SAC3_YEAST
ID SAC3_YEAST Reviewed; 1301 AA.
AC P46674; D6VSD9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Nuclear mRNA export protein SAC3;
DE AltName: Full=Leucine permease transcriptional regulator;
GN Name=SAC3; Synonyms=LEP1; OrderedLocusNames=YDR159W; ORFNames=YD8358.13;
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].
RX PubMed=8873450;
RX DOI=10.1002/(sici)1097-0061(199608)12:10<965::aid-yea999>3.0.co;2-q;
RA Bauer A., Koelling R.;
RT "Characterization of the SAC3 gene of Saccharomyces cerevisiae.";
RL Yeast 12:965-975(1996).
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 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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 189-1301.
RC STRAIN=DBY939;
RX PubMed=10517330; DOI=10.1007/s004380051091;
RA Stella C.A., Korch C., Ramos E.H., Bauer A., Koelling R., Mattoon J.R.;
RT "The Saccharomyces cerevisiae LEP1/SAC3 gene is associated with leucine
RT transport.";
RL Mol. Gen. Genet. 262:332-341(1999).
RN [5]
RP FUNCTION, INTERACTION WITH MEX67, NUP1, SUB2 AND THP1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12411502; DOI=10.1093/emboj/cdf590;
RA Fischer T., Straesser K., Racz A., Rodriguez-Navarro S., Oppizzi M.,
RA Ihrig P., Lechner J., Hurt E.;
RT "The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock
RT at the nucleoplasmic entrance of the nuclear pores.";
RL EMBO J. 21:5843-5852(2002).
RN [6]
RP FUNCTION.
RX PubMed=12702719; DOI=10.1074/jbc.m302900200;
RA Gallardo M., Luna R., Erdjument-Bromage H., Tempst P., Aguilera A.;
RT "Nab2p and the Thp1p-Sac3p complex functionally interact at the interface
RT between transcription and mRNA metabolism.";
RL J. Biol. Chem. 278:24225-24232(2003).
RN [7]
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 [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 INTERACTION WITH SUS1, AND ACETYLATION AT LYS-748.
RX PubMed=14718168; DOI=10.1016/s0092-8674(03)01025-0;
RA Rodriguez-Navarro S., Fischer T., Luo M.-J., Antunez O., Brettschneider S.,
RA Lechner J., Perez-Ortin J.E., Reed R., Hurt E.C.;
RT "Sus1, a functional component of the SAGA histone acetylase complex and the
RT nuclear pore-associated mRNA export machinery.";
RL Cell 116:75-86(2004).
RN [10]
RP INTERACTION WITH CDC31.
RX PubMed=15311284; DOI=10.1038/ncb1163;
RA Fischer T., Rodriguez-Navarro S., Pereira G., Racz A., Schiebel E.,
RA Hurt E.C.;
RT "Yeast centrin Cdc31 is linked to the nuclear mRNA export machinery.";
RL Nat. Cell Biol. 6:840-848(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-866, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-866, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568 AND SER-866, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Component of the SAC3-THP1 complex, which functions in
CC transcription-coupled mRNA export from the nucleus to the cytoplasm.
CC SAC3-THP1 functions in docking export-competent ribonucleoprotein
CC particles (mRNPs) to the nuclear entrance of the nuclear pore complex
CC (nuclear basket), by association with components of the nuclear mRNA
CC export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the
CC nucleoporin NUP1 at the nuclear basket. {ECO:0000269|PubMed:12411502,
CC ECO:0000269|PubMed:12702719}.
CC -!- SUBUNIT: Heterodimer with THP1. The SAC3-THP1 complex interacts with
CC CDC31 and SUS1, and with the mRNA export factor MEX67-MTR2, the TREX
CC complex component SUB2, and the nucleoporin NUP1. SAC3 directly
CC interacts with MEX67, NUP1 and SUB2. {ECO:0000269|PubMed:12411502,
CC ECO:0000269|PubMed:14718168, ECO:0000269|PubMed:15311284}.
