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Annexin A1 (Annexin I) (Annexin-1) (Calpactin II) (Calpactin-2) (Chromobindin-9) (Lipocortin I) (Phospholipase A2 inhibitory protein) (p35)

 ANXA1_HUMAN             Reviewed;         346 AA.
P04083;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 223.
RecName: Full=Annexin A1;
AltName: Full=Annexin I;
AltName: Full=Annexin-1;
AltName: Full=Calpactin II;
AltName: Full=Calpactin-2;
AltName: Full=Chromobindin-9;
AltName: Full=Lipocortin I {ECO:0000303|PubMed:1832554};
AltName: Full=Phospholipase A2 inhibitory protein;
AltName: Full=p35;
Name=ANXA1; Synonyms=ANX1, LPC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=2936963; DOI=10.1038/320077a0;
Wallner B.P., Mattaliano R.J., Hession C., Cate R.L., Tizard R.,
Sinclair L.K., Foeller C., Chow E.P., Browning J.L.,
Ramachandran K.L., Pepinsky R.B.;
"Cloning and expression of human lipocortin, a phospholipase A2
inhibitor with potential anti-inflammatory activity.";
Nature 320:77-81(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1832554; DOI=10.1021/bi00101a015;
Kovacic R.T., Tizard R., Cate R.L., Frey A.Z., Wallner B.P.;
"Correlation of gene and protein structure of rat and human lipocortin
I.";
Biochemistry 30:9015-9021(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=8425544; DOI=10.1111/j.1432-1033.1993.tb19904.x;
Arcone R., Arpaia G., Ruoppolo M., Malorni A., Pucci P., Marino G.,
Ialenti A., di Rosa M., Ciliberto G.;
"Structural characterization of a biologically active human lipocortin
1 expressed in Escherichia coli.";
Eur. J. Biochem. 211:347-355(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION AT TYR-21 BY EGFR AND
SER-27 BY PKC.
PubMed=2457390; DOI=10.1021/bi00410a024;
Varticovski L., Chahwala S.B., Whitman M., Cantley L., Schindler D.,
Chow E.P., Sinclair L.K., Pepinsky R.B.;
"Location of sites in human lipocortin I that are phosphorylated by
protein tyrosine kinases and protein kinases A and C.";
Biochemistry 27:3682-3690(1988).
[6]
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=3303336; DOI=10.1126/science.3303336;
Biemann K., Scoble H.A.;
"Characterization by tandem mass spectrometry of structural
modifications in proteins.";
Science 237:992-998(1987).
[7]
FUNCTION, DIMERIZATION, SUBUNIT, TISSUE SPECIFICITY, PARTIAL PROTEIN
SEQUENCE, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=2532504; DOI=10.1042/bj2630097;
Pepinsky R.B., Sinclair L.K., Chow E.P., O'Brine-Greco B.;
"A dimeric form of lipocortin-1 in human placenta.";
Biochem. J. 263:97-103(1989).
[8]
INTERACTION WITH S100A11, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8557678; DOI=10.1074/jbc.271.2.719;
Mailliard W.S., Haigler H.T., Schlaepfer D.D.;
"Calcium-dependent binding of S100C to the N-terminal domain of
annexin I.";
J. Biol. Chem. 271:719-725(1996).
[9]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10772777; DOI=10.1006/cbir.1999.0468;
Perretti M., Christian H., Wheller S.K., Aiello I., Mugridge K.G.,
Morris J.F., Flower R.J., Goulding N.J.;
"Annexin I is stored within gelatinase granules of human neutrophil
and mobilized on the cell surface upon adhesion but not
phagocytosis.";
Cell Biol. Int. 24:163-174(2000).
[10]
PHOSPHORYLATION AT SER-5 BY TRPM7.
PubMed=15485879; DOI=10.1074/jbc.C400441200;
Dorovkov M.V., Ryazanov A.G.;
"Phosphorylation of annexin I by TRPM7 channel-kinase.";
J. Biol. Chem. 279:50643-50646(2004).
[11]
FUNCTION, AND DOMAIN.
PubMed=15187149; DOI=10.4049/jimmunol.172.12.7669;
Ernst S., Lange C., Wilbers A., Goebeler V., Gerke V., Rescher U.;
"An annexin 1 N-terminal peptide activates leukocytes by triggering
different members of the formyl peptide receptor family.";
J. Immunol. 172:7669-7676(2004).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17008549; DOI=10.1182/blood-2006-05-022798;
D'Acquisto F., Merghani A., Lecona E., Rosignoli G., Raza K.,
Buckley C.D., Flower R.J., Perretti M.;
"Annexin-1 modulates T-cell activation and differentiation.";
Blood 109:1095-1102(2007).
