Gene Information
Gene NameLPC1
OrganismHomo sapiens (Human)
Gene Length346
Protein NamesAnnexin A1 (Annexin I) (Annexin-1) (Calpactin II) (Calpactin-2) (Chromobindin-9) (Lipocortin I) (Phospholipase A2 inhibitory protein) (p35) [Cleaved into: Annexin Ac2-26]
Target NameNA
Target TypeNA
Gene AgeNA
Evolutionary StageNA
AlphaFoldDBP04083
Gene CardANXA1
Uniprot IDP04083
PfamPF00191
In ASDno
Allosteric PredictionNA
Ortholog in AnimalsNA
OhnologsNA
ParalogsNA
TissueNA
Tissue SpecificityDetected 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}.
Pharmacological Animal ModelsNULL(Chimpanzee);0.001000(Mouse);NULL(Rat);NULL(Rabbit)
Gene Ontology
(biological process)
Gene Ontology
(cellular component)
Gene Ontology
(molecular function)
PDB 1AIN  (X-ray  2.50A  )  1BO9  (NMR  -  )  1QLS  (X-ray  2.30A  )  5VFW  (NMR  -  ) 
DBSNP NA 
Subcellular location [CC]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, extracellular 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). Alternatively, the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10;
it results in the protein translocation from the cytoplasm into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059). 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:32272059, ECO:0000269|PubMed:8557678}.
Mouse PG classificationNA
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