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P24551 (ANXA1_RODSP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Annexin A1
Alternative name(s):
Annexin I
Annexin-1
Calpactin II
Calpactin-2
Lipocortin I
Gene names
Name:ANXA1
Synonyms:ANX1
OrganismRodentia sp.
Taxonomic identifier69158 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › unclassified Rodentia

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Subunit structure

Homodimer in placenta (20%); linked by transglutamylation. Interacts with DYSF By similarity.

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.

Caution

Was originally (Ref.1) thought to originate from the sponge Geodia cydonium, but, on the basis of phylogenetic studies (Ref.2) it seems very probable that the DNA sequence coding for this protein comes from a rodent as agreed by the original authors (Ref.3).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 346345Annexin A1
PRO_0000067465

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; by EGFR By similarity
Modified residue271Phosphoserine; by PKC By similarity
Modified residue371Phosphoserine By similarity
Modified residue3121N6-acetyllysine By similarity
Cross-link19Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) By similarity

Sequences

Sequence LengthMass (Da)Tools
P24551 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 99930C41B682D12F

FASTA34639,053
        10         20         30         40         50         60 
MAMVSEFINQ ACYLEKQEQE YIEIVKSYKG GPAHAVSPYP SFDPSSDVAA LHKGIMVNGV 

        70         80         90        100        110        120 
DEATILDLLT KRYNAQRHHL KAVYIQETGE PLDETLKKAL TGHIQELLLA MIKTPAQFDG 

       130        140        150        160        170        180 
NELRAAMKAV GTDEETLIEI LWTRSNQQIR EITSVYREEL KKDIAKYQTS DTSGEFRDAL 

       190        200        210        220        230        240 
LALAKGNRCE DMSVNQDIAD TDARALYQAA ERRNGTDVNV FNTILTTKKY PHLRNKFQNY 

       250        260        270        280        290        300 
RKYTEEDMKK ALDIELKGQI EKCLTTIAKC GTSTPAFFAE KLYEAMKGAG TRHKTLIRIM 

       310        320        330        340 
VSRSEIDSDQ IKVFYQKKYG VPLCQAILDE TKGAYEKILV ALEGGN

« Hide

References

[1]"cDNA structure and expression of calpactin, a peptide involved in Ca2(+)-dependent cell aggregation in sponges."
Robitzki A., Schroeder H.C., Ugarkovic D., Gramzow M., Fritsche U., Batel R., Mueller W.E.G.
Biochem. J. 271:415-420(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Duret L.
Unpublished observations (FEB-1996)
Cited for: DOUBTS ON BIOLOGICAL SOURCE OF PROTEIN.
[3]Mueller W.E.G.
Unpublished observations (APR-1996)
Cited for: AGREEMENT WITH RODENT CONTAMINATION.

Cross-references

Sequence databases

PIRLUJP1. S13044.

3D structure databases

ProteinModelPortalP24551.
SMRP24551. Positions 2-344.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG061815.

Family and domain databases

Gene3D1.10.220.10. 4 hits.
InterProIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002388. AnnexinI.
[Graphical view]
PANTHERPTHR10502. PTHR10502. 1 hit.
PfamPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSPR00196. ANNEXIN.
PR00197. ANNEXINI.
SMARTSM00335. ANX. 4 hits.
[Graphical view]
SUPFAMSSF47874. Annexin. 1 hit.
PROSITEPS00223. ANNEXIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameANXA1_RODSP
AccessionPrimary (citable) accession number: P24551
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 93 of the entry and version 3 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

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