respiratory

The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.

Acts as an ADP-ribosylating toxin, which may transfer the ADP-ribosyl group from NAD(+) to specific amino acids in target proteins. Elicits cytopathic effects in mammalian cells, such as disorganization and disruption of respiratory epithelial integrity in tracheal epithelium and vacuolization in the cytoplasm of CHO and HeLa cells.

Human respiratory syncytial virus (RSV) (strain 18537) Nucleoprotein NP Protein (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 50.9 kDa and the accession number is P24566.

Human respiratory syncytial virus (RSV) glycoprotein G Protein (aa 64-321, His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 29.59 kDa and the accession number is A0A076FRQ0.

Human respiratory syncytial virus (RSV) (subtype A, strain Long) glycoprotein G Protein (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 27 kDa and the accession number is P20895-1.

Human respiratory syncytial virus (RSV) (A, strain Long) Fusion glycoprotein F0 RSV-F Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 56.92 kDa and the accession number is P12568.

Human respiratory syncytial virus (RSV) (A2) Prefusion glycoprotein F RSV-preF Protein is expressed in CHO mammalian cells. The predicted molecular weight is 54.5 kDa.

Human respiratory syncytial virus (RSV) (A, rsb1734) glycoprotein G RSV-G Protein (95% Homology) (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 26.7 kDa and the accession number is P27022-1.

Human respiratory syncytial virus (RSV) (A, rsb1734) glycoprotein G RSV-G Protein (93% Homology) (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 26.3 kDa and the accession number is P27022-1.

Human respiratory syncytial virus (RSV) Fusion Protein (aa 1-526, His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 57.04 kDa and the accession number is A0A023RA53.

Human respiratory syncytial virus (RSV) (strain A2, strain Long) Nucleoprotein Protein (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 44.28 kDa and the accession number is P03418.

Human respiratory syncytial virus (RSV) (A2) Fusion glycoprotein RSV-F Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 57.4 kDa and the accession number is P03420.1.

Human respiratory syncytial virus (RSV) Fusion protein RSV-F (Strain RSS-2) Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 57.8 kDa and the accession number is P11209.

Human respiratory syncytial virus (RSV) (B, strain 18537) Nucleoprotein Protein (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 44.38 kDa and the accession number is P24566.

Human respiratory syncytial virus (RSV) (strain A2) Fusion glycoprotein F0 (B2M & His) is expressed in E. coli expression system with N-6xHis-B2M tag. The predicted molecular weight is 69.9 kDa and the accession number is P03420.

Human respiratory syncytial virus (RSV) Fusion Protein (aa 1-525, His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 57.12 kDa and the accession number is K7WLI9.

Human respiratory syncytial virus (RSV) (B, strain 18537) Fusion glycoprotein F0 RSV-F Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 57.03 kDa and the accession number is P13843.

Human respiratory syncytial virus (RSV) (B, strain 18537) glycoprotein G Protein (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 26.40 kDa and the accession number is P20896.

Human respiratory syncytial virus (RSV) (strain A2) glycoprotein G Protein (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 26.97 kDa and the accession number is P03423.

Human respiratory syncytial virus (RSV) Nucleoprotein Protein (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 44.39 kDa and the accession number is Q6V2F2.

Replication of severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) requires proteolytic processing of the replicase polyprotein by two viral cysteine proteases, a chymotrypsin-like protease (3CLpro) and a papain-like protease (PLpro). These proteases are important targets for development of antiviral drugs that would inhibit viral replication and reduce mortality associated with outbreaks of SARS-CoV. PLpro is a cysteine protease located within the non-structural protein 3 (NS3) section of the viral polypeptide. PLPro activity is required to process the viral polyprotein into functional, mature subunits; specifically, PLPro cleaves a site at the amino-terminus of the viral replicase region. In addition to its role in viral protein maturation, PLPro possesses a deubiquitinating and deISGylating activity. In vivo, this protease antagonizes innate immunity by inhibiting IRF3-induced production of type I interferons.

ACE2 (Angiotensin I Converting Enzyme 2) is a Protein Coding gene. Diseases associated with ACE2 include Severe Acute Respiratory Syndrome and Neurogenic Hypertension.The protein encoded by this gene belongs to the angiotensin-converting enzyme family of dipeptidyl carboxydipeptidases and has considerable homology to human angiotensin 1 converting enzyme. This secreted protein catalyzes the cleavage of angiotensin I into angiotensin 1-9, and angiotensin II into the vasodilator angiotensin 1-7. ACE2 ACEH Protein, Cynomolgus, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 86.5 kDa and the accession number is A0A2K5X283.

