ANXA1_CHICK
ID ANXA1_CHICK Reviewed; 130 AA.
AC Q92108;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 133.
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;
DE AltName: Full=Phospholipase A2 inhibitory protein;
DE AltName: Full=p35;
DE Flags: Fragment;
GN Name=ANXA1; Synonyms=ANX1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8365470; DOI=10.1016/0014-5793(93)80241-l;
RA Sidis Y., Horseman N.D.;
RT "The hinge region of chicken annexin I contains no site for tyrosine
RT phosphorylation.";
RL FEBS Lett. 329:296-300(1993).
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. Plays a role in
CC glucocorticoid-mediated down-regulation of the early phase of the
CC inflammatory response. Promotes resolution of inflammation and wound
CC healing (By similarity). Functions at least in part by activating the
CC formyl peptide receptors and downstream signaling cascades. Promotes
CC chemotaxis of granulocytes and monocytes via activation of the formyl
CC peptide receptors (By similarity). Contributes to the adaptive immune
CC response by enhancing signaling cascades that are triggered by T-cell
CC activation, regulates differentiation and proliferation of activated T-
CC cells. Promotes the differentiation of T-cells into Th1 cells and
CC negatively regulates differentiation into Th2 cells (By similarity).
CC Has no effect on unstimulated T-cells. Promotes rearrangement of the
CC actin cytoskeleton, cell polarization and cell migration. Negatively
CC regulates hormone exocytosis via activation of the formyl peptide
CC receptors and reorganization of the actin cytoskeleton (By similarity).
CC Has high 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 (By similarity). Plays a role in the formation of phagocytic
CC cups and phagosomes. Plays a role in phagocytosis by mediating the
CC Ca(2+)-dependent interaction between phagosomes and the actin
CC cytoskeleton (By similarity). {ECO:0000250|UniProtKB:P04083,
CC ECO:0000250|UniProtKB:P10107, ECO:0000250|UniProtKB:P19619}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07150}. Cytoplasm
CC {ECO:0000250|UniProtKB:P10107}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:P10107}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:P51662}. Lateral cell membrane
CC {ECO:0000250|UniProtKB:P10107}. Cell membrane
CC {ECO:0000250|UniProtKB:P10107}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P10107}. Apical cell membrane
CC {ECO:0000250|UniProtKB:P10107}. Membrane
CC {ECO:0000250|UniProtKB:P10107}; Peripheral membrane protein
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}. Endosome membrane
CC {ECO:0000250|UniProtKB:P07150}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P07150}. Secreted
CC {ECO:0000250|UniProtKB:P10107}. Secreted, extracellular space
CC {ECO:0000250|UniProtKB:P04083}. Cell membrane
CC {ECO:0000250|UniProtKB:P04083}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P04083}; Extracellular side
CC {ECO:0000250|UniProtKB:P04083}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:P10107}. Cytoplasmic vesicle, secretory vesicle
CC lumen {ECO:0000250|UniProtKB:P10107}. Cell projection, phagocytic cup
CC {ECO:0000250|UniProtKB:P10107}. Note=Colocalizes with actin fibers at
CC phagocytic cups. Secreted, at least in part via exosomes and other
CC secretory vesicles. Detected in exosomes and other extracellular
CC vesicles. Secretion is increased in response to wounding and
CC inflammation (By similarity). Alternatively, the secretion is dependent
CC on protein unfolding and facilitated by the cargo receptor TMED10; it
CC results in the protein translocation from the cytoplasm into ERGIC
CC (endoplasmic reticulum-Golgi intermediate compartment) followed by
CC vesicle entry and secretion (By similarity). Detected in gelatinase
CC granules in resting neutrophils. Neutrophil adhesion to endothelial
CC cells stimulates secretion via gelatinase granules, but foreign
CC particle phagocytosis has no effect. Displays calcium-dependent binding
CC to phospholipid membranes (By similarity).
