Transmembrane proteins

type of ion channel transmembrane protein

thumb|350px|Principal interactions of structural proteins at cadherin-based adherens junction. Actin filaments are linked to α-actinin and to the membrane through vinculin. The head domain of vinculin is associated with E-cadherin via α-, β-, and γ-catenins. The tail domain of vinculin binds to membrane lipids and to actin filaments. Cadherins (named for "calcium-dependent adhesion") are cell adhesion molecules important in forming adherens junctions that let cells adhere to each other. Cadherins are a class of type-1 transmembrane proteins, and they depend on calcium (Ca2+) ions to function,

Integrins are transmembrane receptors that help cell–cell and cell–extracellular matrix (ECM) adhesion. Upon ligand binding, integrins activate signal transduction pathways that mediate cellular signals such as regulation of the cell cycle, organization of the intracellular cytoskeleton, and movement of new receptors to the cell membrane. The presence of integrins allows rapid and flexible responses to events at the cell surface (e.g. signal platelets to initiate an interaction with coagulation factors).

class of enzymes

group of transport proteins having channels which consist largely of α-helical or β-strand-type spanners

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.

group of mitochondrial proteins involved in the respiratory chain

Hemolysins or haemolysins are lipids and proteins that cause lysis of red blood cells by disrupting the cell membrane. Although the lytic activity of some microbe-derived hemolysins on red blood cells may be of great importance for nutrient acquisition, many hemolysins produced by pathogens do not cause significant destruction of red blood cells during infection. However, hemolysins are often capable of lysing red blood cells in vitro.

family of membrane transport proteins

protein-pigment complex that may be closely or peripherally associated to photosynthetic reaction centers that participate in harvesting and transferring radiant energy to the reaction center

SERCA (sarcoplasmic/endoplasmic reticulum Ca2+-ATPase or SR Ca2+-ATPase) is a membrane protein that transports calcium from the cytosol into the sarcoplasmic reticulum (SR) of muscle cells. The SR is a structure which stores calcium in muscle cells, similar to the smooth endoplasmic reticulum of other cells. SERCA is a calcium ATPase-type P-ATPase. It uses energy from ATP to actively transport calcium ions across the SR membrane.

In biochemistry, sulfatases are a class of enzymes of the esterase class that catalyze the hydrolysis of sulfate esters into an alcohol and a bisulfate:

classification of membrane proteins including ion channels

family of transport protein supercomplexes consisting of separate complexes in the mitochondrial inner and outer membrane and the space between

The permeases are membrane transport proteins, a class of multipass transmembrane proteins that allow the diffusion of a specific molecule in or out of the cell in the direction of a concentration gradient, a form of facilitated diffusion.

membrane-spanning protein domain

Vacuolar-type ATPase (V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms. V-ATPases acidify a wide array of intracellular organelles and pump protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however, is a proton pump that

Pilin refers to proteins that create pilus structures in bacteria. These structures can be used for the exchange of genetic material, or as a cell adhesion mechanism. Although not all bacteria have pili or fimbriae, bacterial pathogens often use their fimbriae to attach to host cells. In Gram-negative bacteria, where pili are more common, individual pilin molecules are linked by noncovalent protein-protein interactions, while Gram-positive bacteria often have polymerized LPXTG pilin.

class of enzymes

protein-coding gene in the species Homo sapiens

mammalian protein found in Homo sapiens

If terminal sialic acid residues are removed from glycoproteins, the resulting proteins are known as asialoglycoproteins.

class of enzymes

BCL2/adenovirus E1B 19 kDa protein-interacting protein 3 is a protein found in humans that is encoded by the BNIP3 gene.

membrane-bound flavoenzyme complex consisting of four subunits, A, B, C, and D. A and B comprise the membrane-extrinsic catalytic domain and C (InterPro:IPR003510; InterPro:IPR004224) and D (InterPro:IPR003418) link the catalytic centers to the ele

mammalian protein found in Homo sapiens

protein-coding gene in the species Homo sapiens

family of transport proteins

protein-coding gene in the species Homo sapiens

group of ion channel proteins that open in response to the binding of extracellular ATP

Component of photosynthesis

family of transport proteins

class of protein complexes