SEM1_YEAST
ID SEM1_YEAST Reviewed; 89 AA.
AC O94742; D6VSZ2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=26S proteasome complex subunit SEM1;
GN Name=SEM1; Synonyms=DSH1; OrderedLocusNames=YDR363W-A;
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 [MRNA].
RX PubMed=9927667; DOI=10.1073/pnas.96.3.909;
RA Jantti J., Lahdenranta J., Olkkonen V.M., Soderlund H., Keranen S.;
RT "SEM1, a homologue of the split hand/split foot malformation candidate gene
RT Dss1, regulates exocytosis and pseudohyphal differentiation in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:909-914(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90840 / EAY235 / FY23;
RA DeHoratius C., Green M.R.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-12, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [7]
RP INTERACTION WITH CSN12 AND THP3.
RX PubMed=19061648; DOI=10.1016/j.molcel.2008.11.012;
RA Wilmes G.M., Bergkessel M., Bandyopadhyay S., Shales M., Braberg H.,
RA Cagney G., Collins S.R., Whitworth G.B., Kress T.L., Weissman J.S.,
RA Ideker T., Guthrie C., Krogan N.J.;
RT "A genetic interaction map of RNA-processing factors reveals links between
RT Sem1/Dss1-containing complexes and mRNA export and splicing.";
RL Mol. Cell 32:735-746(2008).
RN [8]
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 [9]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBUNIT, AND INTERACTION WITH CSN12 AND
RP THP3.
RX PubMed=19289793; DOI=10.1083/jcb.200810059;
RA Faza M.B., Kemmler S., Jimeno S., Gonzalez-Aguilera C., Aguilera A.,
RA Hurt E., Panse V.G.;
RT "Sem1 is a functional component of the nuclear pore complex-associated
RT messenger RNA export machinery.";
RL J. Cell Biol. 184:833-846(2009).
RN [10]
RP FUNCTION.
RX PubMed=15117943; DOI=10.1074/jbc.m403165200;
RA Sone T., Saeki Y., Toh-e A., Yokosawa H.;
RT "Sem1p is a novel subunit of the 26S proteasome from Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 279:28807-28816(2004).
CC -!- FUNCTION: Versatile protein that might stabilize multiple protein
CC complexes involved in diverse pathways. Subunit of the 26S proteasome
CC which plays a role in ubiquitin-dependent proteolysis. Associates also
CC with the TREX-2 complex that is required for transcription-coupled mRNA
CC export, and the COP9 signalosome, which is involved in deneddylation.
CC {ECO:0000269|PubMed:15117943, ECO:0000269|PubMed:19289793}.
CC -!- SUBUNIT: Part of the 26S proteasome. Associates with the nuclear pore
CC complex (NPC)-associated TREX-2 complex and the COP9 signalosome.
CC Interacts with CSN12 and THP3. {ECO:0000269|PubMed:19061648,
CC ECO:0000269|PubMed:19289793}.
CC -!- INTERACTION:
CC O94742; P38348: HSM3; NbExp=2; IntAct=EBI-31337, EBI-21152;
CC O94742; Q06103: RPN7; NbExp=3; IntAct=EBI-31337, EBI-15940;
CC O94742; Q08231: THP1; NbExp=2; IntAct=EBI-31337, EBI-32097;
CC -!- DISRUPTION PHENOTYPE: Impairs mRNA export and transcription elongation,
CC and induces strong transcription-associated hyperrecombination
CC phenotypes. {ECO:0000269|PubMed:19289793}.
CC -!- MISCELLANEOUS: Present with 5590 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DSS1/SEM1 family. {ECO:0000305}.
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DR EMBL; AF059310; AAD08804.1; -; mRNA.
DR EMBL; AF065136; AAC96096.1; -; Genomic_DNA.
DR EMBL; U28372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY557719; AAS56045.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12202.1; -; Genomic_DNA.
DR PIR; S78744; S78744.
DR RefSeq; NP_010651.3; NM_001184328.3.
DR PDB; 3JCK; EM; 3.50 A; I=1-89.
DR PDB; 3JCO; EM; 4.80 A; Y=1-89.
DR PDB; 3JCP; EM; 4.60 A; Y=1-89.
DR PDB; 3T5V; X-ray; 2.90 A; C/F=1-89.
DR PDB; 4CR2; EM; 7.70 A; Y=1-89.
DR PDB; 4CR3; EM; 9.30 A; Y=1-89.
DR PDB; 4CR4; EM; 8.80 A; Y=1-89.
DR PDB; 4TRQ; X-ray; 3.10 A; C/F=30-89.
DR PDB; 5A5B; EM; 9.50 A; Y=1-89.
DR PDB; 5G5P; EM; 5.30 A; C=1-89.
DR PDB; 5L3T; X-ray; 4.93 A; C=1-89.
DR PDB; 5MPB; EM; 7.80 A; Y=1-89.
DR PDB; 5MPC; EM; 7.70 A; Y=1-89.
DR PDB; 5MPD; EM; 4.10 A; Y=1-89.
DR PDB; 5MPE; EM; 4.50 A; Y=1-89.
DR PDB; 5UBP; X-ray; 2.30 A; C=1-89.
