SAC2_HUMAN
ID SAC2_HUMAN Reviewed; 1132 AA.
AC Q9Y2H2; B3KRF1; D3DRD1; Q2T9J4; Q5W135; Q5W136; Q6NVY2; Q86U97; Q9H3D9;
AC Q9NT51;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Phosphatidylinositide phosphatase SAC2 {ECO:0000305};
DE EC=3.1.3.25 {ECO:0000269|PubMed:25869668, ECO:0000269|PubMed:25869669};
DE AltName: Full=Inositol polyphosphate 5-phosphatase F {ECO:0000312|HGNC:HGNC:17054};
DE AltName: Full=Sac domain-containing inositol phosphatase 2;
DE AltName: Full=Sac domain-containing phosphoinositide 4-phosphatase 2 {ECO:0000305|PubMed:25869668, ECO:0000305|PubMed:25869669};
DE Short=hSAC2;
GN Name=INPP5F {ECO:0000312|HGNC:HGNC:17054}; Synonyms=KIAA0966, SAC2;
GN ORFNames=MSTP007, MSTP047;
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 [MRNA] (ISOFORM 1), ENZYME ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, TISSUE SPECIFICITY, AND CAUTION.
RX PubMed=11274189; DOI=10.1074/jbc.m101579200;
RA Minagawa T., Ijuin T., Mochizuki Y., Takenawa T.;
RT "Identification and characterization of a sac domain-containing
RT phosphoinositide 5-phosphatase.";
RL J. Biol. Chem. 276:22011-22015(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-997.
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
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. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP ASP-997.
RC TISSUE=Placenta, and Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 274-1132 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 956-1132 (ISOFORM 1).
RC TISSUE=Aorta;
RA Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y.,
RA Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y.,
RA Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C.,
RA Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION.
RX PubMed=17322895; DOI=10.1038/nm1552;
RA Trivedi C.M., Luo Y., Yin Z., Zhang M., Zhu W., Wang T., Floss T.,
RA Goettlicher M., Noppinger P.R., Wurst W., Ferrari V.A., Abrams C.S.,
RA Gruber P.J., Epstein J.A.;
RT "Hdac2 regulates the cardiac hypertrophic response by modulating Gsk3 beta
RT activity.";
RL Nat. Med. 13:324-331(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-907 AND SER-1103, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
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 [15]
RP FUNCTION, AND INTERACTION WITH STAT3.
RX PubMed=25476455; DOI=10.1038/srep07330;
RA Kim H.S., Li A., Ahn S., Song H., Zhang W.;
RT "Inositol Polyphosphate-5-Phosphatase F (INPP5F) inhibits STAT3 activity
RT and suppresses gliomas tumorigenicity.";
RL Sci. Rep. 4:7330-7330(2014).
RN [16]
RP INTERACTION WITH INPP4A; INPP5B AND OCRL.
RX PubMed=25869668; DOI=10.1083/jcb.201409064;
RA Nakatsu F., Messa M., Nandez R., Czapla H., Zou Y., Strittmatter S.M.,
RA De Camilli P.;
RT "Sac2/INPP5F is an inositol 4-phosphatase that functions in the endocytic
RT pathway.";
RL J. Cell Biol. 209:85-95(2015).
RN [17]
RP TISSUE SPECIFICITY.
RX PubMed=26203138; DOI=10.1523/jneurosci.1718-15.2015;
RA Zou Y., Stagi M., Wang X., Yigitkanli K., Siegel C.S., Nakatsu F.,
RA Cafferty W.B., Strittmatter S.M.;
RT "Gene-silencing screen for mammalian axon regeneration identifies Inpp5f
RT (Sac2) as an endogenous suppressor of repair after spinal cord injury.";
RL J. Neurosci. 35:10429-10439(2015).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 593-760, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-458.
RX PubMed=25869669; DOI=10.1083/jcb.201408027;
RA Hsu F., Hu F., Mao Y.;
RT "Spatiotemporal control of phosphatidylinositol 4-phosphate by Sac2
RT regulates endocytic recycling.";
RL J. Cell Biol. 209:97-110(2015).
CC -!- FUNCTION: Inositol 4-phosphatase which mainly acts on
CC phosphatidylinositol 4-phosphate. May be functionally linked to OCRL,
CC which converts phosphatidylinositol 4,5-bisphosphate to
CC phosphatidylinositol, for a sequential dephosphorylation of
CC phosphatidylinositol 4,5-bisphosphate at the 5 and 4 position of
CC inositol, thus playing an important role in the endocytic recycling
CC (PubMed:25869669). Regulator of TF:TFRC and integrins recycling
CC pathway, is also involved in cell migration mechanisms
CC (PubMed:25869669). Modulates AKT/GSK3B pathway by decreasing AKT and
CC GSK3B phosphorylation (PubMed:17322895). Negatively regulates STAT3
CC signaling pathway through inhibition of STAT3 phosphorylation and
CC translocation to the nucleus (PubMed:25476455). Functionally important
CC modulator of cardiac myocyte size and of the cardiac response to stress
CC (By similarity). May play a role as negative regulator of axon
CC regeneration after central nervous system injuries (By similarity).
