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UniProtKB - P10107 (ANXA1_MOUSE)

Protein

Annexin A1

Gene

Anxa1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 (PubMed:12475898). Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response (PubMed:12475898). Promotes resolution of inflammation and wound healing (PubMed:25664854). 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 (PubMed:17948261). Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (PubMed:17948261). 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 (PubMed:21245195). Plays a role in phagocytosis by mediating the Ca2+-dependent interaction between phagosomes and the actin cytoskeleton (PubMed:21245195).By similarity4 Publications

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

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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionPhospholipase A2 inhibitor
Biological processAdaptive immunity, Immunity, Inflammatory response, Innate immunity
LigandCalcium, Calcium/phospholipid-binding, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-416476 G alpha (q) signalling events
R-MMU-418594 G alpha (i) signalling events
R-MMU-444473 Formyl peptide receptors bind formyl peptides and many other ligands

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin A1
Alternative name(s):
Annexin I
Annexin-1
Calpactin II
Calpactin-2
Chromobindin-9
Lipocortin I1 Publication
Phospholipase A2 inhibitory protein
p35
Gene namesi
Name:Anxa1
Synonyms:Anx1, Lpc-1, Lpc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:96819 Anxa1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

Mice are born at the expected Mendelian rate, appear healthy and are fertile, but tend to die already after about one year. Mutant mice display an increased inflammatory response during zymosan-induced peritonitis, with increased blood leukocyte migration and increased production of IL1B. In mutant mice, glucocorticoid-mediated down-regulation of the early phase of the inflammatory response is abolished, but there is no effect on glucocorticoid-mediated down-regulation of later phases of the inflammatory response. Peritoneal lavage macrophages from mutant mice display decreased phagocytosis. Besides, glucocorticoid-mediated inhibition of phagocytosis is abolished (PubMed:12475898). Mutant mice display increased susceptibility to dextran sulfate sodium (DSS)-induced colitis with increased mucosal injury, slower recovery and increased morbidity (PubMed:18802107). Mutant mice have an exacerbated allergic response after exposure to ovalbumin (PubMed:17948261). T-cells from mutant mice show skewed differentiation into Th1 and Th2 cells with increased differentiation into Th2 cells and decreased differentiation into Th1 cells (PubMed:17948261).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi257K → R: Strongly decreased sumoylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000674612 – 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 residuei21PhosphotyrosineCombined sources1
Modified residuei27Phosphoserine; by PKCBy similarity1
Modified residuei34PhosphoserineBy similarity1
Modified residuei37PhosphoserineBy similarity1
Modified residuei58N6-acetyllysineCombined sources1
Modified residuei136PhosphothreonineBy similarity1
Cross-linki214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Modified residuei312N6-acetyllysineCombined sources1
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.1 Publication

Keywords - PTMi

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

Proteomic databases

EPDiP10107
PaxDbiP10107
PRIDEiP10107

2D gel databases

COMPLUYEAST-2DPAGEiP10107

PTM databases

iPTMnetiP10107
PhosphoSitePlusiP10107
SwissPalmiP10107

Expressioni

Tissue specificityi

Detected in lung (PubMed:12475898, PubMed:17384087). Detected at the apical membrane of airway epithelial cells (PubMed:17384087). Detected in intestinal epithelial cells (PubMed:18802107). Detected in skeletal muscle (PubMed:14506282). Detected in prostate (PubMed:23727357). Detected in thymus (at protein level) (PubMed:12475898). Detected in stomach, lung, spleen, ovary and uterus, and at lower levels in kidney, thymus and heart (PubMed:12475898).4 Publications

Inductioni

Up-regulated by the synthetic glucocorticoid fluocinolone acetonide.1 Publication

Gene expression databases

BgeeiENSMUSG00000024659 Expressed in 267 organ(s), highest expression level in bone marrow
CleanExiMM_ANXA1
ExpressionAtlasiP10107 baseline and differential
GenevisibleiP10107 MM

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 (PubMed:14506282). Interacts with EGFR (By similarity).By similarity1 Publication

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi201194, 6 interactors
IntActiP10107, 7 interactors
MINTiP10107
STRINGi10090.ENSMUSP00000025561

Structurei

3D structure databases

ProteinModelPortaliP10107
SMRiP10107
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

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiKOG0819 Eukaryota
ENOG410XPUN LUCA
GeneTreeiENSGT00760000118972
HOGENOMiHOG000158803
HOVERGENiHBG061815
InParanoidiP10107
KOiK17091
OMAiVSLCQAI
OrthoDBiEOG091G0H6H
PhylomeDBiP10107
TreeFamiTF105452

Family and domain databases

Gene3Di1.10.220.10, 4 hits
InterProiView protein in InterPro
IPR001464 Annexin
IPR018502 Annexin_repeat
IPR018252 Annexin_repeat_CS
IPR037104 Annexin_sf
IPR002388 ANX1
PANTHERiPTHR10502:SF17 PTHR10502:SF17, 1 hit
PfamiView protein in Pfam
PF00191 Annexin, 4 hits
PRINTSiPR00196 ANNEXIN
PR00197 ANNEXINI
SMARTiView protein in SMART
SM00335 ANX, 4 hits
PROSITEiView protein in PROSITE
PS00223 ANNEXIN, 4 hits

Sequencei

Sequence statusi: Complete.

