ID ANXA1_HUMAN Reviewed; 346 AA. AC P04083; B5BU38; DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 269. 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:1832554}; DE AltName: Full=Phospholipase A2 inhibitory protein; DE AltName: Full=p35; DE Contains: DE RecName: Full=Annexin Ac2-26 {ECO:0000303|PubMed:22879591}; GN Name=ANXA1; Synonyms=ANX1, LPC1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=2936963; DOI=10.1038/320077a0; RA Wallner B.P., Mattaliano R.J., Hession C., Cate R.L., Tizard R., RA Sinclair L.K., Foeller C., Chow E.P., Browning J.L., Ramachandran K.L., RA Pepinsky R.B.; RT "Cloning and expression of human lipocortin, a phospholipase A2 inhibitor RT with potential anti-inflammatory activity."; RL Nature 320:77-81(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1832554; DOI=10.1021/bi00101a015; RA Kovacic R.T., Tizard R., Cate R.L., Frey A.Z., Wallner B.P.; RT "Correlation of gene and protein structure of rat and human lipocortin I."; RL Biochemistry 30:9015-9021(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX PubMed=8425544; DOI=10.1111/j.1432-1033.1993.tb19904.x; RA Arcone R., Arpaia G., Ruoppolo M., Malorni A., Pucci P., Marino G., RA Ialenti A., di Rosa M., Ciliberto G.; RT "Structural characterization of a biologically active human lipocortin 1 RT expressed in Escherichia coli."; RL Eur. J. Biochem. 211:347-355(1993). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cervix, and Lung; 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 [6] RP PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION AT TYR-21 BY EGFR AND SER-27 RP BY PKC. RX PubMed=2457390; DOI=10.1021/bi00410a024; RA Varticovski L., Chahwala S.B., Whitman M., Cantley L., Schindler D., RA Chow E.P., Sinclair L.K., Pepinsky R.B.; RT "Location of sites in human lipocortin I that are phosphorylated by protein RT tyrosine kinases and protein kinases A and C."; RL Biochemistry 27:3682-3690(1988). RN [7] RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=3303336; DOI=10.1126/science.3303336; RA Biemann K., Scoble H.A.; RT "Characterization by tandem mass spectrometry of structural modifications RT in proteins."; RL Science 237:992-998(1987). RN [8] RP FUNCTION, DIMERIZATION, SUBUNIT, TISSUE SPECIFICITY, PARTIAL PROTEIN RP SEQUENCE, PHOSPHORYLATION, AND SUBCELLULAR LOCATION. RX PubMed=2532504; DOI=10.1042/bj2630097; RA Pepinsky R.B., Sinclair L.K., Chow E.P., O'Brine-Greco B.; RT "A dimeric form of lipocortin-1 in human placenta."; RL Biochem. J. 263:97-103(1989). RN [9] RP INTERACTION WITH S100A11, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=8557678; DOI=10.1074/jbc.271.2.719; RA Mailliard W.S., Haigler H.T., Schlaepfer D.D.; RT "Calcium-dependent binding of S100C to the N-terminal domain of annexin RT I."; RL J. Biol. Chem. 271:719-725(1996). RN [10] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=10772777; DOI=10.1006/cbir.1999.0468; RA Perretti M., Christian H., Wheller S.K., Aiello I., Mugridge K.G., RA Morris J.F., Flower R.J., Goulding N.J.; RT "Annexin I is stored within gelatinase granules of human neutrophil and RT mobilized on the cell surface upon adhesion but not phagocytosis."; RL Cell Biol. Int. 24:163-174(2000). RN [11] RP PHOSPHORYLATION AT SER-5 BY TRPM7. RX PubMed=15485879; DOI=10.1074/jbc.c400441200; RA Dorovkov M.V., Ryazanov A.G.; RT "Phosphorylation of annexin I by TRPM7 channel-kinase."; RL J. Biol. Chem. 279:50643-50646(2004). RN [12] RP FUNCTION. RX PubMed=15187149; DOI=10.4049/jimmunol.172.12.7669; RA Ernst S., Lange C., Wilbers A., Goebeler V., Gerke V., Rescher U.; RT "An annexin 1 N-terminal peptide activates leukocytes by triggering RT different members of the formyl peptide receptor family."; RL J. Immunol. 