P46674 (SAC3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear mRNA export protein SAC3

Alternative name(s):
Leucine permease transcriptional regulator

Gene names

Name:	SAC3
Synonyms:	LEP1
Ordered Locus Names:	YDR159W
ORF Names:	YD8358.13

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1301 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the SAC3-THP1 complex, which functions in transcription-coupled mRNA export from the nucleus to the cytoplasm. SAC3-THP1 functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket. Ref.5 Ref.6
Subunit structure	Heterodimer with THP1. The SAC3-THP1 complex interacts with CDC31 and SUS1, and with the mRNA export factor MEX67-MTR2, the TREX complex component SUB2, and the nucleoporin NUP1. SAC3 directly interacts with MEX67, NUP1 and SUB2. Ref.5 Ref.9 Ref.10
Subcellular location	Nucleus envelope. Note: Localizes to the nuclear pores. Ref.5 Ref.7
Miscellaneous	Present with 339 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the SAC3 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Transport mRNA transport
Cellular component	Nucleus
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament-based process Inferred from genetic interaction PubMed 2656401. Source: SGD mRNA 3'-end processing Inferred from mutant phenotype PubMed 18614048. Source: SGD mRNA export from nucleus Inferred from mutant phenotype Ref.5PubMed 12631707. Source: SGD mitosis Inferred from mutant phenotype PubMed 8799844. Source: SGD nuclear retention of pre-mRNA at the site of transcription Inferred from mutant phenotype PubMed 18003937. Source: SGD posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery Inferred from mutant phenotype PubMed 18003937. Source: SGD protein export from nucleus Inferred from mutant phenotype PubMed 10716708. Source: SGD regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW ribosomal small subunit biogenesis Inferred from mutant phenotype PubMed 19806183. Source: SGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription-coupled nucleotide-excision repair Inferred from mutant phenotype PubMed 17537816. Source: SGD
Cellular_component	nuclear pore Inferred from direct assay PubMed 12631707. Source: SGD transcription export complex 2 Inferred from direct assay Ref.10. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC31	P06704	10	EBI-16425,EBI-4259
SUS1	Q6WNK7	13	EBI-16425,EBI-1251050
THP1	Q08231	9	EBI-16425,EBI-32097

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1301

1301

Nuclear mRNA export protein SAC3

PRO_0000097562

Regions

Region

1 – 572

572

Required for interaction with MEX67, SUB2 and THP1

Region

573 – 1301

729

Required for targeting SAC3 to the nuclear pore

Region

733 – 860

128

Interaction with CDC31

Amino acid modifications

Modified residue

600

1

Phosphoserine Ref.12

Modified residue

748

1

N6-acetyllysine Ref.9

Modified residue

866

1

Phosphoserine Ref.11 Ref.12

Modified residue

1180

1

Phosphothreonine Ref.12

Modified residue

1181

1

Phosphoserine Ref.12

Secondary structure

1

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1301

Helix Strand Turn

Details...

