SAC1_PONAB
ID SAC1_PONAB Reviewed; 587 AA.
AC Q5R921;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
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; Synonyms=SAC1 {ECO:0000250|UniProtKB:Q9ES21};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-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) (By similarity).
CC Shows a very robust PtdIns(4)P phosphatase activity when it binds
CC PtdIns(4)P in a 'cis' configuration in the cellular environment, with
CC much less activity seen when it binds PtdIns(4)P in 'trans'
CC configuration (By similarity). PtdIns(4)P phosphatase activity (when it
CC binds PtdIns(4)P in 'trans' configuration) is enhanced in the presence
CC of PLEKHA3 (By similarity). {ECO:0000250|UniProtKB:Q9ES21,
CC ECO:0000250|UniProtKB:Q9NTJ5}.
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 -!- SUBUNIT: Interacts with TMEM39A (By similarity). Interacts with SEC23A
CC and SEC24A; this interaction is reduced in the absence of TMEM39A (By
CC similarity). Interacts with PLEKHA3 and VAPA and/or VAPB to form a
CC ternary complex (By similarity). {ECO:0000250|UniProtKB:Q9NTJ5}.
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}. Note=Trafficking between the
CC ER and Golgi is regulated by nutrient status and by TMEM39A. Localizes
CC to endoplasmic reticulum-plasma membrane contact sites (EPCS) in the
CC presence of phosphatidylinositol-4,5-bisphosphate.
CC {ECO:0000250|UniProtKB:Q9NTJ5}.
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DR EMBL; CR859575; CAH91739.1; -; mRNA.
DR RefSeq; NP_001126010.1; NM_001132538.1.
DR AlphaFoldDB; Q5R921; -.
DR SMR; Q5R921; -.
DR STRING; 9601.ENSPPYP00000015596; -.
DR PRIDE; Q5R921; -.
DR Ensembl; ENSPPYT00000016217; ENSPPYP00000015596; ENSPPYG00000013944.
DR GeneID; 100172954; -.
DR KEGG; pon:100172954; -.
DR CTD; 22908; -.
DR eggNOG; KOG1889; Eukaryota.
DR GeneTree; ENSGT00940000155579; -.
DR HOGENOM; CLU_003016_7_4_1; -.
DR InParanoid; Q5R921; -.
DR OMA; FRDINVH; -.
DR OrthoDB; 359616at2759; -.
DR TreeFam; TF313543; -.
DR Proteomes; UP000001595; Chromosome 3.
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:0006661; P:phosphatidylinositol biosynthetic process; IEA:UniProt.
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 Acetylation; Endoplasmic reticulum; Golgi apparatus; Hydrolase;
KW Lipid metabolism; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..587
FT /note="Phosphatidylinositol-3-phosphatase SAC1"
FT /id="PRO_0000317173"
FT TOPO_DOM 1..520
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9ES21"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..548
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9ES21"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 570..587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9ES21"
FT DOMAIN 122..451
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT REGION 452..587
FT /note="Essential for phosphatidylinositol-4-phosphate
FT phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:Q9NTJ5"
FT MOD_RES 456
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NTJ5"
SQ SEQUENCE 587 AA; 66981 MW; 8E0FC182FCD2BC00 CRC64;
MATAAYEQLK LHITPEKFYV EACDDGADDV LTIDRVSTEV TLAVKKDVPP SAVTRPIFGI
LGTIHLVAGN YLIVITKKIK VGEFFSHVIW KATDFDVLSY KKTMLHLTDI QLQDNKTFLA
MLNHVLNVDG FYFSTTYDLT HTLQRLSNTS PEFQEMSLLE RADQRFVWNG HLLRELSAQP
EVHRFALPVL HGFITMHSCS INGKYFDWIL ISRRSCFRAG VRYYVRGIDS EGHAANFVET
EQIVHYNGSK ASFVQTRGSI PVFWSQRPNL KYKPLPQISK VANHMDGFQR HFDSQVIIYG
KQVIINLINQ KGSEKPLEQT FATMVSSLGS GMMRYIAFDF HKECKNMRWD RLSILLDQVA
EMQDELSYFL VDSAGQVVAN QEGVFRSNCM DCLDRTNVIQ SLLARRSLQA QLQRLGVLHV
GQKLEEQDEF EKIYKNAWAD NANACAKQYA GTGALKTDFT RTGKRTHLGL IMDGWNSMIR
YYKNNFSDGF RQDSIDLFLG NYSVDELESH SPLSVPRDWK FLALPIIMVV AFSMCIICLL
MAGDTWTETL AYVLFWGVAS IGTFFIILYN GKDFVDAPRL VQKEKID
