SAC1_YEAST
ID SAC1_YEAST Reviewed; 623 AA.
AC P32368; D6VWZ1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Phosphatidylinositol-3-phosphatase SAC1;
DE EC=3.1.3.64 {ECO:0000269|PubMed:10625610};
DE AltName: Full=Phosphatidylinositol-4-phosphate phosphatase {ECO:0000303|PubMed:11792713};
DE AltName: Full=Recessive suppressor of secretory defect;
GN Name=SAC1; Synonyms=RSD1; OrderedLocusNames=YKL212W;
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=2687291; DOI=10.1083/jcb.109.6.2939;
RA Cleves A.E., Novick P.J., Bankaitis V.A.;
RT "Mutations in the SAC1 gene suppress defects in yeast Golgi and yeast actin
RT function.";
RL J. Cell Biol. 109:2939-2950(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7941750; DOI=10.1002/yea.320100511;
RA Tzermia M., Horaitis O., Alexandraki D.;
RT "The complete sequencing of a 24.6 kb segment of yeast chromosome XI
RT identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open
RT reading frames including homologues to the threonine dehydratases, membrane
RT transporters, hydantoinases and the phospholipase A2-activating protein.";
RL Yeast 10:663-679(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-145.
RA Hochstrasser M., Gang G.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=8314848; DOI=10.1083/jcb.122.1.79;
RA Whitters E.A., Cleves A.E., McGee T.P., Skinner H.B., Bankaitis V.A.;
RT "SAC1p is an integral membrane protein that influences the cellular
RT requirement for phospholipid transfer protein function and inositol in
RT yeast.";
RL J. Cell Biol. 122:79-94(1993).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10625610; DOI=10.1074/jbc.275.2.801;
RA Hughes W.E., Woscholski R., Cooke F.T., Patrick R.S., Dove S.K.,
RA McDonald N.Q., Parker P.J.;
RT "SAC1 encodes a regulated lipid phosphoinositide phosphatase, defects in
RT which can be suppressed by the homologous Inp52p and Inp53p phosphatases.";
RL J. Biol. Chem. 275:801-808(2000).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11514624; DOI=10.1091/mbc.12.8.2396;
RA Foti M., Audhya A., Emr S.D.;
RT "Sac1 lipid phosphatase and Stt4 phosphatidylinositol 4-kinase regulate a
RT pool of phosphatidylinositol 4-phosphate that functions in the control of
RT the actin cytoskeleton and vacuole morphology.";
RL Mol. Biol. Cell 12:2396-2411(2001).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=11792713; DOI=10.1074/jbc.m200090200;
RA Konrad G., Schlecker T., Faulhammer F., Mayinger P.;
RT "Retention of the yeast Sac1p phosphatase in the endoplasmic reticulum
RT causes distinct changes in cellular phosphoinositide levels and stimulates
RT microsomal ATP transport.";
RL J. Biol. Chem. 277:10547-10554(2002).
RN [10]
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 [11]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [12]
RP IDENTIFICATION IN THE SPOTS COMPLEX.
RX PubMed=20182505; DOI=10.1038/nature08787;
RA Breslow D.K., Collins S.R., Bodenmiller B., Aebersold R., Simons K.,
RA Shevchenko A., Ejsing C.S., Weissman J.S.;
RT "Orm family proteins mediate sphingolipid homeostasis.";
RL Nature 463:1048-1053(2010).
RN [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-246 AND LYS-358, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Phosphoinositide phosphatase which catalyzes the hydrolysis
CC of phosphatidylinositol 3-phosphate (PtdIns(3)P) and
CC phosphatidylinositol 4-phosphate (PtdIns(4)P) (PubMed:10625610,
CC PubMed:11792713). Has low activity towards phosphatidylinositol-3,5-
CC bisphosphate (PtdIns(3,5)P2) (PubMed:10625610). May be involved in the
CC coordination of the activities of the secretory pathway and the actin
CC cytoskeleton (PubMed:11514624). {ECO:0000269|PubMed:10625610,
CC ECO:0000269|PubMed:11514624, ECO:0000269|PubMed:11792713}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64;
CC Evidence={ECO:0000269|PubMed:10625610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12317;
CC Evidence={ECO:0000305|PubMed:10625610};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:55652, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58178;
CC Evidence={ECO:0000269|PubMed:10625610, ECO:0000269|PubMed:11792713};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55653;
CC Evidence={ECO:0000305|PubMed:10625610};
CC -!- SUBUNIT: Component of the SPOTS complex, at least composed of LCB1/2
CC (LCB1 and/or LCB2), ORM1/2 (ORM1 and/or ORM2), SAC1 and TSC3.
CC {ECO:0000269|PubMed:20182505}.
CC -!- INTERACTION:
CC P32368; P38713: OSH3; NbExp=2; IntAct=EBI-16210, EBI-12630;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11514624, ECO:0000269|PubMed:11792713,
CC ECO:0000269|PubMed:8314848}; Multi-pass membrane protein {ECO:0000255}.
CC Golgi apparatus membrane {ECO:0000269|PubMed:8314848}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Present with 48000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-59 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X51672; CAA35979.1; -; Genomic_DNA.
DR EMBL; X75951; CAA53561.1; -; Genomic_DNA.
DR EMBL; Z28212; CAA82057.1; -; Genomic_DNA.