[13]
REVIEW.
PubMed=18641677; DOI=10.1038/bjp.2008.252;
D'Acquisto F., Perretti M., Flower R.J.;
"Annexin-A1: a pivotal regulator of the innate and adaptive immune
systems.";
Br. J. Pharmacol. 155:152-169(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-27; SER-34 AND
SER-45.
PubMed=19625660; DOI=10.1096/fj.09-131391;
McArthur S., Yazid S., Christian H., Sirha R., Flower R.,
Buckingham J., Solito E.;
"Annexin A1 regulates hormone exocytosis through a mechanism involving
actin reorganization.";
FASEB J. 23:4000-4010(2009).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239 AND LYS-312, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-37; THR-41 AND
THR-136, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-214 AND LYS-332, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-214, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[23]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
PubMed=25664854; DOI=10.1172/JCI76693;
Leoni G., Neumann P.A., Kamaly N., Quiros M., Nishio H., Jones H.R.,
Sumagin R., Hilgarth R.S., Alam A., Fredman G., Argyris I.,
Rijcken E., Kusters D., Reutelingsperger C., Perretti M., Parkos C.A.,
Farokhzad O.C., Neish A.S., Nusrat A.;
"Annexin A1-containing extracellular vesicles and polymeric
nanoparticles promote epithelial wound repair.";
J. Clin. Invest. 125:1215-1227(2015).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-214, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[25]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS,
AND CALCIUM-BINDING.
PubMed=8453382; DOI=10.1002/pro.5560020317;
Weng X., Luecke H., Song I.S., Kang D.S., Kim S.-H., Huber R.;
"Crystal structure of human annexin I at 2.5-A resolution.";
Protein Sci. 2:448-458(1993).
[26]
STRUCTURE BY NMR OF 41-113.
PubMed=9915835; DOI=10.1074/jbc.274.5.2971;
Gao J., Li Y., Yan H.;
"NMR solution structure of domain 1 of human annexin I shows an
autonomous folding unit.";
J. Biol. Chem. 274:2971-2977(1999).
[27]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-12 IN COMPLEX WITH
S100A11, AND INTERACTION WITH S100A11.
PubMed=10673436; DOI=10.1016/S0969-2126(00)00093-9;
Rety S., Osterloh D., Arie J.-P., Tabaries S., Seeman J.,
Russo-Marie F., Gerke V., Lewit-Bentley A.;
"Structural basis of the Ca(2+)-dependent association between S100C
(S100A11) and its target, the N-terminal part of annexin I.";
Structure 8:175-184(2000).
-!- FUNCTION: Plays important roles in the innate immune response as
effector of glucocorticoid-mediated responses and regulator of the
inflammatory process. Has anti-inflammatory activity
(PubMed:8425544). Plays a role in glucocorticoid-mediated down-
regulation of the early phase of the inflammatory response (By
similarity). Promotes resolution of inflammation and wound healing
(PubMed:25664854). Functions at least in part by activating the
formyl peptide receptors and downstream signaling cascades
(PubMed:15187149, PubMed:25664854). Promotes chemotaxis of
granulocytes and monocytes via activation of the formyl peptide
receptors (PubMed:15187149). Contributes to the adaptive immune
response by enhancing signaling cascades that are triggered by T-
cell activation, regulates differentiation and proliferation of
activated T-cells (PubMed:17008549). Promotes the differentiation
of T-cells into Th1 cells and negatively regulates differentiation
into Th2 cells (PubMed:17008549). Has no effect on unstimulated T
cells (PubMed:17008549). Promotes rearrangement of the actin
cytoskeleton, cell polarization and cell migration
(PubMed:15187149). Negatively regulates hormone exocytosis via
activation of the formyl peptide receptors and reorganization of
the actin cytoskeleton (PubMed:19625660). Has high affinity for
Ca(2+) and can bind up to eight Ca(2+) ions (By similarity).
Displays Ca(2+)-dependent binding to phospholipid membranes
(PubMed:2532504, PubMed:8557678). Plays a role in the formation of
phagocytic cups and phagosomes. Plays a role in phagocytosis by
mediating the Ca(2+)-dependent interaction between phagosomes and
the actin cytoskeleton (By similarity).
