SAC1_HUMAN
ID SAC1_HUMAN Reviewed; 587 AA.
AC Q9NTJ5; A8K527; B4DK71; O94935; Q7LA14; Q7LA22; Q96AX7; Q9NQ46; Q9NQ57;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 151.
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:0000303|PubMed:24209621, ECO:0000303|PubMed:30659099};
DE AltName: Full=Suppressor of actin mutations 1-like protein;
GN Name=SACM1L;
GN Synonyms=KIAA0851 {ECO:0000303|PubMed:10048485},
GN SAC1 {ECO:0000303|PubMed:29461204, ECO:0000303|PubMed:30659099,
GN ECO:0000303|PubMed:31806350};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [LARGE SCALE MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-434.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP PHE-434.
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-434.
RC TISSUE=Placenta;
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-456, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24209621; DOI=10.1016/j.cell.2013.09.056;
RA Mesmin B., Bigay J., Moser von Filseck J., Lacas-Gervais S., Drin G.,
RA Antonny B.;
RT "A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P
RT exchange by the ER-Golgi tether OSBP.";
RL Cell 155:830-843(2013).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=27044890; DOI=10.1083/jcb.201508106;
RA Dickson E.J., Jensen J.B., Vivas O., Kruse M., Traynor-Kaplan A.E.,
RA Hille B.;
RT "Dynamic formation of ER-PM junctions presents a lipid phosphatase to
RT regulate phosphoinositides.";
RL J. Cell Biol. 213:33-48(2016).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACTIVITY REGULATION,
RP REGION, AND MUTAGENESIS OF CYS-389.
RX PubMed=29461204; DOI=10.7554/elife.35588;
RA Zewe J.P., Wills R.C., Sangappa S., Goulden B.D., Hammond G.R.;
RT "SAC1 degrades its lipid substrate PtdIns4P in the endoplasmic reticulum to
RT maintain a steep chemical gradient with donor membranes.";
RL Elife 7:0-0(2018).
RN [14]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TMEM39A; SEC23A AND SEC24A.
RX PubMed=31806350; DOI=10.1016/j.molcel.2019.10.035;
RA Miao G., Zhang Y., Chen D., Zhang H.;
RT "The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy
RT by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1.";
RL Mol. Cell 0:0-0(2019).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH PLEKHA3 AND VAPA AND/OR
RP VAPB.
RX PubMed=30659099; DOI=10.1083/jcb.201812021;
RA Venditti R., Masone M.C., Rega L.R., Di Tullio G., Santoro M.,
RA Polishchuk E., Serrano I.C., Olkkonen V.M., Harada A., Medina D.L.,
RA La Montagna R., De Matteis M.A.;
RT "The activity of Sac1 across ER-TGN contact sites requires the four-
RT phosphate-adaptor-protein-1.";
RL J. Cell Biol. 218:783-797(2019).
CC -!- FUNCTION: Phosphoinositide phosphatase which catalyzes the hydrolysis
CC of phosphatidylinositol 4-phosphate (PtdIns(4)P) (PubMed:24209621,
CC PubMed:27044890, PubMed:29461204, PubMed:30659099). Can also catalyze
CC the hydrolysis of phosphatidylinositol 3-phosphate (PtdIns(3)P) and has
CC low activity towards phosphatidylinositol-3,5-bisphosphate
CC (PtdIns(3,5)P2) (By similarity). Shows a very robust PtdIns(4)P
CC phosphatase activity when it binds PtdIns(4)P in a 'cis' configuration
CC in the cellular environment, with much less activity seen when it binds
CC PtdIns(4)P in 'trans' configuration (PubMed:29461204, PubMed:24209621,
CC PubMed:30659099). PtdIns(4)P phosphatase activity (when it binds
CC PtdIns(4)P in 'trans' configuration) is enhanced in the presence of
CC PLEKHA3 (PubMed:30659099). {ECO:0000250|UniProtKB:Q9ES21,
CC ECO:0000269|PubMed:24209621, ECO:0000269|PubMed:27044890,
CC ECO:0000269|PubMed:29461204, ECO:0000269|PubMed:30659099}.
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:P32368};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12317;
CC Evidence={ECO:0000250|UniProtKB:P32368};
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:0000269|PubMed:24209621, ECO:0000269|PubMed:27044890,
CC ECO:0000269|PubMed:29461204, ECO:0000269|PubMed:30659099};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55653;
CC Evidence={ECO:0000305|PubMed:29461204};
CC -!- ACTIVITY REGULATION: Inhibited by bis-peroxovanadates and hydrogen
CC peroxide. {ECO:0000269|PubMed:29461204}.
CC -!- SUBUNIT: Interacts with TMEM39A (PubMed:31806350). Interacts with
CC SEC23A and SEC24A; this interaction is reduced in the absence of
CC TMEM39A (PubMed:31806350). Interacts with PLEKHA3 and VAPA and/or VAPB
CC to form a ternary complex (PubMed:30659099).
