Anxa1
entrez
25380
canonical
uniprot
P07150
canonical
ensembl
ENSRNOG00000017469
resolver
ensembl
ENSRNOG00055010464
resolver
ensembl
ENSRNOG00060023625
resolver
ensembl
ENSRNOG00065026926
resolver
ensp
ENSRNOP00000078049
resolver
ensp
ENSRNOP00055014286
resolver
ensp
ENSRNOP00060034086
resolver
ensp
ENSRNOP00065038135
resolver
enst
ENSRNOT00055017732
resolver
enst
ENSRNOT00060041157
resolver
enst
ENSRNOT00065046509
resolver
genesymbol
Anxa1
resolver
genesymbol_syn
Anx1
resolver
uniprot
Q64664
resolver
uniprot_entry
ANXA1_RAT
resolver
uniprot_sec
Q64664
resolver
amino_acid_sequence
MAMVSEFLKQACYIEKQEQEYVQAVKSYKGGPGSAVSPYPSFNPSSDVAALHKAIMVKGVDEATIIDILTKRTNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLAMLKTPAQFDADELRAAMKGLGTDEDTLIEILTTRSNQQIREITRVYREELKRDLAKDITSDTSGDFRNALLALAKGDRCEDMSVNQDLADTDARALYEAGERRKGTDVNVFNTILTTRSYPHLRKVFQNYRKYSQHDMNKALDLELKGDIEKCLTTIVKCATSTPAFFAEKLYEAMKGAGTRHKTLIRIMVSRSEIDMNEIKVFYQKKYGIPLCQAILDETKGDYEKILVALCGGN
uniprot
proteins
function
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 (By similarity). Displays Ca(2+)-dependent binding to phospholipid membranes (PubMed:3020049). 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). In the context of antitumor immunity, interacts with FPR1 on dendritic cells allowing for tumor-associated antigens uptake and cross-presentation to T cells to mount an antitumor specific T cell response. {ECO:0000250|UniProtKB:P04083, ECO:0000250|UniProtKB:P10107, ECO:0000250|UniProtKB:P19619, ECO:0000269|PubMed:3020049}.; FUNCTION: [Annexin Ac2-26]: Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades. Promotes chemotaxis of granulocytes and monocytes via activation of the formyl peptide receptors. Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration. Promotes resolution of inflammation and wound healing. Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2. {ECO:0000250|UniProtKB:P04083}.
uniprot
proteins
mass_dalton
38829
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by protein kinase C, EGFR and TRPM7. Phosphorylated in response to EGF treatment. {ECO:0000250|UniProtKB:P04083}.; PTM: Sumoylated. {ECO:0000250|UniProtKB:P10107}.; PTM: Proteolytically cleaved by cathepsin CTSG to release the active N-terminal peptide Ac2-26. {ECO:0000250|UniProtKB:P04083}.
uniprot
proteins
protein_family
Annexin family
uniprot
proteins
pubmed
12467520
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1832554
uniprot
proteins
pubmed
18641677
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
2958780
uniprot
proteins
pubmed
2969352
uniprot
proteins
pubmed
3020049
uniprot
proteins
sequence_length
346
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12467520}. Cytoplasm {ECO:0000269|PubMed:12467520}. Cell projection, cilium {ECO:0000250|UniProtKB:P10107}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51662}. Lateral cell membrane {ECO:0000250|UniProtKB:P10107}. Cell membrane {ECO:0000250|UniProtKB:P10107}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10107}. Apical cell membrane {ECO:0000250|UniProtKB:P10107}. Membrane {ECO:0000269|PubMed:3020049}; Peripheral membrane protein {ECO:0000269|PubMed:3020049}. Endosome membrane {ECO:0000269|PubMed:3020049}; Peripheral membrane protein {ECO:0000269|PubMed:3020049}. 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}. Early endosome {ECO:0000250|UniProtKB:P19619}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P19619}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19619}. 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}.
uniprot
proteins