Q5R9S3

PR
Gene name
MTM1
Protein name
Myotubularin
Names
Phosphatidylinositol-3,5-bisphosphate 3-phosphatase, Phosphatidylinositol-3-phosphate phosphatase
Species
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
KEGG Pathway
pon:100174495
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)

1-56 (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 Q5R9S3

Entry ID Method Resolution Chain Position Source
AF-Q5R9S3-F1 Predicted AlphaFoldDB

No variants for Q5R9S3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5R9S3

No associated diseases with Q5R9S3

4 regional properties for Q5R9S3

Type Name Position InterPro Accession
conserved_site ATP-dependent RNA helicase DEAD-box, conserved site 318 - 326 IPR000629
domain Helicase, C-terminal 408 - 560 IPR001650
domain DEAD/DEAH box helicase domain 183 - 367 IPR011545
domain Helicase superfamily 1/2, ATP-binding domain 178 - 398 IPR014001

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

6 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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.
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.
sarcomere The repeating unit of a myofibril in a muscle cell, composed of an array of overlapping thick and thin filaments between two adjacent Z discs.

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.

10 GO annotations of biological process

Name Definition
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.
phosphatidylinositol biosynthetic process The chemical reactions and pathways resulting in the formation of phosphatidylinositol, any glycophospholipid in which the sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
phosphatidylinositol dephosphorylation The process of removing one or more phosphate groups from a phosphatidylinositol.
protein dephosphorylation The process of removing one or more phosphoric residues from a protein.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MASASTSKYN SHSLENESIK RTSRDGVNRD LTEAVPRLPG ETLITDKEVI YICPFNGPIK
70 80 90 100 110 120
GRVYITNYRL YLRSLETDSA LILDVPLGVI SRIEKMGGAT SRGENSYGLD ITCKDMRNLR
130 140 150 160 170 180
FALKQEGHSR RDMFEILTRY AFPLAHSLPL FAFLNEEKFN VDGWTVYNPV EEYRRQGLPN
190 200 210 220 230 240
HHWRITFINK CYELCDTYPA PLVVPYRASD DDLRRVATFR SRNRIPVLSW IHPENKTVIV
250 260 270 280 290 300
RCSQPLVGMS GKRNKDDEKY LDVIRETNKQ ISKLTIYDAR PSVNAVANKA TGGGYESDDA
310 320 330 340 350 360
YHNAELFFLD IHNIHVMRES LKKVKDIVYP NVEESHWLSS LESTHWLEHI KLVLTGAIQV
370 380 390 400 410 420
ADKVSSGKSS VLVHCSDGWD RTAQLTSLAM LMLDSFYRSI EGFEILVQKE WISFGHKFAS
430 440 450 460 470 480
RIGHGDKNHT DADRSPIFLQ FIDCVWQMSK QFPTAFEFNE QFLIIILDHL YSCRFGTFLF
490 500 510 520 530 540
NCESARERQK VTERTVSLWS LINSNKEKFK NPFYTKEINR VLYPVASMRH LELWVNYYIR
550 560 570 580 590 600
WNPRIKQQQP NPVEQRYMEL LALRDEYIKR LEELQLANSA KLSDPPTSPS SPSQMMPHVQ
THF