CC {ECO:0000250|UniProtKB:P04083, ECO:0000250|UniProtKB:P10107}.
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 -!- DOMAIN: The N-terminal 26 amino acids are sufficient for its
CC extracellular functions in the regulation of inflammation and wound
CC healing. Acylated peptides that contain the first 26 amino acids of the
CC mature protein can activate signaling via the formyl peptide receptors.
CC {ECO:0000250|UniProtKB:P04083}.
CC -!- MISCELLANEOUS: Was originally identified as calcium and phospholipid
CC binding protein that displays Ca(2+)-dependent binding to phospholipid
CC membranes and can promote membrane aggregation in vitro. Was initially
CC identified as inhibitor of phospholipase A2 activity (in vitro).
CC Inhibition of phospholipase activity is mediated via its phospholipid
CC binding activity that limits the access of phospholipase to its
CC substrates. {ECO:0000250|UniProtKB:P10107}.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
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DR EMBL; S64951; AAB28036.2; -; mRNA.
DR PIR; S36103; S36103.
DR AlphaFoldDB; Q92108; -.
DR SMR; Q92108; -.
DR STRING; 9031.ENSGALP00000032184; -.
DR PaxDb; Q92108; -.
DR VEuPathDB; HostDB:geneid_404271; -.
DR eggNOG; KOG0819; Eukaryota.
DR InParanoid; Q92108; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0031313; C:extrinsic component of endosome membrane; ISS:UniProtKB.
DR GO; GO:0031232; C:extrinsic component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0046632; P:alpha-beta T cell differentiation; IBA:GO_Central.
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; ISS:UniProtKB.
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; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0042063; P:gliogenesis; IBA:GO_Central.
DR GO; GO:0071621; P:granulocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0070365; P:hepatocyte differentiation; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; 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; IBA:GO_Central.
DR GO; GO:0002548; P:monocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; IBA:GO_Central.
DR GO; GO:0045920; P:negative regulation of exocytosis; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0097350; P:neutrophil clearance; IBA:GO_Central.
DR GO; GO:0006909; P:phagocytosis; ISS:UniProtKB.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IBA:GO_Central.
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; ISS: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; ISS:UniProtKB.
DR GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; ISS:UniProtKB.
DR GO; GO:0031340; P:positive regulation of vesicle fusion; IBA:GO_Central.
DR GO; GO:0090303; P:positive regulation of wound healing; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0046883; P:regulation of hormone secretion; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; 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 Gene3D; 1.10.220.10; -; 1.
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; 1.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR00197; ANNEXINI.
DR SMART; SM00335; ANX; 1.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 1.
DR PROSITE; PS51897; ANNEXIN_2; 2.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Annexin; Calcium; Calcium/phospholipid-binding;
KW Cell membrane; Cell projection; Cilium; Cytoplasm; Cytoplasmic vesicle;
KW Endosome; Immunity; Inflammatory response; Innate immunity;
KW Isopeptide bond; Membrane; Metal-binding; Nucleus;
KW Phospholipase A2 inhibitor; Phosphoprotein; Reference proteome; Repeat;
KW Secreted.
FT CHAIN 1..>130
FT /note="Annexin A1"
FT /id="PRO_0000067466"
FT REPEAT 37..108
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 109..>130
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19619"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19619"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19619"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19619"
FT BINDING 95
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 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P19619"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P19619"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P19619"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P19619"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P19619"
FT MOD_RES 24
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250"
FT CROSSLNK 19
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000250"
FT NON_TER 130
SQ SEQUENCE 130 AA; 14398 MW; 003AEF72F910551C CRC64;
MAMVSEFLKQ AWFMDNQEQE CIKSSKGGSS VQSRPNFDPS ADVSALDKAI TVKGVDEATI
IDILTKRTNA QRQQIKAAYQ QAKGKSLEED LKKVLKSHLE DVVVALLKTP AQFDAEELRA
SMKGLGTDRR