{ECO:0000250|UniProtKB:P10107, ECO:0000250|UniProtKB:P19619,
ECO:0000269|PubMed:15187149, ECO:0000269|PubMed:17008549,
ECO:0000269|PubMed:19625660, ECO:0000269|PubMed:2532504,
ECO:0000269|PubMed:25664854, ECO:0000269|PubMed:2936963,
ECO:0000269|PubMed:8425544, ECO:0000269|PubMed:8557678}.
-!- SUBUNIT: Homodimer; non-covalently linked (By similarity).
Homodimer; linked by transglutamylation (PubMed:2532504).
Homodimers linked by transglutamylation are observed in placenta,
but not in other tissues (PubMed:2532504). Interacts with S100A11
(PubMed:8557678, PubMed:10673436). Heterotetramer, formed by two
molecules each of S100A11 and ANXA1 (PubMed:10673436). Interacts
with DYSF (By similarity). Interacts with EGFR (By similarity).
{ECO:0000250|UniProtKB:P10107, ECO:0000250|UniProtKB:P19619,
ECO:0000269|PubMed:10673436, ECO:0000269|PubMed:2532504,
ECO:0000269|PubMed:8557678}.
-!- INTERACTION:
Q9Y6K9:IKBKG; NbExp=6; IntAct=EBI-354007, EBI-81279;
Q13546:RIPK1; NbExp=5; IntAct=EBI-354007, EBI-358507;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10772777,
ECO:0000269|PubMed:19625660}. Cytoplasm
{ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:17008549,
ECO:0000269|PubMed:19625660}. Cell projection, cilium
{ECO:0000250|UniProtKB:P46193}. Cell membrane
{ECO:0000269|PubMed:10772777}. Membrane
{ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:2532504,
ECO:0000269|PubMed:8557678}; Peripheral membrane protein
{ECO:0000269|PubMed:2532504, ECO:0000269|PubMed:8557678}. Endosome
membrane {ECO:0000250|UniProtKB:P07150}; Peripheral membrane
protein {ECO:0000250|UniProtKB:P07150}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P51662}. Apical cell membrane
{ECO:0000250|UniProtKB:P10107}. Lateral cell membrane
{ECO:0000250|UniProtKB:P10107}. Secreted
{ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:19625660,
ECO:0000269|PubMed:25664854}. Secreted, extracellular space
{ECO:0000269|PubMed:25664854}. Cell membrane
{ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:19625660,
ECO:0000269|PubMed:25664854}; Peripheral membrane protein
{ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:19625660,
ECO:0000269|PubMed:25664854}; Extracellular side
{ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:19625660,
ECO:0000269|PubMed:25664854}. Secreted, exosome
{ECO:0000269|PubMed:25664854}. Cytoplasmic vesicle, secretory
vesicle lumen {ECO:0000269|PubMed:10772777}. Cell projection,
phagocytic cup {ECO:0000250|UniProtKB:P10107}. Early endosome
{ECO:0000250|UniProtKB:P19619}. Cytoplasmic vesicle membrane
{ECO:0000250|UniProtKB:P19619}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P19619}. Note=Secreted, at least in part
via exosomes and other secretory vesicles. Detected in exosomes
and other extracellular vesicles (PubMed:25664854). Detected in
gelatinase granules in resting neutrophils (PubMed:10772777).
Secretion is increased in response to wounding and inflammation
(PubMed:25664854). Secretion is increased upon T-cell activation
(PubMed:17008549). Neutrophil adhesion to endothelial cells
stimulates secretion via gelatinase granules, but foreign particle
phagocytosis has no effect (PubMed:10772777). Colocalizes with
actin fibers at phagocytic cups (By similarity). Displays calcium-
dependent binding to phospholipid membranes (PubMed:2532504,
PubMed:8557678). {ECO:0000250|UniProtKB:P10107,
ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:17008549,
ECO:0000269|PubMed:2532504, ECO:0000269|PubMed:25664854,
ECO:0000269|PubMed:8557678}.
-!- TISSUE SPECIFICITY: Detected in resting neutrophils
(PubMed:10772777). Detected in peripheral blood T-cells
(PubMed:17008549). Detected in extracellular vesicles in blood
serum from patients with inflammatory bowel disease, but not in
serum from healthy donors (PubMed:25664854). Detected in placenta
(at protein level) (PubMed:2532504). Detected in liver.
{ECO:0000269|PubMed:2532504, ECO:0000269|PubMed:2936963}.
