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Annexin A1 (Annexin I) (Annexin-1) (Calpactin II) (Calpactin-2) (Chromobindin-9) (Lipocortin I) (Lipocortin-like 33 kDa protein) (Phospholipase A2 inhibitory protein) (p35)

 ANXA1_CAVCU             Reviewed;         346 AA.
P14087;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
30-AUG-2017, entry version 115.
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;
AltName: Full=Lipocortin-like 33 kDa protein;
AltName: Full=Phospholipase A2 inhibitory protein;
AltName: Full=p35;
Name=ANXA1; Synonyms=ANX1;
Cavia cutleri (Guinea pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
Hystricomorpha; Caviidae; Cavia.
NCBI_TaxID=10144;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Neutrophil;
PubMed=2522394; DOI=10.1016/0014-5793(89)81173-1;
Sato E.F., Tanaka Y., Utsumi K.;
"cDNA cloning and nucleotide sequence of lipocortin-like 33 kDa
protein in guinea pig neutrophils.";
FEBS Lett. 244:108-112(1989).
[2]
PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
TISSUE=Neutrophil;
PubMed=2962884; DOI=10.1016/0014-5793(88)80883-4;
Sato E.F., Miyahara M., Utsumi K.;
"Purification and characterization of a lipocortin-like 33 kDa protein
from guinea pig neutrophils.";
FEBS Lett. 227:131-135(1988).
-!- 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. Plays a role
in glucocorticoid-mediated down-regulation of the early phase of
the inflammatory response. Promotes resolution of inflammation and
wound healing (By similarity). Functions at least in part by
activating the formyl peptide receptors and downstream signaling
cascades. Promotes chemotaxis of granulocytes and monocytes via
activation of the formyl peptide receptors (By similarity).
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. Promotes
the differentiation of T-cells into Th1 cells and negatively
regulates differentiation into Th2 cells (By similarity). Has no
effect on unstimulated T-cells. Promotes rearrangement of the
actin cytoskeleton, cell polarization and cell migration.
Negatively regulates hormone exocytosis via activation of the
formyl peptide receptors and reorganization of the actin
cytoskeleton (By similarity). 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:2962884).
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:P04083,
ECO:0000250|UniProtKB:P10107, ECO:0000250|UniProtKB:P19619,
ECO:0000269|PubMed:2962884}.
-!- SUBUNIT: Homodimer; non-covalently linked (By similarity).
Homodimer; linked by transglutamylation. Homodimers linked by
transglutamylation are observed in placenta, but not in other
tissues. Interacts with S100A11. Heterotetramer, formed by two
molecules each of S100A11 and ANXA1 (By similarity). Interacts
with DYSF (By similarity). Interacts with EGFR (By similarity).
{ECO:0000250|UniProtKB:P04083, ECO:0000250|UniProtKB:P10107,
ECO:0000250|UniProtKB:P19619}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07150}.
Cytoplasm {ECO:0000250|UniProtKB:P10107}. Cell projection, cilium
{ECO:0000250|UniProtKB:P10107}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P51662}. Lateral cell membrane
{ECO:0000250|UniProtKB:P10107}. Cell membrane
{ECO:0000250|UniProtKB:P10107}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P10107}. Apical cell membrane
{ECO:0000250|UniProtKB:P10107}. Membrane
{ECO:0000269|PubMed:2962884}; Peripheral membrane protein
{ECO:0000269|PubMed:2962884}. Endosome membrane
{ECO:0000250|UniProtKB:P07150}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P07150}. Secreted
{ECO:0000250|UniProtKB:P10107}. Secreted, extracellular space
{ECO:0000250|UniProtKB:P04083}. Cell membrane
{ECO:0000250|UniProtKB:P04083}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P04083}; Extracellular side
{ECO:0000250|UniProtKB:P04083}. Early endosome
{ECO:0000250|UniProtKB:P19619}. Cytoplasmic vesicle membrane
{ECO:0000250|UniProtKB:P19619}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P19619}. Secreted, exosome
{ECO:0000250|UniProtKB:P10107}. Cytoplasmic vesicle, secretory
vesicle lumen {ECO:0000250|UniProtKB:P10107}. Cell projection,
phagocytic cup {ECO:0000250|UniProtKB:P10107}. Note=Colocalizes
with actin fibers at phagocytic cups. Secreted, at least in part
via exosomes and other secretory vesicles. Detected in exosomes
and other extracellular vesicles. Secretion is increased in
response to wounding and inflammation (By similarity). Detected in
gelatinase granules in resting neutrophils. Neutrophil adhesion to
endothelial cells stimulates secretion via gelatinase granules,
but foreign particle phagocytosis has no effect. Displays calcium-
dependent binding to phospholipid membranes (PubMed:2962884).
