ID   SAC1_XENLA              Reviewed;         586 AA.
AC   Q6GM29;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Phosphatidylinositol-3-phosphatase SAC1;
DE            EC=3.1.3.64 {ECO:0000250|UniProtKB:Q9ES21};
DE   AltName: Full=Phosphatidylinositol-4-phosphate phosphatase {ECO:0000250|UniProtKB:Q9ES21};
DE   AltName: Full=Suppressor of actin mutations 1-like protein;
GN   Name=sacm1l;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphoinositide phosphatase which catalyzes the hydrolysis
CC       of phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol
CC       3-phosphate (PtdIns(3)P) and has low activity towards
CC       phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2).
CC       {ECO:0000250|UniProtKB:Q9ES21}.
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:Q9ES21};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12317;
CC         Evidence={ECO:0000250|UniProtKB:Q9ES21};
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:Q9ES21};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55653;
CC         Evidence={ECO:0000250|UniProtKB:Q9ES21};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9ES21}; Multi-pass membrane protein
CC       {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NTJ5};
CC       Multi-pass membrane protein {ECO:0000255}.
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DR   EMBL; BC074260; AAH74260.1; -; mRNA.
DR   EMBL; BC077608; AAH77608.1; -; mRNA.
DR   RefSeq; NP_001086149.1; NM_001092680.1.
DR   AlphaFoldDB; Q6GM29; -.
DR   SMR; Q6GM29; -.
DR   BioGRID; 102741; 1.
DR   MaxQB; Q6GM29; -.
DR   GeneID; 444578; -.
DR   KEGG; xla:444578; -.
DR   CTD; 444578; -.
DR   Xenbase; XB-GENE-920718; sacm1l.L.
DR   OMA; FRDINVH; -.
DR   OrthoDB; 359616at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 444578; Expressed in zone of skin and 19 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISS:UniProtKB.
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; Lipid metabolism;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..586
FT                   /note="Phosphatidylinositol-3-phosphatase SAC1"
FT                   /id="PRO_0000317177"
FT   TOPO_DOM        1..519
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ES21"
FT   TRANSMEM        520..540
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        541..547
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ES21"
FT   TRANSMEM        548..568
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        569..586
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ES21"
FT   DOMAIN          121..450
FT                   /note="SAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT   REGION          451..586
FT                   /note="Essential for phosphatidylinositol-4-phosphate
FT                   phosphatase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NTJ5"
SQ   SEQUENCE   586 AA;  66957 MW;  32214EF6AB5655EE CRC64;
     MALAYENLKL HITPEKFYVE ACDPGVEDVL TIDRVSTEVT LSGKKDIPPS AITRAIYGIL
     GTIRLVAGMY LIVITRRKKV GDLLNHSIWK ATDFDIISYK KTMLHLTDSQ LQDNKAFLGM
     LSHVLSVDGF YFSVSYDLTH TLQRLANTSP EFQEMSLLER ADQRFVWNGN LLREFSAQPE
     IQKFAIPVVH GFIAIHSCSI NGKYFDWILI SRRSCFRAGV RYYVRGIDSE GHAANFVETE
     QIVHYNGNKA SFVQTRGSIP FYWSQRPNLK YKPKPQISKA VNHMDGFQRH FDSQVISYGK
     QVVLNLVNQK GSEKPLEQEF SQMVSGLGNG MVRYIAFDFH KECSRMRWDR LQILVEQVAE
     TQDEFGYFLV DTEGKVVSQQ DGIFRSNCMD CLDRTNVVQS LLARRSLQYQ LQRLGVLHVG
     QRIEEQIQFE KIYKNAWADN ANACAKQYAG TGALKTDFTR TGKRTQWGLL MDGWNSLIRY
     YKNNFSDGFR QDSIDLFLGN YSVEEAYSTS PLHIQTDWKF LALPIIMVVA FSMCIICLLM
     AGDTWTETLA YVLFWGTASI GTGAIIMYNG KDFVDAPKLV QKEKMD