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P07150 (ANXA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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 By similarity.

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
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processalpha-beta T cell differentiation

Inferred from electronic annotation. Source: Compara

arachidonic acid secretion

Inferred from electronic annotation. Source: Compara

cell cycle

Inferred from electronic annotation. Source: Compara

cell surface receptor signaling pathway

Inferred from direct assay PubMed 12459455. Source: RGD

cellular response to glucocorticoid stimulus

Inferred from direct assay PubMed 2936963. Source: BHF-UCL

cellular response to hydrogen peroxide

Inferred from mutant phenotype PubMed 8607818. Source: RGD

endocrine pancreas development

Inferred from expression pattern PubMed 7527053. Source: RGD

estrous cycle phase

Inferred from expression pattern PubMed 17283243. Source: RGD

gliogenesis

Inferred from expression pattern PubMed 9263577. Source: RGD

hepatocyte differentiation

Inferred from expression pattern PubMed 11668598. Source: RGD

insulin secretion

Inferred from direct assay PubMed 12459455. Source: RGD

keratinocyte differentiation

Inferred from electronic annotation. Source: Compara

negative regulation of acute inflammatory response

Inferred from direct assay PubMed 17917587. Source: RGD

negative regulation of apoptotic process

Inferred from direct assay PubMed 17917587. Source: RGD

negative regulation of protein secretion

Inferred from mutant phenotype PubMed 8559285. Source: RGD

neutrophil clearance

Inferred from electronic annotation. Source: Compara

peptide cross-linking

Inferred from electronic annotation. Source: Compara

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 8607818. Source: RGD

positive regulation of neutrophil apoptotic process

Inferred from electronic annotation. Source: Compara

positive regulation of prostaglandin biosynthetic process

Inferred from mutant phenotype PubMed 8260938. Source: RGD

positive regulation of vesicle fusion

Inferred from electronic annotation. Source: Compara

regulation of cell proliferation

Inferred from electronic annotation. Source: Compara

response to X-ray

Inferred from expression pattern PubMed 9269316. Source: RGD

response to drug

Inferred from expression pattern PubMed 9416328. Source: RGD

response to estradiol stimulus

Inferred from expression pattern PubMed 17283243. Source: RGD

response to interleukin-1

Inferred from expression pattern PubMed 11311405. Source: RGD

response to peptide hormone stimulus

Inferred from expression pattern PubMed 8828496. Source: RGD

   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: Compara

extracellular space

Inferred from direct assay PubMed 10489933. Source: RGD

mitochondrial membrane

Inferred from direct assay PubMed 10806526. Source: RGD

nucleus

Inferred from direct assay PubMed 17994624. Source: RGD

plasma membrane

Inferred from direct assay PubMed 12467520. Source: RGD

protein complex

Inferred from direct assay PubMed 10548514. Source: RGD

sarcolemma

Inferred from electronic annotation. Source: Compara

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent phospholipid binding

Traceable author statement PubMed 12459455. Source: RGD

phospholipase A2 inhibitor activity

Inferred from direct assay PubMed 10806526. Source: RGD

protein homodimerization activity

Inferred from direct assay PubMed 8335093. Source: RGD

structural molecule activity

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 346345Annexin A1
PRO_0000067464

Regions

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

Amino acid modifications

Modified residue21N-acetylalanine Ref.5
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

Experimental info

Sequence conflict3221P → S in AAB19866. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P07150 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F046E5F410AF2CF5

FASTA34638,829
        10         20         30         40         50         60 
MAMVSEFLKQ ACYIEKQEQE YVQAVKSYKG GPGSAVSPYP SFNPSSDVAA LHKAIMVKGV 

        70         80         90        100        110        120 
DEATIIDILT KRTNAQRQQI KAAYLQETGK PLDETLKKAL TGHLEEVVLA MLKTPAQFDA 

       130        140        150        160        170        180 
DELRAAMKGL GTDEDTLIEI LTTRSNQQIR EITRVYREEL KRDLAKDITS DTSGDFRNAL 

       190        200        210        220        230        240 
LALAKGDRCE DMSVNQDLAD TDARALYEAG ERRKGTDVNV FNTILTTRSY PHLRKVFQNY 

       250        260        270        280        290        300 
RKYSQHDMNK ALDLELKGDI EKCLTTIVKC ATSTPAFFAE KLYEAMKGAG TRHKTLIRIM 

       310        320        330        340 
VSRSEIDMNE IKVFYQKKYG IPLCQAILDE TKGDYEKILV ALCGGN 

« Hide

References

« Hide 'large scale' references
[1]"Rat lipocortin I cDNA."
Tamaki M., Nakamura E., Nishikubo C., Sakata T., Shin M., Teraoka H.
Nucleic Acids Res. 15:7637-7637(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
[2]"Molecular cloning anD expression in Escherichia coli of the cDNA coding for rat lipocortin I (calpactin II)."
Shimizu Y., Takabayashi E., Yano S., Shimizu N., Yamada K., Gushima H.
Gene 65:141-147(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Correlation of gene and protein structure of rat and human lipocortin I."
Kovacic R.T., Tizard R., Cate R.L., Frey A.Z., Wallner B.P.
Biochemistry 30:9015-9021(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[4]"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].
Tissue: Prostate.
[5]Bienvenut W.V., von Kriegsheim A., Kolch W.
Submitted (JUN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-9; 59-71; 99-124; 129-144; 167-177; 186-204; 214-228; 251-281 AND 304-312, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY.
Tissue: Fibroblast.
[6]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 99-113; 129-144 AND 215-228, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00446 mRNA. Translation: CAA68500.1.
M19967 mRNA. Translation: AAA40861.1.
S57478 expand/collapse EMBL AC list , S57447, S57450, S57455, S57459, S57463, S57466, S57468, S57470, S57472, S57474, S57476 Genomic DNA. Translation: AAB19866.1.
BC061710 mRNA. Translation: AAH61710.1.
IPIIPI00231615.
PIRLURT1. JT0303.
RefSeqNP_037036.1. NM_012904.2.
UniGeneRn.1792.

3D structure databases

ProteinModelPortalP07150.
SMRP07150. Positions 2-344.
ModBaseSearch...

Protein-protein interaction databases

IntActP07150. 2 interactions.
STRING10116.ENSRNOP00000051674.

PTM databases

PhosphoSiteP07150.

Proteomic databases

PaxDbP07150.
PRIDEP07150.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000023664; ENSRNOP00000023664; ENSRNOG00000017469.
GeneID25380.
KEGGrno:25380.
UCSCRGD:2118. rat.

Organism-specific databases

CTD301.
RGD2118. Anxa1.

Phylogenomic databases

eggNOGNOG282829.
GeneTreeENSGT00680000099735.
HOGENOMHOG000158803.
HOVERGENHBG061815.
OrthoDBEOG48WC2C.

Gene expression databases

ArrayExpressP07150.
GenevestigatorP07150.
GermOnlineENSRNOG00000017469. Rattus norvegicus.

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. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio606425.

Entry information

Entry nameANXA1_RAT
AccessionPrimary (citable) accession number: P07150
Secondary accession number(s): Q64664
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 124 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