ANXA1_MOUSE
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 03-AUG-2022, entry version 215.
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, Pancreas,
RC 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}.
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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; 18.
DR IntAct; P10107; 7.
DR MINT; P10107; -.
DR STRING; 10090.ENSMUSP00000025561; -.
DR iPTMnet; P10107; -.
DR PhosphoSitePlus; P10107; -.
DR SwissPalm; P10107; -.
DR COMPLUYEAST-2DPAGE; P10107; -.
DR EPD; P10107; -.
DR jPOST; P10107; -.
DR PaxDb; P10107; -.
DR PRIDE; P10107; -.
DR ProteomicsDB; 282127; -.
DR Antibodypedia; 2190; 1227 antibodies from 52 providers.
DR DNASU; 16952; -.
DR Ensembl; ENSMUST00000025561; ENSMUSP00000025561; ENSMUSG00000024659.
DR Ensembl; ENSMUST00000235280; ENSMUSP00000158305; ENSMUSG00000024659.
DR GeneID; 16952; -.
DR KEGG; mmu:16952; -.
DR UCSC; uc008gyi.1; mouse.
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; AKADRCE; -.
DR OrthoDB; 856254at2759; -.
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 73 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 232 other tissues.
DR ExpressionAtlas; P10107; baseline and differential.
DR Genevisible; P10107; MM.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
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:0031313; C:extrinsic component of endosome membrane; ISS:UniProtKB.
DR GO; GO:0031232; C:extrinsic component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:MGI.
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: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:0003727; F:single-stranded RNA binding; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; 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: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:1900138; P:negative regulation of phospholipase A2 activity; 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:0018149; P:peptide cross-linking; ISO:MGI.
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; -; 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:SF17; PTHR10502:SF17; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR00197; ANNEXINI.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 4.
DR PROSITE; PS51897; ANNEXIN_2; 4.
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