-!- DOMAIN: The full-length protein can bind eight Ca(2+) ions via the
annexin repeats. Calcium binding causes a major conformation
change that modifies dimer contacts and leads to surface exposure
of the N-terminal phosphorylation sites; in the absence of Ca(2+),
these sites are buried in the interior of the protein core. The N-
terminal region becomes disordered in response to calcium-binding.
{ECO:0000250|UniProtKB:P19619}.
-!- DOMAIN: The N-terminal 26 amino acids are sufficient for its
extracellular functions in the regulation of inflammation and
wound healing (PubMed:25664854). Acylated peptides that contain
the first 26 amino acids of the mature protein can activate
signaling via the formyl peptide receptors (PubMed:15187149,
PubMed:25664854). {ECO:0000269|PubMed:15187149,
ECO:0000269|PubMed:25664854}.
-!- PTM: Phosphorylated by protein kinase C, EGFR and TRPM7
(PubMed:2457390, PubMed:15485879). Phosphorylated in response to
EGF treatment (PubMed:2532504). {ECO:0000269|PubMed:15485879,
ECO:0000269|PubMed:2457390, ECO:0000269|PubMed:2532504}.
-!- PTM: Sumoylated. {ECO:0000250|UniProtKB:P10107}.
-!- PHARMACEUTICAL: Peptides based on the N-terminal sequence might be
used for the treatment of inflammation, e.g. in chronic bowel
diseases and in rheumatoid arthritis. {ECO:0000305}.
-!- MISCELLANEOUS: Was originally identified as calcium and
phospholipid binding protein that displays Ca(2+)-dependent
binding to phospholipid membranes and can promote membrane
aggregation in vitro. Was initially identified as inhibitor of
phospholipase A2 activity (in vitro) (PubMed:2936963,
PubMed:8425544). Inhibition of phospholipase activity is mediated
via its phospholipid binding activity that limits the access of
phospholipase to its substrates. {ECO:0000269|PubMed:2936963,
ECO:0000269|PubMed:8425544, ECO:0000305}.
-!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ANXA1ID653ch9q21.html";
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EMBL; X05908; CAA29338.1; -; mRNA.
EMBL; BC001275; AAH01275.1; -; mRNA.
EMBL; BC035993; AAH35993.1; -; mRNA.
CCDS; CCDS6645.1; -.
PIR; A03080; LUHU.
RefSeq; NP_000691.1; NM_000700.2.
RefSeq; XP_011516911.1; XM_011518609.1.
UniGene; Hs.494173; -.
PDB; 1AIN; X-ray; 2.50 A; A=33-346.
PDB; 1BO9; NMR; -; A=41-113.
PDB; 1QLS; X-ray; 2.30 A; D=2-12.
PDB; 5VFW; NMR; -; A=2-26.
PDBsum; 1AIN; -.
PDBsum; 1BO9; -.
PDBsum; 1QLS; -.
PDBsum; 5VFW; -.
ProteinModelPortal; P04083; -.
SMR; P04083; -.
BioGrid; 106798; 96.
DIP; DIP-32875N; -.
IntAct; P04083; 75.
MINT; MINT-1212274; -.
STRING; 9606.ENSP00000257497; -.
DrugBank; DB00288; Amcinonide.
DrugBank; DB01234; Dexamethasone.
DrugBank; DB00741; Hydrocortisone.
TCDB; 1.A.31.1.3; the annexin (annexin) family.
iPTMnet; P04083; -.
PhosphoSitePlus; P04083; -.
SwissPalm; P04083; -.
BioMuta; ANXA1; -.
DMDM; 113944; -.
DOSAC-COBS-2DPAGE; P04083; -.
REPRODUCTION-2DPAGE; IPI00218918; -.
REPRODUCTION-2DPAGE; P04083; -.
UCD-2DPAGE; P04083; -.
EPD; P04083; -.
PaxDb; P04083; -.
PeptideAtlas; P04083; -.
PRIDE; P04083; -.
DNASU; 301; -.
Ensembl; ENST00000257497; ENSP00000257497; ENSG00000135046.
Ensembl; ENST00000376911; ENSP00000366109; ENSG00000135046.
GeneID; 301; -.
KEGG; hsa:301; -.
CTD; 301; -.
DisGeNET; 301; -.
EuPathDB; HostDB:ENSG00000135046.13; -.
GeneCards; ANXA1; -.
HGNC; HGNC:533; ANXA1.
HPA; CAB013023; -.
HPA; CAB035987; -.
HPA; CAB058693; -.
HPA; HPA011271; -.
