SAC1A_DANRE
ID SAC1A_DANRE Reviewed; 586 AA.
AC A4VCH0; Q1L8A6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Phosphatidylinositol-3-phosphatase SAC1-A;
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 A;
GN Name=sacm1la; ORFNames=si:ch211-222e23.8;
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 GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-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).
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; CR933768; CAK04253.1; -; Genomic_DNA.
DR EMBL; BX537337; CAK04253.1; JOINED; Genomic_DNA.
DR EMBL; BX537337; CAK04562.1; -; Genomic_DNA.
DR EMBL; CR933768; CAK04562.1; JOINED; Genomic_DNA.
DR EMBL; BC139689; AAI39690.1; -; mRNA.
DR RefSeq; NP_001038343.1; NM_001044878.1.
DR AlphaFoldDB; A4VCH0; -.
DR SMR; A4VCH0; -.
DR STRING; 7955.ENSDARP00000083973; -.
DR PaxDb; A4VCH0; -.
DR PeptideAtlas; A4VCH0; -.
DR Ensembl; ENSDART00000089540; ENSDARP00000083973; ENSDARG00000015290.
DR GeneID; 558940; -.
DR KEGG; dre:558940; -.
DR CTD; 558940; -.
DR ZFIN; ZDB-GENE-060503-122; sacm1la.
DR eggNOG; KOG1889; Eukaryota.
DR GeneTree; ENSGT00940000155579; -.
DR HOGENOM; CLU_003016_7_4_1; -.
DR InParanoid; A4VCH0; -.
DR OMA; YFMVNSD; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; A4VCH0; -.
DR TreeFam; TF313543; -.
DR PRO; PR:A4VCH0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000015290; Expressed in zone of skin and 21 other tissues.
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-A"
FT /id="PRO_0000317176"
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"
FT CONFLICT 360
FT /note="D -> E (in Ref. 2; AAI39690)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 67120 MW; 40BEC53DFAE17188 CRC64;
MANAYERFNL HSTPEKFYIE ACDDGADDVL VIDRVSTEMT LAGIKDIPPS GITRPICGVM
GTVRLVAGMY LIVITRKRKV GDLFGHTVWK AVEFDVISYK KTILHLTDIQ MQDNKTFLTM
INNVLNTDGF YFCTDYDLTH TQQRLSNTSP DFQEMSLLER ADQRFMWNGN LLREIIAQPE
LHKFAFPVIH GFIVMKPCCI NGKVFEWIII SRRSCFRAGV RYYVRGIDSE GHAANFVETE
QIVQFNNARA SFVQTRGSIP FFWSQRPNLK YKPKPLISKD TNHMDGLRRH FESQVLIYGK
QVILNLVNQK GSELPLEQAF AKMVSSMENG FIKYIAFDFH KECSKMRWHR LQILVDAVSD
MQEEFGYFMV SSDGKVLSEQ SGTFRSNCMD CLDRTNVIQS LLARRSLQSQ LQRMGVLHVG
QKIEEQADFE KIYKNAWADN ANACAKQYAG TGALKTDFTR TGKRTHWGLV MDGWNSMIRY
YKNNFSDGFR QDSIDLFLGN YSVDETDSLT PLHVKKDWKF LLLPVIMVVA FSMCIICLLM
AGDTWTETLA YVLFWGMASA LTAAVIVVNG REFVDAPKLV QKEKMD
