Persius/hicric huggingface dataset:
MCOLN3
Mucolipin-3 also known as TRPML3 (transient receptor potential cation channel, mucolipin subfamily, member 3) is a protein that in humans is encoded by the MCOLN3 gene.  It is a member of the small family of the TRPML channels, a subgroup of the large protein family of TRP ion channels.

# Gene
In human, the MCOLN3 gene resides on the short arm of chromosome 1 at 1p22.3.  The gene is split in 12 exons, which entail the open reading frame of 1659 nucleotides.  The encoded protein, TRPML3, has 553 amino acid with a predicted molecular weight of 64 kDa.  Computational analyses of the secondary structure predict the presence of six transmembrane domains, an ion transport motif (PF00520) and a transient receptor potential motif (PS50272).
In the mouse, Mcoln3, is located on the distal end of chromosome 3 at cytogenetic band qH2.  Human and mouse TRPML3 proteins share 91% sequence identity.
All vertebrate species, for which a genomic sequence is available, harbor the MCOLN3 gene.  Homologs of MCOLN3 are also present in the genome of insects (Drosophila melanogaster), nematodes (Caenorhabditis elegans), sea urchin (Strongylocentrotus purpuratus) and lower organisms including Hydra and Dictyostelium.

# Expression

# Function
TRPML3 is an inwardly-rectifying cation channel.

# Genetics

# Phenotypes
Mutations of the MCOLN3 gene in mice result in auditory hair cell death and deafness.
MEGF10
Multiple EGF-like-domains 10 is a protein that in humans is encoded by the MEGF10 gene.
MEGF10 is a regulator of satellite cell myogenesis and interacts with Notch1 in myoblasts. It has been shown to be the cause of early-onset myopathy, areflexia, respiratory distress and dysphagia.
MEGF10 and MEGF11, have critical roles in the formation of mosaics by two retinal interneuron subtypes, starburst amacrine cells and horizontal cells in mice. These cells are less likely to be near neighbours of the same subtype than would occur by chance, resulting in 'exclusion zones' that separate them. Mosaic arrangements provide a mechanism to distribute each cell type evenly across the retina, ensuring that all parts of the visual field have access to a full set of processing elements.
MINDY4
MINDY lysine 48 deubiquitinase 4, also known as MINDY4, is a human gene.

# Predictions
The predicted molecular weight is 84,400 Daltons and pI is 6.465. pTARGET predicts the cellular location to be in the golgi apparatus with 93.9% confidence.

# Expression
Based on the human tissue Gene Expression Omnibus profile, C7orf67 shows a marked increase in expression in the teratospermia disease state.
MMACHC
Methylmalonic aciduria and homocystinuria type C protein (MMACHC) is a protein that in humans is encoded by the MMACHC gene.

# Function
The C-terminal region of the product of the MMACHC gene is similar to TonB, a bacterial protein involved in energy transduction for cobalamin uptake. The MMACHC gene product catalyzes the decyanation of cyanocobalamin as well as the dealkylation
-f alkylcobalamins including methylcobalamin and adenosylcobalamin. This function has also been attributed to cobalamin reductases. The MMACHC gene product and cobalamin reductases enable the interconversion of cyano- and alkylcobalamins.

# Clinical significance
Mutations are associated with methylmalonic acidemia.
MMADHC
Methylmalonic aciduria and homocystinuria type D protein, mitochondrial also known as MMADHC is a protein that in humans is encoded by the MMADHC gene.

# Function
This gene encodes a mitochondrial protein that is involved in an early step of vitamin B12 metabolism. Vitamin B12 (cobalamin) is essential for normal development and survival in humans.

# Clinical significance
Mutations in this gene cause methylmalonic aciduria and homocystinuria type cblD (MMADHC), a disorder of cobalamin metabolism that is characterized by decreased levels of the coenzymes adenosylcobalamin and methylcobalamin.
MMS22L
Methyl methanesulfonate-sensitivity protein 22-like also known as MMS22-like, DNA repair protein is a protein that in humans is encoded by the MMS22L gene.

