SAC1_DROME
ID SAC1_DROME Reviewed; 592 AA.
AC Q9W0I6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Phosphatidylinositol-3-phosphatase SAC1;
DE EC=3.1.3.64 {ECO:0000250|UniProtKB:P32368};
DE AltName: Full=Phosphatidylinositol-4-phosphate phosphatase {ECO:0000250|UniProtKB:P32368};
DE AltName: Full=Suppressor of actin mutations 1-like protein;
GN Name=Sac1; Synonyms=Sacm1l; ORFNames=CG9128;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Phosphoinositide phosphatase which catalyzes the hydrolysis
CC of phosphatidylinositol 3-phosphate (PtdIns(3)P) and
CC phosphatidylinositol 4-phosphate (PtdIns(4)P) (By similarity). Has low
CC activity towards phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2)
CC (By similarity). {ECO:0000250|UniProtKB:P32368}.
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:0000250|UniProtKB:P32368};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12317;
CC Evidence={ECO:0000250|UniProtKB:P32368};
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:0000250|UniProtKB:P32368};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55653;
CC Evidence={ECO:0000250|UniProtKB:P32368};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P32368}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P32368};
CC Multi-pass membrane protein {ECO:0000255}.
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DR EMBL; AE014296; AAF47460.1; -; Genomic_DNA.
DR EMBL; AY047571; AAK77303.1; -; mRNA.
DR RefSeq; NP_001189016.1; NM_001202087.1.
DR RefSeq; NP_612087.1; NM_138243.4.
DR AlphaFoldDB; Q9W0I6; -.
DR SMR; Q9W0I6; -.
DR BioGRID; 63683; 4.
DR IntAct; Q9W0I6; 1.
DR STRING; 7227.FBpp0292309; -.
DR PaxDb; Q9W0I6; -.
DR PRIDE; Q9W0I6; -.
DR DNASU; 38137; -.
DR EnsemblMetazoa; FBtr0072652; FBpp0072546; FBgn0283500.
DR EnsemblMetazoa; FBtr0303217; FBpp0292309; FBgn0283500.
DR GeneID; 38137; -.
DR KEGG; dme:Dmel_CG9128; -.
DR UCSC; CG9128-RA; d. melanogaster.
DR CTD; 38137; -.
DR FlyBase; FBgn0283500; Sac1.
DR VEuPathDB; VectorBase:FBgn0283500; -.
DR eggNOG; KOG1889; Eukaryota.
DR GeneTree; ENSGT00940000155579; -.
DR HOGENOM; CLU_003016_7_4_1; -.
DR InParanoid; Q9W0I6; -.
DR OMA; FRDINVH; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; Q9W0I6; -.
DR Reactome; R-DME-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-DME-1660514; Synthesis of PIPs at the Golgi membrane.
DR BioGRID-ORCS; 38137; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38137; -.
DR PRO; PR:Q9W0I6; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0283500; Expressed in embryonic/larval hemocyte (Drosophila) and 33 other tissues.
DR ExpressionAtlas; Q9W0I6; baseline and differential.
DR Genevisible; Q9W0I6; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0071683; C:sensory dendrite; IDA:FlyBase.
DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0052866; F:phosphatidylinositol phosphate phosphatase activity; IDA:FlyBase.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; IMP:FlyBase.
DR GO; GO:0008088; P:axo-dendritic transport; IMP:FlyBase.
DR GO; GO:0016199; P:axon midline choice point recognition; IMP:FlyBase.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:FlyBase.
DR GO; GO:0046664; P:dorsal closure, amnioserosa morphology change; IMP:FlyBase.
DR GO; GO:0035149; P:lumen formation, open tracheal system; HMP:FlyBase.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IMP:FlyBase.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IMP:FlyBase.
DR GO; GO:0060074; P:synapse maturation; IMP:FlyBase.
DR InterPro; IPR002013; SAC_dom.
DR Pfam; PF02383; Syja_N; 1.
DR PROSITE; PS50275; SAC; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Golgi apparatus; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..592
FT /note="Phosphatidylinositol-3-phosphatase SAC1"
FT /id="PRO_0000317178"
FT TOPO_DOM 1..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P32368"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..552
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P32368"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 574..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P32368"
FT DOMAIN 121..451
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
SQ SEQUENCE 592 AA; 67768 MW; 49E0ED77AFD3F249 CRC64;
MDSREENAVY DDMNLYIAPQ SFIIEPNGGD ELLVIGRHDK VTRVQPASGG LVANLRPTRR
ICGVLGTIHL LSCDYLLVAT HRLFVGVLNG AVVWRLAGYD IIPYIPNSFQ RKENENYLRL
LRQTLDTKFF YFSYRYDLTN SLQRQREVAQ SRPEVSGLLQ RAEQRFVWNG YVLRQFNCDK
MEKFQLPLVL GFVSINQVQI NGQTFFWSII TRRSVQRAGT RLFCRGSDEQ GHVANFVETE
QIVEFNGQLT GFVQTRGSMP FHWHQLPNLR YKPRPVLVPG KDHLAACGLH FKEQIRLYGN
NVAVNLVDHK GAEGELEATY ARLVREMGNP QVRYESFDFH SECRKMRWDR LNILIDRLAH
EQDQFGVYHV FDDGKLVSTQ TGVFRTNCID CLDRTNVVQS MLARRSLTAV LQKLGVLHVG
QKVEHASDIF ESIFKGVWAD NADLVSLQYS GTCALKTDFT RTGKRTKSGA MQDGKNSLMR
YYLNNFADGQ RQDSIDLFLG KYLVNDNEGG AVPSPLESKH GWRFFTFPSV LLVAVAMFMI
TMTYPAEFNT ENLLFMLFWG AMIAVSATGI LHYGVEFVQW PRLFPPISFR DP
