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P10107 (ANXA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Annexin A1
Alternative name(s):
Annexin I
Annexin-1
Calpactin II
Calpactin-2
Chromobindin-9
Lipocortin I
Phospholipase A2 inhibitory protein
p35
Gene names
Name:Anxa1
Synonyms:Anx1, Lpc-1, Lpc1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. This protein regulates phospholipase A2 activity. It seems to bind from two to four calcium ions with high affinity.

Subunit structure

Homodimer in placenta (20%); linked by transglutamylation. Interacts with DYSF. Ref.5

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Cell projectioncilium By similarity. Basolateral cell membrane By similarity. Note: Found in the cilium, nucleus and basolateral cell membrane of ciliated cells in the tracheal endothelium By similarity. Found in the cytoplasm of type II pneumocytes and alveolar macrophages By similarity.

Domain

A pair of annexin repeats may form one binding site for calcium and phospholipid.

Post-translational modification

Phosphorylated by protein kinase C, epidermal growth factor receptor/kinase and TRPM7. Phosphorylation results in loss of the inhibitory activity By similarity.

Sequence similarities

Belongs to the annexin family.

Contains 4 annexin repeats.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cilium
Cytoplasm
Membrane
Nucleus
   DomainAnnexin
Repeat
   LigandCalcium
Calcium/phospholipid-binding
   Molecular functionPhospholipase A2 inhibitor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processalpha-beta T cell differentiation

Inferred from mutant phenotype PubMed 20139728. Source: BHF-UCL

arachidonic acid secretion

Inferred from mutant phenotype PubMed 12553880. Source: MGI

cell surface receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

cellular response to glucocorticoid stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

endocrine pancreas development

Inferred from electronic annotation. Source: Ensembl

estrous cycle phase

Inferred from electronic annotation. Source: Ensembl

gliogenesis

Inferred from electronic annotation. Source: Ensembl

hepatocyte differentiation

Inferred from electronic annotation. Source: Ensembl

insulin secretion

Inferred from electronic annotation. Source: Ensembl

keratinocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of acute inflammatory response

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein secretion

Inferred from electronic annotation. Source: Ensembl

neutrophil clearance

Inferred from electronic annotation. Source: Ensembl

neutrophil homeostasis

Inferred from mutant phenotype PubMed 21957127. Source: BHF-UCL

peptide cross-linking

Inferred from electronic annotation. Source: Ensembl

positive regulation of G1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 12553880. Source: MGI

positive regulation of neutrophil apoptotic process

Inferred from mutant phenotype PubMed 21957127. Source: BHF-UCL

positive regulation of prostaglandin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of vesicle fusion

Inferred from electronic annotation. Source: Ensembl

regulation of cell proliferation

Inferred from mutant phenotype PubMed 12553880. Source: MGI

response to X-ray

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

signal transduction

Inferred from mutant phenotype PubMed 12553880. Source: MGI

   Cellular_componentbasolateral plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cilium

Inferred from electronic annotation. Source: UniProtKB-SubCell

cornified envelope

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

mitochondrial membrane

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from electronic annotation. Source: Ensembl

sarcolemma

Inferred from direct assay Ref.5. Source: MGI

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent phospholipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipase A2 inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

structural molecule activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 346345Annexin A1
PRO_0000067461

Regions

Repeat51 – 11161Annexin 1
Repeat123 – 18361Annexin 2
Repeat207 – 26761Annexin 3
Repeat282 – 34261Annexin 4

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue51Phosphoserine; by TRPM7 By similarity
Modified residue211Phosphotyrosine Ref.6
Modified residue271Phosphoserine; by PKC By similarity
Modified residue371Phosphoserine By similarity
Modified residue581N6-acetyllysine Ref.7
Modified residue3121N6-acetyllysine Ref.7
Cross-link19Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) By similarity

Experimental info

Sequence conflict78 – 792QQ → PR in AAA39420. Ref.4
Sequence conflict2121R → I in AAA39437. Ref.2
Sequence conflict2221T → H in AAA39420. Ref.4
Sequence conflict2741T → H in AAA39420. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P10107 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9393A11B24191D3C

