKTILLV LQKCSAVESI TPKFLREEIA
     PEFFQKFWVR RVALDRPLNK VVTYTTVTLA KKLGCSYTID KLLTPLRDEA EPFRTMAVHA
     VTRTVNLLGT ADLDERLETR LIDALLIAFQ EQTNSDSIIF KGFGAVTVSL DIRMKPFLAP
     IVSTILNHLK HKTPLVRQHA ADLCAILIPV IKNCHEFEML NKLNIILYES LGEVYPEVLG
     SIINAMYCIT SVMDLDKLQP PINQILPTLT PILRNKHRKV EVNTIKFVGL IGKLAPTYAP
     PKEWMRICFE LLELLKSTNK EIRRSANATF GFIAEAIGPH DVLVALLNNL KVQERQLRVC
     TAVAIGIVAK VCGPYNVLPV IMNEYTTPET NVQNGVLKAM SFMFEYIGNM SKDYIYFITP
     LLEDALTDRD LVHRQTASNV ITHLALNCSG TGHEDAFIHL MNLLIPNIFE TSPHAIMRIL
     EGLEALSQAL GPGLFMNYIW AGLFHPAKNV RKAFWRVYNN MYVMYQDAMV PFYPVTPDNN
     EEYIEELDLV L
//