HPA; HPA011272; -.
MIM; 151690; gene.
neXtProt; NX_P04083; -.
OpenTargets; ENSG00000135046; -.
PharmGKB; PA24823; -.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
GeneTree; ENSGT00760000118972; -.
HOGENOM; HOG000158803; -.
HOVERGEN; HBG061815; -.
InParanoid; P04083; -.
KO; K17091; -.
OMA; GTRHKTL; -.
OrthoDB; EOG091G0H6H; -.
PhylomeDB; P04083; -.
TreeFam; TF105452; -.
Reactome; R-HSA-416476; G alpha (q) signalling events.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-444473; Formyl peptide receptors bind formyl peptides and many other ligands.
Reactome; R-HSA-445355; Smooth Muscle Contraction.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SignaLink; P04083; -.
SIGNOR; P04083; -.
ChiTaRS; ANXA1; human.
EvolutionaryTrace; P04083; -.
GeneWiki; Annexin_A1; -.
GenomeRNAi; 301; -.
PRO; PR:P04083; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000135046; -.
CleanEx; HS_ANXA1; -.
ExpressionAtlas; P04083; baseline and differential.
Genevisible; P04083; HS.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005913; C:cell-cell adherens junction; IDA:BHF-UCL.
GO; GO:0001533; C:cornified envelope; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0031313; C:extrinsic component of endosome membrane; ISS:UniProtKB.
GO; GO:0031232; C:extrinsic component of external side of plasma membrane; IDA:UniProtKB.
GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
GO; GO:0042629; C:mast cell granule; IEA:Ensembl.
GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl.
GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0036310; F:annealing helicase activity; IEA:Ensembl.
GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:AgBase.
GO; GO:0033676; F:double-stranded DNA-dependent ATPase activity; IEA:Ensembl.
GO; GO:0004386; F:helicase activity; IEA:Ensembl.
GO; GO:0019834; F:phospholipase A2 inhibitor activity; IDA:UniProtKB.
GO; GO:0005543; F:phospholipid binding; TAS:ProtInc.
GO; GO:0030674; F:protein binding, bridging; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0005102; F:receptor binding; TAS:ProtInc.
GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
GO; GO:0003727; F:single-stranded RNA binding; IEA:Ensembl.
GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0046632; P:alpha-beta T cell differentiation; ISS:BHF-UCL.
GO; GO:0050482; P:arachidonic acid secretion; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:BHF-UCL.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0032508; P:DNA duplex unwinding; IEA:Ensembl.
GO; GO:0036292; P:DNA rewinding; IEA:Ensembl.
GO; GO:0031018; P:endocrine pancreas development; IEA:Ensembl.
GO; GO:0044849; P:estrous cycle; IEA:Ensembl.
GO; GO:0007187; P:G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IDA:UniProtKB.
GO; GO:0042063; P:gliogenesis; IEA:Ensembl.
GO; GO:0071621; P:granulocyte chemotaxis; IDA:UniProtKB.
GO; GO:0070365; P:hepatocyte differentiation; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
GO; GO:0030216; P:keratinocyte differentiation; IDA:UniProtKB.
GO; GO:0002548; P:monocyte chemotaxis; IDA:UniProtKB.
GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0045920; P:negative regulation of exocytosis; IMP:UniProtKB.
GO; GO:2000483; P:negative regulation of interleukin-8 secretion; IMP:BHF-UCL.
GO; GO:1900138; P:negative regulation of phospholipase A2 activity; IEA:Ensembl.
GO; GO:0045629; P:negative regulation of T-helper 2 cell differentiation; IDA:UniProtKB.
GO; GO:0097350; P:neutrophil clearance; IMP:BHF-UCL.
GO; GO:0001780; P:neutrophil homeostasis; IMP:BHF-UCL.
GO; GO:0018149; P:peptide cross-linking; IDA:UniProtKB.
GO; GO:0006909; P:phagocytosis; ISS:UniProtKB.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0032743; P:positive regulation of interleukin-2 production; IDA:UniProtKB.
GO; GO:0033031; P:positive regulation of neutrophil apoptotic process; IEA:Ensembl.
GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IEA:Ensembl.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:UniProtKB.
GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; IDA:UniProtKB.
GO; GO:0031340; P:positive regulation of vesicle fusion; IDA:UniProtKB.
GO; GO:0090303; P:positive regulation of wound healing; IDA:UniProtKB.
GO; GO:0070459; P:prolactin secretion; IEA:Ensembl.