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

P10107-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAMVSEFLKQ ARFLENQEQE YVQAVKSYKG GPGSAVSPYP SFNVSSDVAA 
        60         70         80         90        100
LHKAIMVKGV DEATIIDILT KRTNAQRQQI KAAYLQENGK PLDEVLRKAL 
       110        120        130        140        150
TGHLEEVVLA MLKTPAQFDA DELRGAMKGL GTDEDTLIEI LTTRSNEQIR 
       160        170        180        190        200
EINRVYREEL KRDLAKDITS DTSGDFRKAL LALAKGDRCQ DLSVNQDLAD 
       210        220        230        240        250
TDARALYEAG ERRKGTDVNV FTTILTSRSF PHLRRVFQNY GKYSQHDMNK 
       260        270        280        290        300
ALDLELKGDI EKCLTTIVKC ATSTPAFFAE KLYEAMKGAG TRHKALIRIM 
       310        320        330        340 
VSRSEIDMNE IKVFYQKKYG ISLCQAILDE TKGDYEKILV ALCGGN
Length:346
Mass (Da):38,734
Last modified:January 23, 2007 - v2
Checksum:i9393A11B24191D3C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti78 – 79QQ → PR in AAA39420 (PubMed:2522299).Curated2
Sequence conflicti212R → I in AAA39437 (PubMed:1676980).Curated1
Sequence conflicti222T → H in AAA39420 (PubMed:2522299).Curated1
Sequence conflicti274T → H in AAA39420 (PubMed:2522299).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07486 mRNA Translation: CAA30371.1
M69260
, M69250, M69251, M69252, M69253, M69254, M69255, M69256, M69257, M69258, M69259 Genomic DNA Translation: AAA39437.1
BC002289 mRNA Translation: AAH02289.1
BC004594 mRNA Translation: AAH04594.1
M24554 mRNA Translation: AAA39420.1
CCDSiCCDS29692.1
PIRiS02181 LUMS1
RefSeqiNP_034860.2, NM_010730.2
UniGeneiMm.248360

Genome annotation databases

EnsembliENSMUST00000025561; ENSMUSP00000025561; ENSMUSG00000024659
GeneIDi16952
KEGGimmu:16952
UCSCiuc008gyi.1 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07486 mRNA Translation: CAA30371.1
M69260
, M69250, M69251, M69252, M69253, M69254, M69255, M69256, M69257, M69258, M69259 Genomic DNA Translation: AAA39437.1
BC002289 mRNA Translation: AAH02289.1
BC004594 mRNA Translation: AAH04594.1
M24554 mRNA Translation: AAA39420.1
CCDSiCCDS29692.1
PIRiS02181 LUMS1
RefSeqiNP_034860.2, NM_010730.2
UniGeneiMm.248360

3D structure databases

ProteinModelPortaliP10107
SMRiP10107
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201194, 6 interactors
IntActiP10107, 7 interactors
MINTiP10107
STRINGi10090.ENSMUSP00000025561

PTM databases

iPTMnetiP10107
PhosphoSitePlusiP10107
SwissPalmiP10107

2D gel databases

COMPLUYEAST-2DPAGEiP10107

Proteomic databases

EPDiP10107
PaxDbiP10107
PRIDEiP10107

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025561; ENSMUSP00000025561; ENSMUSG00000024659
GeneIDi16952
KEGGimmu:16952
UCSCiuc008gyi.1 mouse

Organism-specific databases

CTDi301
MGIiMGI:96819 Anxa1

Phylogenomic databases

eggNOGiKOG0819 Eukaryota
ENOG410XPUN LUCA
GeneTreeiENSGT00760000118972
HOGENOMiHOG000158803
HOVERGENiHBG061815
InParanoidiP10107
KOiK17091
OMAiVSLCQAI
OrthoDBiEOG091G0H6H
PhylomeDBiP10107
TreeFamiTF105452

Enzyme and pathway databases

ReactomeiR-MMU-416476 G alpha (q) signalling events
R-MMU-418594 G alpha (i) signalling events
R-MMU-444473 Formyl peptide receptors bind formyl peptides and many other ligands

Miscellaneous databases

ChiTaRSiAnxa1 mouse
PROiPR:P10107
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024659 Expressed in 267 organ(s), highest expression level in bone marrow
CleanExiMM_ANXA1
ExpressionAtlasiP10107 baseline and differential
GenevisibleiP10107 MM

Family and domain databases

Gene3Di1.10.220.10, 4 hits
InterProiView protein in InterPro
IPR001464 Annexin
IPR018502 Annexin_repeat
IPR018252 Annexin_repeat_CS
IPR037104 Annexin_sf
IPR002388 ANX1
PANTHERiPTHR10502:SF17 PTHR10502:SF17, 1 hit
PfamiView protein in Pfam
PF00191 Annexin, 4 hits
PRINTSiPR00196 ANNEXIN
PR00197 ANNEXINI
SMARTiView protein in SMART
SM00335 ANX, 4 hits
PROSITEiView protein in PROSITE
PS00223 ANNEXIN, 4 hits
ProtoNetiSearch...

Entry informationi

Entry nameiANXA1_MOUSE
AccessioniPrimary (citable) accession number: P10107
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 191 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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