MTMRD_MOUSE
ID MTMRD_MOUSE Reviewed; 1872 AA.
AC E9PXF8; E9Q305; Q8BJ67; Q8BJD2; Q8BJP4; Q91VH0;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Myotubularin-related protein 13 {ECO:0000305};
DE AltName: Full=Inactive phosphatidylinositol 3-phosphatase 13 {ECO:0000305};
DE AltName: Full=SET-binding factor 2 {ECO:0000312|MGI:MGI:1921831};
GN Name=Sbf2 {ECO:0000312|MGI:MGI:1921831};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000312|EMBL:BAC39860.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-700 (ISOFORMS 1/2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1288-1872 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC39860.1};
RC TISSUE=Eye {ECO:0000312|EMBL:BAC39860.1};
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 [3] {ECO:0000312|EMBL:AAH15069.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1022-1872 (ISOFORM 2).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH15069.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH15069.1};
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 [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16750429; DOI=10.1016/j.modgep.2006.04.005;
RA Kirfel J., Senderek J., Moser M., Roeper A., Stendel C., Bergmann C.,
RA Zerres K., Buettner R.;
RT "Cloning, expression and characterization of the murine orthologue of SBF2,
RT the gene mutated in Charcot-Marie-Tooth disease type 4B2.";
RL Gene Expr. Patterns 6:978-984(2006).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MTMR2, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DOMAIN.
RX PubMed=16399794; DOI=10.1093/hmg/ddi473;
RA Berger P., Berger I., Schaffitzel C., Tersar K., Volkmer B., Suter U.;
RT "Multi-level regulation of myotubularin-related protein-2 phosphatase
RT activity by myotubularin-related protein-13/set-binding factor-2.";
RL Hum. Mol. Genet. 15:569-579(2006).
RN [6] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17855448; DOI=10.1093/hmg/ddm257;
RA Tersar K., Boentert M., Berger P., Bonneick S., Wessig C., Toyka K.V.,
RA Young P., Suter U.;
RT "Mtmr13/Sbf2-deficient mice: an animal model for CMT4B2.";
RL Hum. Mol. Genet. 16:2991-3001(2007).
RN [7] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18349142; DOI=10.1073/pnas.0800742105;
RA Robinson F.L., Niesman I.R., Beiswenger K.K., Dixon J.E.;
RT "Loss of the inactive myotubularin-related phosphatase Mtmr13 leads to a
RT Charcot-Marie-Tooth 4B2-like peripheral neuropathy in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:4916-4921(2008).
RN [8] {ECO:0007744|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [9] {ECO:0000305}
RP INTERACTION WITH PIK3C2A, AND TISSUE SPECIFICITY.
RX PubMed=22648168; DOI=10.1091/mbc.e12-05-0375;
RA Jean S., Cox S., Schmidt E.J., Robinson F.L., Kiger A.;
RT "Sbf/MTMR13 coordinates PI(3)P and Rab21 regulation in endocytic control of
RT cellular remodeling.";
RL Mol. Biol. Cell 23:2723-2740(2012).
RN [10] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23297362; DOI=10.1093/hmg/dds562;
RA Ng A.A., Logan A.M., Schmidt E.J., Robinson F.L.;
RT "The CMT4B disease-causing phosphatases Mtmr2 and Mtmr13 localize to the
RT Schwann cell cytoplasm and endomembrane compartments, where they depend
RT upon each other to achieve wild-type levels of protein expression.";
RL Hum. Mol. Genet. 22:1493-1506(2013).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) which activates
CC RAB21 and possibly RAB28 (By similarity). Promotes the exchange of GDP
CC to GTP, converting inactive GDP-bound Rab proteins into their active
CC GTP-bound form (By similarity). In response to starvation-induced
CC autophagy, activates RAB21 which in turn binds to and regulates SNARE
CC protein VAMP8 endolysosomal transport required for SNARE-mediated
CC autophagosome-lysosome fusion (By similarity). Acts as an adapter for
CC the phosphatase MTMR2 (PubMed:16399794). Increases MTMR2 catalytic
CC activity towards phosphatidylinositol 3,5-bisphosphate and to a lesser
CC extent towards phosphatidylinositol 3-phosphate (PubMed:16399794).
CC {ECO:0000250|UniProtKB:Q86WG5, ECO:0000269|PubMed:16399794}.