CC {ECO:0000269|PubMed:30659099, ECO:0000269|PubMed:31806350}.
CC -!- INTERACTION:
CC Q9NTJ5; O00590: ACKR2; NbExp=3; IntAct=EBI-3917235, EBI-13379418;
CC Q9NTJ5; Q13520: AQP6; NbExp=3; IntAct=EBI-3917235, EBI-13059134;
CC Q9NTJ5; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-3917235, EBI-11343438;
CC Q9NTJ5; P11912: CD79A; NbExp=3; IntAct=EBI-3917235, EBI-7797864;
CC Q9NTJ5; Q9Y678: COPG1; NbExp=3; IntAct=EBI-3917235, EBI-1049127;
CC Q9NTJ5; Q96BA8: CREB3L1; NbExp=6; IntAct=EBI-3917235, EBI-6942903;
CC Q9NTJ5; Q9Y394: DHRS7; NbExp=3; IntAct=EBI-3917235, EBI-1387800;
CC Q9NTJ5; Q15125: EBP; NbExp=3; IntAct=EBI-3917235, EBI-3915253;
CC Q9NTJ5; O15552: FFAR2; NbExp=3; IntAct=EBI-3917235, EBI-2833872;
CC Q9NTJ5; P31513: FMO3; NbExp=3; IntAct=EBI-3917235, EBI-12361463;
CC Q9NTJ5; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-3917235, EBI-11955647;
CC Q9NTJ5; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-3917235, EBI-13345167;
CC Q9NTJ5; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-3917235, EBI-18053395;
CC Q9NTJ5; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-3917235, EBI-10266796;
CC Q9NTJ5; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-3917235, EBI-11956541;
CC Q9NTJ5; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-3917235, EBI-373355;
CC Q9NTJ5; Q49AM1: MTERF2; NbExp=3; IntAct=EBI-3917235, EBI-17857560;
CC Q9NTJ5; Q2M2E3: ODF4; NbExp=3; IntAct=EBI-3917235, EBI-12382569;
CC Q9NTJ5; Q6ZMZ0: RNF19B; NbExp=3; IntAct=EBI-3917235, EBI-2466594;
CC Q9NTJ5; O95197-3: RTN3; NbExp=3; IntAct=EBI-3917235, EBI-11525735;
CC Q9NTJ5; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-3917235, EBI-17247926;
CC Q9NTJ5; Q14973: SLC10A1; NbExp=3; IntAct=EBI-3917235, EBI-3923031;
CC Q9NTJ5; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-3917235, EBI-18159983;
CC Q9NTJ5; Q9BS91: SLC35A5; NbExp=3; IntAct=EBI-3917235, EBI-18915901;
CC Q9NTJ5; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-3917235, EBI-17295964;
CC Q9NTJ5; P30825: SLC7A1; NbExp=3; IntAct=EBI-3917235, EBI-4289564;
CC Q9NTJ5; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-3917235, EBI-17684533;
CC Q9NTJ5; Q9Y320: TMX2; NbExp=3; IntAct=EBI-3917235, EBI-6447886;
CC Q9NTJ5; Q5T4F4: ZFYVE27; NbExp=3; IntAct=EBI-3917235, EBI-3892947;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:27044890, ECO:0000269|PubMed:29461204,
CC ECO:0000269|PubMed:31806350}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:29461204,
CC ECO:0000269|PubMed:31806350}. Note=Trafficking between the ER and Golgi
CC is regulated by nutrient status and by TMEM39A (PubMed:31806350).
CC Localizes to endoplasmic reticulum-plasma membrane contact sites (EPCS)
CC in the presence of phosphatidylinositol-4,5-bisphosphate
CC (PubMed:27044890). {ECO:0000269|PubMed:27044890,
CC ECO:0000269|PubMed:31806350}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NTJ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NTJ5-2; Sequence=VSP_056068, VSP_056069;
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, lung, liver, kidney,
CC pancreas and testis. {ECO:0000269|PubMed:10048485}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74874.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ297357; CAB95945.1; -; Genomic_DNA.
DR EMBL; AJ289880; CAB96871.1; -; Genomic_DNA.
DR EMBL; AB020658; BAA74874.2; ALT_INIT; mRNA.
DR EMBL; AL136831; CAB66765.1; -; mRNA.
DR EMBL; AK291142; BAF83831.1; -; mRNA.
DR EMBL; AK296421; BAG59083.1; -; mRNA.
DR EMBL; AC098476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016559; AAH16559.1; -; mRNA.
DR CCDS; CCDS33745.1; -. [Q9NTJ5-1]
DR PIR; T46447; T46447.
DR RefSeq; NP_001306001.1; NM_001319072.1. [Q9NTJ5-2]
DR RefSeq; NP_001306002.1; NM_001319073.1.
DR RefSeq; NP_054735.3; NM_014016.4. [Q9NTJ5-1]
DR RefSeq; XP_011531802.1; XM_011533500.2. [Q9NTJ5-2]
DR AlphaFoldDB; Q9NTJ5; -.
