UniProtKB - P19619 (ANXA1_PIG)
Annexin A1
ANXA1
Functioni
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. 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. 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 (PubMed:12595246).
Displays Ca2+-dependent binding to phospholipid membranes (PubMed:8885232).
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 similarity2 PublicationsFunctions 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. Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration. Promotes resolution of inflammation and wound healing. Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2.
By similarityMiscellaneous
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 59 | Calcium 1; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 60 | Calcium 1; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 62 | Calcium 1Combined sources | 1 | |
Metal bindingi | 97 | Calcium 2; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 100 | Calcium 2; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 105 | Calcium 2Combined sources | 1 | |
Metal bindingi | 127 | Calcium 3; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 129 | Calcium 3; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 131 | Calcium 3; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 132 | Calcium 4; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 134 | Calcium 4Combined sources | 1 | |
Metal bindingi | 171 | Calcium 3Combined sources | 1 | |
Metal bindingi | 210 | Calcium 5; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 213 | Calcium 5; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 215 | Calcium 5; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 253 | Calcium 6Combined sources | 1 | |
Metal bindingi | 255 | Calcium 5Combined sources | 1 | |
Metal bindingi | 256 | Calcium 6; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 261 | Calcium 6Combined sources | 1 | |
Metal bindingi | 286 | Calcium 7; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 288 | Calcium 7; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 290 | Calcium 7; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 328 | Calcium 8; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 330 | Calcium 7Combined sources | 1 | |
Metal bindingi | 331 | Calcium 8; via carbonyl oxygenCombined sources | 1 | |
Metal bindingi | 336 | Calcium 8Combined sources | 1 |
GO - Molecular functioni
- calcium-dependent phospholipid binding Source: UniProtKB
- calcium ion binding Source: UniProtKB
- phospholipase A2 inhibitor activity Source: UniProtKB-KW
GO - Biological processi
- actin cytoskeleton reorganization Source: UniProtKB
- adaptive immune response Source: UniProtKB-KW
- cellular response to glucocorticoid stimulus Source: UniProtKB
- G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: UniProtKB
- granulocyte chemotaxis Source: UniProtKB
- inflammatory response Source: UniProtKB
- innate immune response Source: UniProtKB-KW
- monocyte chemotaxis Source: UniProtKB
- negative regulation of exocytosis Source: UniProtKB
- negative regulation of T-helper 2 cell differentiation Source: UniProtKB
- neutrophil activation Source: UniProtKB
- phagocytosis Source: UniProtKB
- positive regulation of interleukin-2 production Source: UniProtKB
- positive regulation of T cell proliferation Source: UniProtKB
- positive regulation of T-helper 1 cell differentiation Source: UniProtKB
- positive regulation of wound healing Source: UniProtKB
- 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
Keywordsi
Molecular function | Phospholipase A2 inhibitor |
Biological process | Adaptive immunity, Immunity, Inflammatory response, Innate immunity |
Ligand | Calcium, Calcium/phospholipid-binding, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Annexin A1Alternative name(s): Annexin I1 Publication Annexin-1 Calpactin II Calpactin-2 Chromobindin-9 Lipocortin I Phospholipase A2 inhibitory protein p351 Publication Cleaved into the following chain: Annexin Ac2-26By similarity |
