Integral membrane proteins

phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain

complex that catalyzes the phosphorylation of ADP to ATP, during oxidative phosphorylation

pore-forming membrane protein that allows the passage of ions through a membrane

large protein family of receptors that detect molecules outside the cell and activate internal signal transduction pathways and cellular responses

process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient

superfamily of enzymes containing heme as a cofactor that function as monooxygenases

Cyclooxygenase (COX), officially known as prostaglandin-endoperoxide synthase (PTGS), is an enzyme (specifically, a family of isozymes, ) that is responsible for biosynthesis of prostanoids, including thromboxane and prostaglandins such as prostacyclin, from arachidonic acid. A member of the animal-type heme peroxidase family, it is also known as prostaglandin G/H synthase. The specific reaction catalyzed is the conversion from arachidonic acid to prostaglandin H2 via a short-lived prostaglandin G2 intermediate.

Aquaporins, also called water channels, are channel proteins from a larger family of major intrinsic proteins that form pores in the membrane of biological cells, mainly facilitating transport of water between cells. The cell membranes of a variety of different bacteria, fungi, animal and plant cells contain aquaporins through which water can flow more rapidly into and out of the cell than by diffusing through the phospholipid bilayer. Aquaporins have six membrane-spanning α-helical domains with both carboxylic and amino terminals on the cytoplasmic side. Two hydrophobic loops contain conserve

protein spanning across a biological membrane

200px|thumb|Adenosine triphosphate 200px|thumb|Adenosine diphosphate 200px|thumb|Adenosine monophosphate ATPases (, Adenosine 5'-TriPhosphatase, adenylpyrophosphatase, ATP monophosphatase, triphosphatase, ATP hydrolase, adenosine triphosphatase) are a class of enzymes that catalyze the decomposition of ATP into ADP and a free phosphate ion or the inverse reaction. This dephosphorylation reaction releases energy, which the enzyme (in most cases) harnesses to drive other chemical reactions that would not otherwise occur. This process is widely used in all known forms of life.

type of membrane protein that is permanently attached to the biological membrane

type of ion channel transmembrane protein

complex enzyme found in bacteria, archaea, and mitochondria of eukaryotes

ion channel complex through which calcium ions pass

Bacteriorhodopsin (Bop) is a protein used by Archaea, most notably by Haloarchaea, a class of the Euryarchaeota. It acts as a proton pump; that is, it captures light energy and uses it to move protons across the membrane out of the cell. The resulting proton gradient is subsequently converted into chemical energy.

Photosystems are functional and structural units of protein complexes involved in photosynthesis. Together they carry out the primary photochemistry of photosynthesis: the absorption of light and the transfer of energy and electrons. Photosystems are found in the thylakoid membranes of plants, algae, and cyanobacteria. These membranes are located inside the chloroplasts of plants and algae, and in the cytoplasmic membrane of photosynthetic bacteria. There are two kinds of photosystems: PSI and PSII. center|thumb|650x650px|Model of a photosystem and how it uses light energy to carry out process

InterPro Family

class of transmembrane protein allowing sodium ions in and out

lipoprotein complex

ion channel that selectively passes K+

Gramicidin, also called gramicidin D, is a mix of ionophoric antibiotics, gramicidin A, B and C, which make up about 80%, 5%, and 15% of the mix, respectively. Each has 2 isoforms, so the mix has 6 different types of gramicidin molecules. They can be extracted from Brevibacillus brevis soil bacteria. Gramicidins are linear peptides with 15 amino acids. This is in contrast to unrelated gramicidin S, which is a cyclic peptide.

family of monosaccharide transport proteins

Bcl-2, encoded in humans by the BCL2 gene, is the founding member of the Bcl-2 family of regulator proteins. BCL2 blocks programmed cell death (apoptosis) while other BCL2 family members can either inhibit or induce it. It was the first apoptosis regulator identified in any organism.

class of receptor proteins that bind histamine

class of enzymes

molecular unit responsible for absorbing light in photosynthesis

Connexins (Cx) (TC# 1.A.24), or gap junction proteins, are structurally related transmembrane proteins that assemble to form vertebrate gap junctions. An entirely different family of proteins, the innexins, forms gap junctions in invertebrates. Each gap junction is composed of two hemichannels, or connexons, which consist of homo- or heterohexameric arrays of connexins, and the connexon in one plasma membrane docks end-to-end with a connexon in the membrane of a closely opposed cell. The hemichannel is made of six connexin subunits, each of which consist of four transmembrane segments. Gap jun