CC {ECO:0000250|UniProtKB:Q8CDA1, ECO:0000269|PubMed:17322895,
CC ECO:0000269|PubMed:25476455, ECO:0000269|PubMed:25869669}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC Evidence={ECO:0000269|PubMed:25869668, ECO:0000269|PubMed:25869669};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14.3 uM for PtdIns(4,5)P2 (at pH 6.0)
CC {ECO:0000269|PubMed:11274189};
CC -!- SUBUNIT: Homodimer (PubMed:25869669). Interacts with OCRL and RAB5A
CC (PubMed:25869668). Interacts with INPP5B and INPP4A (PubMed:25869668).
CC Interacts with STAT3; the interaction is independent of STAT3 'TYR-705'
CC phosphorylation status (PubMed:25476455).
CC {ECO:0000250|UniProtKB:Q8CDA1, ECO:0000269|PubMed:25476455,
CC ECO:0000269|PubMed:25869668, ECO:0000269|PubMed:25869669}.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000269|PubMed:25869669}. Early endosome
CC {ECO:0000269|PubMed:25869669}. Recycling endosome
CC {ECO:0000269|PubMed:25869669}. Note=Also found on macropinosomes.
CC {ECO:0000250|UniProtKB:Q8CDA1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9Y2H2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2H2-2; Sequence=VSP_033268, VSP_033269;
CC Name=3;
CC IsoId=Q9Y2H2-3; Sequence=VSP_033266, VSP_033267;
CC Name=4;
CC IsoId=Q9Y2H2-4; Sequence=VSP_046366, VSP_046367;
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:11274189). Highly expressed in
CC brain (PubMed:26203138). {ECO:0000269|PubMed:11274189,
CC ECO:0000269|PubMed:26203138}.
CC -!- CAUTION: INPP5F has been initially described as an inositol
CC polyphosphate 5-phosphatase. {ECO:0000269|PubMed:11274189}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76810.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB023183; BAA76810.2; ALT_INIT; mRNA.
DR EMBL; AK091448; BAG52363.1; -; mRNA.
DR EMBL; AC027672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49379.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49380.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49381.1; -; Genomic_DNA.
DR EMBL; BC052367; AAH52367.1; -; mRNA.
DR EMBL; BC067820; AAH67820.1; -; mRNA.
DR EMBL; BC082755; AAH82755.1; -; mRNA.
DR EMBL; BC111493; AAI11494.1; -; mRNA.
DR EMBL; AL137528; CAB70792.1; -; mRNA.
DR EMBL; AF113227; AAG39298.1; -; mRNA.
DR EMBL; AF109361; AAQ13509.1; -; mRNA.
DR CCDS; CCDS58098.1; -. [Q9Y2H2-4]
DR CCDS; CCDS7616.1; -. [Q9Y2H2-1]
DR CCDS; CCDS81513.1; -. [Q9Y2H2-3]
DR PIR; T46372; T46372.
DR RefSeq; NP_001230123.1; NM_001243194.1. [Q9Y2H2-4]
DR RefSeq; NP_001230124.1; NM_001243195.1. [Q9Y2H2-3]
DR RefSeq; NP_055752.1; NM_014937.3. [Q9Y2H2-1]
DR PDB; 4XUU; X-ray; 2.62 A; A/B/C/D=593-760.
DR PDBsum; 4XUU; -.
DR AlphaFoldDB; Q9Y2H2; -.
DR SMR; Q9Y2H2; -.
DR BioGRID; 116543; 26.
DR ELM; Q9Y2H2; -.
DR IntAct; Q9Y2H2; 2.
DR MINT; Q9Y2H2; -.
DR STRING; 9606.ENSP00000354519; -.
DR DEPOD; INPP5F; -.
DR GlyGen; Q9Y2H2; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2H2; -.
DR PhosphoSitePlus; Q9Y2H2; -.
DR SwissPalm; Q9Y2H2; -.
DR BioMuta; INPP5F; -.
DR DMDM; 187611527; -.
DR EPD; Q9Y2H2; -.
DR jPOST; Q9Y2H2; -.
DR MassIVE; Q9Y2H2; -.
DR MaxQB; Q9Y2H2; -.
DR PaxDb; Q9Y2H2; -.
DR PeptideAtlas; Q9Y2H2; -.
DR PRIDE; Q9Y2H2; -.
DR ProteomicsDB; 65795; -.
