MTMR2_BOVIN
ID MTMR2_BOVIN Reviewed; 643 AA.
AC A6QLT2;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Myotubularin-related protein 2;
DE AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
DE EC=3.1.3.95 {ECO:0000250|UniProtKB:Q13614};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase;
DE EC=3.1.3.64 {ECO:0000250|UniProtKB:Q13614};
GN Name=MTMR2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphatase that acts on lipids with a phosphoinositol
CC headgroup. Has phosphatase activity towards phosphatidylinositol 3-
CC phosphate and phosphatidylinositol 3,5-bisphosphate (By similarity).
CC Binds phosphatidylinositol 4-phosphate, phosphatidylinositol 5-
CC phosphate, phosphatidylinositol 3,5-bisphosphate and
CC phosphatidylinositol 3,4,5-trisphosphate. Stabilizes SBF2/MTMR13 at the
CC membranes. Specifically in peripheral nerves, stabilizes SBF2/MTMR13
CC protein (By similarity). {ECO:0000250|UniProtKB:Q13614,
CC ECO:0000250|UniProtKB:Q9Z2D1}.
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:Q13614};
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:0000250|UniProtKB:Q13614};
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:0000250|UniProtKB:Q13614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC bisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45632,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78911,
CC ChEBI:CHEBI:85342; Evidence={ECO:0000250|UniProtKB:Q13614};
CC -!- ACTIVITY REGULATION: Interaction with SBF1/MTMR5 increases phosphatase
CC activity. {ECO:0000250|UniProtKB:Q13614}.
CC -!- SUBUNIT: Homodimer (via coiled-coil domain). Heterotetramer consisting
CC of one MTMR2 dimer and one SBF2/MTMR13 dimer. Heterodimer with
CC SBF1/MTMR5. Heterodimer with MTMR12. {ECO:0000250|UniProtKB:Q13614}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13614}. Early
CC endosome membrane {ECO:0000250|UniProtKB:Q13614}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q13614}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q13614}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9Z2D1}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q9Z2D1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q13614}. Note=Partly associated with membranes
CC (By similarity). Localizes to vacuoles in hypo-osmotic conditions (By
CC similarity). {ECO:0000250|UniProtKB:Q13614,
CC ECO:0000250|UniProtKB:Q9Z2D1}.
CC -!- DOMAIN: The coiled-coil domain mediates homodimerization. Also mediates
CC interaction with SBF1/MTMR5 (By similarity). By mediating MTMR2
CC homodimerization, indirectly involved in SBF2/MTMR13 and MTMR2
CC heterotetramerization (By similarity). {ECO:0000250|UniProtKB:Q13614,
CC ECO:0000250|UniProtKB:Q9Z2D1}.
CC -!- DOMAIN: The GRAM domain mediates binding to phosphatidylinositol 4-
CC phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,5-
CC bisphosphate and phosphatidylinositol 3,4,5-trisphosphate.
CC {ECO:0000250|UniProtKB:Q9Z2D1}.
CC -!- PTM: Phosphorylation at Ser-58 decreases MTMR2 localization to
CC endocytic vesicular structures. {ECO:0000250|UniProtKB:Q13614}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
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DR EMBL; BC148076; AAI48077.1; -; mRNA.
DR RefSeq; NP_001095664.1; NM_001102194.1.
DR AlphaFoldDB; A6QLT2; -.
DR SMR; A6QLT2; -.
DR STRING; 9913.ENSBTAP00000022028; -.
DR PaxDb; A6QLT2; -.
DR Ensembl; ENSBTAT00000071612; ENSBTAP00000073339; ENSBTAG00000016557.
DR GeneID; 536810; -.
DR KEGG; bta:536810; -.
DR CTD; 8898; -.
DR VEuPathDB; HostDB:ENSBTAG00000016557; -.
DR VGNC; VGNC:31741; MTMR2.
DR eggNOG; KOG4471; Eukaryota.
DR GeneTree; ENSGT00940000153669; -.
DR HOGENOM; CLU_001839_4_1_1; -.
DR InParanoid; A6QLT2; -.
DR OMA; ESYAICD; -.
DR OrthoDB; 824298at2759; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000016557; Expressed in spermatocyte and 108 other tissues.
DR ExpressionAtlas; A6QLT2; baseline and differential.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:Ensembl.
DR GO; GO:0032288; P:myelin assembly; IEA:Ensembl.
DR GO; GO:0031642; P:negative regulation of myelination; IEA:Ensembl.
DR GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISS:UniProtKB.
DR GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; IEA:Ensembl.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR10807; PTHR10807; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00568; GRAM; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Coiled coil; Cytoplasm; Endosome; Hydrolase;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..643
FT /note="Myotubularin-related protein 2"
FT /id="PRO_0000356227"
FT DOMAIN 68..139
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 205..580
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 593..627
FT /evidence="ECO:0000255"
FT COMPBIAS 19..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 417
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 330..333
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 355..356
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 417..423
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2D1"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2D1"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
SQ SEQUENCE 643 AA; 73348 MW; 0BF63C1A07DA9895 CRC64;
MEKSSSCESL GSQPAVARPP SVDSLSSAST SHSENSVHTK SASVVSSDSI STSAENFSPD
LRVLRESNKL AEMEEPPLLP GENIKDMAKD VTYICPFTGA VRGTLTVTNY RLYFKSMERD
PPFVLDASLG VISRVEKIGG ASSRGENSYG LETVCKDIRN LRFAHKPEGR TRRSIFENLM
KYAFPVSNNL SLFAFEYKEV FPENGWKLYD SLSEYRRQGI PNESWRITKV NERYELCDTY
PALLVVPANI PDEELKRVAS FRSRGRIPVL SWIHPESQAT ITRCSQPMVG VSGKRSKEDE
KYLQAIMDSN AQSHKIFIFD ARPSVNAVAN KAKGGGYESE DAYQNAELVF LDIHNIHVMR
ESLRKLKEIV YPNIEETHWL SNLESTHWLE HIKLILAGAL RIADRVESGK TSVVVHCSDG
WDRTAQLTSL AMLMLDGYYR TIRGFEVLVE KEWLSFGHRF QLRVGHGDKN HADADRSPVF
LQFIDCVWQM TRQFPTAFEF NEYFLITILD HLYSCLFGTF LCNSEQQRGK ENLPRRTVSL
WSYINSQLED FTNPLYGSYS NHVLYPVASM RHLELWVGYY VRWNPRMKPQ EPIHNRYKEL
LAKRAELQKK VEELQREISN RSTSSSERAG SPAQCVTPVQ TVV