GO; GO:0030850; P:prostate gland development; IEA:Ensembl.
GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB.
GO; GO:0046883; P:regulation of hormone secretion; IMP:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0032652; P:regulation of interleukin-1 production; ISS:UniProtKB.
GO; GO:0002685; P:regulation of leukocyte migration; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
Gene3D; 1.10.220.10; -; 4.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR037104; Annexin_sf.
InterPro; IPR002388; ANX1.
PANTHER; PTHR10502:SF17; PTHR10502:SF17; 1.
Pfam; PF00191; Annexin; 4.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR00197; ANNEXINI.
SMART; SM00335; ANX; 4.
PROSITE; PS00223; ANNEXIN; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Adaptive immunity; Annexin; Calcium;
Calcium/phospholipid-binding; Cell membrane; Cell projection; Cilium;
Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Direct protein sequencing; Disulfide bond; Endosome; Immunity;
Inflammatory response; Innate immunity; Isopeptide bond; Membrane;
Metal-binding; Nucleus; Pharmaceutical; Phospholipase A2 inhibitor;
Phosphoprotein; Reference proteome; Repeat; Secreted; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3303336}.
CHAIN 2 346 Annexin A1.
/FTId=PRO_0000067460.
REPEAT 51 111 Annexin 1.
REPEAT 123 183 Annexin 2.
REPEAT 207 267 Annexin 3.
REPEAT 282 342 Annexin 4.
METAL 59 59 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 60 60 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 62 62 Calcium 1.
{ECO:0000250|UniProtKB:P19619}.
METAL 97 97 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 100 100 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 105 105 Calcium 2.
{ECO:0000250|UniProtKB:P19619}.
METAL 127 127 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 129 129 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 131 131 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 132 132 Calcium 4; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 134 134 Calcium 4.
{ECO:0000250|UniProtKB:P19619}.
METAL 171 171 Calcium 3.
{ECO:0000250|UniProtKB:P19619}.
METAL 210 210 Calcium 5; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 213 213 Calcium 5; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 215 215 Calcium 5; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 253 253 Calcium 6.
{ECO:0000250|UniProtKB:P19619}.
METAL 255 255 Calcium 5.
{ECO:0000250|UniProtKB:P19619}.
METAL 256 256 Calcium 6; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 261 261 Calcium 6.
{ECO:0000250|UniProtKB:P19619}.
METAL 286 286 Calcium 7; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 288 288 Calcium 7; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 290 290 Calcium 7; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 328 328 Calcium 8; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 330 330 Calcium 7.
{ECO:0000250|UniProtKB:P19619}.
METAL 331 331 Calcium 8; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19619}.
METAL 336 336 Calcium 8.
{ECO:0000250|UniProtKB:P19619}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:3303336}.
MOD_RES 5 5 Phosphoserine; by TRPM7.
{ECO:0000269|PubMed:15485879}.
MOD_RES 21 21 Phosphotyrosine; by EGFR.
{ECO:0000269|PubMed:2457390}.
MOD_RES 27 27 Phosphoserine; by PKC.
{ECO:0000269|PubMed:2457390}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 41 41 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 58 58 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10107}.
MOD_RES 136 136 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 239 239 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 312 312 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
DISULFID 324 343 {ECO:0000250|UniProtKB:P19619}.
CROSSLNK 19 19 Isoglutamyl lysine isopeptide (Gln-Lys)
(interchain with K-?).
CROSSLNK 214 214 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 214 214 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 332 332 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
MUTAGEN 27 27 S->A: Abolishes secretion and modulation
of exocytosis.
{ECO:0000269|PubMed:19625660}.
MUTAGEN 34 34 S->A: No effect on secretion and
modulation of exocytosis.
{ECO:0000269|PubMed:19625660}.
MUTAGEN 45 45 S->A: Abolishes secretion and nearly
abolishes modulation of exocytosis.
{ECO:0000269|PubMed:19625660}.
HELIX 3 10 {ECO:0000244|PDB:1QLS}.
HELIX 46 55 {ECO:0000244|PDB:1BO9}.
STRAND 62 64 {ECO:0000244|PDB:1BO9}.
HELIX 65 71 {ECO:0000244|PDB:1BO9}.
HELIX 77 87 {ECO:0000244|PDB:1BO9}.
HELIX 94 99 {ECO:0000244|PDB:1BO9}.
HELIX 106 109 {ECO:0000244|PDB:1BO9}.
HELIX 110 112 {ECO:0000244|PDB:1BO9}.
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


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