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Protein

Annexin A1

Gene

ANXA1

Organism
Rodentia sp.
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. calcium-dependent phospholipid binding Source: UniProtKB-KW
  2. calcium ion binding Source: InterPro
  3. phospholipase A2 inhibitor activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Phospholipase A2 inhibitor

Keywords - Ligandi

Calcium, Calcium/phospholipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin A1
Alternative name(s):
Annexin I
Annexin-1
Calpactin II
Calpactin-2
Lipocortin I
Gene namesi
Name:ANXA1
Synonyms:ANX1
OrganismiRodentia sp.
Taxonomic identifieri69158 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaunclassified Rodentia

Subcellular locationi

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. Found in the cytoplasm of type II pneumocytes and alveolar macrophages.By similarity

GO - Cellular componenti

  1. basolateral plasma membrane Source: UniProtKB-SubCell
  2. cilium Source: UniProtKB-SubCell
  3. cytoplasm Source: UniProtKB-SubCell
  4. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 346345Annexin A1PRO_0000067465Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei5 – 51Phosphoserine; by TRPM7By similarity
Cross-linki19 – 19Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Modified residuei21 – 211Phosphotyrosine; by EGFRBy similarity
Modified residuei27 – 271Phosphoserine; by PKCBy similarity
Modified residuei37 – 371PhosphoserineBy similarity
Modified residuei312 – 3121N6-acetyllysineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP24551.
SMRiP24551. Positions 2-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati51 – 11161Annexin 1Add
BLAST
Repeati123 – 18361Annexin 2Add
BLAST
Repeati207 – 26761Annexin 3Add
BLAST
Repeati282 – 34261Annexin 4Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the annexin family.Curated
Contains 4 annexin repeats.Curated

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

HOVERGENiHBG061815.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002388. AnnexinI.
[Graphical view]
PANTHERiPTHR10502:SF17. PTHR10502:SF17. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00197. ANNEXINI.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P24551-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMVSEFINQ ACYLEKQEQE YIEIVKSYKG GPAHAVSPYP SFDPSSDVAA
60 70 80 90 100
LHKGIMVNGV DEATILDLLT KRYNAQRHHL KAVYIQETGE PLDETLKKAL
110 120 130 140 150
TGHIQELLLA MIKTPAQFDG NELRAAMKAV GTDEETLIEI LWTRSNQQIR
160 170 180 190 200
EITSVYREEL KKDIAKYQTS DTSGEFRDAL LALAKGNRCE DMSVNQDIAD
210 220 230 240 250
TDARALYQAA ERRNGTDVNV FNTILTTKKY PHLRNKFQNY RKYTEEDMKK
260 270 280 290 300
ALDIELKGQI EKCLTTIAKC GTSTPAFFAE KLYEAMKGAG TRHKTLIRIM
310 320 330 340
VSRSEIDSDQ IKVFYQKKYG VPLCQAILDE TKGAYEKILV ALEGGN
Length:346
Mass (Da):39,053
Last modified:January 23, 2007 - v3
Checksum:i99930C41B682D12F
GO

Sequence databases

PIRiS13044. LUJP1.

Cross-referencesi

Sequence databases

PIRiS13044. LUJP1.

3D structure databases

ProteinModelPortaliP24551.
SMRiP24551. Positions 2-344.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG061815.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002388. AnnexinI.
[Graphical view]
PANTHERiPTHR10502:SF17. PTHR10502:SF17. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00197. ANNEXINI.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Duret L.
    Unpublished observations (JAN-1996)
    Cited for: DOUBTS ON BIOLOGICAL SOURCE OF PROTEIN.
  3. Mueller W.E.G.
    Unpublished observations (MAR-1996)
    Cited for: AGREEMENT WITH RODENT CONTAMINATION.

Entry informationi

Entry nameiANXA1_RODSP
AccessioniPrimary (citable) accession number: P24551
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was originally 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).1 Publication

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.