P10107 (ANXA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 133.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | 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 names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 346 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 projection › cilium 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
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 346 | 345 | Annexin A1 | PRO_0000067461 | |||||
Regions | |||||||||
| Repeat | 51 – 111 | 61 | Annexin 1 | ||||||
| Repeat | 123 – 183 | 61 | Annexin 2 | ||||||
| Repeat | 207 – 267 | 61 | Annexin 3 | ||||||
| Repeat | 282 – 342 | 61 | Annexin 4 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Modified residue | 5 | 1 | Phosphoserine; by TRPM7 By similarity | ||||||
| Modified residue | 21 | 1 | Phosphotyrosine Ref.6 | ||||||
| Modified residue | 27 | 1 | Phosphoserine; by PKC By similarity | ||||||
| Modified residue | 37 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 312 | 1 | N6-acetyllysine By similarity | ||||||
| Cross-link | 19 | Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) By similarity | |||||||
Experimental info | |||||||||
| Sequence conflict | 78 – 79 | 2 | QQ → PR in AAA39420. Ref.4 | ||||||
| Sequence conflict | 212 | 1 | R → I in AAA39437. Ref.2 | ||||||
| Sequence conflict | 222 | 1 | T → H in AAA39420. Ref.4 | ||||||
| Sequence conflict | 274 | 1 | T → H in AAA39420. Ref.4 | ||||||
Sequences
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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, MASS SPECTROMETRY. Tissue: Embryonic fibroblast. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X07486 mRNA. Translation: CAA30371.1. M69260 M69259 Genomic DNA. Translation: AAA39437.1.BC002289 mRNA. Translation: AAH02289.1. BC004594 mRNA. Translation: AAH04594.1. M24554 mRNA. Translation: AAA39420.1. |
| IPI | IPI00230395. |
| PIR | LUMS1. S02181. |
| RefSeq | NP_034860.2. NM_010730.2. |
| UniGene | Mm.248360. |
3D structure databases | |
| ProteinModelPortal | P10107. |
| SMR | P10107. Positions 2-344. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P10107. 4 interactions. |
| MINT | MINT-274958. |
PTM databases | |
| PhosphoSite | P10107. |
2D gel databases | |
| COMPLUYEAST-2DPAGE | P10107. |
Proteomic databases | |
| PaxDb | P10107. |
| PRIDE | P10107. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000025561; ENSMUSP00000025561; ENSMUSG00000024659. |
| GeneID | 16952. |
| KEGG | mmu:16952. |
Organism-specific databases | |
| CTD | 301. |
| MGI | MGI:96819. Anxa1. |
Phylogenomic databases | |
| eggNOG | NOG282829. |
| HOGENOM | HOG000158803. |
| HOVERGEN | HBG061815. |
| OMA | GTRHKTL. |
Gene expression databases | |
| ArrayExpress | P10107. |
| Bgee | P10107. |
| CleanEx | MM_ANXA1. |
| Genevestigator | P10107. |
| GermOnline | ENSMUSG00000024659. Mus musculus. |
Family and domain databases | |
| Gene3D | 1.10.220.10. 4 hits. |
| InterPro | IPR001464. Annexin. IPR018502. Annexin_repeat. IPR018252. Annexin_repeat_CS. IPR002388. AnnexinI. [Graphical view] |
| PANTHER | PTHR10502. PTHR10502. 1 hit. |
| Pfam | PF00191. Annexin. 4 hits. [Graphical view] |
| PRINTS | PR00196. ANNEXIN. PR00197. ANNEXINI. |
| SMART | SM00335. ANX. 4 hits. [Graphical view] |
| SUPFAM | SSF47874. Annexin. 1 hit. |
| PROSITE | PS00223. ANNEXIN. 4 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | ANXA1. mouse. |
| NextBio | 291004. |
| SOURCE | Search... |
Entry information
| Entry name | ANXA1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P10107 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