Gene namesi | Name:ANXA1 Synonyms:ANX1 |
Organismi | Sus scrofa (Pig) |
Taxonomic identifieri | 9823 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Suina › Suidae › Sus |
Proteomesi |
|
Subcellular locationi
Nucleus
- Nucleus By similarity
Endosome
- Early endosome 2 Publications
- Endosome By similarity
Cytoplasm and Cytosol
- Cytoplasm 2 Publications
Extracellular region or secreted
- Secreted By similarity
- extracellular space By similarity
- extracellular exosome By similarity
Plasma membrane
- Basolateral cell membrane By similarity
- Lateral cell membrane By similarity
- Cell membrane 2 Publications; Peripheral membrane protein 1 Publication
- Apical cell membrane By similarity
- Cell membrane By similarity; Peripheral membrane protein By similarity; Extracellular side By similarity
Other locations
- cilium By similarity
- Cytoplasmic vesicle membrane 2 Publications; Peripheral membrane protein Curated; Cytoplasmic side Curated
- Membrane By similarity; Peripheral membrane protein By similarity
- secretory vesicle lumen By similarity
- phagocytic 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). 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 (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
Endosome
- early endosome membrane Source: UniProtKB
- extrinsic component of endosome membrane Source: UniProtKB
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
- extracellular space Source: UniProtKB
Nucleus
- nucleus Source: UniProtKB
Plasma Membrane
- apical plasma membrane Source: UniProtKB
- basolateral plasma membrane Source: UniProtKB-SubCell
- extrinsic component of external side of plasma membrane Source: UniProtKB
- lateral plasma membrane Source: UniProtKB
- phagocytic cup Source: UniProtKB-SubCell
- plasma membrane Source: UniProtKB
Other locations
- motile cilium Source: UniProtKB
Keywords - Cellular componenti
Cell membrane, Cell projection, Cilium, Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane, Nucleus, SecretedPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 171 | D → A: Abolishes calcium-dependent interaction with membranes. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000067462 | 2 – 346 | Annexin A1Add BLAST | 345 | |
PeptideiPRO_0000454559 | 2 – 26 | Annexin Ac2-26By similarityAdd BLAST | 25 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineBy similarity | 1 | |
Modified residuei | 5 | Phosphoserine; by TRPM7By similarity | 1 | |
Cross-linki | 19 | Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity | ||
Modified residuei | 21 | Phosphotyrosine; by EGFR1 Publication | 1 | |
Modified residuei | 34 | PhosphoserineBy similarity | 1 | |
Modified residuei | 37 | PhosphoserineBy similarity | 1 | |
Modified residuei | 41 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 58 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 136 | PhosphothreonineBy similarity | 1 | |
Cross-linki | 214 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity | ||
Cross-linki | 214 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Modified residuei | 239 | N6-acetyllysineBy similarity | 1 | |
Cross-linki | 257 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity | ||
Modified residuei | 312 | N6-acetyllysineBy similarity | 1 | |
Disulfide bondi | 324 ↔ 343 | Combined sources | ||
Cross-linki | 332 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 26 – 27 | Cleavage; by CTSGBy similarity | 2 |
Keywords - PTMi
Acetylation, Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | P19619 |
PeptideAtlasi | P19619 |
PRIDEi | P19619 |
PTM databases
iPTMneti | P19619 |
Expressioni
Tissue specificityi
Interactioni
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 similarityProtein-protein interaction databases