172:7669-7676(2004). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=17008549; DOI=10.1182/blood-2006-05-022798; RA D'Acquisto F., Merghani A., Lecona E., Rosignoli G., Raza K., Buckley C.D., RA Flower R.J., Perretti M.; RT "Annexin-1 modulates T-cell activation and differentiation."; RL Blood 109:1095-1102(2007). RN [14] 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 [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [16] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-27; SER-34 AND RP SER-45. RX PubMed=19625660; DOI=10.1096/fj.09-131391; RA McArthur S., Yazid S., Christian H., Sirha R., Flower R., Buckingham J., RA Solito E.; RT "Annexin A1 regulates hormone exocytosis through a mechanism involving RT actin reorganization."; RL FASEB J. 23:4000-4010(2009). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239 AND LYS-312, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP FUNCTION, AND PROTEOLYTIC CLEAVAGE. RX PubMed=22879591; DOI=10.1074/jbc.m112.394452; RA Woloszynek J.C., Hu Y., Pham C.T.; RT "Cathepsin G-regulated release of formyl peptide receptor agonists modulate RT neutrophil effector functions."; RL J. Biol. Chem. 287:34101-34109(2012). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-37; THR-41 AND RP THR-136, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-214 AND LYS-332, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-214, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [25] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. 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). RN [26] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-214, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, AND RP CALCIUM-BINDING. RX PubMed=8453382; DOI=10.1002/pro.5560020317; RA Weng X., Luecke H., Song I.S., Kang D.S., Kim S.-H., Huber R.; RT "Crystal structure of human annexin I at 2.5-A resolution."; RL Protein Sci. 2:448-458(1993). RN [28] RP STRUCTURE BY NMR OF 41-113. RX PubMed=9915835; DOI=10.1074/jbc.274.5.2971; RA Gao J., Li Y., Yan H.; RT "NMR solution structure of domain 1 of human annexin I shows an autonomous RT folding unit."; RL J. Biol. Chem. 274:2971-2977(1999). RN [29] RP SUBCELLULAR LOCATION. RX PubMed=32272059; DOI=10.1016/j.cell.2020.03.031; RA Zhang M., Liu L., Lin X., Wang Y., Li Y., Guo Q., Li S., Sun Y., Tao X., RA Zhang D., Lv X., Zheng L., Ge L.; RT "A Translocation Pathway for Vesicle-Mediated Unconventional Protein RT Secretion."; RL Cell 181:637-652(2020). RN [30] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-12 IN COMPLEX WITH S100A11, AND RP INTERACTION WITH S100A11. RX PubMed=10673436; DOI=10.1016/s0969-2126(00)00093-9; RA Rety S., Osterloh D., Arie J.-P., Tabaries S., Seeman J., Russo-Marie F., RA Gerke V., Lewit-Bentley A.; RT "Structural basis of the Ca(2+)-dependent association between S100C RT (S100A11) and its target, the N-terminal part of annexin I."; RL Structure 8:175-184(2000). 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:8425544). CC Plays a role in glucocorticoid-mediated down-regulation of the early CC phase of the inflammatory response (By similarity). Contributes to the CC 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:17008549). Promotes the CC differentiation of T-cells into Th1 cells and negatively regulates CC differentiation into Th2 cells (PubMed:17008549). Has no effect on CC unstimulated T cells (PubMed:17008549). Negatively regulates hormone CC exocytosis via activation of the formyl peptide receptors and CC reorganization of the actin cytoskeleton (PubMed:19625660). Has high CC affinity for Ca(2+) and can bind up to eight Ca(2+) ions (By