Ferroportin-1, also known as solute carrier family 40 member 1 (SLC40A1) or iron-regulated transporter 1 (IREG1), is a protein that in humans is encoded by the SLC40A1 gene. Ferroportin is a transmembrane protein that transports iron from the inside of a cell to the outside of the cell. Ferroportin is the only known iron exporter.

thumb|Structure of a flippase, showing the two major subunits of the enzyme|249x249px

membrane proteins

group of ion-selective channel proteins that are activated by changes in the electrical membrane potential near the channel

thumb|A comparison of transport proteins An antiporter (also called exchanger or counter-transporter) is an integral membrane protein that uses secondary active transport to move two or more molecules in opposite directions across a phospholipid membrane. It is a type of cotransporter, which means that uses the energetically favorable movement of one molecule down its electrochemical gradient to power the energetically unfavorable movement of another molecule up its electrochemical gradient. This is in contrast to symporters, which are another type of cotransporter that moves two or more ions

mammalian protein found in Homo sapiens

enzyme of the respiratory chain consisting of several polypeptide chains; L-shaped with a horizontal arm lying in the membrane, and a vertical arm that projects into the cytoplasm of prokaryotes, or the matrix of mitochondria.

family of transport proteins

The translocon (also called a translocator or translocation channel) is a general term for a protein channel in biological membranes that functions to move polypeptides across the membrane or insert them into the lipid bilayer. This structure is a key component of the protein translocation pathway in all organisms, from bacteria, archaea, and eukaryotes.

Group of protiens

right|thumb|250px|Comparison of transport proteins

thumb|Hypothetical model of the tetraspanin function

Complex that transfers electrons from reduced plastoquinone to oxidized plastocyanin and translocates protons from the stroma to the lumen

Phototropins are blue light photoreceptor proteins (more specifically, flavoproteins) that mediate phototropism responses across many species of algae, fungi and higher plants. Phototropins can be found throughout the leaves of a plant. Along with cryptochromes and phytochromes they allow plants to respond and alter their growth in response to the light environment. When phototropins are hit with blue light, they induce a signal transduction pathway that alters the plant cells' functions in different ways.

Small pigmented organelle used in single-celled organisms to detect light

In molecular biology, caveolins are a family of integral membrane proteins that are the principal components of caveolae membranes and involved in receptor-independent endocytosis. Caveolins may act as scaffolding proteins within caveolar membranes by compartmentalizing and concentrating signaling molecules. They also induce positive (inward) membrane curvature by way of oligomerization, and hairpin insertion. Various classes of signaling molecules, including G-protein subunits, receptor and non-receptor tyrosine kinases, endothelial nitric oxide synthase (eNOS), and small GTPases, bind Cav-1

protein-coding gene in the species Homo sapiens

class of transport proteins

protein complex that forms a transmembrane channel through which calcium ions may pass in response to changes in membrane potential

right|thumb|250px|Comparison of Membrane transport protein|transport proteins A symporter is an integral membrane protein that is involved in the transport of two (or more) different molecules across the cell membrane in the same direction. The symporter works in the plasma membrane and molecules are transported across the cell membrane at the same time, and is, therefore, a type of cotransporter. The transporter is called a symporter, because the molecules will travel in the same direction in relation to each other. This is in contrast to the antiport transporter. Typically, the ion(s) will m

Molecular photoreceptors

group of membrane proteins that facilitate Na⁺ reabsorption across the apical membranes of epithelia in the distal nephron, respiratory and reproductive tracts and exocrine glands of animals

mammalian protein found in Homo sapiens

class of membrane transport proteins

InterPro Family

class of enzymes

Synaptosomal-Associated Protein, 25kDa (SNAP-25) is a Target Soluble NSF (N-ethylmaleimide-sensitive factor) Attachment Protein Receptor (t-SNARE) protein encoded by the SNAP25 gene found on chromosome 20p12.2 in humans. SNAP-25 is a component of the trans-SNARE complex, which accounts for membrane fusion specificity and directly executes fusion by forming a tight complex that brings the synaptic vesicle and plasma membranes together.

Calnexin (CNX) is a 67kDa integral protein (that appears variously as a 90kDa, 80kDa, or 75kDa band on western blotting depending on the source of the antibody) of the endoplasmic reticulum (ER). It consists of a large (50 kDa) N-terminal calcium-binding lumenal domain, a single transmembrane helix and a short (90 residues), acidic cytoplasmic tail. In humans, calnexin is encoded by the gene CANX.

mammalian protein found in Homo sapiens

InterPro Family

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Aquaporin 1 (AQP-1) is a protein that in humans is encoded by the AQP1 gene.

Aquaporin-2 (AQP-2) is found in the apical cell membranes of the kidney's collecting duct principal cells and in intracellular vesicles located throughout the cell. It is encoded by the gene.