CC -!- INTERACTION:
CC P46674; P06704: CDC31; NbExp=10; IntAct=EBI-16425, EBI-4259;
CC P46674; Q6WNK7: SUS1; NbExp=11; IntAct=EBI-16425, EBI-1251050;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:12411502,
CC ECO:0000269|PubMed:14562095}. Note=Localizes to the nuclear pores.
CC -!- MISCELLANEOUS: Present with 339 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SAC3 family. {ECO:0000305}.
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DR EMBL; Z47805; CAA87767.1; -; Genomic_DNA.
DR EMBL; Z50046; CAA90379.1; -; Genomic_DNA.
DR EMBL; U35227; AAA79056.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11999.1; -; Genomic_DNA.
DR PIR; S51323; S51323.
DR RefSeq; NP_010443.3; NM_001180466.3.
DR PDB; 3FWB; X-ray; 2.50 A; B=752-805.
DR PDB; 3FWC; X-ray; 2.70 A; B/F/J/N=723-805.
DR PDB; 3T5V; X-ray; 2.90 A; A/D=250-563.
DR PDB; 4C31; X-ray; 3.00 A; A/D=757-787.
DR PDB; 4MBE; X-ray; 2.61 A; B/E=753-805.
DR PDB; 4TRQ; X-ray; 3.10 A; A/D=253-551.
DR PDB; 5G5P; EM; 5.30 A; A=1-805.
DR PDB; 5L3T; X-ray; 4.93 A; A=1-1301.
DR PDBsum; 3FWB; -.
DR PDBsum; 3FWC; -.
DR PDBsum; 3T5V; -.
DR PDBsum; 4C31; -.
DR PDBsum; 4MBE; -.
DR PDBsum; 4TRQ; -.
DR PDBsum; 5G5P; -.
DR PDBsum; 5L3T; -.
DR AlphaFoldDB; P46674; -.
DR SMR; P46674; -.
DR BioGRID; 32210; 918.
DR ComplexPortal; CPX-1686; TREX-2 transcription-export complex.
DR ComplexPortal; CPX-1687; Thp1-Sac3 complex.
DR DIP; DIP-2444N; -.
DR IntAct; P46674; 14.
DR MINT; P46674; -.
DR STRING; 4932.YDR159W; -.
DR TCDB; 3.A.22.1.1; the transcription-coupled trex/tap nuclear mrna export complex (trex) family.
DR iPTMnet; P46674; -.
DR MaxQB; P46674; -.
DR PaxDb; P46674; -.
DR PRIDE; P46674; -.
DR EnsemblFungi; YDR159W_mRNA; YDR159W; YDR159W.
DR GeneID; 851737; -.
DR KEGG; sce:YDR159W; -.
DR SGD; S000002566; SAC3.
DR VEuPathDB; FungiDB:YDR159W; -.
DR eggNOG; KOG1860; Eukaryota.
DR GeneTree; ENSGT00940000160988; -.
DR HOGENOM; CLU_006094_0_0_1; -.
DR InParanoid; P46674; -.
DR OMA; FQGTCLD; -.
DR BioCyc; YEAST:G3O-29749-MON; -.
DR EvolutionaryTrace; P46674; -.
DR PRO; PR:P46674; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P46674; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0070390; C:transcription export complex 2; IDA:SGD.
DR GO; GO:0030029; P:actin filament-based process; IGI:SGD.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:SGD.
DR GO; GO:0031124; P:mRNA 3'-end processing; IMP:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR GO; GO:0006611; P:protein export from nucleus; IMP:SGD.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:SGD.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:SGD.
DR DisProt; DP02481; -.
DR IDEAL; IID50280; -.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR017173; Sac3.
DR InterPro; IPR045107; SAC3/GANP/THP3.
DR InterPro; IPR005062; SAC3/GANP/THP3_conserved.
DR InterPro; IPR024293; SAC3_helical.
DR PANTHER; PTHR12436; PTHR12436; 1.
DR Pfam; PF12209; SAC3; 1.
DR Pfam; PF03399; SAC3_GANP; 1.
DR PIRSF; PIRSF037320; mRNA_export_factor_Sac3; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; mRNA transport; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Transport.