CC similarity). Displays Ca(2+)-dependent binding to phospholipid CC membranes (PubMed:2532504, PubMed:8557678). Plays a role in the CC formation of phagocytic cups and phagosomes. Plays a role in CC phagocytosis by mediating the Ca(2+)-dependent interaction between CC phagosomes and the actin cytoskeleton (By similarity). CC {ECO:0000250|UniProtKB:P10107, ECO:0000250|UniProtKB:P19619, CC ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:19625660, CC ECO:0000269|PubMed:2532504, ECO:0000269|PubMed:2936963, CC ECO:0000269|PubMed:8425544, ECO:0000269|PubMed:8557678}. CC -!- FUNCTION: [Annexin Ac2-26]: Functions at least in part by activating CC the formyl peptide receptors and downstream signaling cascades CC (PubMed:22879591, PubMed:15187149, PubMed:25664854). Promotes CC chemotaxis of granulocytes and monocytes via activation of the formyl CC peptide receptors (PubMed:15187149). Promotes rearrangement of the CC actin cytoskeleton, cell polarization and cell migration CC (PubMed:15187149). Promotes resolution of inflammation and wound CC healing (PubMed:25664854). Acts via neutrophil N-formyl peptide CC receptors to enhance the release of CXCL2 (PubMed:22879591). CC {ECO:0000269|PubMed:15187149, ECO:0000269|PubMed:22879591, CC ECO:0000269|PubMed:25664854}. CC -!- SUBUNIT: Homodimer; non-covalently linked (By similarity). Homodimer; CC linked by transglutamylation (PubMed:2532504). Homodimers linked by CC transglutamylation are observed in placenta, but not in other tissues CC (PubMed:2532504). Interacts with S100A11 (PubMed:8557678, CC PubMed:10673436). Heterotetramer, formed by two molecules each of CC S100A11 and ANXA1 (PubMed:10673436). Interacts with DYSF (By CC similarity). Interacts with EGFR (By similarity). CC {ECO:0000250|UniProtKB:P10107, ECO:0000250|UniProtKB:P19619, CC ECO:0000269|PubMed:10673436, ECO:0000269|PubMed:2532504, CC ECO:0000269|PubMed:8557678}. CC -!- INTERACTION: CC P04083; P00533: EGFR; NbExp=3; IntAct=EBI-354007, EBI-297353; CC P04083; Q9NVM1: EVA1B; NbExp=3; IntAct=EBI-354007, EBI-10314666; CC P04083; Q9Y6K9: IKBKG; NbExp=6; IntAct=EBI-354007, EBI-81279; CC P04083; Q6P5S2: LEG1; NbExp=3; IntAct=EBI-354007, EBI-11750531; CC P04083; Q9C0E8-2: LNPK; NbExp=3; IntAct=EBI-354007, EBI-11024283; CC P04083; Q13546: RIPK1; NbExp=5; IntAct=EBI-354007, EBI-358507; CC P04083; Q96EF9: ZHX1-C8orf76; NbExp=3; IntAct=EBI-354007, EBI-25830993; CC P04083; A0A0F6AZQ1: pipB; Xeno; NbExp=2; IntAct=EBI-354007, EBI-27033737; CC P04083; A0A0F6B5H5: pipB2; Xeno; NbExp=2; IntAct=EBI-354007, EBI-27033185; CC P04083; A0A0F6B1Q8: sseJ; Xeno; NbExp=3; IntAct=EBI-354007, EBI-10760263; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10772777, CC ECO:0000269|PubMed:19625660}. Cytoplasm {ECO:0000269|PubMed:10772777, CC ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:19625660}. Cell CC projection, cilium {ECO:0000250|UniProtKB:P46193}. Cell membrane CC {ECO:0000269|PubMed:10772777}. Membrane {ECO:0000269|PubMed:17008549, CC ECO:0000269|PubMed:2532504, ECO:0000269|PubMed:8557678}; Peripheral CC membrane protein {ECO:0000269|PubMed:2532504, CC ECO:0000269|PubMed:8557678}. Endosome membrane CC {ECO:0000250|UniProtKB:P07150}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P07150}. Basolateral cell membrane CC {ECO:0000250|UniProtKB:P51662}. Apical cell membrane CC {ECO:0000250|UniProtKB:P10107}. Lateral cell membrane CC {ECO:0000250|UniProtKB:P10107}. Secreted {ECO:0000269|PubMed:17008549, CC ECO:0000269|PubMed:19625660, ECO:0000269|PubMed:25664854}. Secreted, CC extracellular space {ECO:0000269|PubMed:25664854}. Cell membrane CC {ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:19625660, CC