ID ANXA1_MOUSE Reviewed; 346 AA. AC P10107; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 224. DE RecName: Full=Annexin A1; DE AltName: Full=Annexin I; DE AltName: Full=Annexin-1; DE AltName: Full=Calpactin II; DE AltName: Full=Calpactin-2; DE AltName: Full=Chromobindin-9; DE AltName: Full=Lipocortin I {ECO:0000303|PubMed:2974946}; DE AltName: Full=Phospholipase A2 inhibitory protein; DE AltName: Full=p35; DE Contains: DE RecName: Full=Annexin Ac2-26 {ECO:0000250|UniProtKB:P04083}; GN Name=Anxa1; Synonyms=Anx1, Lpc-1, Lpc1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2974946; DOI=10.1093/nar/16.24.11818; RA Sakata T., Iwagami S., Tsuruta Y., Suzuki R., Hojo K., Sato K., Teraoka H.; RT "Mouse lipocortin I cDNA."; RL Nucleic Acids Res. 16:11818-11818(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1676980; DOI=10.1016/0888-7543(91)90321-5; RA Horlick K.R., Cheng I.C., Wong W.T., Wakeland E.K., Nick H.S.; RT "Mouse lipocortin I gene structure and chromosomal assignment: gene RT duplication and the origins of a gene family."; RL Genomics 10:365-374(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-346, AND INDUCTION BY GLUCOCORTICOIDS. RX PubMed=2522299; DOI=10.1016/0006-291x(89)92417-0; RA Philipps C., Rose-John S., Rincke G., Fuerstenberger G., Marks F.; RT "cDNA-cloning, sequencing and expression in glucocorticoid-stimulated RT quiescent Swiss 3T3 fibroblasts of mouse lipocortin I."; RL Biochem. Biophys. Res. Commun. 159:155-162(1989). RN [5] RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=12475898; DOI=10.1096/fj.02-0239fje; RA Hannon R., Croxtall J.D., Getting S.J., Roviezzo F., Yona S., RA Paul-Clark M.J., Gavins F.N., Perretti M., Morris J.F., Buckingham J.C., RA Flower R.J.; RT "Aberrant inflammation and resistance to glucocorticoids in annexin RT 1-/- mouse."; RL FASEB J. 17:253-255(2003). RN [6] RP INTERACTION WITH DYSF, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=14506282; DOI=10.1074/jbc.m307247200; RA Lennon N.J., Kho A., Bacskai B.J., Perlmutter S.L., Hyman B.T., RA Brown R.H. Jr.; RT "Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal RT wound-healing."; RL J. Biol. Chem. 278:50466-50473(2003). RN [7] RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE RP SPECIFICITY. RX PubMed=17384087; DOI=10.1152/ajplung.00014.2007; RA Reynolds S.D., Reynolds P.R., Snyder J.C., Whyte F., Paavola K.J., RA Stripp B.R.; RT "CCSP regulates cross talk between secretory cells and both ciliated cells RT and macrophages of the conducting airway."; RL Am. J. Physiol. 293:L114-L123(2007). RN [8] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=17948261; DOI=10.1002/eji.200636792; RA D'Acquisto F., Paschalidis N., Sampaio A.L., Merghani A., Flower R.J., RA Perretti M.; RT "Impaired T cell activation and increased Th2 lineage commitment in RT Annexin-1-deficient T cells."; RL Eur. J. Immunol. 37:3131-3142(2007). RN [9] RP REVIEW. RX PubMed=18641677; DOI=10.1038/bjp.2008.252; RA D'Acquisto F., Perretti M., Flower R.J.; RT "Annexin-A1: a pivotal regulator of the innate and adaptive immune RT systems."; RL Br. J. Pharmacol. 155:152-169(2008). RN [10] RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=18802107; DOI=10.4049/jimmunol.181.7.5035; RA Babbin B.A., Laukoetter M.G., Nava P., Koch S., Lee W.Y., Capaldo C.T., RA Peatman E., Severson E.A., Flower R.J., Perretti M., Parkos C.A., RA Nusrat A.; RT "Annexin A1 regulates intestinal mucosal injury, inflammation, and RT repair."; RL J. Immunol. 181:5035-5044(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-21, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [12] RP REVIEW. RX PubMed=19104500; DOI=10.1038/nri2470; RA Perretti M., D'Acquisto F.; RT "Annexin A1 and glucocorticoids as effectors of the resolution of RT inflammation."; RL Nat. Rev. Immunol. 9:62-70(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=21245195; DOI=10.1242/jcs.076208; RA Patel D.M., Ahmad S.F., Weiss D.G., Gerke V., Kuznetsov S.A.; RT "Annexin A1 is a new functional linker between actin filaments and RT phagosomes during phagocytosis."; RL J. Cell Sci. 124:578-588(2011). RN [15] RP SUMOYLATION AT LYS-257, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF LYS-257. RX PubMed=23727357; DOI=10.1016/j.cellsig.2013.05.028; RA Caron D., Maaroufi H., Michaud S., Tanguay R.M., Faure R.L.; RT "Annexin A1 is regulated by domains cross-talk through post-translational RT phosphorylation and SUMOYlation."; RL Cell. Signal. 