FT CHAIN 1..1301
FT /note="Nuclear mRNA export protein SAC3"
FT /id="PRO_0000097562"
FT DOMAIN 333..524
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..572
FT /note="Required for interaction with MEX67, SUB2 and THP1"
FT /evidence="ECO:0000269|PubMed:12411502"
FT REGION 54..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..1301
FT /note="Required for targeting SAC3 to the nuclear pore"
FT REGION 689..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..860
FT /note="Interaction with CDC31"
FT /evidence="ECO:0000269|PubMed:15311284"
FT REGION 1164..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 748
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:14718168"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT HELIX 258..271
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:3T5V"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 280..296
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 302..324
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 331..354
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 362..372
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 378..383
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 394..406
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 426..433
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 440..446
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 450..464
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 474..480
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 486..495
FT /evidence="ECO:0007829|PDB:3T5V"
FT TURN 502..504
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:3T5V"
FT STRAND 514..517
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 530..537
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 541..545
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 753..803
FT /evidence="ECO:0007829|PDB:3FWB"
SQ SEQUENCE 1301 AA; 149569 MW; 0679DB1673DDACEB CRC64;
MNTSFGSVVP STNFNFFKGH GNNDNTSANS TVNNSNFFLN SNETKPSKNV FMVHSTSQKK
SQQPLQNLSH SPSYTENKPD KKKKYMINDA KTIQLVGPLI SSPDNLGFQK RSHKARELPR
FLINQEPQLE KRAFVQDPWD KANQEKMISL EESIDDLNEL YETLKKMRNT ERSIMEEKGL
VDKADSAKDL YDAIVFQGTC LDMCPTFERS RRNVEYTVYS YEKNQPNDKK ASRTKALKVF
ARPAAAAAPP LPSDVRPPHI LVKTLDYIVD NLLTTLPESE GFLWDRMRSI RQDFTYQNYS
GPEAVDCNER IVRIHLLILH IMVKSNVEFS LQQELEQLHK SLITLSEIYD DVRSSGGTCP
NEAEFRAYAL LSKIRDPQYD ENIQRLPKHI FQDKLVQMAL CFRRVISNSA YTERGFVKTE
NCLNFYARFF QLMQSPSLPL LMGFFLQMHL TDIRFYALRA LSHTLNKKHK PIPFIYLENM
LLFNNRQEII EFCNYYSIEI INGDAADLKT LQHYSHKLSE TQPLKKTYLT CLERRLQKTT
YKGLINGGED NLASSVYVKD PKKDRIPSIA DQSFLMENFQ NNYNEKLNQN SSVKPQINTS
PKRVATRPNH FPFSQESKQL PQISQSHTLS TNPLLTPQVH GDLSEQKQQQ IKTVTDGGSP
FVFDQSAQNS TVEASKAHMI STTSNGAYDE KLSSEQEEMR KKEEQRIEEE KTQLKKKQEN
ADKQVITEQI ANDLVKEVVN SSVISIVKRE FSEANYRKDF IDTMTRELYD AFLHERLYLI
YMDSRAELKR NSTLKKKFFE KWQASYSQAK KNRILEEKKR EEIKLVSHQL GVPGFKKSTC
LFRTPYKGNV NSSFMLSSSD KNLIFSPVND EFNKFATHLT KISKLWRPLE MQSIYYDNLT
KKFPSNSLTP ANLFIYAKDW TSLSNRWILS KFNLQTAQDS KKFSNNIISS RIICIDDEYE
PSDFSDLQLL IFNTGVTNPD IFDLEMKLKD DGEELIKLIT GISLNTNICF SLLIIYWESA
ENTLSESTIK HLLKLNRISK NYSSVIERID LMNLTEESPH KCLEDKLSEI SHSYVYKLTE
RGKYDKTLRQ KRSLAGIHSR STQLQTTKDI DQKMKKMLEK EKNKYQQQIG ERNTYAHLES
HIDASPRSKK RKLPILLSTS HSSQFKTPLA SRLNTSGSST SPPLPSHLAM KFRKNSRVTS
LHTVLPVSTP SHSNNIPAAS FSGNNTTDIQ SQQLIENQKS TSVYLNNVSE RILGNQEICQ
TPINPVTPVL DGADQGKEDI PDSILELKIL IDSVKKKVNN D