ECO:0000269|PubMed:25664854}; Peripheral membrane protein CC {ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:19625660, CC ECO:0000269|PubMed:25664854}; Extracellular side CC {ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:19625660, CC ECO:0000269|PubMed:25664854}. Secreted, extracellular exosome CC {ECO:0000269|PubMed:25664854}. Cytoplasmic vesicle, secretory vesicle CC lumen {ECO:0000269|PubMed:10772777}. Cell projection, phagocytic cup CC {ECO:0000250|UniProtKB:P10107}. Early endosome CC {ECO:0000250|UniProtKB:P19619}. Cytoplasmic vesicle membrane CC {ECO:0000250|UniProtKB:P19619}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P19619}. Note=Secreted, at least in part via CC exosomes and other secretory vesicles. Detected in exosomes and other CC extracellular vesicles (PubMed:25664854). Alternatively, the secretion CC is dependent on protein unfolding and facilitated by the cargo receptor CC TMED10; it results in the protein translocation from the cytoplasm into CC ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed CC by vesicle entry and secretion (PubMed:32272059). Detected in CC gelatinase granules in resting neutrophils (PubMed:10772777). Secretion CC is increased in response to wounding and inflammation CC (PubMed:25664854). Secretion is increased upon T-cell activation CC (PubMed:17008549). Neutrophil adhesion to endothelial cells stimulates CC secretion via gelatinase granules, but foreign particle phagocytosis CC has no effect (PubMed:10772777). Colocalizes with actin fibers at CC phagocytic cups (By similarity). Displays calcium-dependent binding to CC phospholipid membranes (PubMed:2532504, PubMed:8557678). CC {ECO:0000250|UniProtKB:P10107, ECO:0000269|PubMed:10772777, CC ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:2532504, CC ECO:0000269|PubMed:25664854, ECO:0000269|PubMed:32272059, CC ECO:0000269|PubMed:8557678}. CC -!- TISSUE SPECIFICITY: Detected in resting neutrophils (PubMed:10772777). CC Detected in peripheral blood T-cells (PubMed:17008549). Detected in CC extracellular vesicles in blood serum from patients with inflammatory CC bowel disease, but not in serum from healthy donors (PubMed:25664854). CC Detected in placenta (at protein level) (PubMed:2532504). Detected in CC liver. {ECO:0000269|PubMed:2532504, ECO:0000269|PubMed:2936963}. 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 CC (PubMed:2457390, PubMed:15485879). Phosphorylated in response to EGF CC treatment (PubMed:2532504). {ECO:0000269|PubMed:15485879, CC ECO:0000269|PubMed:2457390, ECO:0000269|PubMed:2532504}. CC -!- PTM: Sumoylated. {ECO:0000250|UniProtKB:P10107}. CC -!- PTM: Proteolytically cleaved by cathepsin CTSG to release the active N- CC terminal peptide Ac2-26. {ECO:0000269|PubMed:22879591}. CC -!- PHARMACEUTICAL: Peptides based on the N-terminal sequence might be used CC for the treatment of inflammation, e.g. in chronic bowel diseases and CC in rheumatoid arthritis. {ECO:0000305}. 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 (PubMed:2936963, PubMed:8425544). Inhibition of phospholipase activity CC is mediated via its phospholipid binding activity that limits the CC access of phospholipase to its substrates. {ECO:0000269|PubMed:2936963, CC ECO:0000269|PubMed:8425544, ECO:0000305}. CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE- CC ProRule:PRU01245, ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/653/ANXA1"; 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; X05908; CAA29338.1; -; mRNA. DR EMBL; AB451274; BAG70088.1; -; mRNA. DR EMBL; AB451401; BAG70215.1; -; mRNA. DR EMBL; BC001275; AAH01275.1; -; mRNA. DR EMBL; BC035993; AAH35993.1; -; mRNA. DR CCDS; CCDS6645.1; -. DR