KDELR

Last updated

KDEL (Lys-Asp-Glu-Leu) endoplasmic reticulum protein retention receptors (KDELR) are the members of a group of receptor proteins:

Related Research Articles

Endoplasmic reticulum irregular network of membranes coterminous with the outer nuclear membrane in eukaryote cytoplasm that form a meshwork of tubular channels, often expanded into cisternae

The endoplasmic reticulum (ER) is a type of organelle found in eukaryotic cells that forms an interconnected network of flattened, membrane-enclosed sacs or tube-like structures known as cisternae. The membranes of the ER are continuous with the outer nuclear membrane. The endoplasmic reticulum occurs in most types of eukaryotic cells, but is absent from red blood cells and spermatozoa.

Enfuvirtide (INN) is an HIV fusion inhibitor, the first of a class of antiretroviral drugs used in combination therapy for the treatment of HIV-1 infection. It is marketed under the trade name Fuzeon (Roche).

COPI

COPI is a coatomer, a protein complex that coats vesicles transporting proteins from the cis end of the Golgi complex back to the rough endoplasmic reticulum (ER), where they were originally synthesized, and between Golgi compartments. This type of transport is termed as retrograde transport, in contrast to the anterograde transport associated with the COPII protein. The name "COPI" refers to the specific coat protein complex that initiates the budding process on the cis-Golgi membrane. The coat consists of large protein subcomplexes that are made of seven different protein subunits, namely α, β, β', γ, δ, ε and ζ.

The C-terminus is the end of an amino acid chain, terminated by a free carboxyl group (-COOH). When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The convention for writing peptide sequences is to put the C-terminal end on the right and write the sequence from N- to C-terminus.

ER retention refers to proteins that are retained in the endoplasmic reticulum, or ER, after folding; these are known as ER resident proteins.

Neurophysin I is a carrier protein with a size of 10 KDa and contains 90 to 97 aminoacids. It is a cleavage product of preprooxyphysin. It is a neurohypophysial hormone that is transported in vesicles with oxytocin, the other cleavage product, along axons, from magnocellular neurons of the hypothalamus to the posterior lobe of the pituitary. Although it is stored in neurosecretory granules with oxytocin and released with oxytocin, its biological action is unclear.

Growth hormone–releasing hormone (GHRH), also known as somatocrinin or by several other names in its endogenous forms and as somatorelin (INN) in its pharmaceutical form, is a releasing hormone of growth hormone (GH). It is a 44-amino acid peptide hormone produced in the arcuate nucleus of the hypothalamus.

Neurophysin II cleavage product of the coding protein of AVP gene

Neurophysin II is a carrier protein with a size of 19,687.3 Da and is made up of a dimer of two virtually identical chains of amino acids. Neurophysin II is a cleavage product of the prepro-vasopressin. It is a neurohypophysial hormone that is transported in vesicles with vasopressin, the other cleavage product, along axons, from magnocellular neurons of the hypothalamus to the posterior lobe of the pituitary. Although it is stored in neurosecretory granules with vasopressin and released with vasopressin into the bloodstream, its biological action is unclear. Neurophysin II is also known as a stimulator of prolactin secretion.

Tazarotene-induced gene-1 (TIG1) is a protein which has been implicated as a putative tumor suppressor. It is structurally similar to the protein latexin, which has also been shown to demonstrate some tumor suppression activity. TIG1 is thought to be a transmembrane protein, and its mechanism of tumor suppression is largely unknown.

GRIA2 protein-coding gene in the species Homo sapiens

Glutamate ionotropic receptor AMPA type subunit 2 is a protein that in humans is encoded by the GRIA2 gene.

GRIK1 protein-coding gene in the species Homo sapiens

Glutamate receptor, ionotropic, kainate 1, also known as GRIK1, is a protein that in humans is encoded by the GRIK1 gene.

KDELR1 protein-coding gene in the species Homo sapiens

KDEL (Lys-Asp-Glu-Leu) endoplasmic reticulum protein retention receptor 1, also known as KDELR1, is a protein which in humans is encoded by the KDELR1 gene.

KDELR2 protein-coding gene in the species Homo sapiens

ER lumen protein retaining receptor 2 is a protein that in humans is encoded by the KDELR2 gene.

TMED2 protein-coding gene in the species Homo sapiens

Transmembrane emp24 domain-containing protein 2 is a protein that in humans is encoded by the TMED2 gene.

KDELR3 protein-coding gene in the species Homo sapiens

ER lumen protein retaining receptor 3 is a protein that in humans is encoded by the KDELR3 gene.

Reticulocalbin 2 protein-coding gene in the species Homo sapiens

Reticulocalbin-2 is a protein that in humans is encoded by the RCN2 gene.

KDEL in mammals or "HDEL" in yeast. Plants are known to utilize both "KDEL" and "HDEL" signaling sequences.

Auxin binding protein

In molecular biology, the auxin binding protein family is a family of proteins which bind auxin. They are located in the lumen of the endoplasmic reticulum (ER). The primary structure of these proteins contains an N-terminal hydrophobic leader sequence of 30-40 amino acids, which could represent a signal for translocation of the protein to the ER. The mature protein comprises around 165 residues, and contains a number of potential N-glycosylation sites. In vitro transport studies have demonstrated co-translational glycosylation. Retention within the lumen of the ER correlates with an additional signal located at the C terminus, represented by the sequence Lys-Asp-Glu-Leu, known to be responsible for preventing secretion of proteins from the lumen of the ER in eukaryotic cells.

A target peptide is a short peptide chain that directs the transport of a protein to a specific region in the cell, including the nucleus, mitochondria, endoplasmic reticulum (ER), chloroplast, apoplast, peroxisome and plasma membrane. Some target peptides are cleaved from the protein by signal peptidases after the proteins are transported.

KKXX and for some proteins XKXX is a target peptide motif located in the C terminus in the amino acid structure of a protein responsible for retrieval of endoplasmic reticulum (ER) membrane proteins to and from the Golgi apparatus.These ER membrane proteins are transmembrane proteins that are then embedded into the ER membrane after transport from the Golgi. This motif is exclusively cytoplasmic and interacts with the COPI protein complex to target the ER from the cis end of the Golgi apparatus by retrograde transport.

References