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] (P10107)
Organism: Mus musculus (Mouse)
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. 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 (By similarity). Displays Ca(2+)-dependent binding to phospholipid membranes (By similarity). 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.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P07150}. Cytoplasm {ECO:0000269|PubMed:18802107, ECO:0000269|PubMed:21245195}. Cell projection, cilium {ECO:0000269|PubMed:17384087}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51662}. Lateral cell membrane {ECO:0000269|PubMed:18802107}. Cell membrane {ECO:0000269|PubMed:14506282, ECO:0000269|PubMed:21245195}; Peripheral membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:17384087, ECO:0000269|PubMed:18802107}. Membrane {ECO:0000269|PubMed:23727357}; Peripheral membrane protein {ECO:0000269|PubMed:23727357}. Early endosome {ECO:0000250|UniProtKB:P19619}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P19619}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19619}. Endosome membrane {ECO:0000250|UniProtKB:P07150}; Peripheral membrane protein {ECO:0000250|UniProtKB:P07150}. Secreted {ECO:0000269|PubMed:25664854}. 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:0000269|PubMed:25664854}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000269|PubMed:25664854}. Cell projection, phagocytic cup {ECO:0000269|PubMed:21245195}. Note=Colocalizes with actin fibers at phagocytic cups (PubMed:21245195). Secreted, at least in part via exosomes and other secretory vesicles. Detected in exosomes and other extracellular vesicles (PubMed:25664854). Secretion is increased in response to wounding and inflammation (PubMed:25664854). 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 (By similarity). {ECO:0000250|UniProtKB:P04083, ECO:0000269|PubMed:25664854}.
Interaction partners:
- Formyl peptide receptor-related sequence 1
- fMet-Leu-Phe receptor
- Formyl peptide receptor 2
- Protein S100-A11
- Annexin A2
- Dysferlin
- Protein S100-A10
- Protein S100-A4
- Tripartite motif-containing protein 72
- Annexin A6
Sequence:
MAMVSEFLKQARFLENQEQEYVQAVKSYKGGPGSAVSPYPSFNVSSDVAALHKAIMVKGVDEATIIDILTKRTNAQRQQIKAAYLQENGKPLDEVLRKALTGHLEEVVLAMLKTPAQFDADELRGAMKGLGTDEDTLIEILTTRSNEQIREINRVYREELKRDLAKDITSDTSGDFRKALLALAKGDRCQDLSVNQDLADTDARALYEAGERRKGTDVNVFTTILTSRSFPHLRRVFQNYGKYSQHDMNKALDLELKGDIEKCLTTIVKCATSTPAFFAEKLYEAMKGAGTRHKALIRIMVSRSEIDMNEIKVFYQKKYGISLCQAILDETKGDYEKILVALCGGN