SAD1_YEAST
ID SAD1_YEAST Reviewed; 448 AA.
AC P43589; D6VTN5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Pre-mRNA-splicing factor SAD1;
DE AltName: Full=snRNP assembly-defective protein 1;
GN Name=SAD1; OrderedLocusNames=YFR005C;
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=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
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 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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10022888; DOI=10.1128/mcb.19.3.2008;
RA Lygerou Z., Christophides G., Seraphin B.;
RT "A novel genetic screen for snRNP assembly factors in yeast identifies a
RT conserved protein, Sad1p, also required for pre-mRNA splicing.";
RL Mol. Cell. Biol. 19:2008-2020(1999).
RN [5]
RP IDENTIFICATION IN U1.U2.U4/U6.U5 PENTA-SNRNP COMPLEX, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=11804584; DOI=10.1016/s1097-2765(02)00436-7;
RA Stevens S.W., Ryan D.E., Ge H.Y., Moore R.E., Young M.K., Lee T.D.,
RA Abelson J.;
RT "Composition and functional characterization of the yeast spliceosomal
RT penta-snRNP.";
RL Mol. Cell 9:31-44(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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Promotes the assembly of newly synthesized U4 snRNA into the
CC U4/U6 snRNP particle. Required for splicing of pre-mRNA.
CC {ECO:0000269|PubMed:10022888}.
CC -!- SUBUNIT: Component of the 45S U1.U2.U4/U6.U5 penta-snRNP particle, a
CC subcomplex of the spliceosome. {ECO:0000269|PubMed:11804584}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10022888,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 167 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; D50617; BAA09244.1; -; Genomic_DNA.
DR EMBL; AY692766; AAT92785.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12445.1; -; Genomic_DNA.
DR PIR; S56260; S56260.
DR RefSeq; NP_116660.1; NM_001179970.1.
DR PDB; 4MSX; X-ray; 1.87 A; A=1-448.
DR PDBsum; 4MSX; -.
DR AlphaFoldDB; P43589; -.
DR SMR; P43589; -.
DR BioGRID; 31153; 449.
DR ComplexPortal; CPX-25; U4/U6.U5 tri-small nuclear ribonucleoprotein complex.
DR STRING; 4932.YFR005C; -.
DR MEROPS; C19.972; -.
DR iPTMnet; P43589; -.
DR MaxQB; P43589; -.
DR PaxDb; P43589; -.
DR PRIDE; P43589; -.
DR EnsemblFungi; YFR005C_mRNA; YFR005C; YFR005C.
DR GeneID; 850555; -.
DR KEGG; sce:YFR005C; -.
DR SGD; S000001901; SAD1.
DR VEuPathDB; FungiDB:YFR005C; -.
DR eggNOG; KOG2026; Eukaryota.
DR GeneTree; ENSGT00940000176217; -.
DR HOGENOM; CLU_016848_2_1_1; -.
DR InParanoid; P43589; -.
DR OMA; CGKYLQG; -.
DR BioCyc; YEAST:G3O-30458-MON; -.
DR PRO; PR:P43589; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43589; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IC:ComplexPortal.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:SGD.
DR GO; GO:0000245; P:spliceosomal complex assembly; IDA:SGD.
DR CDD; cd02669; Peptidase_C19M; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR033809; USP39.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646:SF16; PTHR21646:SF16; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Metal-binding; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Ribonucleoprotein; Spliceosome; Zinc;
KW Zinc-finger.
FT CHAIN 1..448
FT /note="Pre-mRNA-splicing factor SAD1"
FT /id="PRO_0000202682"
FT DOMAIN 150..447
FT /note="USP"
FT ZN_FING 27..124
FT /note="UBP-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:4MSX"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:4MSX"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:4MSX"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4MSX"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:4MSX"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:4MSX"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:4MSX"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:4MSX"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:4MSX"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:4MSX"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:4MSX"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:4MSX"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:4MSX"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:4MSX"
FT HELIX 232..246
FT /evidence="ECO:0007829|PDB:4MSX"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 281..291
FT /evidence="ECO:0007829|PDB:4MSX"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:4MSX"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:4MSX"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:4MSX"
FT TURN 355..358
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 375..388
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 403..412
FT /evidence="ECO:0007829|PDB:4MSX"
FT TURN 413..416
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 425..429
FT /evidence="ECO:0007829|PDB:4MSX"
FT HELIX 431..436
FT /evidence="ECO:0007829|PDB:4MSX"
FT STRAND 437..446
FT /evidence="ECO:0007829|PDB:4MSX"
SQ SEQUENCE 448 AA; 52167 MW; D5D7C324E60AEC01 CRC64;
MEVDNKRRHS EDELKQEAVK KIKSQEPNYA YLETVVREKL DFDSEKICCI TLSPLNVYCC
LVCGHYYQGR HEKSPAFIHS IDENHHVFLN LTSLKFYMLP QNVQILHDGE VQLLNSIKFA
AYPTYCPKDL EDFPRQCFDL SNRTYLNGFI GFTNAATYDY AHSVLLLISH MVPVRDHFLL
NHFDNQGEFI KRLSICVKKI WSPKLFKHHL SVDDFVSYLK VREGLNLNPI DPRLFLLWLF
NKICSSSNDL KSILNHSCKG KVKIAKVENK PEASESVTGK VIVKPFWVLT LDLPEFSPFE
DGNSVDDLPQ INITKLLTKF TKSRSSSTST VFELTRLPQF LIFHFNRFDR NSDHPVKNRN
QTLVEFSSEL EILHVKYRLK ANVVHVVIKQ PSTDGNAFNG DEKSHWITQL YDNKSEKWIE
IDGINTTERE AELLFLKETF IQVWEKQE