PIR; A03080; LUHU. DR RefSeq; NP_000691.1; NM_000700.2. DR RefSeq; XP_011516911.1; XM_011518609.1. DR PDB; 1AIN; X-ray; 2.50 A; A=33-346. DR PDB; 1BO9; NMR; -; A=41-113. DR PDB; 1QLS; X-ray; 2.30 A; D=2-12. DR PDB; 5VFW; NMR; -; A=2-26. DR PDBsum; 1AIN; -. DR PDBsum; 1BO9; -. DR PDBsum; 1QLS; -. DR PDBsum; 5VFW; -. DR AlphaFoldDB; P04083; -. DR SMR; P04083; -. DR BioGRID; 106798; 250. DR DIP; DIP-32875N; -. DR IntAct; P04083; 120. DR MINT; P04083; -. DR STRING; 9606.ENSP00000366109; -. DR DrugBank; DB00288; Amcinonide. DR DrugBank; DB14669; Betamethasone phosphate. DR DrugBank; DB01222; Budesonide. DR DrugBank; DB01013; Clobetasol propionate. DR DrugBank; DB01380; Cortisone acetate. DR DrugBank; DB01234; Dexamethasone. DR DrugBank; DB14649; Dexamethasone acetate. DR DrugBank; DB00591; Fluocinolone acetonide. DR DrugBank; DB00741; Hydrocortisone. DR DrugBank; DB14538; Hydrocortisone aceponate. DR DrugBank; DB14539; Hydrocortisone acetate. DR DrugBank; DB14540; Hydrocortisone butyrate. DR DrugBank; DB14541; Hydrocortisone cypionate. DR DrugBank; DB14542; Hydrocortisone phosphate. DR DrugBank; DB14543; Hydrocortisone probutate. DR DrugBank; DB14544; Hydrocortisone valerate. DR DrugBank; DB00959; Methylprednisolone. DR DrugBank; DB14631; Prednisolone phosphate. DR DrugCentral; P04083; -. DR TCDB; 1.A.31.1.3; the annexin (annexin) family. DR GlyGen; P04083; 2 sites, 2 O-linked glycans (2 sites). DR iPTMnet; P04083; -. DR MetOSite; P04083; -. DR PhosphoSitePlus; P04083; -. DR SwissPalm; P04083; -. DR BioMuta; ANXA1; -. DR DMDM; 113944; -. DR DOSAC-COBS-2DPAGE; P04083; -. DR REPRODUCTION-2DPAGE; IPI00218918; -. DR REPRODUCTION-2DPAGE; P04083; -. DR CPTAC; CPTAC-1377; -. DR CPTAC; CPTAC-1378; -. DR CPTAC; CPTAC-1379; -. DR CPTAC; CPTAC-1380; -. DR CPTAC; CPTAC-311; -. DR CPTAC; CPTAC-312; -. DR CPTAC; CPTAC-5939; -. DR CPTAC; CPTAC-5940; -. DR CPTAC; CPTAC-696; -. DR CPTAC; CPTAC-697; -. DR EPD; P04083; -. DR jPOST; P04083; -. DR MassIVE; P04083; -. DR PaxDb; 9606-ENSP00000366109; -. DR PeptideAtlas; P04083; -. DR PRIDE; P04083; -. DR ProteomicsDB; 51649; -. DR ABCD; P04083; 2 sequenced antibodies. DR Antibodypedia; 2190; 1427 antibodies from 52 providers. DR CPTC; P04083; 5 antibodies. DR DNASU; 301; -. DR Ensembl; ENST00000257497.11; ENSP00000257497.6; ENSG00000135046.14. DR Ensembl; ENST00000376911.1; ENSP00000366109.1; ENSG00000135046.14. DR GeneID; 301; -. DR KEGG; hsa:301; -. DR MANE-Select; ENST00000257497.11; ENSP00000257497.6; NM_000700.3; NP_000691.1. DR AGR; HGNC:533; -. DR CTD; 301; -. DR DisGeNET; 301; -. DR GeneCards; ANXA1; -. DR HGNC; HGNC:533; ANXA1. DR HPA; ENSG00000135046; Tissue enhanced (esophagus). DR MIM; 151690; gene. DR neXtProt; NX_P04083; -. DR OpenTargets; ENSG00000135046; -. DR PharmGKB; PA24823; -. DR VEuPathDB; HostDB:ENSG00000135046; -. DR eggNOG; KOG0819; Eukaryota. DR GeneTree; ENSGT00940000155221; -. DR HOGENOM; CLU_025300_0_0_1; -. DR InParanoid; P04083; -. DR OMA; FMENQEQ; -. DR OrthoDB; 1500773at2759; -. DR PhylomeDB; P04083; -. DR TreeFam; TF105452; -. DR PathwayCommons; P04083; -. DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR Reactome; R-HSA-444473; Formyl peptide receptors bind formyl peptides and many other ligands. DR Reactome; R-HSA-445355; Smooth Muscle Contraction. DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling. DR SignaLink; P04083; -. DR SIGNOR; P04083; -. DR BioGRID-ORCS; 301; 13 hits in 1173 CRISPR screens. DR ChiTaRS; ANXA1; human. DR EvolutionaryTrace; P04083; -. DR GeneWiki; Annexin_A1; -. DR GenomeRNAi; 301; -. DR Pharos; P04083; Tbio. DR PRO; PR:P04083; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P04083; Protein. DR Bgee; ENSG00000135046; Expressed in oral cavity and 202 other cell types or tissues. DR ExpressionAtlas; P04083; baseline and differential. DR GO; GO:0005912; C:adherens junction; HDA:BHF-UCL. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0001533; C:cornified envelope; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB. DR GO; GO:0005768; C:endosome; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB. DR GO; GO:0031514; C:motile cilium; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl. DR GO; GO:0031982; C:vesicle; HDA:UniProtKB. DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; HDA:BHF-UCL. DR GO; GO:0005509; F:calcium ion binding; EXP:DisProt. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB. DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:GO_Central. DR GO; GO:0008289; F:lipid binding; EXP:DisProt. DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IDA:UniProtKB. DR GO; GO:0005543; F:phospholipid binding; TAS:ProtInc. DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc. DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0046632; P:alpha-beta T cell differentiation; ISS:BHF-UCL. DR GO; GO:0050482; P:arachidonic acid secretion; IBA:GO_Central. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central. DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:BHF-UCL. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IBA:GO_Central. DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:BHF-UCL. DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central. DR GO; GO:0031018; P:endocrine pancreas development; IBA:GO_Central. DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IDA:UniProtKB. DR GO; GO:0042063; P:gliogenesis; IBA:GO_Central. DR GO; GO:0071621; P:granulocyte chemotaxis; IDA:UniProtKB. DR GO; GO:0070365; P:hepatocyte differentiation; IBA:GO_Central. DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0030073; P:insulin secretion; IBA:GO_Central. DR GO; GO:0030216; P:keratinocyte differentiation; IDA:UniProtKB. DR GO; GO:0051179; P:localization; EXP:DisProt. DR GO; GO:0002548; P:monocyte chemotaxis; IDA:UniProtKB. DR GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; IBA:GO_Central. DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB. DR GO; GO:0045920; P:negative regulation of exocytosis; IMP:UniProtKB. DR GO; GO:0032717; P:negative regulation of interleukin-8 production; IMP:BHF-UCL. DR GO; GO:0045629; P:negative regulation of T-helper 2 cell differentiation; IDA:UniProtKB. DR GO; GO:0042119; P:neutrophil activation; IDA:UniProtKB. DR GO; GO:0097350; P:neutrophil clearance; IMP:BHF-UCL. DR GO; GO:0001780; P:neutrophil homeostasis; IMP:BHF-UCL. DR GO; GO:0018149; P:peptide cross-linking; IDA:UniProtKB. DR GO; GO:0006909; P:phagocytosis; ISS:UniProtKB. DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IDA:BHF-UCL. DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central. DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IDA:UniProtKB. DR GO; GO:0033031; P:positive regulation of neutrophil apoptotic process; IBA:GO_Central. DR GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IBA:GO_Central. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:UniProtKB. DR GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; IDA:UniProtKB. DR GO; GO:0031340; P:positive regulation of vesicle fusion; IDA:UniProtKB. DR GO; GO:0090303; P:positive regulation of wound healing; IDA:UniProtKB. DR GO; GO:0070459; P:prolactin secretion; IBA:GO_Central. DR GO; GO:0030850; P:prostate gland development; IBA:GO_Central. DR GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB. DR GO; GO:0046883; P:regulation of hormone secretion; IMP:UniProtKB. DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB. DR GO; GO:0032652; P:regulation of interleukin-1 production; ISS:UniProtKB. DR GO; GO:0002685; P:regulation of leukocyte migration; ISS: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; TAS:UniProtKB. DR DisProt; DP01951; -. DR Gene3D; 1.10.220.10; Annexin; 4. DR IDEAL; IID00137; -. 