CC -!- SUBUNIT: Homodimer (PubMed:16399794). Heterotetramer consisting of one
CC MTMR2 dimer and one SBF2/MTMR13 dimer (PubMed:16399794). Interacts with
CC class II PI3-kinase PIK3C2A (PubMed:22648168). Interacts (via DENN
CC domain) with RAB21 (in GDP-bound form) in response to starvation; the
CC interaction activates RAB21 (By similarity). Interacts with VAMP8 in
CC response to starvation (By similarity). {ECO:0000250|UniProtKB:Q86WG5,
CC ECO:0000269|PubMed:16399794, ECO:0000269|PubMed:22648168}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16399794,
CC ECO:0000269|PubMed:16750429, ECO:0000269|PubMed:23297362}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:16750429}. Membrane
CC {ECO:0000250|UniProtKB:Q86WG5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q86WG5}. Endosome membrane
CC {ECO:0000269|PubMed:23297362}; Peripheral membrane protein
CC {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:23297362}.
CC Note=Associated with membranes (By similarity). Localizes to vacuoles
CC in hypo-osmotic conditions (PubMed:16399794). Membrane localization is
CC likely to be mediated via its interaction with MTMR2 (PubMed:23297362).
CC {ECO:0000250|UniProtKB:Q86WG5, ECO:0000269|PubMed:16399794,
CC ECO:0000269|PubMed:23297362}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305};
CC IsoId=E9PXF8-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=E9PXF8-2; Sequence=VSP_060070;
CC -!- TISSUE SPECIFICITY: Expressed in sciatic nerve and in Schwann cells (at
CC protein level) (PubMed:16750429, PubMed:16399794, PubMed:17855448,
CC PubMed:18349142, PubMed:23297362). Expressed in brain (at protein
CC level) (PubMed:18349142, PubMed:22648168). Highly expressed in brain,
CC heart, kidney and testis, and to a lesser extent in lung, stomach,
CC small intestine, skeletal muscle, liver and placenta (PubMed:16750429).
CC Expressed in spinal cord and eye (PubMed:16750429). Not expressed in
CC thymus and spleen (PubMed:16750429). {ECO:0000269|PubMed:16399794,
CC ECO:0000269|PubMed:16750429, ECO:0000269|PubMed:17855448,
CC ECO:0000269|PubMed:18349142, ECO:0000269|PubMed:22648168,
CC ECO:0000269|PubMed:23297362}.
CC -!- DEVELOPMENTAL STAGE: In 9 dpc embryos, strongly expressed in the
CC craniofacial region, the branchial arches and in limb buds. Also
CC expressed in brain and along the neural tube. At 9 dpc and 10 dpc, no
CC expression is detected in the heart but at later stages expressed
CC weakly in the ventricle. At 11 dpc and 12 dpc, highly expressed in the
CC neural tube, limb bud, dorsal trunk and tail mesenchyme. In the brain
CC of 13 dpc embryos, highly expressed in the cortex and the dorsal spinal
CC cord and weakly in midbrain. {ECO:0000269|PubMed:16750429}.
CC -!- DOMAIN: The C-terminal domain mediates homodimerization
CC (PubMed:16399794). By mediating SBF2/MTMR13 homodimerization,
CC indirectly involved in SBF2/MTMR13 and MTMR2 homotetramerization
CC (PubMed:16399794). {ECO:0000269|PubMed:16399794}.
CC -!- DOMAIN: The GRAM domain mediates binding to phosphatidylinositol 4-
CC phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,5-
CC biphosphate and phosphatidylinositol 3,4,5-trisphosphate.
CC {ECO:0000269|PubMed:16399794}.
CC -!- DOMAIN: The PH domain binds preferentially phosphatidylinositol 3,4,5-
CC trisphosphate (PubMed:16399794). Appears to be dispensable for
CC localization to membranes (PubMed:23297362).
CC {ECO:0000269|PubMed:16399794, ECO:0000269|PubMed:23297362}.
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate
CC (PubMed:18349142). Display demyelinating peripheral neuropathy
CC characterized by slowed nerve conduction velocity, axon degeneration,
CC and myelin outfolding and infolding in motor and sensory peripheral
CC nerves (PubMed:17855448, PubMed:18349142, PubMed:23297362). Defects in
CC myelination start to appear at postnatal day 3 (P3) (PubMed:23297362).
CC The neuropathy severity increases with age (PubMed:17855448,
CC PubMed:23297362). {ECO:0000269|PubMed:17855448,
CC ECO:0000269|PubMed:18349142, ECO:0000269|PubMed:23297362}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000255}.
CC -!- CAUTION: Although it belongs to the non-receptor class myotubularin
CC subfamily, lacks the conserved active site cysteine residue at position
CC 1433 in the dsPTPase catalytic loop, suggesting that it has no
CC phosphatase activity. {ECO:0000305}.
