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Protein

Phosphoinositide phosphatase SAC1

Gene

SAC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Phosphoinositide phosphatase that hydrolyzes PtdIns3P and PtdIns4P. Has low activity towards PtdIns(3,5)P2. May be involved in the coordination of the activities of the secretory pathway and the actin cytoskeleton.2 Publications

GO - Molecular functioni

  • phosphatase activity Source: SGD
  • phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity Source: SGD
  • phosphatidylinositol-3-phosphatase activity Source: SGD
  • phosphatidylinositol-4-phosphate phosphatase activity Source: SGD

GO - Biological processi

  • phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  • phosphatidylinositol dephosphorylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15189.
YEAST:G3O-31970-MONOMER.
YEAST:MONOMER3O-55.
ReactomeiR-SCE-1483248. Synthesis of PIPs at the ER membrane.
R-SCE-1660514. Synthesis of PIPs at the Golgi membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoinositide phosphatase SAC1 (EC:3.1.3.-)
Alternative name(s):
Recessive suppressor of secretory defect
Gene namesi
Name:SAC1
Synonyms:RSD1
Ordered Locus Names:YKL212W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL212W.
SGDiS000001695. SAC1.

Subcellular locationi

  • Endoplasmic reticulum membrane 1 Publication; Single-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 521521ExtracellularSequence analysisAdd
BLAST
Transmembranei522 – 54423HelicalSequence analysisAdd
BLAST
Topological domaini545 – 62379CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • Golgi medial cisterna Source: SGD
  • integral component of endoplasmic reticulum membrane Source: SGD
  • integral component of Golgi membrane Source: SGD
  • SPOTS complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 623623Phosphoinositide phosphatase SAC1PRO_0000209737Add
BLAST

Proteomic databases

MaxQBiP32368.
PeptideAtlasiP32368.

Interactioni

Subunit structurei

Component of the SPOTS complex, at least composed of LCB1/2 (LCB1 and/or LCB2), ORM1/2 (ORM1 and/or ORM2), SAC1 and TSC3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
OSH3P387132EBI-16210,EBI-12630

Protein-protein interaction databases

BioGridi33953. 616 interactions.
DIPiDIP-6610N.
IntActiP32368. 20 interactions.
MINTiMINT-1355209.

Structurei

Secondary structure

1
623
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Beta strandi13 – 208Combined sources
Beta strandi28 – 325Combined sources
Turni33 – 353Combined sources
Beta strandi38 – 414Combined sources
Helixi43 – 453Combined sources
Beta strandi48 – 503Combined sources
Beta strandi53 – 6412Combined sources
Beta strandi67 – 8216Combined sources
Beta strandi85 – 9814Combined sources
Turni101 – 1033Combined sources
Helixi106 – 12116Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi128 – 1303Combined sources
Helixi136 – 1427Combined sources
Helixi148 – 1503Combined sources
Turni153 – 1553Combined sources
Turni157 – 1593Combined sources
Helixi160 – 1623Combined sources
Helixi163 – 1697Combined sources
Helixi173 – 1786Combined sources
Beta strandi183 – 19412Combined sources
Beta strandi197 – 20711Combined sources
Beta strandi213 – 2153Combined sources
Beta strandi218 – 2214Combined sources
Beta strandi230 – 24011Combined sources
Turni242 – 2443Combined sources
Beta strandi247 – 25711Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi269 – 2713Combined sources
Helixi279 – 29618Combined sources
Beta strandi297 – 3048Combined sources
Helixi313 – 32513Combined sources
Beta strandi330 – 3356Combined sources
Turni341 – 3433Combined sources
Helixi344 – 35916Combined sources
Beta strandi366 – 3716Combined sources
Beta strandi377 – 3826Combined sources
Beta strandi386 – 3916Combined sources
Helixi396 – 41722Combined sources
Helixi427 – 4293Combined sources
Helixi431 – 44818Combined sources
Turni449 – 4513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LWTX-ray1.96X1-504[»]
4TU3X-ray3.19X1-623[»]
ProteinModelPortaliP32368.
SMRiP32368. Positions 1-456.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32368.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini115 – 454340SACPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi507 – 52115Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 SAC domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000063393.
HOGENOMiHOG000189112.
InParanoidiP32368.
OMAiNSITRYC.
OrthoDBiEOG7DRJBN.