DR ProteomicsDB; 85781; -. [Q9Y2H2-1]
DR ProteomicsDB; 85782; -. [Q9Y2H2-2]
DR ProteomicsDB; 85783; -. [Q9Y2H2-3]
DR Antibodypedia; 32161; 99 antibodies from 18 providers.
DR DNASU; 22876; -.
DR Ensembl; ENST00000369081.3; ENSP00000489864.1; ENSG00000198825.15. [Q9Y2H2-3]
DR Ensembl; ENST00000650409.1; ENSP00000496955.1; ENSG00000198825.15. [Q9Y2H2-4]
DR Ensembl; ENST00000650623.2; ENSP00000497527.1; ENSG00000198825.15. [Q9Y2H2-1]
DR GeneID; 22876; -.
DR KEGG; hsa:22876; -.
DR MANE-Select; ENST00000650623.2; ENSP00000497527.1; NM_014937.4; NP_055752.1.
DR UCSC; uc001leo.4; human. [Q9Y2H2-1]
DR CTD; 22876; -.
DR DisGeNET; 22876; -.
DR GeneCards; INPP5F; -.
DR HGNC; HGNC:17054; INPP5F.
DR HPA; ENSG00000198825; Tissue enhanced (brain).
DR MIM; 609389; gene.
DR neXtProt; NX_Q9Y2H2; -.
DR OpenTargets; ENSG00000198825; -.
DR PharmGKB; PA134927878; -.
DR VEuPathDB; HostDB:ENSG00000198825; -.
DR eggNOG; KOG1890; Eukaryota.
DR GeneTree; ENSGT00940000155996; -.
DR HOGENOM; CLU_008079_0_0_1; -.
DR InParanoid; Q9Y2H2; -.
DR OMA; CWRDKQG; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; Q9Y2H2; -.
DR TreeFam; TF313543; -.
DR BioCyc; MetaCyc:HS12255-MON; -.
DR PathwayCommons; Q9Y2H2; -.
DR Reactome; R-HSA-1660516; Synthesis of PIPs at the early endosome membrane.
DR SABIO-RK; Q9Y2H2; -.
DR SignaLink; Q9Y2H2; -.
DR BioGRID-ORCS; 22876; 19 hits in 1077 CRISPR screens.
DR ChiTaRS; INPP5F; human.
DR GenomeRNAi; 22876; -.
DR Pharos; Q9Y2H2; Tbio.
DR PRO; PR:Q9Y2H2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9Y2H2; protein.
DR Bgee; ENSG00000198825; Expressed in pons and 200 other tissues.
DR ExpressionAtlas; Q9Y2H2; baseline and differential.
DR Genevisible; Q9Y2H2; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0034596; F:phosphatidylinositol phosphate 4-phosphatase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0034595; F:phosphatidylinositol phosphate 5-phosphatase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; ISS:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB.
DR GO; GO:0048681; P:negative regulation of axon regeneration; ISS:BHF-UCL.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; IDA:UniProtKB.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR GO; GO:0031161; P:phosphatidylinositol catabolic process; ISS:UniProtKB.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
DR GO; GO:0001921; P:positive regulation of receptor recycling; IDA:ParkinsonsUK-UCL.
DR GO; GO:2000145; P:regulation of cell motility; IMP:UniProtKB.
DR GO; GO:2001135; P:regulation of endocytic recycling; IMP:UniProtKB.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IEA:Ensembl.
DR InterPro; IPR034753; hSac2.
DR InterPro; IPR022158; Inositol_phosphatase.
DR InterPro; IPR002013; SAC_dom.
DR Pfam; PF12456; hSac2; 1.
DR Pfam; PF02383; Syja_N; 1.
DR PROSITE; PS51791; HSAC2; 1.
DR PROSITE; PS50275; SAC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coated pit; Endosome; Hydrolase;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..1132
FT /note="Phosphatidylinositide phosphatase SAC2"
FT /id="PRO_0000331621"
FT DOMAIN 167..518
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT DOMAIN 593..760
FT /note="hSac2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01127"
FT REGION 846..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CDA1"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CDA1"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CDA1"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CDA1"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CDA1"
FT MOD_RES 1103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..19
FT /note="MELFQAKDHYILQQGERAL -> MCHDVIFMAWLKQQFSECT (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046366"
FT VAR_SEQ 20..629
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046367"
FT VAR_SEQ 206..219
FT /note="DDRFFWNKYMIQDL -> PLTARRAGFALGKK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033266"
FT VAR_SEQ 220..1132
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033267"
FT VAR_SEQ 373..375
FT /note="VII -> QQK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033268"
FT VAR_SEQ 376..1132
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033269"
FT VARIANT 453
FT /note="I -> V (in dbSNP:rs3736822)"
FT /id="VAR_042907"
FT VARIANT 997
FT /note="N -> D (in dbSNP:rs3188055)"
FT /evidence="ECO:0000269|PubMed:10231032,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_042908"
FT MUTAGEN 458
FT /note="C->S: Loss of inositol 4-phosphatase activity.