STRINGi | 9823.ENSSSCP00000005658 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P19619 |
SMRi | P19619 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P19619 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 42 – 113 | Annexin 1PROSITE-ProRule annotationAdd BLAST | 72 | |
Repeati | 114 – 185 | Annexin 2PROSITE-ProRule annotationAdd BLAST | 72 | |
Repeati | 197 – 269 | Annexin 3PROSITE-ProRule annotationAdd BLAST | 73 | |
Repeati | 273 – 344 | Annexin 4PROSITE-ProRule annotationAdd BLAST | 72 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 25 – 47 | DisorderedSequence analysisAdd BLAST | 23 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Annexin, RepeatPhylogenomic databases
eggNOGi | KOG0819, Eukaryota |
InParanoidi | P19619 |
OrthoDBi | 856254at2759 |
Family and domain databases
DisProti | DP01963 |
Gene3Di | 1.10.220.10, 4 hits |
InterProi | View protein in InterPro IPR001464, Annexin IPR018502, Annexin_repeat IPR018252, Annexin_repeat_CS IPR037104, Annexin_sf IPR002388, ANX1 |
PANTHERi | PTHR10502:SF17, PTHR10502:SF17, 1 hit |
Pfami | View protein in Pfam PF00191, Annexin, 4 hits |
PRINTSi | PR00196, ANNEXIN PR00197, ANNEXINI |
SMARTi | View protein in SMART SM00335, ANX, 4 hits |
SUPFAMi | SSF47874, SSF47874, 1 hit |
PROSITEi | View protein in PROSITE PS00223, ANNEXIN_1, 3 hits PS51897, ANNEXIN_2, 4 hits |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MAMVSEFLKQ AWFIDNEEQE YIKTVKGSKG GPGSAVSPYP TFNPSSDVEA
60 70 80 90 100
SHKAITVKGV DEATIIEIHT KRTNAQRQQI KAAYLQEKGK PLDEALKKAL
110 120 130 140 150
TGHLEEVALA LLKTPAQFDA DELRAAMKGL GTDEDTLNEI LASRTNREIR
160 170 180 190 200
EINRVYKEEL KRDLAKDITS DTSGDYQKAL LSLAKGDRSE DLAINDDLAD
210 220 230 240 250
TDARALYEAG ERRKGTDLNV FITILTTRSY LHLRRVFQKY SKYSKHDMNK
260 270 280 290 300
VLDLELKGDI ENCLTVVVKC ATSKPMFFAE KLHQAMKGNG TRHKTLIRIM
310 320 330 340
VSRSEIDMND IKACYQKLYG ISLCQAILDE TKGDYEKILV ALCGGD
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 41 | T → S AA sequence (PubMed:3020049).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X95108 mRNA Translation: CAA64477.1 |
RefSeqi | NP_001157470.1, NM_001163998.1 |
Genome annotation databases
GeneIDi | 396942 |
KEGGi | ssc:396942 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X95108 mRNA Translation: CAA64477.1 |
RefSeqi | NP_001157470.1, NM_001163998.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1HM6 | X-ray | 1.80 | A/B | 1-346 | [»] | |
1MCX | X-ray | 2.03 | A | 1-346 | [»] | |
AlphaFoldDBi | P19619 | |||||
SMRi | P19619 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 9823.ENSSSCP00000005658 |
PTM databases
iPTMneti | P19619 |
Proteomic databases
PaxDbi | P19619 |
PeptideAtlasi | P19619 |
PRIDEi | P19619 |
Genome annotation databases
GeneIDi | 396942 |
KEGGi | ssc:396942 |
Organism-specific databases
CTDi | 301 |
Phylogenomic databases
eggNOGi | KOG0819, Eukaryota |
InParanoidi | P19619 |
OrthoDBi | 856254at2759 |
Miscellaneous databases
EvolutionaryTracei | P19619 |
Family and domain databases
DisProti | DP01963 |
Gene3Di | 1.10.220.10, 4 hits |
InterProi | View protein in InterPro IPR001464, Annexin IPR018502, Annexin_repeat IPR018252, Annexin_repeat_CS IPR037104, Annexin_sf IPR002388, ANX1 |
PANTHERi | PTHR10502:SF17, PTHR10502:SF17, 1 hit |
Pfami | View protein in Pfam PF00191, Annexin, 4 hits |
PRINTSi | PR00196, ANNEXIN PR00197, ANNEXINI |
SMARTi | View protein in SMART SM00335, ANX, 4 hits |
SUPFAMi | SSF47874, SSF47874, 1 hit |
PROSITEi | View protein in PROSITE PS00223, ANNEXIN_1, 3 hits PS51897, ANNEXIN_2, 4 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | ANXA1_PIG | |
Accessioni | P19619Primary (citable) accession number: P19619 Secondary accession number(s): Q29547 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1991 |
Last sequence update: | January 23, 2002 | |
Last modified: | May 25, 2022 | |
This is version 163 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families