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] (P04083)
Organism: Homo sapiens (Human)
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 (By similarity). 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. 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. 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:0000269|PubMed:10772777, ECO:0000269|PubMed:19625660}. Cytoplasm {ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:19625660}. Cell projection, cilium {ECO:0000250|UniProtKB:P46193}. Cell membrane {ECO:0000269|PubMed:10772777}. Membrane {ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:2532504, ECO:0000269|PubMed:8557678}; Peripheral membrane protein {ECO:0000269|PubMed:2532504, ECO:0000269|PubMed:8557678}. Endosome membrane {ECO:0000250|UniProtKB:P07150}; Peripheral membrane protein {ECO:0000250|UniProtKB:P07150}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51662}. Apical cell membrane {ECO:0000250|UniProtKB:P10107}. Lateral cell membrane {ECO:0000250|UniProtKB:P10107}. Secreted {ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:19625660, ECO:0000269|PubMed:25664854}. Secreted, extracellular space {ECO:0000269|PubMed:25664854}. Cell membrane {ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:19625660, ECO:0000269|PubMed:25664854}; Peripheral membrane protein {ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:19625660, ECO:0000269|PubMed:25664854}; Extracellular side {ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:19625660, ECO:0000269|PubMed:25664854}. Secreted, extracellular exosome {ECO:0000269|PubMed:25664854}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000269|PubMed:10772777}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:P10107}. Early endosome {ECO:0000250|UniProtKB:P19619}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P19619}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19619}. Note=Secreted, at least in part via exosomes and other secretory vesicles. Detected in exosomes and other extracellular vesicles (PubMed:25664854). 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 (PubMed:32272059). Detected in gelatinase granules in resting neutrophils (PubMed:10772777). Secretion is increased in response to wounding and inflammation (PubMed:25664854). Secretion is increased upon T-cell activation (PubMed:17008549). Neutrophil adhesion to endothelial cells stimulates secretion via gelatinase granules, but foreign particle phagocytosis has no effect (PubMed:10772777). Colocalizes with actin fibers at phagocytic cups (By similarity). Displays calcium-dependent binding to phospholipid membranes (PubMed:2532504, PubMed:8557678). {ECO:0000250|UniProtKB:P10107, ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:2532504, ECO:0000269|PubMed:25664854, ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:8557678}.
Interaction partners:
- fMet-Leu-Phe receptor
- N-formyl peptide receptor 2
- Protein S100-A11
- Annexin A2
- Dysferlin
- Protein S100-A10
- N-formyl peptide receptor 3
- Tripartite motif-containing protein 72
- Caveolin-3
- Protein S100-A6
Sequence:
MAMVSEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTKRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN