SAC1_DICDI
ID SAC1_DICDI Reviewed; 581 AA.
AC Q55AW9; Q86AE0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
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};
GN Name=sac1; ORFNames=DDB_G0271630;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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; AAFI02000006; EAL71679.1; -; Genomic_DNA.
DR RefSeq; XP_645577.1; XM_640485.1.
DR AlphaFoldDB; Q55AW9; -.
DR SMR; Q55AW9; -.
DR STRING; 44689.DDB0233948; -.
DR PaxDb; Q55AW9; -.
DR EnsemblProtists; EAL71679; EAL71679; DDB_G0271630.
DR GeneID; 8618030; -.
DR KEGG; ddi:DDB_G0271630; -.
DR dictyBase; DDB_G0271630; sac1.
DR eggNOG; KOG1889; Eukaryota.
DR HOGENOM; CLU_003016_7_4_1; -.
DR InParanoid; Q55AW9; -.
DR OMA; FRDINVH; -.
DR PhylomeDB; Q55AW9; -.
DR Reactome; R-DDI-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-DDI-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-DDI-1660516; Synthesis of PIPs at the early endosome membrane.
DR PRO; PR:Q55AW9; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0140220; C:pathogen-containing vacuole; HDA:dictyBase.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; ISS:dictyBase.
DR GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; ISS:dictyBase.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISS:dictyBase.
DR InterPro; IPR002013; SAC_dom.
DR Pfam; PF02383; Syja_N; 1.
DR PROSITE; PS50275; SAC; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Golgi apparatus; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..581
FT /note="Phosphatidylinositol-3-phosphatase SAC1"
FT /id="PRO_0000328520"
FT TOPO_DOM 1..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P32368"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 533..535
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P32368"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..581
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P32368"
FT DOMAIN 119..445
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
SQ SEQUENCE 581 AA; 66551 MW; 327EDC3A1C5F9566 CRC64;
MNIELINTNE RFILINNGNK DKSLNIDKHS VKASISVGVP KNNEKVLTRI ENVKGIIGCI
QLVSGHYLMI FKEHNHVATV TGKKIYQMKD VELIPFFPNQ QSLVSIPDQD AEEQHLSMIR
WLLSSENFYF SYDYDFTLTL QRQYSTTTTT TSGSSLGERC DSRFFWNEKY VTILSKEHGL
GDWILPITMG FVESKTLGGT CQFTLISRRN LNRSGTRYNV RGIDKKGNVA NNVETEQIIE
IKENTFTSFV QVRGSIPLLW SQFPTLKYKP SVKFYGDEKE NSQALEQHFK QLHQLYGSTT
VVNLIDRKGA ELKLGEAYEE RVKSLKDVHY VWFDFHSICK GMRYDKLSIL MDQLKDDLKQ
YGFFFVEDGK IVQKQQGVFR TNCIDNLDRT NVVQSLITRH SLENQMASVL NKQIPSTTFK
GDQFEYVFKN IWADHGDAIS TQYSGTGALK NDFTRTGKRN FQGVLRDGEN SVKRYYLNNF
KDGFRQDSYF LFTNPSVDLT TAKQHESKPP SPLIWIFSFV FAAIFLANLY LPSATSSIGG
FISQTTVLVG SVFFALKLAM KYQASIVDKP TLFKLDSIYK N