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 UCD-2DPAGE; P04083; -. DR Genevisible; P04083; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Adaptive immunity; Annexin; Calcium; KW Calcium/phospholipid-binding; Cell membrane; Cell projection; Cilium; KW Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; KW Endosome; Immunity; Inflammatory response; Innate immunity; KW Isopeptide bond; Membrane; Metal-binding; Nucleus; Pharmaceutical; KW Phospholipase A2 inhibitor; Phosphoprotein; Reference proteome; Repeat; KW Secreted; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:3303336" FT CHAIN 2..346 FT /note="Annexin A1" FT /id="PRO_0000067460" FT PEPTIDE 2..26 FT /note="Annexin Ac2-26" FT /evidence="ECO:0000269|PubMed:22879591" FT /id="PRO_0000454556" 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:0000269|PubMed:22879591" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:3303336" FT MOD_RES 5 FT /note="Phosphoserine; by TRPM7" FT /evidence="ECO:0000269|PubMed:15485879" FT MOD_RES 21 FT /note="Phosphotyrosine; by EGFR" FT /evidence="ECO:0000269|PubMed:2457390" FT MOD_RES 27 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000269|PubMed:2457390" FT MOD_RES 34 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 37 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 41 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 58 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P10107" FT MOD_RES 136 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 239 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 312 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" 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 CROSSLNK 214 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 214 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 257 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000250|UniProtKB:P10107" FT CROSSLNK 332 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0007744|PubMed:25114211" FT MUTAGEN 27 FT /note="S->A: Abolishes secretion and modulation of FT exocytosis." FT /evidence="ECO:0000269|PubMed:19625660" FT MUTAGEN 34 FT /note="S->A: No effect on secretion and modulation of FT exocytosis." FT /evidence="ECO:0000269|PubMed:19625660" FT MUTAGEN 45 FT /note="S->A: Abolishes secretion and nearly abolishes FT modulation of exocytosis." FT /evidence="ECO:0000269|PubMed:19625660" FT CONFLICT 118 FT /note="F -> L (in Ref. 4; BAG70088/BAG70215)" FT /evidence="ECO:0000305" FT HELIX 3..10 FT /evidence="ECO:0007829|PDB:1QLS" FT HELIX 16..18 FT /evidence="ECO:0007829|PDB:5VFW" FT HELIX 46..55 FT /evidence="ECO:0007829|PDB:1BO9" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:1BO9" FT HELIX 65..71 FT /evidence="ECO:0007829|PDB:1BO9" FT HELIX 77..87 FT /evidence="ECO:0007829|PDB:1BO9" FT HELIX 94..99 FT /evidence="ECO:0007829|PDB:1BO9" FT HELIX 106..109 FT /evidence="ECO:0007829|PDB:1BO9" FT HELIX 110..112 FT /evidence="ECO:0007829|PDB:1BO9" SQ SEQUENCE 346 AA; 38714 MW; 14B42E1FA4178EC0 CRC64; MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA LHKAIMVKGV DEATIIDILT KRNNAQRQQI KAAYLQETGK PLDETLKKAL TGHLEEVVLA LLKTPAQFDA DELRAAMKGL GTDEDTLIEI LASRTNKEIR DINRVYREEL KRDLAKDITS DTSGDFRNAL LSLAKGDRSE DFGVNEDLAD SDARALYEAG ERRKGTDVNV FNTILTTRSY PQLRRVFQKY TKYSKHDMNK VLDLELKGDI EKCLTAIVKC ATSKPAFFAE KLHQAMKGVG TRHKALIRIM VSRSEIDMND IKAFYQKMYG ISLCQAILDE TKGDYEKILV ALCGGN //