Helix

258 – 271

14

Helix

273 – 275

3

Turn

276 – 278

3

Helix

280 – 296

17

Helix

302 – 324

23

Helix

331 – 354

24

Helix

362 – 372

11

Helix

378 – 383

6

Helix

388 – 391

4

Helix

394 – 406

13

Helix

426 – 433

8

Helix

440 – 446

7

Helix

447 – 449

3

Helix

450 – 464

15

Helix

474 – 480

7

Helix

486 – 495

10

Turn

502 – 504

3

Helix

508 – 510

3

Beta strand

514 – 517

4

Helix

530 – 537

8

Helix

541 – 545

5

Helix

753 – 803

51

Sequences

	Sequence		Length	Mass (Da)
	P46674 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 0679DB1673DDACEB	FASTA	1,301	149,569
	10 20 30 40 50 60 MNTSFGSVVP STNFNFFKGH GNNDNTSANS TVNNSNFFLN SNETKPSKNV FMVHSTSQKK 70 80 90 100 110 120 SQQPLQNLSH SPSYTENKPD KKKKYMINDA KTIQLVGPLI SSPDNLGFQK RSHKARELPR 130 140 150 160 170 180 FLINQEPQLE KRAFVQDPWD KANQEKMISL EESIDDLNEL YETLKKMRNT ERSIMEEKGL 190 200 210 220 230 240 VDKADSAKDL YDAIVFQGTC LDMCPTFERS RRNVEYTVYS YEKNQPNDKK ASRTKALKVF 250 260 270 280 290 300 ARPAAAAAPP LPSDVRPPHI LVKTLDYIVD NLLTTLPESE GFLWDRMRSI RQDFTYQNYS 310 320 330 340 350 360 GPEAVDCNER IVRIHLLILH IMVKSNVEFS LQQELEQLHK SLITLSEIYD DVRSSGGTCP 370 380 390 400 410 420 NEAEFRAYAL LSKIRDPQYD ENIQRLPKHI FQDKLVQMAL CFRRVISNSA YTERGFVKTE 430 440 450 460 470 480 NCLNFYARFF QLMQSPSLPL LMGFFLQMHL TDIRFYALRA LSHTLNKKHK PIPFIYLENM 490 500 510 520 530 540 LLFNNRQEII EFCNYYSIEI INGDAADLKT LQHYSHKLSE TQPLKKTYLT CLERRLQKTT 550 560 570 580 590 600 YKGLINGGED NLASSVYVKD PKKDRIPSIA DQSFLMENFQ NNYNEKLNQN SSVKPQINTS 610 620 630 640 650 660 PKRVATRPNH FPFSQESKQL PQISQSHTLS TNPLLTPQVH GDLSEQKQQQ IKTVTDGGSP 670 680 690 700 710 720 FVFDQSAQNS TVEASKAHMI STTSNGAYDE KLSSEQEEMR KKEEQRIEEE KTQLKKKQEN 730 740 750 760 770 780 ADKQVITEQI ANDLVKEVVN SSVISIVKRE FSEANYRKDF IDTMTRELYD AFLHERLYLI 790 800 810 820 830 840 YMDSRAELKR NSTLKKKFFE KWQASYSQAK KNRILEEKKR EEIKLVSHQL GVPGFKKSTC 850 860 870 880 890 900 LFRTPYKGNV NSSFMLSSSD KNLIFSPVND EFNKFATHLT KISKLWRPLE MQSIYYDNLT 910 920 930 940 950 960 KKFPSNSLTP ANLFIYAKDW TSLSNRWILS KFNLQTAQDS KKFSNNIISS RIICIDDEYE 970 980 990 1000 1010 1020 PSDFSDLQLL IFNTGVTNPD IFDLEMKLKD DGEELIKLIT GISLNTNICF SLLIIYWESA 1030 1040 1050 1060 1070 1080 ENTLSESTIK HLLKLNRISK NYSSVIERID LMNLTEESPH KCLEDKLSEI SHSYVYKLTE 1090 1100 1110 1120 1130 1140 RGKYDKTLRQ KRSLAGIHSR STQLQTTKDI DQKMKKMLEK EKNKYQQQIG ERNTYAHLES 1150 1160 1170 1180 1190 1200 HIDASPRSKK RKLPILLSTS HSSQFKTPLA SRLNTSGSST SPPLPSHLAM KFRKNSRVTS 1210 1220 1230 1240 1250 1260 LHTVLPVSTP SHSNNIPAAS FSGNNTTDIQ SQQLIENQKS TSVYLNNVSE RILGNQEICQ 1270 1280 1290 1300 TPINPVTPVL DGADQGKEDI PDSILELKIL IDSVKKKVNN D

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the SAC3 gene of Saccharomyces cerevisiae." Bauer A., Koelling R. Yeast 12:965-975(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"The Saccharomyces cerevisiae LEP1/SAC3 gene is associated with leucine transport." Stella C.A., Korch C., Ramos E.H., Bauer A., Koelling R., Mattoon J.R. Mol. Gen. Genet. 262:332-341(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 189-1301. Strain: DBY939.
[5]	"The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores." Fischer T., Straesser K., Racz A., Rodriguez-Navarro S., Oppizzi M., Ihrig P., Lechner J., Hurt E. EMBO J. 21:5843-5852(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MEX67, NUP1, SUB2 AND THP1, SUBCELLULAR LOCATION.
[6]	"Nab2p and the Thp1p-Sac3p complex functionally interact at the interface between transcription and mRNA metabolism." Gallardo M., Luna R., Erdjument-Bromage H., Tempst P., Aguilera A. J. Biol. Chem. 278:24225-24232(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery." Rodriguez-Navarro S., Fischer T., Luo M.-J., Antunez O., Brettschneider S., Lechner J., Perez-Ortin J.E., Reed R., Hurt E.C. Cell 116:75-86(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SUS1, ACETYLATION AT LYS-748.
[10]	"Yeast centrin Cdc31 is linked to the nuclear mRNA export machinery." Fischer T., Rodriguez-Navarro S., Pereira G., Racz A., Schiebel E., Hurt E.C. Nat. Cell Biol. 6:840-848(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CDC31.
[11]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-866, MASS SPECTROMETRY. Strain: ADR376.
[12]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-866; THR-1180 AND SER-1181, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z47805 Genomic DNA. Translation: CAA87767.1.
Z50046 Genomic DNA. Translation: CAA90379.1.
U35227 Genomic DNA. Translation: AAA79056.1.
BK006938 Genomic DNA. Translation: DAA11999.1.

PIR

S51323.

RefSeq

NP_010443.3. NM_001180466.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FWB	X-ray	2.50	B	752-805	[»]
3FWC	X-ray	2.70	B/F/J/N	723-805	[»]
3T5V	X-ray	2.90	A/D	250-563	[»]

ProteinModelPortal

P46674.

SMR

P46674. Positions 252-550, 723-805.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2444N.

IntAct

P46674. 13 interactions.

MINT

MINT-596858.

STRING

4932.YDR159W.

Proteomic databases

PaxDb

P46674.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR159W; YDR159W; YDR159W.

GeneID

851737.

KEGG

sce:YDR159W.
sce:YDR163W.

Organism-specific databases

CYGD

YDR159w.

SGD

S000002566. SAC3.

Phylogenomic databases

eggNOG

COG5079.

GeneTree

ENSGT00530000063781.

HOGENOM

HOG000065955.

KO

K12863.

OMA

WDRMRSI.

OrthoDB

EOG49GPR5.

Gene expression databases

Genevestigator

P46674.

GermOnline

YDR159W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR017173. mRNA_export_fac_Sac3.
IPR005062. SAC3/GANP/Nin1/mts3/eIF-3-p25.
IPR024293. SAC3_helical.
[Graphical view]

Pfam

PF12209. SAC3. 1 hit.
PF03399. SAC3_GANP. 1 hit.
[Graphical view]

PIRSF

PIRSF037320. mRNA_export_factor_Sac3. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P46674.

NextBio

969466.

Entry information

Entry name

SAC3_YEAST

Accession

Primary (citable) accession number: P46674
Secondary accession number(s): D6VSD9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program