SAC1_BOVIN
ID SAC1_BOVIN Reviewed; 587 AA.
AC A6QL88;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal medulla;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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; BC147878; AAI47879.1; -; mRNA.
DR RefSeq; NP_001095601.1; NM_001102131.2.
DR AlphaFoldDB; A6QL88; -.
DR SMR; A6QL88; -.
DR STRING; 9913.ENSBTAP00000004549; -.
DR PaxDb; A6QL88; -.
DR PRIDE; A6QL88; -.
DR Ensembl; ENSBTAT00000004549; ENSBTAP00000004549; ENSBTAG00000003501.
DR GeneID; 530577; -.
DR KEGG; bta:530577; -.
DR CTD; 22908; -.
DR VEuPathDB; HostDB:ENSBTAG00000003501; -.
DR VGNC; VGNC:34259; SACM1L.
DR eggNOG; KOG1889; Eukaryota.
DR GeneTree; ENSGT00940000155579; -.
DR HOGENOM; CLU_003016_7_4_1; -.
DR InParanoid; A6QL88; -.
DR OMA; FRDINVH; -.
DR OrthoDB; 359616at2759; -.
DR TreeFam; TF313543; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000003501; Expressed in spiral colon and 106 other tissues.
DR ExpressionAtlas; A6QL88; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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 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_0000317170"
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; 67093 MW; 91736BEC3ACFC763 CRC64;
MAATTYERLK LHVTPEKFYV EACDDGADDV LIIDRVSTEV TLSVKKDIPP SAVTRPIFGI
LGTIHLVAGN YLIVITKKKK IGEFFNHVIW KATDFDVLSY KKTMLHLTDI QLQDNKTFLA
MMNHVLSMDG FYFSTTYDLT HTLQRLSNTS PEFQEMSLLE RADQRFVWNG HLLRELSAQP
EVHRFALPVL HGFITMHSCS INGKYFDWIL ISRRSCFRAG VRYYVRGIDS EGHAANFVET
EQIVHYNGSR ASFVQTRGSI PLYWSQRPNL KYKPLPLINK VANHMDGFQR HFDSQIIIYG
KQVIINLVNQ KGSEKPLEQA FATMVSSLGN GMIRYIAFDF HKECKNMRWD RLSILLDQVA
EMQDELSYFL VDPAGVVLST QEGVFRSNCM DCLDRTNVIQ SLLARRSLQA QLQRLGVLHV
GQKLEEQDEF EKIYKNAWAD NANACAKQYA GTGALKTDFT RTGKRTQLGL IMDGWNSLIR
YYKNNFSDGF RQDSIDLFLG NYSVDELESH SPLSVPRDLK FLALPIIMVV AFSMCIICLL
MAGDTWTETL AYVLFWGVAS IGTFFIILYN GKDFVDAPRL VQKEKID
