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Annexin A1



Rattus norvegicus (Rat)
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli


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 ofthe 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 Ca2+ and can bind up to eight Ca2+ ions (By similarity). Displays Ca2+-dependent binding to phospholipid membranes (PubMed:3020049). Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca2+-dependent interaction between phagosomes and the actin cytoskeleton (By similarity).By similarity1 Publication


Was originally identified as calcium and phospholipid binding protein that displays Ca2+-dependent binding to phospholipid membranes and can promote membrane aggregation in vitro. Was initially identified as inhibitor of phospholipase A2 activity (in vitro). Inhibition of phospholipase activity is mediated via its phospholipid binding activity that limits the access of phospholipase to its substrates.By similarity


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi59Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi60Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi62Calcium 1By similarity1
Metal bindingi97Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi100Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi105Calcium 2By similarity1
Metal bindingi127Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi129Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi131Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi132Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi134Calcium 4By similarity1
Metal bindingi171Calcium 3By similarity1
Metal bindingi210Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi213Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi215Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi253Calcium 6By similarity1
Metal bindingi255Calcium 5By similarity1
Metal bindingi256Calcium 6; via carbonyl oxygenBy similarity1
Metal bindingi261Calcium 6By similarity1
Metal bindingi286Calcium 7; via carbonyl oxygenBy similarity1
Metal bindingi288Calcium 7; via carbonyl oxygenBy similarity1
Metal bindingi290Calcium 7; via carbonyl oxygenBy similarity1
Metal bindingi328Calcium 8; via carbonyl oxygenBy similarity1
Metal bindingi330Calcium 7By similarity1
Metal bindingi331Calcium 8; via carbonyl oxygenBy similarity1
Metal bindingi336Calcium 8By similarity1

GO - Molecular functioni

  • annealing helicase activity Source: RGD
  • cadherin binding involved in cell-cell adhesion Source: Ensembl
  • calcium-dependent phospholipid binding Source: UniProtKB
  • calcium-dependent protein binding Source: Ensembl
  • calcium ion binding Source: UniProtKB
  • double-stranded DNA-dependent ATPase activity Source: RGD
  • helicase activity Source: RGD
  • phospholipase A2 inhibitor activity Source: RGD
  • phospholipid binding Source: RGD
  • protein binding, bridging Source: Ensembl
  • protein homodimerization activity Source: RGD
  • single-stranded DNA binding Source: RGD
  • structural molecule activity Source: Ensembl

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • adaptive immune response Source: UniProtKB-KW
  • alpha-beta T cell differentiation Source: Ensembl
  • arachidonic acid secretion Source: Ensembl
  • cell surface receptor signaling pathway Source: RGD
  • cellular response to glucocorticoid stimulus Source: BHF-UCL
  • cellular response to hydrogen peroxide Source: RGD
  • DNA duplex unwinding Source: RGD
  • DNA rewinding Source: RGD
  • endocrine pancreas development Source: RGD
  • estrous cycle Source: RGD
  • gliogenesis Source: RGD
  • G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: UniProtKB
  • granulocyte chemotaxis Source: UniProtKB
  • hepatocyte differentiation Source: RGD
  • inflammatory response Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
  • insulin secretion Source: RGD
  • keratinocyte differentiation Source: Ensembl
  • monocyte chemotaxis Source: UniProtKB
  • myoblast migration involved in skeletal muscle regeneration Source: Ensembl
  • negative regulation of exocytosis Source: UniProtKB
  • negative regulation of interleukin-8 secretion Source: Ensembl
  • negative regulation of phospholipase A2 activity Source: RGD
  • negative regulation of protein secretion Source: RGD
  • negative regulation of T-helper 2 cell differentiation Source: UniProtKB
  • neutrophil clearance Source: Ensembl
  • peptide cross-linking Source: Ensembl
  • phagocytosis Source: UniProtKB
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  • positive regulation of interleukin-2 production Source: UniProtKB
  • positive regulation of neutrophil apoptotic process Source: Ensembl
  • positive regulation of prostaglandin biosynthetic process Source: RGD
  • positive regulation of T cell proliferation Source: UniProtKB
  • positive regulation of T-helper 1 cell differentiation Source: UniProtKB
  • positive regulation of vesicle fusion Source: Ensembl
  • positive regulation of wound healing Source: UniProtKB
  • prolactin secretion Source: RGD
  • prostate gland development Source: RGD
  • regulation of cell shape Source: UniProtKB
  • regulation of hormone secretion Source: UniProtKB
  • regulation of inflammatory response Source: UniProtKB
  • regulation of interleukin-1 production Source: UniProtKB
  • regulation of leukocyte migration Source: UniProtKB
  • response to corticosteroid Source: RGD
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to glucocorticoid Source: RGD
  • response to hormone Source: RGD
  • response to interleukin-1 Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to peptide hormone Source: RGD
  • response to X-ray Source: RGD


Molecular functionPhospholipase A2 inhibitor
Biological processAdaptive immunity, Immunity, Inflammatory response, Innate immunity
LigandCalcium, Calcium/phospholipid-binding, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-416476. G alpha (q) signalling events.
R-RNO-418594. G alpha (i) signalling events.
R-RNO-444473. Formyl peptide receptors bind formyl peptides and many other ligands.