ACE2 (Angiotensin I Converting Enzyme 2) is a Protein Coding gene. Diseases associated with ACE2 include Severe Acute Respiratory Syndrome and Neurogenic Hypertension.The protein encoded by this gene belongs to the angiotensin-converting enzyme family of dipeptidyl carboxydipeptidases and has considerable homology to human angiotensin 1 converting enzyme. This secreted protein catalyzes the cleavage of angiotensin I into angiotensin 1-9, and angiotensin II into the vasodilator angiotensin 1-7. ACE2 ACEH Protein, Cynomolgus, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 86.5 kDa and the accession number is A0A2K5X283.

May play a role in the respiratory chain. C2orf69 Protein, Human, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag. The predicted molecular weight is 44.7 kDa and the accession number is Q8N8R5.

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

Lipocalin-2, also known as Neutrophil Gelatinase-Associated Lipocalin (NGAL), is a secretory protein of the lipocalin superfamily. Lipocalin-2 contains a signal peptide that enables it to be secreted and form complexes with matrix metalloproteinase-9 (MMP-9) through disulfide bonds. Similar to other lipocalin family members, Lipocalin-2 is involved in diverse cellular processes, including the transport of small hydrophobic molecules, protection of MMP-9 from proteolytic degradation, and cell signaling. Furthermore, Lipocalin-2 can tightly bind to bacterial siderophore through a cell surface receptor, possibly serving as a potent bacteriostatic agent by sequestering iron, regulating innate immunity and protecting kidney epithelial cells from ischemia–reperfusion injury. This protein is mainly expressed in neutrophils and in lower levels in the kidney, prostate, and epithelia of the respiratory and alimentary tracts.Recent evidence also suggests its role as a biomarker for renal injury and inflammation.

OSMR is targeted to the mitochondrial matrix via the presequence translocase-associated motor complex components, mtHSP70 and TIM44. OSMR interacts with NADH ubiquinone oxidoreductase 1 2 (NDUFS1 2) of complex I and promotes mitochondrial respiration. Deletion of OSMR impairs spare respiratory capacity, increases reactive oxygen species, and sensitizes BTSCs to IR-induced cell death. OSMR Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 82.04 kDa and the accession number is A0A2K5UFW5.

The pathogenesis of severe acute respiratory disease syndrome (SARS) is not fully understood. One case-control study has reported an association between susceptibility to SARS and mannan-binding lectin (MBL) in China. As the downstream protein of MBL, variants of the MBL-associated serine protease-2 (MASP2) gene may be associated with SARS coronavirus (SARS-CoV) infection in the same population.

Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.

Protein with pleiotropic attributes mediated in a cell-compartment- and tissue-specific manner, which include the plasma membrane-associated cell signaling functions, mitochondrial chaperone, and transcriptional co-regulator of transcription factors in the nucleus. Plays a role in adipose tissue and glucose Homeostasis in a sex-specific manner. Contributes to pulmonary vascular remodeling by accelerating proliferation of pulmonary arterial smooth muscle cells.; In the mitochondria, together with PHB2, forms large ring complexes (prohibitin complexes) in the inner mitochondrial membrane (IMM) and functions as chaperone protein that stabilizes mitochondrial respiratory enzymes and maintains mitochondrial integrity in the IMM, which is required for mitochondrial morphogenesis, neuronal survival, and normal lifespan (Probable). The prohibitin complex, with DNAJC19, regulates cardiolipin remodeling and the protein turnover of OMA1 in a cardiolipin-binding manner. Regulates mitochondrial respiration activity playing a role in cellular aging. The prohibitin complex plays a role of mitophagy receptor involved in targeting mitochondria for autophagic degradation. Involved in mitochondrial-mediated antiviral innate immunity, activates DDX58 RIG-I-mediated signal transduction and production of IFNB1 and proinflammatory cytokine IL6.; In the nucleus, acts as a transcription coregulator, enhances promoter binding by TP53, a transcription factor it activates, but reduces the promoter binding by E2F1, a transcription factor it represses. Interacts with STAT3 to affect IL17 secretion in T-helper Th17 cells.; In the plasma membrane, cooperates with CD86 to mediate CD86-signaling in B lymphocytes that regulates the level of IgG1 produced through the activation of distal signaling intermediates. Upon CD40 engagement, required to activate NF-kappa-B signaling pathway via phospholipase C and protein kinase C activation.; (Microbial infection) In neuronal cells, cell surface-expressed PHB is involved in human enterovirus 71 EV-71 entry into neuronal cells specifically, while membrane-bound mitochondrial PHB associates with the virus replication complex and facilitates viral replication. May serve as a receptor for EV71.

Cytochrome C oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain. It is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane. The complex consists of 13 mitochondrial- and nuclear-encoded subunits. The mitochondrially-encoded subunits perform the electron transfer and proton pumping activities. The functions of the nuclear-encoded subunits are unknown but they may play a role in the regulation and assembly of the complex. This gene encodes the nuclear-encoded subunit Vb of the human mitochondrial respiratory chain enzyme.

Dog dander is an important cause of respiratory allergy but its content of allergenic components is still incompletely known. The size and the amino acid composition of the ligand-binding pocket indicate that Can f 4 is capable of binding only relatively small hydrophobic molecules which are different from those that Can f 2 is able to bind. The crystal structure of Can f 4 contained both monomeric and dimeric forms of the allergen, suggesting that Can f 4 is able to form transient (weak) dimers. The existence of transient dimers in solution was confirmed by use of native mass spectrometry. The dimeric structure of Can f 4 is formed when the ends of four β-strands are packed against the same strands from the second monomer.

Protein SCO1 Homolog, Mitochondrial (SCO1) is a member of the SCO1 2 family. SCO1 has a homodimer structure. SCO1 is located in mitochondrion and is highly expressed in muscle, heart, and brain. It is characterized by high rates of Oxidative Phosphorylation (OxPhos). SCO1 is thought to play a important role in cellular copper homeostasis, mitochondrial redox signaling and insertion of copper into the active site of COX. The defects of SCO1 can result in Mitochondrial Complex IV Deficiency (MT-C4D). A disorder of the mitochondrial respiratory chain has heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs.

The Severe Acute Respiratory Syndrome (SARS) Coronavirus (CoV) is an enveloped, positive-stranded RNA viruses that can cause a severe respiratory disease. Its genome consists of a ∼30 kb linear, non-segmented, capped, polycistronic, polyadenylated RNA molecule, the first two-third of which is directly translated into two large polyproteins. These two polypeptides are processed into 16 non-structural proteins (nsps), forming the replicase complex, which is active in the cytoplasm in close association with cellular membranes. Nsp1 was proved to be able to suppress host gene expression by promoting host mRNA degradation and was involved in cellular chemokine deregulation. This virus evades the host innate immune response in part through the expression of its non-structural protein (nsp) 1, which inhibits both host gene expression and virus- and interferon (IFN)-dependent signaling. Thus, nsp1 is a promising target for drugs, as inhibition of nsp1 would make SARS-CoV more susceptible to the host antiviral defenses.

ACE2 (Angiotensin I Converting Enzyme 2) is a Protein Coding gene. Diseases associated with ACE2 include Severe Acute Respiratory Syndrome and Neurogenic Hypertension.The protein encoded by this gene belongs to the angiotensin-converting enzyme family of dipeptidyl carboxydipeptidases and has considerable homology to human angiotensin 1 converting enzyme. This secreted protein catalyzes the cleavage of angiotensin I into angiotensin 1-9, and angiotensin II into the vasodilator angiotensin 1-7. ACE2 ACEH Protein, Human, Recombinant (hFc & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-hFc-Avi tag. The predicted molecular weight is 111.2 kDa and the accession number is Q9BYF1-1.

ACE2 (Angiotensin I Converting Enzyme 2) is a Protein Coding gene. Diseases associated with ACE2 include Severe Acute Respiratory Syndrome and Neurogenic Hypertension.The protein encoded by this gene belongs to the angiotensin-converting enzyme family of dipeptidyl carboxydipeptidases and has considerable homology to human angiotensin 1 converting enzyme. This secreted protein catalyzes the cleavage of angiotensin I into angiotensin 1-9, and angiotensin II into the vasodilator angiotensin 1-7. ACE2 ACEH Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 86.5 kDa and the accession number is Q9BYF1-1.

Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain.

The IFNLR1 IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand receptor complex stimulate the activation of the JAK STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state. Determines the cell type specificity of the lambda interferon action. Shows a more restricted pattern of expression in the epithelial tissues thereby limiting responses to lambda interferons primarily to epithelial cells of the respiratory, gastrointestinal, and reproductive tracts. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium.

Pulmonary surfactant-associated protein B, also known as SFTPB and SP-B, contains one saposin A-type domain and three saposin B-type domains. SP-B is produced primarily by alveolar type II cells (AEC2) but also by nonciliated respiratory epithelial cells lining distal portions of the respiratory tract. Its secretion promotes alveolar homeostasis, stabilizing lipid layers and lowering surface tension at the air-liquid interface in the peripheral air spaces. Alveolar SP-B influences surfactant formation, effector cell functions, and innate host defense. Deficiency is associated with respiratory distress syndrome (RDS), pulmonary surfactant metabolism dysfunction 1 (SMDP1), and other human lung diseases. Gene addition and editing therapies show promise by complementing SP-B expression in AEC2s, restoring the phenotypic defect in vitro and in vivo.