25:1962-1969(2013). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58 AND LYS-312, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [17] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=25664854; DOI=10.1172/jci76693; RA Leoni G., Neumann P.A., Kamaly N., Quiros M., Nishio H., Jones H.R., RA Sumagin R., Hilgarth R.S., Alam A., Fredman G., Argyris I., Rijcken E., RA Kusters D., Reutelingsperger C., Perretti M., Parkos C.A., Farokhzad O.C., RA Neish A.S., Nusrat A.; RT "Annexin A1-containing extracellular vesicles and polymeric nanoparticles RT promote epithelial wound repair."; RL J. Clin. Invest. 125:1215-1227(2015). CC -!- FUNCTION: Plays important roles in the innate immune response as CC effector of glucocorticoid-mediated responses and regulator of the CC inflammatory process. Has anti-inflammatory activity (PubMed:12475898). CC Plays a role in glucocorticoid-mediated down-regulation of the early CC phase of the inflammatory response (PubMed:12475898). Contributes to CC the adaptive immune response by enhancing signaling cascades that are CC triggered by T-cell activation, regulates differentiation and CC proliferation of activated T-cells (PubMed:17948261). Promotes the CC differentiation of T-cells into Th1 cells and negatively regulates CC differentiation into Th2 cells (PubMed:17948261). Has no effect on CC unstimulated T-cells. Negatively regulates hormone exocytosis via CC activation of the formyl peptide receptors and reorganization of the CC actin cytoskeleton (By similarity). Has high affinity for Ca(2+) and CC can bind up to eight Ca(2+) ions (By similarity). Displays Ca(2+)- CC dependent binding to phospholipid membranes (By similarity). Plays a CC role in the formation of phagocytic cups and phagosomes CC (PubMed:21245195). Plays a role in phagocytosis by mediating the CC Ca(2+)-dependent interaction between phagosomes and the actin CC cytoskeleton (PubMed:21245195). {ECO:0000250|UniProtKB:P04083, CC ECO:0000250|UniProtKB:P19619, ECO:0000269|PubMed:12475898, CC ECO:0000269|PubMed:17948261, ECO:0000269|PubMed:21245195, CC ECO:0000269|PubMed:25664854}. CC -!- FUNCTION: [Annexin Ac2-26]: Functions at least in part by activating CC the formyl peptide receptors and downstream signaling cascades. CC Promotes chemotaxis of granulocytes and monocytes via activation of the CC formyl peptide receptors. Promotes rearrangement of the actin CC cytoskeleton, cell polarization and cell migration. Promotes resolution CC of inflammation and wound healing. Acts via neutrophil N-formyl peptide CC receptors to enhance the release of CXCL2. CC {ECO:0000250|UniProtKB:P04083}. CC -!- SUBUNIT: Homodimer; non-covalently linked (By similarity). Homodimer; CC linked by transglutamylation. Homodimers linked by transglutamylation CC are observed in placenta, but not in other tissues. Interacts with CC S100A11. Heterotetramer, formed by two molecules each of S100A11 and CC ANXA1 (By similarity). Interacts with DYSF (PubMed:14506282). Interacts CC with EGFR (By similarity). {ECO:0000250|UniProtKB:P04083, CC ECO:0000250|UniProtKB:P19619, ECO:0000269|PubMed:14506282}. CC -!- INTERACTION: CC P10107; A0A0F6B5H5: pipB2; Xeno; NbExp=5; IntAct=EBI-647848, EBI-27033185; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07150}. Cytoplasm CC {ECO:0000269|PubMed:18802107, ECO:0000269|PubMed:21245195}. Cell CC projection, cilium {ECO:0000269|PubMed:17384087}. Basolateral cell CC membrane {ECO:0000250|UniProtKB:P51662}. Lateral cell membrane CC {ECO:0000269|PubMed:18802107}. Cell membrane CC {ECO:0000269|PubMed:14506282, ECO:0000269|PubMed:21245195}; Peripheral CC membrane protein {ECO:0000305}. Apical cell membrane CC {ECO:0000269|PubMed:17384087, ECO:0000269|PubMed:18802107}. Membrane CC {ECO:0000269|PubMed:23727357}; Peripheral membrane protein CC {ECO:0000269|PubMed:23727357}. Early endosome CC {ECO:0000250|UniProtKB:P19619}. Cytoplasmic vesicle membrane CC {ECO:0000250|UniProtKB:P19619}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P19619}. Endosome membrane CC {ECO:0000250|UniProtKB:P07150}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P07150}. Secreted {ECO:0000269|PubMed:25664854}. CC Secreted, extracellular space {ECO:0000250|UniProtKB:P04083}. Cell CC membrane {ECO:0000250|UniProtKB:P04083}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P04083}; Extracellular side CC {ECO:0000250|UniProtKB:P04083}. Secreted, extracellular exosome CC {ECO:0000269|PubMed:25664854}. Cytoplasmic vesicle, secretory vesicle CC lumen {ECO:0000269|PubMed:25664854}. Cell projection, phagocytic cup CC {ECO:0000269|PubMed:21245195}. Note=Colocalizes with actin fibers at CC phagocytic cups (PubMed:21245195). Secreted, at least in part via CC exosomes and other secretory vesicles. Detected in exosomes and other CC extracellular vesicles (PubMed:25664854). Secretion is increased in CC response to wounding and inflammation (PubMed:25664854). Detected in CC gelatinase granules in resting neutrophils. Neutrophil adhesion to CC endothelial cells stimulates secretion via gelatinase granules, but CC foreign particle phagocytosis has no effect. Displays calcium-dependent CC binding to phospholipid membranes (By similarity). CC {ECO:0000250|UniProtKB:P04083, ECO:0000269|PubMed:25664854}. CC -!- TISSUE SPECIFICITY: Detected in lung (PubMed:12475898, CC PubMed:17384087). Detected at the apical membrane of airway epithelial CC cells (PubMed:17384087). Detected in intestinal epithelial cells CC (PubMed:18802107). Detected in skeletal muscle (PubMed:14506282). CC Detected in prostate (PubMed:23727357). Detected in thymus (at protein CC level) (PubMed:12475898). Detected in stomach, lung, spleen, ovary and CC uterus, and at lower levels in kidney, thymus and heart CC (PubMed:12475898). {ECO:0000269|PubMed:12475898, CC ECO:0000269|PubMed:14506282, ECO:0000269|PubMed:17384087, CC ECO:0000269|PubMed:23727357}. CC -!- INDUCTION: Up-regulated by the synthetic glucocorticoid fluocinolone CC acetonide. {ECO:0000269|PubMed:2522299}. CC -!- DOMAIN: The full-length protein can bind eight Ca(2+) ions via the CC annexin repeats. Calcium binding causes a major conformation change CC that modifies dimer contacts and leads to surface exposure of the N- CC terminal phosphorylation sites; in the absence of Ca(2+), these sites CC are buried in the interior of the protein core. The N-terminal region CC becomes disordered in response to calcium-binding. CC {ECO:0000250|UniProtKB:P19619}. CC -!- PTM: Phosphorylated by protein kinase C, EGFR and TRPM7. Phosphorylated CC in response to EGF treatment. {ECO:0000250|UniProtKB:P04083}. CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:23727357}. CC -!- PTM: Proteolytically cleaved by cathepsin CTSG to release the active N- CC terminal peptide Ac2-26. {ECO:0000250|UniProtKB:P04083}. CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate, CC appear healthy and are fertile, but tend to die already after about one CC year. Mutant mice display an increased inflammatory response during CC zymosan-induced peritonitis, with increased blood leukocyte migration CC and increased production of IL1B. In mutant mice, glucocorticoid- CC mediated down-regulation of the early phase of the inflammatory CC response is abolished, but there is no effect on glucocorticoid- CC mediated down-regulation of later phases of the inflammatory response. CC Peritoneal lavage macrophages from mutant mice display decreased CC phagocytosis. Besides, glucocorticoid-mediated inhibition of CC phagocytosis is abolished (PubMed:12475898). Mutant mice display CC increased susceptibility to dextran sulfate sodium (DSS)-induced CC colitis with increased mucosal injury, slower recovery and increased CC morbidity (PubMed:18802107). Mutant mice have an exacerbated allergic CC response after exposure to ovalbumin (PubMed:17948261). T-cells from CC mutant mice show skewed differentiation into Th1 and Th2 cells with CC increased differentiation into Th2 cells and decreased differentiation CC into Th1 cells (PubMed:17948261). {ECO:0000269|PubMed:12475898, CC ECO:0000269|PubMed:17948261, ECO:0000269|PubMed:18802107}. CC -!