ID MTMR3_HUMAN Reviewed; 1198 AA. AC Q13615; A5PL26; A7MD32; Q9NYN5; Q9NYN6; Q9UDX6; Q9UEG3; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2003, sequence version 3. DT 27-MAR-2024, entry version 205. DE RecName: Full=Myotubularin-related protein 3 {ECO:0000305}; DE EC=3.1.3.48 {ECO:0000269|PubMed:10733931}; DE AltName: Full=FYVE domain-containing dual specificity protein phosphatase 1; DE Short=FYVE-DSP1; DE AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase; DE EC=3.1.3.95 {ECO:0000269|PubMed:11676921}; DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase; DE EC=3.1.3.64 {ECO:0000269|PubMed:11676921}; DE AltName: Full=Zinc finger FYVE domain-containing protein 10; GN Name=MTMR3 {ECO:0000312|HGNC:HGNC:7451}; Synonyms=KIAA0371, ZFYVE10; 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 (ISOFORMS A; B AND C), CHARACTERIZATION, CATALYTIC RP ACTIVITY, AND FUNCTION. RX PubMed=10733931; DOI=10.1006/bbrc.2000.2417; RA Zhao R., Qi Y., Zhao Z.J.; RT "FYVE-DSP1, a dual-specificity protein phosphatase containing an FYVE RT domain."; RL Biochem. Biophys. Res. Commun. 270:222-229(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). RC TISSUE=Brain; RX PubMed=9205841; DOI=10.1093/dnares/4.2.141; RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. VII. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 4:141-150(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C). 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 OF 374-578. RX PubMed=9736772; DOI=10.1093/hmg/7.11.1703; RA Laporte J., Blondeau F., Buj-Bello A., Tentler D., Kretz C., Dahl N., RA Mandel J.-L.; RT "Characterization of the myotubularin dual specificity phosphatase gene RT family from yeast to human."; RL Hum. Mol. Genet. 7:1703-1712(1998). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 381-463. RX PubMed=8640223; DOI=10.1038/ng0696-175; RA Laporte J., Hu L.-J., Kretz C., Mandel J.-L., Kioschis P., Coy J., RA Klauck S.M., Poutska A., Dahl N.; RT "A gene mutated in X-linked myotubular myopathy defines a new putative RT tyrosine phosphatase family conserved in yeast."; RL Nat. Genet. 13:175-182(1996). RN [9] RP FUNCTION, MUTAGENESIS OF CYS-413, CATALYTIC ACTIVITY, AND SUBCELLULAR RP LOCATION. RX PubMed=11676921; DOI=10.1016/s0960-9822(01)00501-2; RA Walker D.M., Urbe S., Dove S.K., Tenza D., Raposo G., Clague M.J.; RT "Characterization of MTMR3. an inositol lipid 3-phosphatase with novel RT substrate specificity."; RL Curr. Biol. 11:1600-1605(2001). RN [10] RP CATALYTIC ACTIVITY. RX PubMed=12646134; DOI=10.1016/s0960-9822(03)00132-5; RA Schaletzky J., Dove S.K., Short B., Lorenzo O., Clague M.J., Barr F.A.; RT "Phosphatidylinositol-5-phosphate activation and conserved substrate RT specificity of the myotubularin phosphatidylinositol 3-phosphatases."; RL Curr. Biol. 13:504-509(2003). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-647, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633; SER-647 AND THR-731, AND 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 [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-613; SER-647; SER-651; RP THR-731; SER-906 AND SER-909, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-731, AND IDENTIFICATION BY RP 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 [16] RP VARIANT [LARGE SCALE ANALYSIS] LEU-221. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [17] RP MUTAGENESIS OF CYS-413. RX PubMed=32690950; DOI=10.1038/s41590-020-0730-5; RA Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L., RA Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F., RA Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T., RA Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T., RA Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O., RA Thomsen M.K., Paludan S.R.; RT "STEEP mediates STING ER exit and activation of signaling."; RL Nat. Immunol. 