DR EMBL; U39947; AAA82257.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08957.1; -; Genomic_DNA.
DR PIR; A33622; A33622.
DR RefSeq; NP_012710.1; NM_001179777.1.
DR PDB; 3LWT; X-ray; 1.96 A; X=1-504.
DR PDB; 4TU3; X-ray; 3.19 A; X=1-623.
DR PDBsum; 3LWT; -.
DR PDBsum; 4TU3; -.
DR AlphaFoldDB; P32368; -.
DR SMR; P32368; -.
DR BioGRID; 33953; 1079.
DR ComplexPortal; CPX-3158; SPOTS complex.
DR DIP; DIP-6610N; -.
DR IntAct; P32368; 24.
DR MINT; P32368; -.
DR STRING; 4932.YKL212W; -.
DR SwissLipids; SLP:000001848; -.
DR iPTMnet; P32368; -.
DR MaxQB; P32368; -.
DR PaxDb; P32368; -.
DR PRIDE; P32368; -.
DR EnsemblFungi; YKL212W_mRNA; YKL212W; YKL212W.
DR GeneID; 853668; -.
DR KEGG; sce:YKL212W; -.
DR SGD; S000001695; SAC1.
DR VEuPathDB; FungiDB:YKL212W; -.
DR eggNOG; KOG1889; Eukaryota.
DR GeneTree; ENSGT00940000155579; -.
DR HOGENOM; CLU_003016_7_4_1; -.
DR InParanoid; P32368; -.
DR OMA; FRDINVH; -.
DR BioCyc; MetaCyc:G3O-31970-MON; -.
DR BioCyc; YEAST:G3O-31970-MON; -.
DR Reactome; R-SCE-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-SCE-1660514; Synthesis of PIPs at the Golgi membrane.
DR EvolutionaryTrace; P32368; -.
DR PRO; PR:P32368; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P32368; protein.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005797; C:Golgi medial cisterna; IDA:SGD.
DR GO; GO:0072517; C:host cell viral assembly compartment; IMP:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0035339; C:SPOTS complex; IDA:UniProtKB.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IDA:SGD.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IDA:SGD.
DR GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0090156; P:cellular sphingolipid homeostasis; IC:ComplexPortal.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:SGD.
DR InterPro; IPR002013; SAC_dom.
DR Pfam; PF02383; Syja_N; 1.
DR PROSITE; PS50275; SAC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Golgi apparatus; Hydrolase;
KW Isopeptide bond; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..623
FT /note="Phosphatidylinositol-3-phosphatase SAC1"
FT /id="PRO_0000209737"
FT TOPO_DOM 1..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11792713"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..552
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:11792713"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 574..623
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11792713"
FT DOMAIN 115..454
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT CROSSLNK 246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 358
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:3LWT"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:3LWT"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 53..64
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 67..82
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 85..98
FT /evidence="ECO:0007829|PDB:3LWT"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:4TU3"
FT HELIX 106..121
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4TU3"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:3LWT"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:3LWT"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3LWT"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:3LWT"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:3LWT"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3LWT"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:3LWT"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 183..194
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 197..207
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 230..240
FT /evidence="ECO:0007829|PDB:3LWT"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 247..257
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3LWT"
FT HELIX 279..296
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:3LWT"
FT HELIX 313..325
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:3LWT"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:3LWT"
FT HELIX 344..359
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:3LWT"
FT STRAND 386..391
FT /evidence="ECO:0007829|PDB:3LWT"
FT HELIX 396..417
FT /evidence="ECO:0007829|PDB:3LWT"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:3LWT"
FT HELIX 431..448
FT /evidence="ECO:0007829|PDB:3LWT"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:3LWT"
SQ SEQUENCE 623 AA; 71125 MW; 73DB1FA163BC17AE CRC64;
MTGPIVYVQN ADGIFFKLAE GKGTNDAVIH LANQDQGVRV LGAEEFPVQG EVVKIASLMG
FIKLKLNRYA IIANTVEETG RFNGHVFYRV LQHSIVSTKF NSRIDSEEAE YIKLLELHLK
NSTFYFSYTY DLTNSLQRNE KVGPAASWKT ADERFFWNHY LTEDLRNFAH QDPRIDSFIQ
PVIYGYAKTV DAVLNATPIV LGLITRRSIF RAGTRYFRRG VDKDGNVGNF NETEQILLAE
NPESEKIHVF SFLQTRGSVP IYWAEINNLK YKPNLVLGEN SLDATKKHFD QQKELYGDNY
LVNLVNQKGH ELPVKEGYES VVHALNDPKI HYVYFDFHHE CRKMQWHRVK LLIDHLEKLG
LSNEDFFHKV IDSNGNTVEI VNEQHSVVRT NCMDCLDRTN VVQSVLAQWV LQKEFESADV
VATGSTWEDN APLLTSYQNL WADNADAVSV AYSGTGALKT DFTRTGKRTR LGAFNDFLNS
ASRYYQNNWT DGPRQDSYDL FLGGFRPHTA SIKSPFPDRR PVYIQLIPMI ICAALTVLGA
TIFFPKDRFT SSKNLLYFAG ASIVLALSTK FMFKNGIQFV NWPKLVDVGF LVVHQTHDKE
QQFKGLKYAQ SPKFSKPDPL KRD