CC -!- CAUTION: MTMR2 protein levels are decreased in sciatic nerves but not
CC in the brain (PubMed:18349142, PubMed:23297362). However, MTMR2 protein
CC levels have also been shown not to be affected in sciatic nerves
CC (PubMed:17855448). {ECO:0000269|PubMed:17855448,
CC ECO:0000269|PubMed:18349142, ECO:0000269|PubMed:23297362}.
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DR EMBL; AC122921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK029568; BAC26517.1; -; mRNA.
DR EMBL; AK080952; BAC38090.1; -; mRNA.
DR EMBL; AK087396; BAC39860.1; -; mRNA.
DR EMBL; BC015069; AAH15069.1; -; mRNA.
DR CCDS; CCDS52361.1; -. [E9PXF8-1]
DR RefSeq; NP_796298.2; NM_177324.2. [E9PXF8-1]
DR RefSeq; XP_006507989.1; XM_006507926.1. [E9PXF8-2]
DR AlphaFoldDB; E9PXF8; -.
DR SMR; E9PXF8; -.
DR IntAct; E9PXF8; 1.
DR STRING; 10090.ENSMUSP00000033058; -.
DR iPTMnet; E9PXF8; -.
DR PhosphoSitePlus; E9PXF8; -.
DR SwissPalm; E9PXF8; -.
DR jPOST; E9PXF8; -.
DR MaxQB; E9PXF8; -.
DR PaxDb; E9PXF8; -.
DR PeptideAtlas; E9PXF8; -.
DR PRIDE; E9PXF8; -.
DR ProteomicsDB; 346740; -.
DR ProteomicsDB; 347539; -. [E9PXF8-1]
DR Antibodypedia; 24321; 42 antibodies from 11 providers.
DR DNASU; 319934; -.
DR Ensembl; ENSMUST00000033058; ENSMUSP00000033058; ENSMUSG00000038371. [E9PXF8-1]
DR Ensembl; ENSMUST00000164759; ENSMUSP00000132072; ENSMUSG00000038371. [E9PXF8-2]
DR GeneID; 319934; -.
DR KEGG; mmu:319934; -.
DR UCSC; uc009jfe.2; mouse. [E9PXF8-1]
DR CTD; 81846; -.
DR MGI; MGI:1921831; Sbf2.
DR VEuPathDB; HostDB:ENSMUSG00000038371; -.
DR eggNOG; KOG1090; Eukaryota.
DR eggNOG; KOG4471; Eukaryota.
DR GeneTree; ENSGT00940000155385; -.
DR HOGENOM; CLU_002298_1_1_1; -.
DR InParanoid; E9PXF8; -.
DR OMA; QQFWEDA; -.
DR OrthoDB; 45015at2759; -.
DR PhylomeDB; E9PXF8; -.
DR TreeFam; TF318583; -.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 319934; 0 hits in 60 CRISPR screens.
DR ChiTaRS; Sbf2; mouse.
DR PRO; PR:E9PXF8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; E9PXF8; protein.
DR Bgee; ENSMUSG00000038371; Expressed in paneth cell and 263 other tissues.
DR ExpressionAtlas; E9PXF8; baseline and differential.
DR Genevisible; E9PXF8; MM.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IDA:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0019902; F:phosphatase binding; IPI:MGI.
DR GO; GO:0019208; F:phosphatase regulator activity; IDA:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:MGI.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR CDD; cd13339; PH-GRAM_MTMR13; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.40.50.11500; -; 1.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR030567; MTMR13.
DR InterPro; IPR037823; MTMR13_PH-GRAM.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR022096; SBF1/SBF2.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR005113; uDENN_dom.
DR PANTHER; PTHR10807; PTHR10807; 1.
DR PANTHER; PTHR10807:SF4; PTHR10807:SF4; 1.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF12335; SBF2; 1.