DR SMR; Q9NTJ5; -.
DR BioGRID; 116572; 152.
DR IntAct; Q9NTJ5; 65.
DR MINT; Q9NTJ5; -.
DR STRING; 9606.ENSP00000373713; -.
DR DEPOD; SACM1L; -.
DR iPTMnet; Q9NTJ5; -.
DR PhosphoSitePlus; Q9NTJ5; -.
DR SwissPalm; Q9NTJ5; -.
DR BioMuta; SACM1L; -.
DR DMDM; 167016563; -.
DR EPD; Q9NTJ5; -.
DR jPOST; Q9NTJ5; -.
DR MassIVE; Q9NTJ5; -.
DR MaxQB; Q9NTJ5; -.
DR PaxDb; Q9NTJ5; -.
DR PeptideAtlas; Q9NTJ5; -.
DR PRIDE; Q9NTJ5; -.
DR ProteomicsDB; 4433; -.
DR ProteomicsDB; 82620; -. [Q9NTJ5-1]
DR Antibodypedia; 45721; 133 antibodies from 21 providers.
DR DNASU; 22908; -.
DR Ensembl; ENST00000389061.10; ENSP00000373713.4; ENSG00000211456.13. [Q9NTJ5-1]
DR Ensembl; ENST00000672477.1; ENSP00000500361.1; ENSG00000211456.13. [Q9NTJ5-1]
DR GeneID; 22908; -.
DR KEGG; hsa:22908; -.
DR MANE-Select; ENST00000389061.10; ENSP00000373713.4; NM_014016.5; NP_054735.3.
DR UCSC; uc003cos.3; human. [Q9NTJ5-1]
DR CTD; 22908; -.
DR DisGeNET; 22908; -.
DR GeneCards; SACM1L; -.
DR HGNC; HGNC:17059; SACM1L.
DR HPA; ENSG00000211456; Low tissue specificity.
DR MIM; 606569; gene.
DR neXtProt; NX_Q9NTJ5; -.
DR OpenTargets; ENSG00000211456; -.
DR PharmGKB; PA34925; -.
DR VEuPathDB; HostDB:ENSG00000211456; -.
DR eggNOG; KOG1889; Eukaryota.
DR GeneTree; ENSGT00940000155579; -.
DR InParanoid; Q9NTJ5; -.
DR OMA; FRDINVH; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; Q9NTJ5; -.
DR TreeFam; TF313543; -.
DR BioCyc; MetaCyc:HS11932-MON; -.
DR PathwayCommons; Q9NTJ5; -.
DR Reactome; R-HSA-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-HSA-1660514; Synthesis of PIPs at the Golgi membrane.
DR SignaLink; Q9NTJ5; -.
DR SIGNOR; Q9NTJ5; -.
DR BioGRID-ORCS; 22908; 775 hits in 1093 CRISPR screens.
DR ChiTaRS; SACM1L; human.
DR GeneWiki; SACM1L; -.
DR GenomeRNAi; 22908; -.
DR Pharos; Q9NTJ5; Tbio.
DR PRO; PR:Q9NTJ5; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NTJ5; protein.
DR Bgee; ENSG00000211456; Expressed in secondary oocyte and 212 other tissues.
DR ExpressionAtlas; Q9NTJ5; baseline and differential.
DR Genevisible; Q9NTJ5; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA: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:0034596; F:phosphatidylinositol phosphate 4-phosphatase activity; TAS:Reactome.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; TAS:Reactome.
DR GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA: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; Alternative splicing; Endoplasmic reticulum; Golgi apparatus;
KW Hydrolase; Lipid metabolism; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..587
FT /note="Phosphatidylinositol-3-phosphatase SAC1"
FT /id="PRO_0000450055"
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:0000269|PubMed:29461204"
FT MOD_RES 456
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..49
FT /note="MATAAYEQLKLHITPEKFYVEACDDGADDVLTIDRVSTEVTLAVKKDVP ->
FT MWKLVMMEQMTYLPLTVCPQRLPLQSRKMFLLQLSQDQYLVYWAQSIWW (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056068"
FT VAR_SEQ 50..110
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056069"
FT VARIANT 434
FT /note="Y -> F (in dbSNP:rs1468542)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_038484"
FT MUTAGEN 389
FT /note="C->S: Loss of phosphatidylinositol-4-phosphate
FT phosphatase activity."
FT /evidence="ECO:0000269|PubMed:29461204"
FT CONFLICT 45
FT /note="K -> E (in Ref. 4; BAF83831)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="Q -> R (in Ref. 3; CAB66765)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 587 AA; 66967 MW; 3E0FC7515D15A071 CRC64;
MATAAYEQLK LHITPEKFYV EACDDGADDV LTIDRVSTEV TLAVKKDVPP SAVTRPIFGI
LGTIHLVAGN YLIVITKKIK VGEFFSHVVW 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
