SAC1_MOUSE
ID SAC1_MOUSE Reviewed; 587 AA.
AC Q9EP69; Q80TQ1; Q99K33;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
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=Kiaa0851, Sac1 {ECO:0000250|UniProtKB:Q9ES21};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11352561; DOI=10.1006/geno.2000.6498;
RA Kiss H., Kedra D., Kiss C., Kost-Alimova M., Yang Y., Klein G., Imreh S.,
RA Dumanski J.P.;
RT "The LZTFL1 gene is a part of a transcriptional map covering 250 kb within
RT the common eliminated region 1 (C3CER1) in 3p21.3.";
RL Genomics 73:10-19(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Boehmelt G., Tsang E., Smith C., Mak T.W.;
RT "Cloning and characterization of the murine homolog of S.cerevisiae SAC1
RT (suppressor of actin mutations).";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- INTERACTION:
CC Q9EP69; A0A0F6B5H5: pipB2; Xeno; NbExp=3; IntAct=EBI-6908224, EBI-27033185;
CC Q9EP69; A0A0F6B423: sseL; Xeno; NbExp=4; IntAct=EBI-6908224, EBI-13953897;
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}.
CC -!- TISSUE SPECIFICITY: Detected in brain, lung, liver and kidney, and at
CC lower levels in spleen and skeletal muscle.
CC {ECO:0000269|PubMed:11352561}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65672.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ297526; CAC01937.1; -; mRNA.
DR EMBL; AJ245720; CAC20672.1; -; mRNA.
DR EMBL; AK122390; BAC65672.1; ALT_INIT; mRNA.
DR EMBL; AK089174; BAC40778.1; -; mRNA.
DR EMBL; AK161111; BAE36196.1; -; mRNA.
DR EMBL; AK171080; BAE42234.1; -; mRNA.
DR EMBL; BC005489; AAH05489.1; -; mRNA.
DR EMBL; BC117752; AAI17753.1; -; mRNA.
DR EMBL; BC117753; AAI17754.1; -; mRNA.
DR CCDS; CCDS40816.1; -.
DR RefSeq; NP_109617.1; NM_030692.4.
DR AlphaFoldDB; Q9EP69; -.
DR SMR; Q9EP69; -.
DR BioGRID; 219937; 24.
DR IntAct; Q9EP69; 20.
DR MINT; Q9EP69; -.
DR STRING; 10090.ENSMUSP00000026270; -.
DR iPTMnet; Q9EP69; -.
DR PhosphoSitePlus; Q9EP69; -.
DR SwissPalm; Q9EP69; -.
DR EPD; Q9EP69; -.
DR jPOST; Q9EP69; -.
DR MaxQB; Q9EP69; -.
DR PaxDb; Q9EP69; -.
DR PeptideAtlas; Q9EP69; -.
DR PRIDE; Q9EP69; -.
DR ProteomicsDB; 256582; -.
DR Antibodypedia; 45721; 133 antibodies from 21 providers.
DR DNASU; 83493; -.
DR Ensembl; ENSMUST00000026270; ENSMUSP00000026270; ENSMUSG00000025240.
DR Ensembl; ENSMUST00000238984; ENSMUSP00000158880; ENSMUSG00000025240.
DR GeneID; 83493; -.
DR KEGG; mmu:83493; -.
DR UCSC; uc009sgh.1; mouse.
DR CTD; 22908; -.
DR MGI; MGI:1933169; Sacm1l.
DR VEuPathDB; HostDB:ENSMUSG00000025240; -.
DR eggNOG; KOG1889; Eukaryota.
DR GeneTree; ENSGT00940000155579; -.
DR HOGENOM; CLU_003016_7_4_1; -.
DR InParanoid; Q9EP69; -.
DR OMA; FRDINVH; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; Q9EP69; -.
DR TreeFam; TF313543; -.
DR Reactome; R-MMU-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-MMU-1660514; Synthesis of PIPs at the Golgi membrane.
DR BioGRID-ORCS; 83493; 28 hits in 76 CRISPR screens.
DR ChiTaRS; Sacm1l; mouse.
DR PRO; PR:Q9EP69; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9EP69; protein.
DR Bgee; ENSMUSG00000025240; Expressed in cerebellar nuclear complex and 253 other tissues.
DR ExpressionAtlas; Q9EP69; baseline and differential.
DR Genevisible; Q9EP69; MM.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
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:0030176; C:integral component of endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0034593; F:phosphatidylinositol bisphosphate phosphatase activity; ISO:MGI.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; ISO:MGI.
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 1: Evidence at protein 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_0000317172"
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; 66944 MW; BCC73A3A2B912C98 CRC64;
MAAAAYEHLK LHITPEKFYV EACDDGADDV LIIDRVSTEV TLAVKKDVPP SAVTRPIFGI
LGTIHLVAGN YLVVITKKMK VGECFNHAVW RATDFDVLSY KKTMLHLTDI QLQDNKTFLA
MLNHVLSMDG FYFSTTYDLT HTLQRLSNTS PEFQEMSLLE RADQRFVWNG HLLRELSAQP
EVHRFALPVL HGFITMHSCS INGKYFDWIL ISRRSCFRAG VRYYVRGIDS EGHAANFVET
EQIVHYSGNR ASFVQTRGSI PIFWSQRPNL KYKPHPQISK VANHMDGFQR HFDSQVIIYG
KQVIINLVNH KGSEKPLEQT FANMVSSLGS GMIRYIAFDF HKECKNMRWD RLSILLDQVA
EMQDELSYFL VDSAGKVVTN QDGVFRSNCM DCLDRTNVIQ SLLARRSLQA QLQRLGVLHV
GQKLEEQDEF EKTYKNAWAD NANACAKQYA GTGALKTDFT RTGKRTQLGL LMDGFNSLLR
YYKNNFSDGF RQDSIDLFLG NYSVDELESH SPLSVPRDWK FLALPIIMVV AFSMCIICLL
MAGDTWTETL AYVLFWGVAS IGTFFIILYN GKDFVDAPRL VQKEKID