DR Pfam; PF03456; uDENN; 1.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00568; GRAM; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00800; uDENN; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50211; DENN; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cell projection; Cytoplasm; Endosome;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1872
FT /note="Myotubularin-related protein 13"
FT /id="PRO_0000446366"
FT DOMAIN 7..172
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 191..324
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 326..427
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 869..1004
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 1106..1607
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT DOMAIN 1766..1870
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1652..1705
FT /note="Required for homodimerization and interaction with
FT MTMR2"
FT /evidence="ECO:0000250|UniProtKB:Q86WG5,
FT ECO:0000269|PubMed:16399794"
FT REGION 1697..1720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WG5"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WG5"
FT VAR_SEQ 1263..1287
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_060070"
FT CONFLICT 300
FT /note="I -> F (in Ref. 2; BAC39860)"
FT /evidence="ECO:0000305"
FT CONFLICT 1496
FT /note="L -> F (in Ref. 3; AAH15069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1872 AA; 210458 MW; F3D86BAEA404F561 CRC64;
MARLADYFIV VGYDHEKPAG PGEGLGKIIQ RFPQQDWDDT PFPQGIELFC QPGGWHLSRE
RKQPTFFVVV LTDIDSDRHY CSCLTFYEAE INLQGTKKEE IEGEEVSGLI QPAEVFAPKS
LVLVSRLDYP EIFRACLGLI YTVYVDSMSV SLESLIANLC ACLVPAAGGS QKLFSLGAGD
RQLIQTPLHD SLPVTGTSVA LLFQQLGIQN VLNLFCAVLT ENKVLFHSAS FQRLSDACRA
LESLMFPLKY SYPYIPILPA QLLEVLSSPT PFIIGVHSIF KTDVHELLDV IIADLDGGTI
KIPECIHLSS LPEPLLHQTQ SALSLILHPD LEVADHAFPP PRTALSHSKM LDKEVRAVFL
RLFAQLFQGY RSCLQLIRIH AEPVIHFHKT AFLGQRGLVE NDFLTKVLNG MAFAGFVSER
GPPYRACDLF DELVAFEVER IKVEEKNPLK MIKHIRELAE QLFKNENPNP HMAFQKVPRP
TEGSHLRVHI LPFPKINEAR VQELIQENLA KNQNAPPATR IEKKCVVPAG PPVVSIMEKV
ITVFNSAQRL EVVRNCISFI FENKTLETEK TLPAALRALK GKAARQCLTD ELGLHVQQNR
AILDHQQFDY IIRMMNCTLQ DCSSLEEYNI AAALLPLTSA FYRKLAPGVS QFAYTCVQDH
PIWTNQQFWE TTFYNAVQEQ VRSLYLSAKD DNHIPHLKQK LPDGQHQEKT AMDLAAEQLR
LWPTLSKSTQ QELVQHEEST VFSQAIHFAN LMVNLLVPLD TSKNKLLRAS APGDWESGSN
SIVTNSIAGS VAESYDTESG FEDSENSDVA NSVVRFIARF IDKVCTESGV TQDHIRSLHC
MIPGIVAMHI ETLEAVHRES RRLPPIQKPK ILRPALLPGE EIVCEGLRVL LDPDGREEAT
GGLLGGPQLL PAEGALFLTT YRILFRGTPH DQLVGEQTVV RSFPIASITK EKKITMQNQL
QQSVQEGLQI TSASFQLIKV AFDEEVSPEV VDIFKKQLMK FRYPQSIFST FAFAAGQTTP
QIILPKQKEK NTSFRTFSKT IVKGAKKAGK MTIGRQYLLK KRTGTIVEER VNRPGWNEED
DISVSDDSEL PTSTTLKASE KSTMEQLVEK ACFRDYQRLG LGTISGNSSR SKPEYFRVTA
SNRLYSLCRS YPGLLVIPQA VQDSSLPRVA RCYRHNRLPV VCWKNSRSGT LLLRSGGFHG
KGVVGLFKSQ NSPQAVSTSS LESSSSIEQE KYLQALLTAV IVHQKLRGSS TLTVRPALAL
SPVHGYRDKS FTQSNPKSSA KEPVHNQGVW ASLRSSTRLI SSPTSFIDVG ARLAGKDHSA
SFSNSTYLQN QLLKRQAALY IFGEKSQLRS SKVEFAFNCE FVPVEFHEIR QVKASFKKLM
RACIPSTIPT DSEVTFLKAL GDSEWFPQLH RIMQLAVVVS EVLENGSSVW VCLEEGWDIT
TQVTSLAQLL SDPFYRTIAG FRTLVEKEWL SFGHKFSQRS SLALNSQGGG FAPIFLQFLD
CVHQVHNQYP TEFEFNLYYL KFLAFHYVSN RFKTFLLDSD YERLEHGTLF DDKGDKHAKK
GVCIWECIDK MHTRSPIFFN YLYSPVEVEA LKPNVNVSSL KKWDYYTEET LSAGPSYDWM
MLTPKHFPYE ESDVAGGAGP QSQRKTVWPC YDDVTCSQPD ALTRLFSEIE KLEHKLNQTP
ERWHQLWEKV TTDLKEEPRT AHSLRHSAGS PGIASTNVPS YQKRPALHPL HRGLGEDQST
TTAPSNGVEH RAATLYSQYT SKNDENRSFE GTLYKRGALL KGWKPRWFVL DVTKHQLRYY
DSGEDTSCKG HIDLAEVEMV IPAGPSMGAP KYTSDKAFFD LKTSKRVYNF CAQDGQSAQQ
WMDRIQSCIS DA
