Protein: Annexin A1 (Annexin I) (Annexin-1) (Calpactin II) (Calpactin-2) (Chromobindin-9) (Lipocortin I) (Phospholipase A2 inhibitory protein) (p35) [Cleaved into: Annexin Ac2-26] (P19619)
Organism: Sus scrofa (Pig)
Function: Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity. Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response. Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T-cell activation, regulates differentiation and proliferation of activated T-cells. Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (By similarity). Has no effect on unstimulated T-cells. Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (By similarity). Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions. Displays Ca(2+)-dependent binding to phospholipid membranes. Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P07150}. Cytoplasm {ECO:0000269|PubMed:11058080, ECO:0000269|PubMed:15581623}. Cell projection, cilium {ECO:0000250|UniProtKB:P10107}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51662}. Lateral cell membrane {ECO:0000250|UniProtKB:P10107}. Early endosome {ECO:0000269|PubMed:11058080, ECO:0000269|PubMed:8885232}. Cell membrane {ECO:0000269|PubMed:15581623, ECO:0000269|PubMed:3020049}; Peripheral membrane protein {ECO:0000269|PubMed:3020049}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:11058080, ECO:0000269|PubMed:15581623}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:P10107}. Membrane {ECO:0000250|UniProtKB:P10107}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10107}. Endosome {ECO:0000250|UniProtKB:P07150}. Secreted {ECO:0000250|UniProtKB:P10107}. Secreted, extracellular space {ECO:0000250|UniProtKB:P04083}. Cell membrane {ECO:0000250|UniProtKB:P04083}; Peripheral membrane protein {ECO:0000250|UniProtKB:P04083}; Extracellular side {ECO:0000250|UniProtKB:P04083}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P10107}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:P10107}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:P10107}. Note=Colocalizes with actin fibers at phagocytic cups. Secreted, at least in part via exosomes and other secretory vesicles. Detected in exosomes and other extracellular vesicles. Secretion is increased in response to wounding and inflammation (By similarity). Alternatively, the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in the protein translocation from the cytoplasm into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (By similarity). Detected in gelatinase granules in resting neutrophils. Neutrophil adhesion to endothelial cells stimulates secretion via gelatinase granules, but foreign particle phagocytosis has no effect. Displays calcium-dependent binding to phospholipid membranes (PubMed:3020049). {ECO:0000250|UniProtKB:P04083, ECO:0000250|UniProtKB:P10107, ECO:0000269|PubMed:3020049}.
Interaction partners:
- Protein S100-A11
- Annexin A2
- Protein S100-A10
- Cellular tumor antigen p53
- Protein S100
- G protein subunit beta 2
- Tetraspanin
- Plasminogen
- CD9 antigen
- Protein S100-A6
Sequence:
MAMVSEFLKQAWFIDNEEQEYIKTVKGSKGGPGSAVSPYPTFNPSSDVEASHKAITVKGVDEATIIEIHTKRTNAQRQQIKAAYLQEKGKPLDEALKKALTGHLEEVALALLKTPAQFDADELRAAMKGLGTDEDTLNEILASRTNREIREINRVYKEELKRDLAKDITSDTSGDYQKALLSLAKGDRSEDLAINDDLADTDARALYEAGERRKGTDLNVFITILTTRSYLHLRRVFQKYSKYSKHDMNKVLDLELKGDIENCLTVVVKCATSKPMFFAEKLHQAMKGNGTRHKTLIRIMVSRSEIDMNDIKACYQKLYGISLCQAILDETKGDYEKILVALCGGD