SAC1B_DANRE
ID SAC1B_DANRE Reviewed; 586 AA.
AC A1L244;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Phosphatidylinositol-3-phosphatase SAC1-B;
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 B;
GN Name=sacm1lb; ORFNames=zgc:158642;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) 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; BC129344; AAI29345.1; -; mRNA.
DR RefSeq; NP_001074093.1; NM_001080624.1.
DR AlphaFoldDB; A1L244; -.
DR SMR; A1L244; -.
DR STRING; 7955.ENSDARP00000077948; -.
DR PaxDb; A1L244; -.
DR PeptideAtlas; A1L244; -.
DR GeneID; 791142; -.
DR KEGG; dre:791142; -.
DR CTD; 791142; -.
DR ZFIN; ZDB-GENE-070112-542; sacm1lb.
DR eggNOG; KOG1889; Eukaryota.
DR InParanoid; A1L244; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; A1L244; -.
DR Reactome; R-DRE-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-DRE-1660514; Synthesis of PIPs at the Golgi membrane.
DR PRO; PR:A1L244; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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: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; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..586
FT /note="Phosphatidylinositol-3-phosphatase SAC1-B"
FT /id="PRO_0000317175"
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; 66932 MW; 501148B8A763F25D CRC64;
MASTYNSFNL HTTAEKFYIE ACDDGVGDVL AIDRVSTEKT LTVRKDVPPS AVTRPICGIM
GTIRLVAGVY LIVITKKKKV GDLLGHAVWK ASDFDIISYK KTVLHLTDNQ MQDNKVFLSM
LNSVLNTDGF YFATDYDLTH TLQRLSNTSP EFQEMTLLER ADQRFVWNGH LLREFMAQPE
LHRFVFPVIH GFIAMRSCCI NGKIFDWNLI SRRSCFRAGV RYYVRGIDSE GHAANFVETE
QIIQYNGAKA SFIQTRGSIP FYWSQRPNLK YKPKPQISKS INHLDGFQRH FDSQIIIYGK
QVILNLVNQK GSEKPLEQAF AKMVGSLGNG MIKYIAFDFH KECSRMRWHR LQILVDTVAE
LQDEFGYFLV DSDGSVQMQQ DGTFRSNCMD CLDRTNVVQS LLARRSLQSQ LERMAVLHVG
QRIEEQADFE KIYKNAWADN ANACAKQYAG TGALKTDFTR TGKRTQWGLL MDGWNSMIRY
YKNNFSDGFR QDSIDLFLGN YAVEEADMNT PLHEPKDWKF LTLPIIMVVA FSMCIICLLM
AGDTWTETLA YVLFWGSASV VTGGVILFNG RDFVDAPRLV QKEKMD