Family and domain databases

InterProiIPR002013. SAC_dom.
[Graphical view]
PfamiPF02383. Syja_N. 1 hit.
[Graphical view]
PROSITEiPS50275. SAC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32368-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGPIVYVQN ADGIFFKLAE GKGTNDAVIH LANQDQGVRV LGAEEFPVQG
60 70 80 90 100
EVVKIASLMG FIKLKLNRYA IIANTVEETG RFNGHVFYRV LQHSIVSTKF
110 120 130 140 150
NSRIDSEEAE YIKLLELHLK NSTFYFSYTY DLTNSLQRNE KVGPAASWKT
160 170 180 190 200
ADERFFWNHY LTEDLRNFAH QDPRIDSFIQ PVIYGYAKTV DAVLNATPIV
210 220 230 240 250
LGLITRRSIF RAGTRYFRRG VDKDGNVGNF NETEQILLAE NPESEKIHVF
260 270 280 290 300
SFLQTRGSVP IYWAEINNLK YKPNLVLGEN SLDATKKHFD QQKELYGDNY
310 320 330 340 350
LVNLVNQKGH ELPVKEGYES VVHALNDPKI HYVYFDFHHE CRKMQWHRVK
360 370 380 390 400
LLIDHLEKLG LSNEDFFHKV IDSNGNTVEI VNEQHSVVRT NCMDCLDRTN
410 420 430 440 450
VVQSVLAQWV LQKEFESADV VATGSTWEDN APLLTSYQNL WADNADAVSV
460 470 480 490 500
AYSGTGALKT DFTRTGKRTR LGAFNDFLNS ASRYYQNNWT DGPRQDSYDL
510 520 530 540 550
FLGGFRPHTA SIKSPFPDRR PVYIQLIPMI ICAALTVLGA TIFFPKDRFT
560 570 580 590 600
SSKNLLYFAG ASIVLALSTK FMFKNGIQFV NWPKLVDVGF LVVHQTHDKE
610 620
QQFKGLKYAQ SPKFSKPDPL KRD
Length:623
Mass (Da):71,125
Last modified:October 1, 1993 - v1
Checksum:i73DB1FA163BC17AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51672 Genomic DNA. Translation: CAA35979.1.
X75951 Genomic DNA. Translation: CAA53561.1.
Z28212 Genomic DNA. Translation: CAA82057.1.
U39947 Genomic DNA. Translation: AAA82257.1.
BK006944 Genomic DNA. Translation: DAA08957.1.
PIRiA33622.
RefSeqiNP_012710.1. NM_001179777.1.

Genome annotation databases

EnsemblFungiiYKL212W; YKL212W; YKL212W.
GeneIDi853668.
KEGGisce:YKL212W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51672 Genomic DNA. Translation: CAA35979.1.
X75951 Genomic DNA. Translation: CAA53561.1.
Z28212 Genomic DNA. Translation: CAA82057.1.
U39947 Genomic DNA. Translation: AAA82257.1.
BK006944 Genomic DNA. Translation: DAA08957.1.
PIRiA33622.
RefSeqiNP_012710.1. NM_001179777.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LWTX-ray1.96X1-504[»]
4TU3X-ray3.19X1-623[»]
ProteinModelPortaliP32368.
SMRiP32368. Positions 1-456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33953. 616 interactions.
DIPiDIP-6610N.
IntActiP32368. 20 interactions.
MINTiMINT-1355209.

Proteomic databases

MaxQBiP32368.
PeptideAtlasiP32368.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL212W; YKL212W; YKL212W.
GeneIDi853668.
KEGGisce:YKL212W.

Organism-specific databases

EuPathDBiFungiDB:YKL212W.
SGDiS000001695. SAC1.

Phylogenomic databases

GeneTreeiENSGT00530000063393.
HOGENOMiHOG000189112.
InParanoidiP32368.
OMAiNSITRYC.
OrthoDBiEOG7DRJBN.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15189.
YEAST:G3O-31970-MONOMER.
YEAST:MONOMER3O-55.
ReactomeiR-SCE-1483248. Synthesis of PIPs at the ER membrane.
R-SCE-1660514. Synthesis of PIPs at the Golgi membrane.

Miscellaneous databases

EvolutionaryTraceiP32368.
NextBioi974608.
PROiP32368.

Family and domain databases

InterProiIPR002013. SAC_dom.
[Graphical view]
PfamiPF02383. Syja_N. 1 hit.
[Graphical view]
PROSITEiPS50275. SAC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mutations in the SAC1 gene suppress defects in yeast Golgi and yeast actin function."
    Cleves A.E., Novick P.J., Bankaitis V.A.
    J. Cell Biol. 109:2939-2950(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete sequencing of a 24.6 kb segment of yeast chromosome XI identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open reading frames including homologues to the threonine dehydratases, membrane transporters, hydantoinases and the phospholipase A2-activating protein."
    Tzermia M., Horaitis O., Alexandraki D.
    Yeast 10:663-679(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Hochstrasser M., Gang G.
    Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-145.
  6. "SAC1 encodes a regulated lipid phosphoinositide phosphatase, defects in which can be suppressed by the homologous Inp52p and Inp53p phosphatases."
    Hughes W.E., Woscholski R., Cooke F.T., Patrick R.S., Dove S.K., McDonald N.Q., Parker P.J.
    J. Biol. Chem. 275:801-808(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Sac1 lipid phosphatase and Stt4 phosphatidylinositol 4-kinase regulate a pool of phosphatidylinositol 4-phosphate that functions in the control of the actin cytoskeleton and vacuole morphology."
    Foti M., Audhya A., Emr S.D.
    Mol. Biol. Cell 12:2396-2411(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  10. Cited for: IDENTIFICATION IN THE SPOTS COMPLEX.
  11. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSAC1_YEAST
AccessioniPrimary (citable) accession number: P32368
Secondary accession number(s): D6VWZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 11, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 48000 molecules/cell in log phase SD medium.1 Publication

Caution

It is uncertain whether Met-1 or Met-59 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.