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin A1
Alternative name(s):
Annexin I
Calpactin II1 Publication
Lipocortin I1 Publication
Phospholipase A2 inhibitory protein
Gene namesi
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi2118. Anxa1.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication
  • Cell projectioncilium By similarity
  • Basolateral cell membrane By similarity
  • Lateral cell membrane By similarity
  • Cell membrane By similarity; Peripheral membrane protein By similarity
  • Apical cell membrane By similarity
  • Membrane 1 Publication; Peripheral membrane protein 1 Publication
  • Endosome membrane 1 Publication; Peripheral membrane protein 1 Publication
  • Secreted By similarity
  • Secretedextracellular space By similarity
  • Cell membrane By similarity; Peripheral membrane protein By similarity; Extracellular side By similarity
  • Early endosome By similarity
  • Cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity
  • Secretedexosome By similarity
  • Cytoplasmic vesiclesecretory vesicle lumen By similarity
  • Cell projectionphagocytic cup By similarity

  • 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:3020049).By similarity1 Publication

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • basolateral plasma membrane Source: UniProtKB-SubCell
  • cell-cell adherens junction Source: Ensembl
  • cornified envelope Source: Ensembl
  • cytoplasm Source: RGD
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • cytosol Source: Ensembl
  • early endosome membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: RGD
  • extrinsic component of endosome membrane Source: UniProtKB
  • extrinsic component of external side of plasma membrane Source: UniProtKB
  • focal adhesion Source: Ensembl
  • lateral plasma membrane Source: UniProtKB
  • mast cell granule Source: RGD
  • mitochondrial membrane Source: RGD
  • motile cilium Source: UniProtKB
  • nucleoplasm Source: Ensembl
  • nucleus Source: RGD
  • phagocytic cup Source: UniProtKB-SubCell
  • plasma membrane Source: RGD
  • protein complex Source: RGD
  • sarcolemma Source: Ensembl

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000674642 – 346Annexin A1Add BLAST345

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei5Phosphoserine; by TRPM7By similarity1
Cross-linki19Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Modified residuei21Phosphotyrosine; by EGFRBy similarity1
Modified residuei27Phosphoserine; by PKCBy similarity1
Modified residuei34PhosphoserineBy similarity1
Modified residuei37PhosphoserineBy similarity1
Modified residuei58N6-acetyllysineBy similarity1
Modified residuei136PhosphothreonineBy similarity1
Cross-linki214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei312N6-acetyllysineBy similarity1
Disulfide bondi324 ↔ 343By similarity
Cross-linki332Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

Post-translational modificationi

Phosphorylated by protein kinase C, EGFR and TRPM7. Phosphorylated in response to EGF treatment.By similarity
Sumoylated.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases


PTM databases



Tissue specificityi

Detected in eosinophils (PubMed:12467520). Detected in lung, placenta, spleen and thymus (at protein level) (PubMed:3020049).2 Publications

Gene expression databases

GenevisibleiP07150. RN.


Subunit structurei

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).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi247419. 2 interactors.
IntActiP07150. 2 interactors.


3D structure databases


Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati51 – 111Annexin 1Add BLAST61
Repeati123 – 183Annexin 2Add BLAST61
Repeati207 – 267Annexin 3Add BLAST61
Repeati282 – 342Annexin 4Add BLAST61


The full-length protein can bind eight Ca2+ 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 Ca2+, these sites are buried in the interior of the protein core. The N-terminal region becomes disordered in response to calcium-binding.By similarity
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.By similarity

Sequence similaritiesi

Belongs to the annexin family.Curated

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiView protein in InterPro
IPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002388. ANX1.
PANTHERiPTHR10502:SF141. PTHR10502:SF141. 1 hit.
PfamiView protein in Pfam
PF00191. Annexin. 4 hits.
SMARTiView protein in SMART
SM00335. ANX. 4 hits.
PROSITEiView protein in PROSITE
PS00223. ANNEXIN. 4 hits.


Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07150-1 [UniParc]FASTAAdd to basket

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310 320 330 340
Mass (Da):38,829
Last modified:January 23, 2007 - v2

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti322P → S in AAB19866 (PubMed:1832554).Curated1

Sequence databases

Select the link destinations:
Links Updated
Y00446 mRNA. Translation: CAA68500.1.
M19967 mRNA. Translation: AAA40861.1.
, S57447, S57450, S57455, S57459, S57463, S57466, S57468, S57470, S57472, S57474, S57476 Genomic DNA. Translation: AAB19866.1.
BC061710 mRNA. Translation: AAH61710.1.
PIRiJT0303. LURT1.
RefSeqiNP_037036.1. NM_012904.2.
XP_008758517.1. XM_008760295.2.

Genome annotation databases

EnsembliENSRNOT00000023664; ENSRNOP00000023664; ENSRNOG00000017469.
UCSCiRGD:2118. rat.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiANXA1_RAT
AccessioniPrimary (citable) accession number: P07150
Secondary accession number(s): Q64664
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: July 5, 2017
This is version 162 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program


Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome


  1. SIMILARITY comments
    Index of protein domains and families