BPIFB1, also known as LPLUNC1, belongs to the BPI LBP Plunc superfamily, plunc family. BPIFB1 may be involved in the innate immune response to bacterial exposure in the mouth, nasal cavities, and lungs. BPIFB1 is expressed in the upper respiratory tract and oral cavity, which may function in host defence. The expression of BPIF proteins is associated with CF lung disease in humans and mice. It is unclear if this elevation of protein production, which results from phenotypic alteration of the cells within the diseased epithelium, plays a role in the pathogenesis of the disease. BPIFB1 is an abundant, secreted product of goblet cells and minor mucosal glands of the respiratory tract and oral cavity and suggest that the protein functions in the complex milieu that protects the mucosal surfaces in these locations.

Cytochrome b5 type B (CYB5B) is a membrane of the cytochrome b5 family. It contains 1 cytochrome b5 heme-binding domain. Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. In the mitochondrion of eukaryotes and in aerobic prokaryotes, cytochrome b is a component of respiratory chain complex III also known as the bc1 complex or ubiquinol-cytochrome c reductase.

OSMR is targeted to the mitochondrial matrix via the presequence translocase-associated motor complex components, mtHSP70 and TIM44. OSMR interacts with NADH ubiquinone oxidoreductase 1 2 (NDUFS1 2) of complex I and promotes mitochondrial respiration. Deletion of OSMR impairs spare respiratory capacity, increases reactive oxygen species, and sensitizes BTSCs to IR-induced cell death. OSMR Protein, Canine, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 81.73 kDa and the accession number is A0A8I3MI11.

Desmoglein-2 (DSG-2) as the primary high-affinity receptor used by adenoviruses Ad3, Ad7, Ad11 and Ad14. These serotypes represent key human pathogens causing respiratory and urinary tract infections. In epithelial cells, adenovirus binding of DSG-2 triggers events reminiscent of epithelial-to-mesenchymal transition, leading to transient opening of intercellular junctions. DSG-2 Desmoglein-2 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 63.7 kDa and the accession number is O55111.

Cytochrome b-c1 complex subunit 6, mitochondrial (UQCRH) belongs to the UQCRH QCR6 family, it is a subunit of the respiratory chain protein Ubiquinol Cytochrome c Reductase. This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. UQCRH may mediate formation of the complex between cytochromes c and c1. It may mediate formation of the complex between cytochromes c and c1.

Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Activated in response to various mitochondrial stress, leading to the proteolytic cleavage of target proteins, such as OPA1, UQCC3 and DELE1. Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of OPA1 at S1 position, leading to OPA1 inactivation and negative regulation of mitochondrial fusion. Also acts as a regulator of apoptosis: upon BAK and BAX aggregation, mediates cleavage of OPA1, leading to the remodeling of mitochondrial cristae and allowing the release of cytochrome c from mitochondrial cristae. In depolarized mitochondria, may also act as a backup protease for PINK1 by mediating PINK1 cleavage and promoting its subsequent degradation by the proteasome. May also cleave UQCC3 in response to mitochondrial depolarization. Also acts as an activator of the integrated stress response (ISR): in response to mitochondrial stress, mediates cleavage of DELE1 to generate the processed form of DELE1 (S-DELE1), which translocates to the cytosol and activates EIF2AK1 HRI to trigger the ISR. Its role in mitochondrial quality control is essential for regulating lipid metabolism as well as to maintain body temperature and energy expenditure under cold-stress conditions. Binds cardiolipin, possibly regulating its protein turnover. Required for the stability of the respiratory supercomplexes.

Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of the eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotoxin F which may have 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway. When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the HC forms pores that allows the light chain (LC) to translocate into the cytosol. Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release. Whole toxin only has protease activity after reduction, which releases LC. Requires complex eukaryotic host polysialogangliosides for full neurotoxicity. It is not clear whether a synaptic vesicle protein acts as its receptor; there is evidence for and against SV2 fulfilling this function.; Has proteolytic activity. After translocation into the eukaryotic host cytosol, inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '60-Gln-|-Lys-61' bond of synaptobrevin-1 VAMP1 and the equivalent 'Gln-|-Lys' sites in VAMP2 and VAMP3. Cleaves the '48-Gln-|-Lys-49' bond of A.californica synaptobrevin (AC P35589).; Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD). The RBD is responsible for the adherence of the toxin to the cell surface. It simultaneously recognizes 2 coreceptors; polysialated gangliosides and the receptor protein SV2A, SV2B and SV2C in close proximity on host synaptic vesicles; although not all evidence indicates these are the receptors. The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) in the active site; it may also prevent premature LC dissociation from the translocation channel and protect toxin prior to translocation. The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol.

Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc.

Alterations in GFER gene have been associated with progressive mitochondrial myopathy, congenital cataracts, hearing loss, developmental delay, lactic acidosis and respiratory chain deficiency in 3 siblings born to consanguineous Moroccan parents by homozygosity mapping and candidate gene approach. Using homozygosity mapping, we discovered that a mutation in the GFER gene causes an infantile mitochondrial disorder.