ANXA1_HUMAN
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 03-AUG-2022, entry version 260.
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="http://atlasgeneticsoncology.org/Genes/ANXA1ID653ch9q21.html";
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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; 191.
DR DIP; DIP-32875N; -.
DR IntAct; P04083; 116.
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; 1 site, 1 O-linked glycan (1 site).
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 UCD-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-696; -.
DR CPTAC; CPTAC-697; -.
DR EPD; P04083; -.
DR jPOST; P04083; -.
DR MassIVE; P04083; -.
DR PaxDb; P04083; -.
DR PeptideAtlas; P04083; -.
DR PRIDE; P04083; -.
DR ProteomicsDB; 51649; -.
DR ABCD; P04083; 2 sequenced antibodies.
DR Antibodypedia; 2190; 1227 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 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; AKADRCE; -.
DR OrthoDB; 856254at2759; -.
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; 11 hits in 1088 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 200 other tissues.
DR ExpressionAtlas; P04083; baseline and differential.
DR Genevisible; P04083; HS.
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:0031313; C:extrinsic component of endosome membrane; ISS:UniProtKB.
DR GO; GO:0031232; C:extrinsic component of external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; 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; ISS:UniProtKB.
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: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:0031532; P:actin cytoskeleton reorganization; 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: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:1900138; P:negative regulation of phospholipase A2 activity; IBA:GO_Central.
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; -; 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: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 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
