Encodes a syntaxin localized at the plasma membrane (SYR1, Syntaxin Related Protein 1, also known as SYP121, PENETRATION1/PEN1). SYR1/PEN1 is a member of the SNARE superfamily proteins. SNARE proteins are involved in cell signaling, vesicle traffic, growth and development. SYR1/PEN1 functions in positioning anchoring of the KAT1 K+ channel protein at the plasma membrane. Transcription is upregulated by abscisic acid, suggesting a role in ABA signaling. Also functions in non-host resistance against barley powdery mildew, Blumeria graminis sp. hordei. SYR1/PEN1 is a nonessential component of the preinvasive resistance against Colletotrichum fungus. Required for mlo resistance.
syntaxin protein, involved in the negative regulation of defense pathways such as programmed cell death, salicylic acid signalling pathway, jasmonic acid signalling pathway
Encodes a plasma membrane localized protein with similarity to synaptotagmins, a class of membrane trafficking proteins. SYT1 is expressed in all tissues. Loss of function mutations show hypersensitivity to NaCl and electrolyte leakage from the plasma membrane. SYT1 also affects calcium dependent freezing tolerance. SYT1 probably plays a role in membrane repair such as membrane resealing after freezing induced damage.
The process of targeting specific proteins to particular membrane-bounded subcellular organelles. Usually requires an organelle specific protein sequence motif.
The targeting of proteins to a membrane that occurs during translation. The transport of most secretory proteins, particularly those with more than 100 amino acids, into the endoplasmic reticulum lumen occurs in this manner, as does the import of some proteins into mitochondria.
The targeting of proteins to a membrane that occurs after their translation. Some secretory proteins exhibit posttranslational transport into the endoplasmic reticulum (ER) lumen: they are synthesized in their entirety on free cytosolic ribosomes and then released into the cytosol, where they are bound by chaperones which keep them in an unfolded state, and subsequently are translocated across the ER membrane.
The process of directing proteins towards a membrane using signals contained within the protein, occurring during ubiquitin-dependent protein catabolism via the MVB pathway; the destruction of a protein or peptide covalently tagged with a ubiquitin, via the multivesicular body (MVB) sorting pathway.
The import of proteins into the chloroplast thylakoid membranes. Proteins that are destined for the thylakoid lumen require two uptake-targeting sequences: the first targets the protein to the stroma, and the second targets the protein from the stroma to the thylakoid lumen. Four separate thylakoid-import systems deal with the proteins once they are in the stroma.
The import of proteins into the mitochondria inner membrane. Inner membrane proteins are first imported into the matrix space where the matrix-targeting sequence is removed; how these proteins then are incorporated into the inner membrane is not known.
The import of proteins into the outer membrane of the mitochondrion. Outer membrane proteins have a short matrix-targeting sequence followed by a long stretch of hydrophobic amino acids at the N-terminus. The hydrophobic sequence functions as a stop-transfer sequence that both prevents transfer of the protein into the matrix and anchors it as an integral protein in the outer membrane.
The targeting of proteins into the peroxisomal membrane. The process is not well understood, but both signals and mechanism differ from those involved in peroxisomal matrix protein import.