{ECO:0000250|UniProtKB:P04083, ECO:0000250|UniProtKB:P10107,
ECO:0000269|PubMed:2962884}.
-!- 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. Acylated peptides that contain the first 26 amino
acids of the mature protein can activate signaling via the formyl
peptide receptors. {ECO:0000250|UniProtKB:P04083}.
-!- PTM: Phosphorylated by protein kinase C, EGFR and TRPM7.
Phosphorylated in response to EGF treatment.
{ECO:0000250|UniProtKB:P04083}.
-!- PTM: Sumoylated. {ECO:0000250|UniProtKB:P10107}.
-!- 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:2962884). Inhibition
of phospholipase activity is mediated via its phospholipid binding
activity that limits the access of phospholipase to its
substrates. {ECO:0000250|UniProtKB:P10107,
ECO:0000269|PubMed:2962884}.
-!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X14635; CAA32783.1; -; mRNA.
ProteinModelPortal; P14087; -.
SMR; P14087; -.
MINT; MINT-4996460; -.
PRIDE; P14087; -.
HOVERGEN; HBG061815; -.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0031313; C:extrinsic component of endosome membrane; ISS:UniProtKB.
GO; GO:0031232; C:extrinsic component of external side of plasma membrane; ISS:UniProtKB.
GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
GO; GO:0007187; P:G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; ISS:UniProtKB.
GO; GO:0071621; P:granulocyte chemotaxis; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0002548; P:monocyte chemotaxis; ISS:UniProtKB.
GO; GO:0045920; P:negative regulation of exocytosis; ISS:UniProtKB.
GO; GO:0045629; P:negative regulation of T-helper 2 cell differentiation; ISS:UniProtKB.
GO; GO:0006909; P:phagocytosis; ISS:UniProtKB.
GO; GO:0032743; P:positive regulation of interleukin-2 production; ISS:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; ISS:UniProtKB.
GO; GO:0090303; P:positive regulation of wound healing; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
GO; GO:0046883; P:regulation of hormone secretion; ISS: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.
Gene3D; 1.10.220.10; -; 4.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR002388; ANX1.
PANTHER; PTHR10502:SF141; PTHR10502:SF141; 1.
Pfam; PF00191; Annexin; 4.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR00197; ANNEXINI.
SMART; SM00335; ANX; 4.
PROSITE; PS00223; ANNEXIN; 4.
1: Evidence at protein level;
Acetylation; Adaptive immunity; Annexin; Calcium;
Calcium/phospholipid-binding; Cell membrane; Cell projection; Cilium;
Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
Disulfide bond; Endosome; Immunity; Inflammatory response;
Innate immunity; Isopeptide bond; Membrane; Metal-binding; Nucleus;
Phospholipase A2 inhibitor; Phosphoprotein; Repeat; Secreted;
Ubl conjugation.
CHAIN 1 346 Annexin A1.
/FTId=PRO_0000067458.
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 5 5 Phosphoserine; by TRPM7.
{ECO:0000250|UniProtKB:P04083}.
MOD_RES 21 21 Phosphotyrosine; by EGFR.
{ECO:0000250|UniProtKB:P04083}.
MOD_RES 27 27 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P04083}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000250|UniProtKB:P04083}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000250|UniProtKB:P04083}.
MOD_RES 58 58 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10107}.
MOD_RES 136 136 Phosphothreonine.
{ECO:0000250|UniProtKB:P04083}.
MOD_RES 239 239 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04083}.
MOD_RES 312 312 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04083}.
DISULFID 324 343 {ECO:0000250|UniProtKB:P19619}.
CROSSLNK 19 19 Isoglutamyl lysine isopeptide (Gln-Lys)
(interchain with K-?). {ECO:0000250}.
CROSSLNK 214 214 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P04083}.
CROSSLNK 214 214 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P04083}.
CROSSLNK 332 332 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P04083}.
SEQUENCE 346 AA; 38555 MW; 63A638C2A95CE954 CRC64;
MSMVSEFLKQ AYFIDNQEQD YVKTVKSSKG GPGSAVSPYP SFDASSDVAA LHKAITVKGV
DEATIIDILT KRNNAQRQQI KAAYLQEKGK PLDEALKKAL TGHLEEVVLA LLKTPAQLDA
DELRAAMKGL GTDEDTLIEI LVSRKNREIK EINRVYRDEL KRDLAKDITS DTSGDFQKAL
LSLAKGDRCE DLSVNDDLAD SDARALYEAG ERRKGTDVNV FITILTTRSY SHLRRVFQKY
TKYSQHDMNK ALDLELKGDI ENCLTAIVKC ATSTPAFFAE KLHLAMKGAG TRHKALIRIM
VSRSEIDMND IKVYYQKMYG ISLCQAILDE TKGDYEKILV ALCGGQ


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