# Model organisms
Model organisms have been used in the study of MMS22L function. A conditional knockout mouse line, called Mms22ltm1a(EUCOMM)Wtsi was generated as part of the International Knockout Mouse Consortium program  a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty six tests were carried out on mutant mice and two significant abnormalities were observed. No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice; no additional significant abnormalities were observed in these animals.
MOGAT2
2-Acylglycerol O-acyltransferase 2 also known as acyl-CoA:monoacylglycerol acyltransferase 2 (MGAT2) or Diacylglycerol O-acyltransferase candidate 5 (DC5)  is an enzyme that in humans is encoded by the MOGAT2 gene.
MOGAT2 and the related MOGAT3 genes are members of the acylglycerol o-acyltransferase family (DGAT2/MOGAT) and are involved in the synthesis of diacylglycerol (DAG) and triacylglycerol (TAG) from monoacylglycerol (MAG).
MOGAT2 and also MOGAT3 are single copy genes in almost all mammals. However, in ruminants both genes have undergone tandem gene expansion, indicate of evolving functionality. MOGAT2 has more than five tandemly duplicated copies in sheep with the first copy expressed in the duodenum and the last copy expressed in the skin, with no expression of any copy detected in the liver.
MRE11A
Double-strand break repair protein MRE11A is a protein that in humans is encoded by the MRE11A gene.

# Function
This gene encodes a nuclear protein involved in homologous recombination, telomere length maintenance, and DNA double-strand break repair. By itself, the protein has 3' to 5' exonuclease activity and endonuclease activity. The protein forms a complex with the RAD50 homolog; this complex is required for nonhomologous joining of DNA ends and possesses increased single-stranded DNA endonuclease and 3' to 5' exonuclease activities. In conjunction with a DNA ligase, this protein promotes the joining of noncomplementary ends in vitro using short homologies near the ends of the DNA fragments. This gene has a pseudogene on chromosome 3. Alternative splicing of this gene results in two transcript variants encoding different isoforms.

# Orthologs
Mre11, an ortholog of human MRE11A, occurs in the prokaryote archaeon Sulfolobus acidocaldarius.  In this organism the Mre11 protein interacts with the Rad50 protein and appears to have an active role in the repair of DNA damages experimentally introduced by gamma radiation.  Similarly, during meiosis in the eukaryotic protist Tetrahymena Mre11 is required for repair of DNA damages, in this case double-strand breaks, by a process that likely involves homologous recombination.  These observations suggest that human MRE11A is descended from prokaryotic and protist ancestral Mre11 proteins that served a role in early processes for repairing DNA damage.

# Overexpression in cancer
MRE11 has a role in microhomology-mediated end joining (MMEJ) repair of double strand breaks.  It is one of 6 enzymes required for this error prone DNA repair pathway.  MRE11 is over-expressed in breast cancers.
Cancers are very often deficient in expression of one or more DNA repair genes, but over-expression of a DNA repair gene is less usual in cancer.  For instance, at least 36 DNA repair enzymes, when mutationally defective in germ line cells, cause increased risk of cancer (hereditary cancer syndromes).  (Also see DNA repair-deficiency disorder.)  Similarly, at least 12 DNA repair genes have frequently been found to be epigenetically repressed in one or more cancers. (See also Epigenetically reduced DNA repair and cancer.)  Ordinarily, deficient expression of a DNA repair enzyme results in increased un-repaired DNA damages which, through replication errors (translesion synthesis), lead to mutations and cancer. However, MRE11 mediated MMEJ repair is highly inaccurate, so in this case, over-expression, rather than under-expression, apparently leads to cancer.

# Interactions
MRE11A has been shown to interact with:
- ATM,
- BRCA1,
- Ku70,
- MDC1,
- NBN,
- Rad50,  and
- TERF2.
MT-ND5
NADH-ubiquinone oxidoreductase chain 5 is a protein that in humans is encoded by the mitochondrial gene MT-ND5. The ND5 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain. Variations in MT-ND5 are associated with mitochondrial encephalomyopathy, lactic acidosis, and stroke-like episodes (MELAS) as well as some symptoms of Leigh's syndrome and Leber's hereditary optic neuropathy (LHON).

# Structure
MT-ND5 is located in mitochondrial DNA from base pair 12,337 to 14,148. The MT-ND5 gene produces a 67 kDa protein composed of 603 amino acids. MT-ND5 is one of seven mitochondrially-encoded subunits of the enzyme NADH dehydrogenase (ubiquinone). Also known as Complex I, it is the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centres and the NADH binding site. MT-ND5 and the rest of the mitochondrially encoded subunits are the most hydrophobic of the subunits of Complex I and form the core of the transmembrane region.