- MISCELLANEOUS: Was originally identified as calcium and phospholipid CC binding protein that displays Ca(2+)-dependent binding to phospholipid CC membranes and can promote membrane aggregation in vitro. Was initially CC identified as inhibitor of phospholipase A2 activity (in vitro). CC Inhibition of phospholipase activity is mediated via its phospholipid CC binding activity that limits the access of phospholipase to its CC substrates. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE- CC ProRule:PRU01245, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X07486; CAA30371.1; -; mRNA. DR EMBL; M69260; AAA39437.1; -; Genomic_DNA. DR EMBL; M69250; AAA39437.1; JOINED; Genomic_DNA. DR EMBL; M69251; AAA39437.1; JOINED; Genomic_DNA. DR EMBL; M69252; AAA39437.1; JOINED; Genomic_DNA. DR EMBL; M69253; AAA39437.1; JOINED; Genomic_DNA. DR EMBL; M69254; AAA39437.1; JOINED; Genomic_DNA. DR EMBL; M69255; AAA39437.1; JOINED; Genomic_DNA. DR EMBL; M69256; AAA39437.1; JOINED; Genomic_DNA. DR EMBL; M69257; AAA39437.1; JOINED; Genomic_DNA. DR EMBL; M69258; AAA39437.1; JOINED; Genomic_DNA. DR EMBL; M69259; AAA39437.1; JOINED; Genomic_DNA. DR EMBL; BC002289; AAH02289.1; -; mRNA. DR EMBL; BC004594; AAH04594.1; -; mRNA. DR EMBL; M24554; AAA39420.1; -; mRNA. DR CCDS; CCDS29692.1; -. DR PIR; S02181; LUMS1. DR RefSeq; NP_034860.2; NM_010730.2. DR AlphaFoldDB; P10107; -. DR SMR; P10107; -. DR BioGRID; 201194; 24. DR IntAct; P10107; 7. DR MINT; P10107; -. DR STRING; 10090.ENSMUSP00000025561; -. DR GlyGen; P10107; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P10107; -. DR PhosphoSitePlus; P10107; -. DR SwissPalm; P10107; -. DR EPD; P10107; -. DR jPOST; P10107; -. DR PaxDb; 10090-ENSMUSP00000025561; -. DR ProteomicsDB; 282127; -. DR Antibodypedia; 2190; 1427 antibodies from 52 providers. DR DNASU; 16952; -. DR Ensembl; ENSMUST00000025561.8; ENSMUSP00000025561.8; ENSMUSG00000024659.16. DR Ensembl; ENSMUST00000235280.2; ENSMUSP00000158305.2; ENSMUSG00000024659.16. DR GeneID; 16952; -. DR KEGG; mmu:16952; -. DR UCSC; uc008gyi.1; mouse. DR AGR; MGI:96819; -. DR CTD; 301; -. DR MGI; MGI:96819; Anxa1. DR VEuPathDB; HostDB:ENSMUSG00000024659; -. DR eggNOG; KOG0819; Eukaryota. DR GeneTree; ENSGT00940000155221; -. DR HOGENOM; CLU_025300_0_0_1; -. DR InParanoid; P10107; -. DR OMA; FMENQEQ; -. DR OrthoDB; 1500773at2759; -. DR PhylomeDB; P10107; -. DR TreeFam; TF105452; -. DR Reactome; R-MMU-416476; G alpha (q) signalling events. DR Reactome; R-MMU-418594; G alpha (i) signalling events. DR Reactome; R-MMU-444473; Formyl peptide receptors bind formyl peptides and many other ligands. DR BioGRID-ORCS; 16952; 2 hits in 78 CRISPR screens. DR ChiTaRS; Anxa1; mouse. DR PRO; PR:P10107; -. DR Proteomes; UP000000589; Chromosome 19. DR RNAct; P10107; Protein. DR Bgee; ENSMUSG00000024659; Expressed in stroma of bone marrow and 234 other cell types or tissues. DR ExpressionAtlas; P10107; baseline and differential. DR GO; GO:0005884; C:actin filament; IEA:Ensembl. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0001533; C:cornified envelope; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB. DR GO; GO:0005768; C:endosome; ISO:MGI. DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB. DR GO; GO:0042629; C:mast cell granule; ISO:MGI. DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI. DR GO; GO:0031514; C:motile cilium; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IMP:CACAO. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0042383; C:sarcolemma; IDA:MGI. DR GO; GO:0097060; C:synaptic membrane; ISO:MGI. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB. DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI. DR GO; GO:1990814; F:DNA/DNA annealing activity; ISO:MGI. DR GO; GO:0036121; F:double-stranded DNA helicase activity; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0008289; F:lipid binding; ISO:MGI. DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; ISO:MGI. DR GO; GO:0005543; F:phospholipid binding; ISO:MGI. DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI. DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0046632; P:alpha-beta T cell differentiation; IMP:BHF-UCL. DR GO; GO:0050482; P:arachidonic acid secretion; IMP:MGI. DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI. DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IMP:UniProtKB. