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Protein

Annexin A1

Gene

ANXA1

Organism
Oryctolagus cuniculus (Rabbit)
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 ofthe 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi59 – 591Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi60 – 601Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi62 – 621Calcium 1By similarity
Metal bindingi97 – 971Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi100 – 1001Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi105 – 1051Calcium 2By similarity
Metal bindingi127 – 1271Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi129 – 1291Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi131 – 1311Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi132 – 1321Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi134 – 1341Calcium 4By similarity
Metal bindingi171 – 1711Calcium 3By similarity
Metal bindingi210 – 2101Calcium 5; via carbonyl oxygenBy similarity
Metal bindingi213 – 2131Calcium 5; via carbonyl oxygenBy similarity
Metal bindingi215 – 2151Calcium 5; via carbonyl oxygenBy similarity
Metal bindingi253 – 2531Calcium 6By similarity
Metal bindingi255 – 2551Calcium 5By similarity
Metal bindingi256 – 2561Calcium 6; via carbonyl oxygenBy similarity
Metal bindingi261 – 2611Calcium 6By similarity
Metal bindingi286 – 2861Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi288 – 2881Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi290 – 2901Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi328 – 3281Calcium 8; via carbonyl oxygenBy similarity
Metal bindingi330 – 3301Calcium 7By similarity
Metal bindingi331 – 3311Calcium 8; via carbonyl oxygenBy similarity
Metal bindingi336 – 3361Calcium 8By similarity

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 I
Annexin-1
Calpactin II
Calpactin-2
Chromobindin-9
Lipocortin I
Phospholipase A2 inhibitory protein
p35
Gene namesi
Name:ANXA1
Synonyms:ANX1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication
  • Cell projectioncilium 1 Publication
  • Basolateral cell membrane 1 Publication
  • 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
  • Endosome membrane By similarity; Peripheral membrane protein By similarity
  • Early endosome By similarity
  • Cytoplasmic vesicle 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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 346345Annexin A1PRO_0000067463Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei5 – 51Phosphoserine; by TRPM7By similarity
Cross-linki19 – 19Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Modified residuei21 – 211Phosphotyrosine; by EGFRBy similarity
Modified residuei34 – 341PhosphoserineBy similarity
Modified residuei37 – 371PhosphoserineBy similarity
Modified residuei58 – 581N6-acetyllysineBy similarity
Cross-linki214 – 214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei239 – 2391N6-acetyllysineBy similarity
Cross-linki257 – 257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei312 – 3121N6-acetyllysineBy similarity
Disulfide bondi324 ↔ 343By 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

PRIDEiP51662.

Expressioni

Tissue specificityi

In the lung, expressed in the ciliated cells of the tracheal endothelium, but not in the goblet cells. Expressed in type II pneumocytes and alveolar macrophages.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

Structurei

3D structure databases

ProteinModelPortaliP51662.
SMRiP51662. Positions 2-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati51 – 11161Annexin 1Add
BLAST
Repeati123 – 18361Annexin 2Add
BLAST
Repeati207 – 26761Annexin 3Add
BLAST
Repeati282 – 34261Annexin 4Add
BLAST

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

HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP51662.
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.

P51662-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMVSEFLKQ AWFIDNEEQD YINTVKTYKG GPGSAVSPYP AFNPSSDVAA
60 70 80 90 100
LHQAIMVKGV DEATIIDILT KRNNAQRQQI KAAYLQEKGK PLDEVLKKAL
110 120 130 140 150
TGHLEEVVLA LLKTPAQFDA DELRAAMKGL GTDEDTLIEI LASRNNKEIR
160 170 180 190 200
EINRVYREEL KRDLAKDIAS DTSGDFQKAL LSLAKGDRSE DFGVNEDLAD
210 220 230 240 250
TDARALYEAG ERRKGADVNV FTTILTTRSY LHLRRVFQKY SKYSQHDMNK
260 270 280 290 300
VLDLELKGDI EKCLTAIVQC ATCKPAYFAE KLYQAMKGAG TRHKALIRIM
310 320 330 340
VSRSEVDMND IKAFYQKKYG VSLCQAILDE TKGDYEKILV ALCGGN
Length:346
Mass (Da):38,735
Last modified:October 1, 1996 - v1
Checksum:i64EEBAF889D06A3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24656 Genomic DNA. Translation: AAC78495.1.
RefSeqiNP_001164623.1. NM_001171152.1.
UniGeneiOcu.1705.

Genome annotation databases

GeneIDi100328962.
KEGGiocu:100328962.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24656 Genomic DNA. Translation: AAC78495.1.
RefSeqiNP_001164623.1. NM_001171152.1.
UniGeneiOcu.1705.

3D structure databases

ProteinModelPortaliP51662.
SMRiP51662. Positions 2-344.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP51662.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100328962.
KEGGiocu:100328962.

Organism-specific databases

CTDi301.

Phylogenomic databases

HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP51662.
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]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing and expression of rabbit lung annexin I."
    Tsao F.H.C., Wen C., Hu J.
    Med. Biochem. 1:73-81(1998)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Lung.
  2. "Cellular and subcellular localizations of annexins I, IV, and VI in lung epithelia."
    Mayran N., Traverso V., Maroux S., Massey-Harroche D.
    Am. J. Physiol. 270:L863-L871(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-44, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Lung.

Entry informationi

Entry nameiANXA1_RABIT
AccessioniPrimary (citable) accession number: P51662
Secondary accession number(s): Q9TQY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 17, 2016
This is version 107 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, Direct protein sequencing, 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.