# Function
MT-ND5 is a subunit of the respiratory chain Complex I that is believed to belong to the minimal assembly of core proteins required to catalyze NADH dehydrogenation and electron transfer to ubiquinone (coenzyme Q10). Initially, NADH binds to Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2. The electrons are transferred through a series of iron-sulfur (Fe-S) clusters in the prosthetic arm and finally to coenzyme Q10 (CoQ), which is reduced to ubiquinol (CoQH2). The flow of electrons changes the redox state of the protein, resulting in a conformational change and pK shift of the ionizable side chain, which pumps four hydrogen ions out of the mitochondrial matrix.

# Clinical Significance
A small percentage of mitochondrial encephalomyopathy, lactic acidosis, and stroke-like episodes (MELAS) are caused by a G>A mutation at base pair 13513 in the MT-ND5 gene. Mutations in the MT-ND5 gene cause impaired Complex I function of the mitochondrial electron transport system, impairing those tissues that require significant energy input, such as the brain and muscles. Cardiac and renal involvement as well as symptoms such as myopathy and lactic acidosis can also be observed. Those with MT-ND5 mutations can display the major features of MELAS and MERRF in some patients, as well as symptoms of Leigh's syndrome and/or Leber's hereditary optic neuropathy (LHON) in others.

# Interactions
MT-ND5 interacts with Glutamine synthetase (GLUL), LIG4 and YME1L1.
MT-TL1
Mitochondrially encoded tRNA leucine 1 (UUA/G) also known as MT-TL1 is a transfer RNA which in humans is encoded by the mitochondrial MT-TL1 gene.

# Structure
The MT-TL1 gene is located on the p arm of the mitochondrial DNA at position 12 and it spans 75 base pairs. The structure of a tRNA molecule is a distinctive folded structure which contains three hairpin loops and resembles a three-leafed clover.

# Function
MT-TL1 is a small 75 nucleotide RNA (human mitochondrial map position 3230-3304) that transfers the amino acid leucine to a growing polypeptide chain at the ribosome site of protein synthesis during translation.

# Clinical significance

## Mitochondrial encephalomyopathy, lactic acidosis, and stroke-like episodes
Mutations in MT-TL1 can result in multiple mitochondrial deficiencies and associated disorders. It is associated with mitochondrial encephalomyopathy, lactic acidosis, and stroke-like episodes (MELAS). MELAS is a rare mitochondrial disorder known to affect many parts of the body, especially the nervous system and the brain. Symptoms of MELAS include recurrent severe headaches, muscle weakness (myopathy), hearing loss, stroke-like episodes with a loss of consciousness, seizures, and other problems affecting the nervous system. A common mutation is A3243G. This mutation has been theorized to be associated with several other mitochondrial diseases, including diabetes mellitus and deafness. Diabetes mellitus and deafness is characterized by diabetes combined with hearing loss, particularly of high pitches. Additional symptoms includemuscle weakness (myopathy) and various problems with a patient's eyes, heart, or kidneys.

## Complex I deficiency
MT-TP mutations may result in complex I deficiency of the mitochondrial respiratory chain, which may cause a wide variety of signs and symptoms affecting many organs and systems of the body, particularly the nervous system, the heart, and the muscles used for movement (skeletal muscles). These signs and symptoms can appear at any time from birth to adulthood. Phenotypes of the condition include encephalopathy, epilepsy, dystonia, hypotonia, myalgia, exercise intolerance, and more. A 3302A>G mutation has been found in a patient with the deficiency.
MT-TL2
Mitochondrially encoded tRNA leucine 2 (CUN) also known as MT-TL2 is a transfer RNA which in humans is encoded by the mitochondrial MT-TL2 gene.

# Function
MT-TL2 is a small 71 nucleotide RNA (human mitochondrial map position 12266-12336) that transfers the amino acid leucine to a growing polypeptide chain at the ribosome site of protein synthesis during translation.

# Structure
The MT-TL2 gene is located on the p arm of the mitochondrial DNA at position 12 and it spans 75 base pairs. The structure of a tRNA molecule is a distinctive folded structure which contains three hairpin loops and resembles a three-leafed clover.