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI. DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISO:MGI. DR GO; GO:0032508; P:DNA duplex unwinding; ISO:MGI. DR GO; GO:0031018; P:endocrine pancreas development; IBA:GO_Central. DR GO; GO:0044849; P:estrous cycle; IBA:GO_Central. DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; ISS:UniProtKB. DR GO; GO:0042063; P:gliogenesis; IBA:GO_Central. DR GO; GO:0071621; P:granulocyte chemotaxis; ISS:UniProtKB. DR GO; GO:0070365; P:hepatocyte differentiation; IBA:GO_Central. DR GO; GO:0006954; P:inflammatory response; IMP:UniProtKB. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0030073; P:insulin secretion; ISO:MGI. DR GO; GO:0030216; P:keratinocyte differentiation; ISO:MGI. DR GO; GO:0051179; P:localization; ISO:MGI. DR GO; GO:0002548; P:monocyte chemotaxis; ISS:UniProtKB. DR GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; IDA:CACAO. DR GO; GO:0045920; P:negative regulation of exocytosis; ISS:UniProtKB. DR GO; GO:0032717; P:negative regulation of interleukin-8 production; ISO:MGI. DR GO; GO:0050709; P:negative regulation of protein secretion; ISO:MGI. DR GO; GO:0045629; P:negative regulation of T-helper 2 cell differentiation; ISS:UniProtKB. DR GO; GO:0042119; P:neutrophil activation; ISS:UniProtKB. DR GO; GO:0097350; P:neutrophil clearance; ISO:MGI. DR GO; GO:0001780; P:neutrophil homeostasis; IMP:BHF-UCL. DR GO; GO:0006909; P:phagocytosis; IMP:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI. DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:MGI. DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:MGI. DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISS:UniProtKB. DR GO; GO:0033031; P:positive regulation of neutrophil apoptotic process; IMP:BHF-UCL. DR GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; ISO:MGI. DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB. DR GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; ISS:UniProtKB. DR GO; GO:0031340; P:positive regulation of vesicle fusion; ISO:MGI. DR GO; GO:0090303; P:positive regulation of wound healing; ISS:UniProtKB. DR GO; GO:0070459; P:prolactin secretion; ISO:MGI. DR GO; GO:0030850; P:prostate gland development; IBA:GO_Central. DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI. DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB. DR GO; GO:0046883; P:regulation of hormone secretion; ISS:UniProtKB. DR GO; GO:0050727; P:regulation of inflammatory response; IMP:UniProtKB. DR GO; GO:0032652; P:regulation of interleukin-1 production; IMP:UniProtKB. DR GO; GO:0002685; P:regulation of leukocyte migration; IMP:UniProtKB. DR GO; GO:0032355; P:response to estradiol; IBA:GO_Central. DR GO; GO:0070555; P:response to interleukin-1; IBA:GO_Central. DR GO; GO:0043434; P:response to peptide hormone; IBA:GO_Central. DR GO; GO:0010165; P:response to X-ray; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; IMP:MGI. DR Gene3D; 1.10.220.10; Annexin; 4. DR InterPro; IPR001464; Annexin. DR InterPro; IPR018502; Annexin_repeat. DR InterPro; IPR018252; Annexin_repeat_CS. DR InterPro; IPR037104; Annexin_sf. DR InterPro; IPR002388; ANX1. DR PANTHER; PTHR10502; ANNEXIN; 1. DR PANTHER; PTHR10502:SF17; ANNEXIN A1; 1. DR Pfam; PF00191; Annexin; 4. DR PRINTS; PR00196; ANNEXIN. DR PRINTS; PR00197; ANNEXINI. DR SMART; SM00335; ANX; 4. DR SUPFAM; SSF47874; Annexin; 1. DR PROSITE; PS00223; ANNEXIN_1; 4. DR PROSITE; PS51897; ANNEXIN_2; 4. DR COMPLUYEAST-2DPAGE; P10107; -. DR Genevisible; P10107; MM. PE 1: Evidence at protein level; KW Acetylation; Adaptive immunity; Annexin; Calcium; KW Calcium/phospholipid-binding; Cell membrane; Cell projection; Cilium; KW Cytoplasm; Cytoplasmic vesicle; Disulfide bond; Endosome; Immunity; KW Inflammatory response; Innate immunity; Isopeptide bond; Membrane; KW Metal-binding; Nucleus; Phospholipase A2 inhibitor; Phosphoprotein; KW Reference proteome; Repeat; Secreted; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P04083" FT CHAIN 2..346 FT /note="Annexin A1" FT /id="PRO_0000067461" FT PEPTIDE 2..26 FT /note="Annexin Ac2-26" FT /evidence="ECO:0000250|UniProtKB:P04083" FT /id="PRO_0000454557" FT REPEAT 42..113 FT /note="Annexin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245" FT REPEAT 114..185 FT /note="Annexin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245" FT