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   27-MAR-2024, entry version 170.
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; 454.
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; 4932-YFR005C; -.
DR   PeptideAtlas; P43589; -.
DR   EnsemblFungi; YFR005C_mRNA; YFR005C; YFR005C.
DR   GeneID; 850555; -.
DR   KEGG; sce:YFR005C; -.
DR   AGR; SGD:S000001901; -.
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; LNVYCCL; -.
DR   OrthoDB; 719409at2759; -.
DR   BioCyc; YEAST:G3O-30458-MONOMER; -.
DR   BioGRID-ORCS; 850555; 1 hit in 10 CRISPR screens.
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; NAS:ComplexPortal.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; NAS:ComplexPortal.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
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; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
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; U4_U6.U5 TRI-SNRNP-ASSOCIATED PROTEIN 2; 1.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 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
//