FT Alters TFRC distribution and delays TF recycling."
FT /evidence="ECO:0000269|PubMed:25869669"
FT CONFLICT 386
FT /note="I -> V (in Ref. 6; AAI11494)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="Y -> N (in Ref. 3; BAG52363)"
FT /evidence="ECO:0000305"
FT CONFLICT 1008
FT /note="P -> L (in Ref. 3; BAG52363)"
FT /evidence="ECO:0000305"
FT CONFLICT 1019
FT /note="S -> P (in Ref. 3; BAG52363)"
FT /evidence="ECO:0000305"
FT HELIX 595..610
FT /evidence="ECO:0007829|PDB:4XUU"
FT STRAND 617..625
FT /evidence="ECO:0007829|PDB:4XUU"
FT STRAND 639..654
FT /evidence="ECO:0007829|PDB:4XUU"
FT STRAND 656..668
FT /evidence="ECO:0007829|PDB:4XUU"
FT HELIX 669..671
FT /evidence="ECO:0007829|PDB:4XUU"
FT STRAND 672..679
FT /evidence="ECO:0007829|PDB:4XUU"
FT STRAND 683..685
FT /evidence="ECO:0007829|PDB:4XUU"
FT STRAND 689..698
FT /evidence="ECO:0007829|PDB:4XUU"
FT STRAND 701..710
FT /evidence="ECO:0007829|PDB:4XUU"
FT HELIX 720..736
FT /evidence="ECO:0007829|PDB:4XUU"
FT STRAND 743..746
FT /evidence="ECO:0007829|PDB:4XUU"
SQ SEQUENCE 1132 AA; 128407 MW; 853719FC0AD455CD CRC64;
MELFQAKDHY ILQQGERALW CSRRDGGLQL RPATDLLLAW NPICLGLVEG VIGKIQLHSD
LPWWLILIRQ KALVGKLPGD HEVCKVTKIA VLSLSEMEPQ DLELELCKKH HFGINKPEKI
IPSPDDSKFL LKTFTHIKSN VSAPNKKKVK ESKEKEKLER RLLEELLKMF MDSESFYYSL
TYDLTNSVQR QSTGERDGRP LWQKVDDRFF WNKYMIQDLT EIGTPDVDFW IIPMIQGFVQ
IEELVVNYTE SSDDEKSSPE TPPQESTCVD DIHPRFLVAL ISRRSRHRAG MRYKRRGVDK
NGNVANYVET EQLIHVHNHT LSFVQTRGSV PVFWSQVGYR YNPRPRLDRS EKETVAYFCA
HFEEQLNIYK KQVIINLVDQ AGREKIIGDA YLKQVLLFNN SHLTYVSFDF HEHCRGMKFE
NVQTLTDAIY DIILDMKWCW VDEAGVICKQ EGIFRVNCMD CLDRTNVVQA AIARVVMEQQ
LKKLGVMPPE QPLPVKCNRI YQIMWANNGD SISRQYAGTA ALKGDFTRTG ERKLAGVMKD
GVNSANRYYL NRFKDAYRQA VIDLMQGIPV TEDLYSIFTK EKEHEALHKE NQRSHQELIS
QLLQSYMKLL LPDDEKFHGG WALIDCDPSL IDATHRDVDV LLLLSNSAYY VAYYDDEVDK
VNQYQRLSLE NLEKIEIGPE PTLFGKPKFS CMRLHYRYKE ASGYFHTLRA VMRNPEEDGK
DTLQCIAEML QITKQAMGSD LPIIEKKLER KSSKPHEDII GIRSQNQGSL AQGKNFLMSK
FSSLNQKVKQ TKSNVNIGNL RKLGNFTKPE MKVNFLKPNL KVNLWKSDSS LETMENTGVM
DKVQAESDGD MSSDNDSYHS DEFLTNSKSD EDRQLANSLE SVGPIDYVLP SCGIIASAPR
LGSRSQSLSS TDSSVHAPSE ITVAHGSGLG KGQESPLKKS PSAGDVHILT GFAKPMDIYC
HRFVQDAQNK VTHLSETRSV SQQASQERNQ MTNQVSNETQ SESTEQTPSR PSQLDVSLSA
TGPQFLSVEP AHSVASQKTP TSASSMLELE TGLHVTPSPS ESSSSRAVSP FAKIRSSMVQ
VASITQAGLT HGINFAVSKV QKSPPEPEII NQVQQNELKK MFIQCQTRII QI
