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Protein

Annexin A1

Gene

ANXA1

Organism
Pan troglodytes (Chimpanzee)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 Fthe 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 (By similarity). 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 similarity

Sites

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

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-1
Gene namesi
Name:ANXA1
OrganismiPan troglodytes (Chimpanzee)
Taxonomic identifieri9598 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan
Proteomesi
  • UP000002277 Componenti: Unplaced

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity
  • 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 By similarity; Peripheral membrane protein By similarity
  • Early endosome By similarity
  • Cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity
  • Endosome membrane By similarity; Peripheral membrane protein 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 (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

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 methionineiRemovedBy similarity
ChainiPRO_00002952842 – 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 EGFRBy similarity1
Modified residuei27Phosphoserine; by PKCBy similarity1
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 ↔ 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

PaxDbiA5A6M2.
PRIDEiA5A6M2.

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

STRINGi9598.ENSPTRP00000049279.

Structurei

3D structure databases

ProteinModelPortaliA5A6M2.
ModBaseiSearch...
MobiDBiSearch...

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.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
Contains 4 annexin repeats.Curated

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiA5A6M2.
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. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A5A6M2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA
60 70 80 90 100
LHKAIMVKGV DEATIIDILT RRNNAQRQQI KAAYLQETGK PLDETLKKAL
110 120 130 140 150
TGHLEEVVLA LLKTPAQFDA DELRAAMKGL GTDEDTLIEI LASRTNKEIR
160 170 180 190 200
DINRVYREEL KRDLAKDITS DTSGDFRNAL LSLAKGDRSE DFGVNEDLAD
210 220 230 240 250
SDARALYEAG ERRKGTDVNV FNTILTTRSY PQLRRVFQKY TKYSKHDMNK
260 270 280 290 300
VLDLELKGDI EKCLTAIVKC ATSKPAFFAE KLHQAMKGVG TRHKALIRIM
310 320 330 340
VSRSEIDMND IKAFYQKMYG ISLCQAILDE TKGDYEKILV ALCGGN
Length:346
Mass (Da):38,742
Last modified:June 12, 2007 - v1
Checksum:i27591E1B5183BECA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB222150 mRNA. Translation: BAF62395.1.
RefSeqiNP_001092037.1. NM_001098567.1.
UniGeneiPtr.909.

Genome annotation databases

GeneIDi472953.
KEGGiptr:472953.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB222150 mRNA. Translation: BAF62395.1.
RefSeqiNP_001092037.1. NM_001098567.1.
UniGeneiPtr.909.

3D structure databases

ProteinModelPortaliA5A6M2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9598.ENSPTRP00000049279.

Proteomic databases

PaxDbiA5A6M2.
PRIDEiA5A6M2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi472953.
KEGGiptr:472953.

Organism-specific databases

CTDi301.

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiA5A6M2.
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. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiANXA1_PANTR
AccessioniPrimary (citable) accession number: A5A6M2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: June 12, 2007
Last modified: October 5, 2016
This is version 63 of the entry and version 1 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.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.