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Protein

Annexin A1

Gene

ANXA1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. 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 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 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi59Calcium 1; via carbonyl oxygenCombined sources1
Metal bindingi60Calcium 1; via carbonyl oxygenCombined sources1
Metal bindingi62Calcium 1Combined sources1
Metal bindingi97Calcium 2; via carbonyl oxygenCombined sources1
Metal bindingi100Calcium 2; via carbonyl oxygenCombined sources1
Metal bindingi105Calcium 2Combined sources1
Metal bindingi127Calcium 3; via carbonyl oxygenCombined sources1
Metal bindingi129Calcium 3; via carbonyl oxygenCombined sources1
Metal bindingi131Calcium 3; via carbonyl oxygenCombined sources1
Metal bindingi132Calcium 4; via carbonyl oxygenCombined sources1
Metal bindingi134Calcium 4Combined sources1
Metal bindingi171Calcium 3Combined sources1
Metal bindingi210Calcium 5; via carbonyl oxygenCombined sources1
Metal bindingi213Calcium 5; via carbonyl oxygenCombined sources1
Metal bindingi215Calcium 5; via carbonyl oxygenCombined sources1
Metal bindingi253Calcium 6Combined sources1
Metal bindingi255Calcium 5Combined sources1
Metal bindingi256Calcium 6; via carbonyl oxygenCombined sources1
Metal bindingi261Calcium 6Combined sources1
Metal bindingi286Calcium 7; via carbonyl oxygenCombined sources1
Metal bindingi288Calcium 7; via carbonyl oxygenCombined sources1
Metal bindingi290Calcium 7; via carbonyl oxygenCombined sources1
Metal bindingi328Calcium 8; via carbonyl oxygenCombined sources1
Metal bindingi330Calcium 7Combined sources1
Metal bindingi331Calcium 8; via carbonyl oxygenCombined sources1
Metal bindingi336Calcium 8Combined sources1

GO - Molecular functioni

  • calcium-dependent phospholipid binding Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • phospholipase A2 inhibitor activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Phospholipase A2 inhibitor

Keywords - Biological processi

Adaptive immunity, Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

Calcium, Calcium/phospholipid-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin A1
Alternative name(s):
Annexin I1 Publication
Annexin-1
Calpactin II
Calpactin-2
Chromobindin-9
Lipocortin I
Phospholipase A2 inhibitory protein
p351 Publication
Gene namesi
Name:ANXA1
Synonyms:ANX1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm 2 Publications
  • Cell projectioncilium By similarity
  • Basolateral cell membrane By similarity
  • Lateral cell membrane By similarity
  • Early endosome 2 Publications
  • Cell membrane 2 Publications; Peripheral membrane protein 1 Publication
  • Cytoplasmic vesicle membrane 2 Publications; Peripheral membrane protein Curated; Cytoplasmic side Curated
  • Apical cell membrane By similarity
  • Membrane By similarity; Peripheral membrane protein By similarity
  • Endosome By similarity
  • Secreted By similarity
  • Secretedextracellular space By similarity
  • Cell membrane By similarity; Peripheral membrane protein By similarity; Extracellular side 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

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi171D → A: Abolishes calcium-dependent interaction with membranes. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000674622 – 346Annexin A1Add BLAST345

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei5Phosphoserine; by TRPM7By similarity1
Cross-linki19Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Modified residuei21Phosphotyrosine; by EGFR1 Publication1
Modified residuei34PhosphoserineBy similarity1
Modified residuei37PhosphoserineBy similarity1
Modified residuei41PhosphothreonineBy 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 residuei239N6-acetyllysineBy similarity1
Modified residuei312N6-acetyllysineBy similarity1
Disulfide bondi324 ↔ 343Combined sources
Cross-linki332Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

Post-translational modificationi

Phosphorylated by EGFR (PubMed:3020049). Phosphorylated by protein kinase C and TRPM7 (By similarity). Phosphorylated in response to EGF treatment (PubMed:3020049).By similarity1 Publication
Sumoylated.By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiP19619.
PeptideAtlasiP19619.
PRIDEiP19619.

PTM databases

iPTMnetiP19619.

Expressioni

Tissue specificityi

Detected in lung and spleen (at protein level).1 Publication

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 similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000005658.

Structurei

Secondary structure

1346
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 16Combined sources14
Helixi18 – 27Combined sources10
Helixi44 – 55Combined sources12
Helixi62 – 70Combined sources9
Helixi74 – 88Combined sources15
Helixi92 – 99Combined sources8
Helixi102 – 112Combined sources11
Helixi115 – 127Combined sources13
Beta strandi128 – 130Combined sources3
Helixi134 – 143Combined sources10
Helixi146 – 158Combined sources13
Helixi164 – 171Combined sources8
Helixi174 – 184Combined sources11
Helixi196 – 209Combined sources14
Turni210 – 212Combined sources3
Beta strandi213 – 215Combined sources3
Helixi218 – 227Combined sources10
Helixi230 – 241Combined sources12
Helixi248 – 255Combined sources8
Helixi258 – 272Combined sources15
Helixi274 – 286Combined sources13
Beta strandi287 – 290Combined sources4
Helixi293 – 302Combined sources10
Turni303 – 306Combined sources4
Helixi308 – 319Combined sources12
Helixi323 – 330Combined sources8
Helixi333 – 343Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HM6X-ray1.80A/B1-346[»]
1MCXX-ray2.03A1-346[»]
ProteinModelPortaliP19619.
SMRiP19619.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19619.

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

Domaini

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.1 Publication
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
Contains 4 annexin repeats.Curated

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP19619.
KOiK17091.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002388. AnnexinI.
[Graphical view]
PANTHERiPTHR10502:SF17. PTHR10502:SF17. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00197. ANNEXINI.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P19619-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:346
Mass (Da):38,759
Last modified:January 23, 2002 - v3
Checksum:i925845C5DEBCBAB2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti41T → S AA sequence (PubMed:3020049).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95108 mRNA. Translation: CAA64477.1.
RefSeqiNP_001157470.1. NM_001163998.1.
UniGeneiSsc.14559.

Genome annotation databases

GeneIDi396942.
KEGGissc:396942.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95108 mRNA. Translation: CAA64477.1.
RefSeqiNP_001157470.1. NM_001163998.1.
UniGeneiSsc.14559.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HM6X-ray1.80A/B1-346[»]
1MCXX-ray2.03A1-346[»]
ProteinModelPortaliP19619.
SMRiP19619.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000005658.

PTM databases

iPTMnetiP19619.

Proteomic databases

PaxDbiP19619.
PeptideAtlasiP19619.
PRIDEiP19619.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396942.
KEGGissc:396942.

Organism-specific databases

CTDi301.

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP19619.
KOiK17091.

Miscellaneous databases

EvolutionaryTraceiP19619.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002388. AnnexinI.
[Graphical view]
PANTHERiPTHR10502:SF17. PTHR10502:SF17. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00197. ANNEXINI.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiANXA1_PIG
AccessioniPrimary (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: November 2, 2016
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.