FASTA34638,734
        10         20         30         40         50         60 
MAMVSEFLKQ ARFLENQEQE YVQAVKSYKG GPGSAVSPYP SFNVSSDVAA LHKAIMVKGV 

        70         80         90        100        110        120 
DEATIIDILT KRTNAQRQQI KAAYLQENGK PLDEVLRKAL TGHLEEVVLA MLKTPAQFDA 

       130        140        150        160        170        180 
DELRGAMKGL GTDEDTLIEI LTTRSNEQIR EINRVYREEL KRDLAKDITS DTSGDFRKAL 

       190        200        210        220        230        240 
LALAKGDRCQ DLSVNQDLAD TDARALYEAG ERRKGTDVNV FTTILTSRSF PHLRRVFQNY 

       250        260        270        280        290        300 
GKYSQHDMNK ALDLELKGDI EKCLTTIVKC ATSTPAFFAE KLYEAMKGAG TRHKALIRIM 

       310        320        330        340 
VSRSEIDMNE IKVFYQKKYG ISLCQAILDE TKGDYEKILV ALCGGN 

« Hide

References

« Hide 'large scale' references
[1]"Mouse lipocortin I cDNA."
Sakata T., Iwagami S., Tsuruta Y., Suzuki R., Hojo K., Sato K., Teraoka H.
Nucleic Acids Res. 16:11818-11818(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Mouse lipocortin I gene structure and chromosomal assignment: gene duplication and the origins of a gene family."
Horlick K.R., Cheng I.C., Wong W.T., Wakeland E.K., Nick H.S.
Genomics 10:365-374(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary gland.
[4]"cDNA-cloning, sequencing and expression in glucocorticoid-stimulated quiescent Swiss 3T3 fibroblasts of mouse lipocortin I."
Philipps C., Rose-John S., Rincke G., Fuerstenberger G., Marks F.
Biochem. Biophys. Res. Commun. 159:155-162(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-346.
[5]"Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing."
Lennon N.J., Kho A., Bacskai B.J., Perlmutter S.L., Hyman B.T., Brown R.H. Jr.
J. Biol. Chem. 278:50466-50473(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DYSF.
[6]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[7]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58 AND LYS-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07486 mRNA. Translation: CAA30371.1.
M69260 expand/collapse EMBL AC list , 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.
PIRLUMS1. S02181.
RefSeqNP_034860.2. NM_010730.2.
UniGeneMm.248360.

3D structure databases

ProteinModelPortalP10107.
SMRP10107. Positions 2-344.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201194. 4 interactions.
IntActP10107. 6 interactions.
MINTMINT-274958.

PTM databases

PhosphoSiteP10107.

2D gel databases

COMPLUYEAST-2DPAGEP10107.

Proteomic databases

PaxDbP10107.
PRIDEP10107.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025561; ENSMUSP00000025561; ENSMUSG00000024659.
GeneID16952.
KEGGmmu:16952.
UCSCuc008gyi.1. mouse.

Organism-specific databases

CTD301.
MGIMGI:96819. Anxa1.

Phylogenomic databases

eggNOGNOG282829.
HOGENOMHOG000158803.
HOVERGENHBG061815.
KOK17091.
OMAMNDIKAC.
OrthoDBEOG74XS72.
PhylomeDBP10107.
TreeFamTF105452.

Gene expression databases

ArrayExpressP10107.
BgeeP10107.
CleanExMM_ANXA1.
GenevestigatorP10107.

Family and domain databases

Gene3D1.10.220.10. 4 hits.
InterProIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002388. AnnexinI.
[Graphical view]
PfamPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSPR00196. ANNEXIN.
PR00197. ANNEXINI.
SMARTSM00335. ANX. 4 hits.
[Graphical view]
PROSITEPS00223. ANNEXIN. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSANXA1. mouse.
NextBio291004.
PROP10107.
SOURCESearch...

Entry information

Entry nameANXA1_MOUSE
AccessionPrimary (citable) accession number: P10107
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot