A6QLT4

PR
Gene name
MTM1
Protein name
Myotubularin
Names
Phosphatidylinositol-3,5-bisphosphate 3-phosphatase, Phosphatidylinositol-3-phosphate phosphatase
Species
Bos taurus (Bovine)
KEGG Pathway
bta:533622
EC number
3.1.3.64: Phosphoric monoester hydrolases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-55 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for A6QLT4

Entry ID Method Resolution Chain Position Source
AF-A6QLT4-F1 Predicted AlphaFoldDB

107 variants for A6QLT4

Variant ID(s) Position Change Description Diseaes Association Provenance
rs464154323 10 N>S No EVA
rs434712706 17 E>Q No EVA
rs453166551 21 R>M No EVA
rs473576909 39 P>L No EVA
rs440114148 43 R>C No EVA
rs461836772 44 I>M No EVA
rs476466991 77 T>M No EVA
rs471349720 82 I>L No EVA
rs441481262 86 P>S No EVA
rs459983195 105 N>D No EVA
rs481592382 105 N>T No EVA
rs448669892 106 S>P No EVA
rs463465934 107 Y>* No EVA
rs481875424 112 T>A No EVA
rs445628198 113 C>S No EVA
rs464121091 114 K>N No EVA
rs473121572 118 N>I No EVA
rs461610378 119 L>P No EVA
rs479996828 120 R>M No EVA
rs443968456 120 R>S No EVA
rs444996866 135 E>D No EVA
rs478105849 135 E>G No EVA
rs460351428 146 H>D No EVA
rs471314084 149 P>Q No EVA
rs453558721 150 I>K No EVA
rs453558721 150 I>R No EVA
rs442208104 151 F>S No EVA
rs481921960 152 A>G No EVA
rs463440825 152 A>P No EVA
rs463440825 152 A>S No EVA
rs481921960 152 A>V No EVA
rs457731100 154 L>F No EVA
rs479559722 155 N>I No EVA
rs446675710 155 N>K No EVA
rs468238580 156 E>* No EVA
rs468238580 156 E>K No EVA
rs480244925 157 E>K No EVA
rs450621385 158 K>N No EVA
rs470282568 159 F>I No EVA
rs452467559 160 N>I No EVA
rs437282821 160 N>Y No EVA
rs435111517 161 V>E No EVA
rs435111517 161 V>G No EVA
rs464537421 161 V>L No EVA
rs464537421 161 V>M No EVA
rs453644908 162 D>A No EVA
rs475719152 162 D>E No EVA
rs453644908 162 D>G No EVA
rs457495945 164 W>G No EVA
rs475546868 165 T>A No EVA
rs475546868 165 T>P No EVA
rs472789266 167 Y>* No EVA
rs457691686 167 Y>F No EVA
rs461884124 169 P>R No EVA
rs439925300 169 P>S No EVA
rs480283688 172 E>* No EVA
rs467414374 189 N>T No EVA
rs479073232 232 H>P No EVA
rs464322078 265 R>S No EVA
rs454005356 306 L>F No EVA
rs472387718 327 I>L No EVA
rs442775971 345 H>Y No EVA
rs455163034 348 E>K No EVA
rs476888662 349 H>P No EVA
rs474757710 361 A>S No EVA
rs463348785 372 V>G No EVA
rs439133956 373 V>A No EVA
rs439133956 373 V>G No EVA
rs475458356 373 V>L No EVA
rs479471556 374 H>L No EVA
rs457882959 374 H>N No EVA
rs446638492 375 C>R No EVA
rs461950197 377 D>V No EVA
rs481601196 385 L>M No EVA
rs134841965 388 L>P No EVA
rs448584347 390 M>L No EVA
rs470245599 392 M>I No EVA
rs446023895 393 L>* No EVA
rs464903114 393 L>F No EVA
rs437200163 393 L>V No EVA
rs435074547 409 K>R No EVA
rs453469560 411 W>S No EVA
rs136474688 426 D>E No EVA
rs465909671 490 K>E No EVA
rs436156085 491 V>G No EVA
rs456372049 508 K>R No EVA
rs471933478 509 F>L No EVA
rs439049904 510 K>N No EVA
rs460819306 517 E>* No EVA
rs479276342 521 V>A No EVA
rs461010428 537 Y>F No EVA
rs482758120 542 N>T No EVA
rs481465280 549 Q>K No EVA
rs448448550 553 V>L No EVA
rs470530037 559 E>* No EVA
rs437472004 563 L>V No EVA
rs452764581 568 I>S No EVA
rs464776593 575 Q>P No EVA
rs434953477 578 N>I No EVA
rs474671792 587 A>S No EVA
rs441648132 588 S>P No EVA
rs456768787 591 S>R No EVA
rs475535279 595 M>L No EVA
rs439446394 599 V>G No EVA
rs479678746 600 Q>* No EVA
rs440145878 601 T>P No EVA
rs479259034 602 H>P No EVA

No associated diseases with A6QLT4

2 regional properties for A6QLT4

Type Name Position InterPro Accession
domain Alpha/beta hydrolase fold-1 166 - 430 IPR000073
conserved_site AB hydrolase 4, conserved site 354 - 395 IPR000952

Functions

Description
EC Number 3.1.3.64 Phosphoric monoester hydrolases
Subcellular Localization
  • Cytoplasm
  • Cell membrane ; Peripheral membrane protein
  • Cell projection, filopodium
  • Cell projection, ruffle
  • Late endosome
  • Cytoplasm, myofibril, sarcomere
  • Localizes as a dense cytoplasmic network
  • Also localizes to the plasma membrane, including plasma membrane extensions such as filopodia and ruffles
  • Predominantly located in the cytoplasm following interaction with MTMR12
  • Recruited to the late endosome following EGF stimulation (By similarity)
  • In skeletal muscles, co-localizes with MTMR12 in the sarcomere (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
filopodium Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft.
I band A region of a sarcomere that appears as a light band on each side of the Z disc, comprising a region of the sarcomere where thin (actin) filaments are not overlapped by thick (myosin) filaments; contains actin, troponin, and tropomyosin; each sarcomere includes half of an I band at each end.
late endosome A prelysosomal endocytic organelle differentiated from early endosomes by lower lumenal pH and different protein composition. Late endosomes are more spherical than early endosomes and are mostly juxtanuclear, being concentrated near the microtubule organizing center.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
ruffle Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork.

5 GO annotations of molecular function

Name Definition
intermediate filament binding Binding to an intermediate filament, a distinct elongated structure, characteristically 10 nm in diameter, that occurs in the cytoplasm of higher eukaryotic cells. Intermediate filaments form a fibrous system, composed of chemically heterogeneous subunits and involved in mechanically integrating the various components of the cytoplasmic space.
phosphatidylinositol binding Binding to an inositol-containing glycerophospholipid, i.e. phosphatidylinositol (PtdIns) and its phosphorylated derivatives.
phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O = a 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate + 2 H+.
phosphatidylinositol-3-phosphatase activity Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + phosphate.
phosphoprotein phosphatase activity Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cellular proteins and thereby provide an important mechanism for regulating cellular activity.

19 GO annotations of biological process

Name Definition
autophagosome assembly The formation of a double membrane-bounded structure, the autophagosome, that occurs when a specialized membrane sac, called the isolation membrane, starts to enclose a portion of the cytoplasm.
endosome to lysosome transport The directed movement of substances from endosomes to lysosomes.
intermediate filament organization Control of the spatial distribution of intermediate filaments; includes organizing filaments into meshworks, bundles, or other structures, as by cross-linking.
mitochondrion distribution Any process that establishes the spatial arrangement of mitochondria between and within cells.
mitochondrion morphogenesis The process in which the anatomical structures of a mitochondrion are generated and organized.
muscle cell cellular homeostasis The cellular homeostatic process that preserves a muscle cell in a stable functional or structural state.
negative regulation of autophagosome assembly Any process that stops, prevents or reduces the frequency, rate or extent of autophagosome assembly.
negative regulation of proteasomal ubiquitin-dependent protein catabolic process Any process that stops, prevents, or reduces the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
negative regulation of protein kinase B signaling Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B.
negative regulation of TOR signaling Any process that stops, prevents, or reduces the frequency, rate or extent of TOR signaling.
phosphatidylinositol dephosphorylation The process of removing one or more phosphate groups from a phosphatidylinositol.
positive regulation of skeletal muscle tissue growth Any process that activates, maintains or increases the rate of skeletal muscle growth.
proteasome-mediated ubiquitin-dependent protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
protein dephosphorylation The process of removing one or more phosphoric residues from a protein.
protein kinase B signaling A series of reactions, mediated by the intracellular serine/threonine kinase protein kinase B (also called AKT), which occurs as a result of a single trigger reaction or compound.
protein transport The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
regulation of vacuole organization Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of a vacuole.
skeletal muscle tissue growth The increase in size or mass of a skeletal muscle. This may be due to a change in the fiber number or size.
TOR signaling The series of molecular signals mediated by TOR (Target of rapamycin) proteins, members of the phosphoinositide (PI) 3-kinase related kinase (PIKK) family that act as serine/threonine kinases in response to nutrient availability or growth factors.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q13496 MTM1 Myotubularin Homo sapiens (Human) PR
Q9Z2C5 Mtm1 Myotubularin Mus musculus (Mouse) PR
Q5EB32 mtm1 Myotubularin Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
10 20 30 40 50 60
MASAPTSKYN SHSLENESIK RTSRDGVNRD VGETLPRLPG EIRITDKEVI YICPFNGPIK
70 80 90 100 110 120
GRVYITNYRL YLRSLETDSA LILDVPLGVI SRIEKMGGAT SRGENSYGLD ITCKDLRNLR
130 140 150 160 170 180
FALKQEGHSR RDMFEILTRY AFPLAHSLPI FAFLNEEKFN VDGWTVYNPV EEYRRQGLPN
190 200 210 220 230 240
HHWRITFINK CYKLCDTYPA LLVVPYRASD EDLRRVATFR SRNRIPVLSW IHPENKTVIV
250 260 270 280 290 300
RCSQPLVGMS GKRNKEDERY LDVIRETNRQ VNKLTIYDAR PNVNAVANKA TGGGYESDDV
310 320 330 340 350 360
YHNAELFFLD IHNIHVMRES LKKVKDIVYP NVEESHWLSS LESTHWLEHI KLVLTGAIQV
370 380 390 400 410 420
ADRVSSGKSS VVVHCSDGWD RTAQLTSLAM LMLDSFYRSI EGFEILVQKE WISFGHKFAS
430 440 450 460 470 480
RIGHGDKNHA DADRSPIFLQ FIDCVWQMSK QFPTAFEFNE RFLITILDHL YSCRFGTFLY
490 500 510 520 530 540
NCESAREKQK VTERTVSLWS LINSNKDKFK NPFYTKEINR VLYPVASMRH LELWVNYYIR
550 560 570 580 590 600
WNPRIKQQQP NPVEQRYMEL LALRDEYIKR LDELQLANSA KLSDPSASPS SPSQMMPHVQ
THF