21:868-879(2020). RN [18] RP ERRATUM OF PUBMED:32690950. RX PubMed=32929276; DOI=10.1038/s41590-020-0803-5; RA Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L., RA Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F., RA Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T., RA Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T., RA Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O., RA Thomsen M.K., Paludan S.R.; RL Nat. Immunol. 21:1468-1469(2020). CC -!- FUNCTION: Phosphatase that acts on lipids with a phosphoinositol CC headgroup (PubMed:11676921). Has phosphatase activity towards CC phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5- CC bisphosphate (PubMed:11676921). May also dephosphorylate proteins CC phosphorylated on Ser, Thr, and Tyr residues (PubMed:10733931). CC {ECO:0000269|PubMed:10733931, ECO:0000269|PubMed:11676921}. 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:0000269|PubMed:11676921}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5- CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:39019, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795, CC ChEBI:CHEBI:57923; EC=3.1.3.95; CC Evidence={ECO:0000269|PubMed:11676921}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10044, ECO:0000269|PubMed:10733931}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3- CC phosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo- CC inositol) + phosphate; Xref=Rhea:RHEA:45640, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:72835, ChEBI:CHEBI:78995; CC Evidence={ECO:0000269|PubMed:11676921}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5- CC phosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo- CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45636, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78994, CC ChEBI:CHEBI:84968; Evidence={ECO:0000269|PubMed:11676921}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3- CC phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo- CC inositol) + phosphate; Xref=Rhea:RHEA:42328, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78934; CC Evidence={ECO:0000269|PubMed:12646134}; CC -!- INTERACTION: CC Q13615; Q9NQT4: EXOSC5; NbExp=3; IntAct=EBI-371938, EBI-371876; CC Q13615; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-371938, EBI-2341787; CC Q13615; P42345: MTOR; NbExp=3; IntAct=EBI-371938, EBI-359260; CC Q13615; Q8N122: RPTOR; NbExp=3; IntAct=EBI-371938, EBI-1567928; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11676921}. Membrane CC {ECO:0000269|PubMed:11676921}; Peripheral membrane protein CC {ECO:0000269|PubMed:11676921}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=B; Synonyms=FYVE-DSP1b; CC IsoId=Q13615-1; Sequence=Displayed; CC Name=A; Synonyms=FYVE-DSP1a; CC IsoId=Q13615-2; Sequence=VSP_007781, VSP_007782; CC Name=C; Synonyms=FYVE-DSP1c; CC IsoId=Q13615-3; Sequence=VSP_007781; CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class myotubularin subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA20826.2; 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; AF233436; AAF40203.2; -; mRNA. DR EMBL; AF233437; AAF40204.1; -; mRNA. DR EMBL; AF233438; AAF40205.1; -; mRNA. DR EMBL; AB002369; BAA20826.2; ALT_INIT; mRNA. DR EMBL; CR456525; CAG30411.1; -; mRNA. DR EMBL; CH471095; EAW59852.1; -; Genomic_DNA. DR EMBL; CH471095; EAW59855.1; -; Genomic_DNA. DR EMBL; BC142713; AAI42714.1; -; mRNA. DR EMBL; BC148216; AAI48217.1; -; mRNA. DR EMBL; BC152455; AAI52456.1; -; mRNA. DR EMBL; AC003071; AAB83949.1; -; Genomic_DNA. DR EMBL; U58034; AAC79119.1; -; Genomic_DNA. DR CCDS; CCDS13870.1; -. [Q13615-1] DR CCDS; CCDS13871.1; -. [Q13615-2] DR CCDS; CCDS46682.1; -. [Q13615-3] DR RefSeq; NP_066576.1; NM_021090.3. [Q13615-1] DR RefSeq; NP_694690.1; NM_153050.2. [Q13615-2] DR RefSeq; NP_694691.1; NM_153051.2. [Q13615-3] DR RefSeq; XP_016884521.1; XM_017029032.1. DR AlphaFoldDB; Q13615; -. DR SMR; Q13615; -. DR BioGRID; 114414; 68. DR IntAct; Q13615; 34. DR MINT; Q13615; -. DR STRING; 9606.ENSP00000384651; -. DR SwissLipids; SLP:000001134; -. DR DEPOD; MTMR3; -. DR GlyCosmos; Q13615; 3 sites, 1 glycan. DR GlyGen; Q13615; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q13615; -. DR PhosphoSitePlus; Q13615; -. DR