# Clinical significance
Mutations in MT-TL2 can result in multiple mitochondrial deficiencies and associated disorders, including cardiopathy, myopathy, and encephalomyopathy. A patient with a mutation G12315A was found with encephalomyopathy with ragged-red muscle fibers. A patient with a mutation of A12320G exhibited mitochondrial myopathy, and showed signs of mitochondrial myopathy. In addition, multiple individuals with a T12297C substitution showed signs of cardiomyopathy accompanied with varying degrees.
MT-TL2 mutations have also been associated with complex IV deficiency of the mitochondrial respiratory chain, also known as the cytochrome c oxidase deficiency. Cytochrome c oxidase deficiency is a rare genetic condition that can affect multiple parts of the body, including skeletal muscles, the heart, the brain, or the liver. Common clinical manifestations include myopathy, hypotonia, and encephalomyopathy, lactic acidosis, and hypertrophic cardiomyopathy. A patient with a 12316G>A mutation in MT-TL2 was found with the deficiency.
MTRF1L
Mitochondrial translational release factor 1-like is a protein that in humans is encoded by the MTRF1L gene.
Mitochondrial DNA encodes 13 proteins that play essential roles in the respiratory chain, while all proteins involved in mitochondrial translation are encoded by nuclear genes that are imported from the cytoplasm. MTRF1L is a nuclear-encoded protein that functions as a releasing factor that recognizes termination codons and releases mitochondrial ribosomes from the synthesized protein (summary by Nozaki et al., 2008 )..

# Model organisms
Model organisms have been used in the study of MTRF1L function. A conditional knockout mouse line, called Mtrf1ltm1a(KOMP)Wtsi was generated as part of the International Knockout Mouse Consortium program  a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists  at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty six tests were carried out on mutant mice and three significant abnormalities were observed. No homozygous mutant embryos were recorded during gestation and, in a separate study, no homozygous animals were observed at weaning. The remaining tests were carried out on adult heterozygous mutant animals and males displayed an increased circulating free fatty acid level.
MYO15A
Myosin-XV is a protein that in humans is encoded by the MYO15A gene.

# Gene
Read-through transcript containing an upstream gene and this gene have been identified, but they are not thought to encode a fusion protein. Several alternatively spliced transcript variants have been described, but their full length sequences have not been determined.

# Function
This gene encodes an unconventional myosin. This protein differs from other myosins in that it has a long N-terminal extension preceding the conserved motor domain. Studies in mice suggest that this protein is necessary for actin organization in the hair cells of the cochlea.

# Clinical significance
Mutations in this gene have been associated with profound, congenital, neurosensory,                 non syndromic deafness            . This gene is located within the Smith-Magenis syndrome region on chromosome 17.
Maalox
Maalox is a brand name antacid containing Aluminium hydroxide and Magnesium hydroxide to neutralize or reduce stomach acid. It helps relieve symptoms of excessive stomach acidity in patients with indigestion, heartburn, gastroesophageal reflux disease (GERD {US} or GORD {UK}), or stomach or duodenal ulcers. In large doses, it can act as a laxative.
The mixture of Aluminium hydroxide and Magnesium hydroxide is sometimes referred to as Magaldrate.

# Ingredients
Liquid Maalox Regular Strength contains magnesium hydroxide, aluminum hydroxide and simethicone.

# Uses
Treatment of moderate symptoms of burning sensation in the stomach or chest area with accompanying bloating and/or gas pain. Usually occurs after a meal.
Maalox is also used in scientific research to simulate for silt/mud/soil in water, along with other dissolved particulates. The particulate size exceeds 11 micrometres.
Macula
The macula or macula lutea (from Latin macula, "spot" + lutea, "yellow") is an oval yellow spot near the center of the retina of the human eye. It has a diameter of about 1.5 mm and is often histologically defined as having two or more layers of ganglion cells. Near its center is the fovea, a small pit that contains the largest concentration of cone cells in the eye and is responsible for central vision.
It is specialized for high acuity vision. Within the macula are the fovea and foveola which contain a high density of cones (photoreceptors with high acuity).