DR PDB; 5WVI; EM; 6.30 A; Y=1-89.
DR PDB; 5WVK; EM; 4.20 A; Y=1-89.
DR PDB; 6FVT; EM; 4.10 A; Y=1-89.
DR PDB; 6FVU; EM; 4.50 A; Y=1-89.
DR PDB; 6FVV; EM; 5.40 A; Y=1-89.
DR PDB; 6FVW; EM; 4.50 A; Y=1-89.
DR PDB; 6FVX; EM; 4.90 A; Y=1-89.
DR PDB; 6FVY; EM; 6.10 A; Y=1-89.
DR PDB; 6J2C; EM; 7.00 A; Y=1-89.
DR PDB; 6J2N; EM; 7.50 A; Y=1-89.
DR PDB; 6J2Q; EM; 3.80 A; Y=1-89.
DR PDB; 6J2X; EM; 3.80 A; Y=1-89.
DR PDB; 6J30; EM; 4.50 A; Y=1-89.
DR PDB; 7QO3; EM; 6.10 A; Y=1-89.
DR PDB; 7QO5; EM; 6.00 A; Y=1-89.
DR PDB; 7QO6; EM; 6.30 A; Y=1-89.
DR PDBsum; 3JCK; -.
DR PDBsum; 3JCO; -.
DR PDBsum; 3JCP; -.
DR PDBsum; 3T5V; -.
DR PDBsum; 4CR2; -.
DR PDBsum; 4CR3; -.
DR PDBsum; 4CR4; -.
DR PDBsum; 4TRQ; -.
DR PDBsum; 5A5B; -.
DR PDBsum; 5G5P; -.
DR PDBsum; 5L3T; -.
DR PDBsum; 5MPB; -.
DR PDBsum; 5MPC; -.
DR PDBsum; 5MPD; -.
DR PDBsum; 5MPE; -.
DR PDBsum; 5UBP; -.
DR PDBsum; 5WVI; -.
DR PDBsum; 5WVK; -.
DR PDBsum; 6FVT; -.
DR PDBsum; 6FVU; -.
DR PDBsum; 6FVV; -.
DR PDBsum; 6FVW; -.
DR PDBsum; 6FVX; -.
DR PDBsum; 6FVY; -.
DR PDBsum; 6J2C; -.
DR PDBsum; 6J2N; -.
DR PDBsum; 6J2Q; -.
DR PDBsum; 6J2X; -.
DR PDBsum; 6J30; -.
DR PDBsum; 7QO3; -.
DR PDBsum; 7QO5; -.
DR PDBsum; 7QO6; -.
DR AlphaFoldDB; O94742; -.
DR SMR; O94742; -.
DR BioGRID; 32420; 498.
DR ComplexPortal; CPX-1686; TREX-2 transcription-export complex.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-8754N; -.
DR IntAct; O94742; 18.
DR MINT; O94742; -.
DR STRING; 4932.YDR363W-A; -.
DR iPTMnet; O94742; -.
DR MaxQB; O94742; -.
DR PaxDb; O94742; -.
DR PRIDE; O94742; -.
DR EnsemblFungi; YDR363W-A_mRNA; YDR363W-A; YDR363W-A.
DR GeneID; 851967; -.
DR KEGG; sce:YDR363W-A; -.
DR SGD; S000007235; SEM1.
DR VEuPathDB; FungiDB:YDR363W-A; -.
DR eggNOG; KOG4764; Eukaryota.
DR HOGENOM; CLU_141774_1_0_1; -.
DR InParanoid; O94742; -.
DR OMA; TLWENNW; -.
DR BioCyc; YEAST:G3O-30088-MON; -.
DR PRO; PR:O94742; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; O94742; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0000502; C:proteasome complex; IPI:ComplexPortal.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IDA:SGD.
DR GO; GO:0034515; C:proteasome storage granule; IDA:SGD.
DR GO; GO:0070390; C:transcription export complex 2; IDA:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0030447; P:filamentous growth; IMP:SGD.
DR GO; GO:0016578; P:histone deubiquitination; IMP:SGD.
DR GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IMP:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0043248; P:proteasome assembly; IMP:SGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:SGD.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:SGD.
DR GO; GO:0072742; P:SAGA complex localization to transcription regulatory region; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR DisProt; DP01014; -.
DR InterPro; IPR007834; DSS1_SEM1.
DR PANTHER; PTHR16771; PTHR16771; 1.
DR Pfam; PF05160; DSS1_SEM1; 1.
DR SMART; SM01385; DSS1_SEM1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Phosphoprotein; Proteasome; Reference proteome;
KW Transcription.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:15665377"
FT CHAIN 2..89
FT /note="26S proteasome complex subunit SEM1"
FT /id="PRO_0000122970"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:5UBP"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:5UBP"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 72..87
FT /evidence="ECO:0007829|PDB:5UBP"
SQ SEQUENCE 89 AA; 10386 MW; B66B578ABB01E672 CRC64;
MSTDVAAAQA QSKIDLTKKK NEEINKKSLE EDDEFEDFPI DTWANGETIK SNAVTQTNIW
EENWDDVEVD DDFTNELKAE LDRYKRENQ