REPEAT 197..269 FT /note="Annexin 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245" FT REPEAT 273..344 FT /note="Annexin 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245" FT BINDING 59 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 60 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 62 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 97 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 100 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 105 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 127 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 129 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 131 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 132 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 134 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 171 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 210 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 213 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 215 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 253 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 255 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 256 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 261 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 286 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="7" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 288 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="7" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 290 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="7" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 328 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="8" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 330 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="7" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 331 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="8" FT /evidence="ECO:0000250|UniProtKB:P19619" FT BINDING 336 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="8" FT /evidence="ECO:0000250|UniProtKB:P19619" FT SITE 26..27 FT /note="Cleavage; by CTSG" FT /evidence="ECO:0000250|UniProtKB:P04083" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P04083" FT MOD_RES 5 FT /note="Phosphoserine; by TRPM7" FT /evidence="ECO:0000250|UniProtKB:P04083" FT MOD_RES 21 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:19131326" FT MOD_RES 27 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000250|UniProtKB:P04083" FT MOD_RES 34 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04083" FT MOD_RES 37 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04083" FT MOD_RES 58 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 136 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P04083" FT MOD_RES 312 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT DISULFID 324..343 FT /evidence="ECO:0000250|UniProtKB:P19619" FT CROSSLNK 19 FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain FT with K-?)" FT /evidence="ECO:0000250" FT CROSSLNK 214 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P04083" FT CROSSLNK 214 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P04083" FT CROSSLNK 257 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000305|PubMed:23727357" FT CROSSLNK 332 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000250|UniProtKB:P04083" FT MUTAGEN 257 FT /note="K->R: Strongly decreased sumoylation." FT /evidence="ECO:0000269|PubMed:23727357" FT CONFLICT 78..79 FT /note="QQ -> PR (in Ref. 4; AAA39420)" FT /evidence="ECO:0000305" FT CONFLICT 212 FT /note="R -> I (in Ref. 2; AAA39437)" FT /evidence="ECO:0000305" FT CONFLICT 222 FT /note="T -> H (in Ref. 4; AAA39420)" FT /evidence="ECO:0000305" FT CONFLICT 274 FT /note="T -> H (in Ref. 4; AAA39420)" FT /evidence="ECO:0000305" SQ SEQUENCE 346 AA; 38734 MW; 9393A11B24191D3C CRC64; MAMVSEFLKQ ARFLENQEQE YVQAVKSYKG GPGSAVSPYP SFNVSSDVAA LHKAIMVKGV DEATIIDILT KRTNAQRQQI KAAYLQENGK PLDEVLRKAL TGHLEEVVLA MLKTPAQFDA DELRGAMKGL GTDEDTLIEI LTTRSNEQIR EINRVYREEL KRDLAKDITS DTSGDFRKAL LALAKGDRCQ DLSVNQDLAD TDARALYEAG ERRKGTDVNV FTTILTSRSF PHLRRVFQNY GKYSQHDMNK ALDLELKGDI EKCLTTIVKC ATSTPAFFAE KLYEAMKGAG TRHKALIRIM VSRSEIDMNE IKVFYQKKYG ISLCQAILDE TKGDYEKILV ALCGGN //