# Clinical significance
Whereas loss of peripheral vision may go unnoticed for some time, damage to the macula will result in loss of central vision, which is usually immediately obvious. 
The progressive destruction of the macula is a disease known as macular degeneration and leads to the creation of a macular hole. Macular holes can rarely be caused by trauma, if a severe blow is delivered perfectly it can burst the blood vessels going to the macula, destroying it.
Visual input to the macula occupies a substantial portion of the brain's visual capacity.  As a result, some forms of visual field loss can occur without involving the macula; this is termed macular sparing.  (For example, visual field testing might demonstrate homonymous hemianopsia with macular sparing.)  This finding can be very informative for the ophthalmologist.
Malate

# Overview
Malate (OOC-CH2-CH(OH)-COO) is the ionized form of malic acid. It is an important chemical compound in biochemistry. In the C4 carbon fixation process, malate is a source of CO2 in the Calvin cycle.
In the citric acid cycle, (S)-malate is an intermediate formed by the addition of an -OH group on the si face of fumarate; it can also be formed from pyruvate via anaplerotic reactions. Malate dehydrogenase catalyzes the reversible conversion of malate into oxaloacetate using NAD as a cofactor.
Malate is also produced from starch in guard cells of plant leaves.  A build up of malate leads to a low water potential. Water then flows into the guard cells causing the stoma to open. However, this process does not always induce the opening of stomas.
Meatus
In anatomy, a meatus is a natural body opening or canal (Latin, 4th declension pl. meatus, or meatuses - often incorrectly meati).
Examples include:
- the external acoustic meatus, the opening of the ear canal
- The internal auditory meatus, a canal in the temporal bone of the skull
- the urinary meatus, which is the opening of the urethra, situated on the glans penis in males, and in the vulva in females
- the superior meatus, middle meatus and inferior meatus of the nose
miR-27
miR-27 is a family of microRNA precursors found in animals, including humans. MicroRNAs are typically transcribed as ~70 nucleotide precursors and subsequently processed by the Dicer enzyme to give a ~22 nucleotide product. The excised region or, mature product, of the miR-27 precursor is the microRNA mir-27.
Herpesvirus saimiri expresses several non-coding RNAs (HSURs) which have been found to significantly reduce the level of mir-27 in a host cell. It has been proposed that miR-27 operates together with miR-23 and mir-24 in a co-operative cluster.

# Regulation of adipocyte differentiation
miR-27 is one of a number of microRNAs implicated in cholesterol homeostasis and fatty acid metabolism. The miR-27 gene family has been shown to be downregulated during the differentiation of adipocytes. miR-27 inhibits adipocyte formation when overexpressed, acting by blocking the expression of two main regulators of adipogenesis. MicroRNAs miR-27a and -27b have been found to negatively regulate adipocyte differentiation through regulation of the peroxisome proliferator-activated receptor gamma (PPAR) post-transcriptionally, as well as C/EBP alpha in the case of miR-27b.   miR-27 can be identified both as an adipogenic inhibitor and as playing an important role in the development of obesity.

# Wnt signalling pathway
miR-27 is an activator of the Wnt signalling pathway, affecting the differentiation of mesenchymal stem cells into osteoblasts. miR-27 has been found to target and inhibit gene expression of the adenomatous polyposis coli (APC) protein, enabling it to regulate osteoblast differentiation. Expression levels of miR-27 are positively correlated with beta-catenin, a key protein in Wnt signalling. There is activation of Wnt signalling through nuclear accumulation of this protein, which is in response to inhibition of the beta-catenin destruction complex. This in turn is brought about by APC inhibition of miR-27.

# Cancer Regulation
miR-27 is known to regulate components involved in numerous types of cancer, including breast and ovarian. miR-27a has been identified as an oncogenic microRNA and, specifically, is highly expressed in breast cancer cells. mir-27b expression is associated with survival in triple negative breast cancer patients. Inhibition of miR-27 by antisense molecules decreases cell proliferation. Antisense RNA directed against miR-27a has been shown to decrease the percentage of cells in S phase whilst also increasing those in the G2-M phase.
The FOXO (Forkhead Box O) gene sub-family encodes tumour-suppressive transcription factors that regulate multiple aspects of cell cycle progression and survival. FOXO1 protein expression is down-regulated in breast tumour tissue samples; miR-27a has been identified as one of three miRNAS (along with miR-96 and miR-182) which directly target FOXO1 and regulate its endogenous expression. Suppression of miR-27a results in a FOXO1 protein increase and a consequent cell number decrease.