BioMuta; MTMR3; -. DR DMDM; 33112668; -. DR EPD; Q13615; -. DR jPOST; Q13615; -. DR MassIVE; Q13615; -. DR MaxQB; Q13615; -. DR PaxDb; 9606-ENSP00000384651; -. DR PeptideAtlas; Q13615; -. DR ProteomicsDB; 59601; -. [Q13615-1] DR ProteomicsDB; 59602; -. [Q13615-2] DR ProteomicsDB; 59603; -. [Q13615-3] DR Pumba; Q13615; -. DR Antibodypedia; 35237; 91 antibodies from 20 providers. DR DNASU; 8897; -. DR Ensembl; ENST00000333027.7; ENSP00000331649.3; ENSG00000100330.16. [Q13615-2] DR Ensembl; ENST00000351488.7; ENSP00000307271.6; ENSG00000100330.16. [Q13615-3] DR Ensembl; ENST00000401950.7; ENSP00000384651.3; ENSG00000100330.16. [Q13615-1] DR Ensembl; ENST00000406629.1; ENSP00000384077.1; ENSG00000100330.16. [Q13615-2] DR GeneID; 8897; -. DR KEGG; hsa:8897; -. DR MANE-Select; ENST00000401950.7; ENSP00000384651.3; NM_021090.4; NP_066576.1. DR UCSC; uc003agu.5; human. [Q13615-1] DR AGR; HGNC:7451; -. DR CTD; 8897; -. DR DisGeNET; 8897; -. DR GeneCards; MTMR3; -. DR HGNC; HGNC:7451; MTMR3. DR HPA; ENSG00000100330; Tissue enhanced (bone). DR MIM; 603558; gene. DR neXtProt; NX_Q13615; -. DR OpenTargets; ENSG00000100330; -. DR PharmGKB; PA31254; -. DR VEuPathDB; HostDB:ENSG00000100330; -. DR eggNOG; KOG4471; Eukaryota. DR GeneTree; ENSGT00940000157272; -. DR HOGENOM; CLU_001839_2_2_1; -. DR InParanoid; Q13615; -. DR OMA; FNEAFLX; -. DR OrthoDB; 5474662at2759; -. DR PhylomeDB; Q13615; -. DR TreeFam; TF315197; -. DR BioCyc; MetaCyc:HS02045-MONOMER; -. DR BRENDA; 3.1.3.95; 2681. DR PathwayCommons; Q13615; -. DR Reactome; R-HSA-1632852; Macroautophagy. DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane. DR SignaLink; Q13615; -. DR SIGNOR; Q13615; -. DR BioGRID-ORCS; 8897; 26 hits in 1176 CRISPR screens. DR ChiTaRS; MTMR3; human. DR GeneWiki; MTMR3; -. DR GenomeRNAi; 8897; -. DR Pharos; Q13615; Tbio. DR PRO; PR:Q13615; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q13615; Protein. DR Bgee; ENSG00000100330; Expressed in oocyte and 197 other cell types or tissues. DR ExpressionAtlas; Q13615; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IDA:UniProtKB. DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IDA:UniProtKB. DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IDA:FlyBase. DR GO; GO:0042149; P:cellular response to glucose starvation; IMP:ParkinsonsUK-UCL. DR GO; GO:0016236; P:macroautophagy; TAS:Reactome. DR GO; GO:1904562; P:phosphatidylinositol 5-phosphate metabolic process; IDA:ParkinsonsUK-UCL. DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome. DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB. DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB. DR GO; GO:2000785; P:regulation of autophagosome assembly; IMP:ParkinsonsUK-UCL. DR GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central. DR GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; IDA:UniProtKB. DR CDD; cd15732; FYVE_MTMR3; 1. DR CDD; cd13341; PH-GRAM_MTMR3; 1. DR CDD; cd14586; PTP-MTMR3; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR035888; MTMR3_PH-GRAM. DR InterPro; IPR046352; MTMR3_PTP. DR InterPro; IPR010569; Myotubularin-like_Pase_dom. DR InterPro; IPR030564; Myotubularin_fam. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR003595; Tyr_Pase_cat. DR InterPro; IPR000306; Znf_FYVE. DR InterPro; IPR017455; Znf_FYVE-rel. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1. DR PANTHER; PTHR10807:SF66; MYOTUBULARIN-RELATED PROTEIN 3; 1. DR Pfam; PF01363; FYVE; 1. DR Pfam; PF06602; Myotub-related; 1. DR SMART; SM00064; FYVE; 1. DR SMART; SM00404; PTPc_motif; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50178; ZF_FYVE; 1. DR Genevisible; Q13615; HS. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Cytoplasm; Hydrolase; Lipid metabolism; KW Membrane; Metal-binding; Phosphoprotein; Protein phosphatase; KW Reference proteome; Zinc; Zinc-finger. FT CHAIN 1..1198 FT /note="Myotubularin-related protein 3" FT /id="PRO_0000094936" FT DOMAIN 155..576 FT /note="Myotubularin phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669" FT ZN_FING 1119..1179 FT /note="FYVE-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT REGION 265..285 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 590..612 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 650..669 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 716..735 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 855..891 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 933..974 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 993..1019 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1029..1062 FT /evidence="ECO:0000255" FT COMPBIAS 265..283 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 872..891 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 934..954 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 413 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044, FT ECO:0000305" FT BINDING 326..329 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 351..352 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 413..419 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 459 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 1125 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1128 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1141 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1144 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1149 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1152 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1171 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1174 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT MOD_RES 8 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 613 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 633 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 647 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 651 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 731 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 906 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 909 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1064 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8K296" FT VAR_SEQ 1076..1112 FT /note="Missing (in isoform A and isoform C)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007781" FT VAR_SEQ 1142 FT /note="R -> RDTDRVDQTW (in isoform A)" FT /evidence="ECO:0000305" FT /id="VSP_007782" FT VARIANT 221 FT /note="V -> L (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035656" FT MUTAGEN 413 FT /note="C->S: Loss of lipid phosphatase activity." FT /evidence="ECO:0000269|PubMed:11676921, FT ECO:0000305|PubMed:32690950" FT CONFLICT 560..578 FT /note="LYPVCHVRNLMLWSAVYLP -> CILQPFHCGQQKEFGVGYI (in Ref. FT 7)" FT /evidence="ECO:0000305" SQ SEQUENCE 1198 AA; 133619 MW; FE6F4B165074D5F8 CRC64; MDEETRHSLE CIQANQIFPR KQLIREDENL QVPFLELHGE STEFVGRAED AIIALSNYRL HIKFKESLVN VPLQLIESVE CRDIFQLHLT CKDCKVIRCQ FSTFEQCQEW LKRLNNAIRP PAKIEDLFSF AYHAWCMEVY ASEKEQHGDL CRPGEHVTSR FKNEVERMGF DMNNAWRISN INEKYKLCGS YPQELIVPAW ITDKELESVS SFRSWKRIPA VIYRHQSNGA VIARCGQPEV SWWGWRNADD EHLVQSVAKA CASDSRSSGS KLSTRNTSRD FPNGGDLSDV EFDSSLSNAS GAESLAIQPQ KLLILDARSY AAAVANRAKG GGCECPEYYP NCEVVFMGMA NIHSIRRSFQ SLRLLCTQMP DPGNWLSALE STKWLHHLSV LLKSALLVVH AVDQDQRPVL VHCSDGWDRT PQIVALAKLL LDPYYRTIEG FQVLVEMEWL DFGHKFADRC GHGENSDDLN ERCPVFLQWL DCVHQLQRQF PCSFEFNEAF LVKLVQHTYS CLFGTFLCNN AKERGEKHTQ ERTCSVWSLL RAGNKAFKNL LYSSQSEAVL YPVCHVRNLM LWSAVYLPCP SPTTPVDDSC APYPAPGTSP DDPPLSRLPK TRSYDNLTTA CDNTVPLASR RCSDPSLNEK WQEHRRSLEL SSLAGPGEDP LSADSLGKPT RVPGGAELSV AAGVAEGQME NILQEATKEE SGVEEPAHRA GIEIQEGKED PLLEKESRRK TPEASAIGLH QDPELGDAAL RSHLDMSWPL FSQGISEQQS GLSVLLSSLQ VPPRGEDSLE VPVEQFRIEE IAEGREEAVL PIPVDAKVGY GTSQSCSLLP SQVPFETRGP NVDSSTDMLV EDKVKSVSGP QGHHRSCLVN SGKDRLPQTM EPSPSETSLV ERPQVGSVVH RTSLGSTLSL TRSPCALPLA ECKEGLVCNG APETENRASE QPPGLSTLQM YPTPNGHCAN GEAGRSKDSL SRQLSAMSCS SAHLHSRNLH HKWLHSHSGR PSATSSPDQP SRSHLDDDGM SVYTDTIQQR LRQIESGHQQ EVETLKKQVQ ELKSRLESQY LTSSLHFNGD FGDEVTSIPD SESNLDQNCL SRCSTEIFSE ASWEQVDKQD TEMTRWLPDH LAAHCYACDS AFWLASRKHH CRNCGNVFCS SCCNQKVPVP SQQLFEPSRV CKSCYSSLHP TSSSIDLELD KPIAATSN //