Annexin

Annexin

Pfam_box
Symbol = Annexin
Name =



width = 220
caption = Structure of human annexin III.
Pfam= PF00191
InterPro= IPR001464
SMART=
PROSITE= PDOC00195
SCOP = 2ran
TCDB = 1.A.31
OPM family= 43
OPM protein= 1w3w
PDB=PDB3|1n00A:14-79 PDB3|1dk5B:15-80 PDB3|1aeiF:89-154PDB3|1dm5B:89-154 PDB3|1w3wA:25-90 PDB3|1w45B:25-90PDB3|1sav :19-84 PDB3|1anxB:19-84 PDB3|1hve :19-84PDB3|1hvg :19-84 PDB3|1anwB:19-84 PDB3|1hvd :19-84PDB3|1hakA:19-84 PDB3|1hvf :19-84 PDB3|1avr :19-84PDB3|1avhA:19-84 PDB3|1n41A:17-82 PDB3|2ran :17-82PDB3|1bc1 :17-82 PDB3|1a8b :17-82 PDB3|1bcw :17-82PDB3|1bc3 :17-82 PDB3|1n44A:17-82 PDB3|1bcy :17-82PDB3|1n42A:17-82 PDB3|1bcz :17-82 PDB3|1g5nA:17-82PDB3|1bc0 :17-82 PDB3|1a8a :17-82 PDB3|1yj0A:19-84PDB3|1yiiA:19-84 PDB3|1ala :19-84 PDB3|1ann :18-83PDB3|1i4aA:18-83 PDB3|1aow :18-83 PDB3|1m9iA:367-432PDB3|1avc :312-377 PDB3|1aii :22-87 PDB3|1axn :22-87PDB3|1xjlA:37-102 PDB3|1w7bA:37-102 PDB3|1mcxA:46-111PDB3|1hm6B:46-111 PDB3|1bo9A:46-111

Annexin is a common name for a group of cellular proteins. The annexins are a family of proteins, first described in the 1980s, that bind phospholipid membrane in a calcium-dependent manner. They are found in all kingdoms (animal, plant and fungi) with the exception of the bacteria.

In humans, the annexins are found inside the cell. However some annexins (Annexin A1, Annexin A2, and Annexin A5) have also been found outside the cellular environment, for example, in blood. How the annexins are transported out of the cell into the blood is a mystery because they lack a signal peptide necessary for proteins to be transported out of the cell. Fact|date=June 2007

Annexin is also known as "lipocortin". [MeshName|Annexins] . Lipocortins suppress phospholipase A2. [ [http://www.biochem.northwestern.edu/holmgren/Glossary/Definitions/Def-L/lipocortin.html lipocortin definition ] ] This is the mechanism by which glucocorticoids (primarily cortisol) inhibits inflammation.

Types/Subfamilies

*Annexin, type I InterPro|IPR002388
*Annexin, type II InterPro|IPR002389
*Annexin, type III InterPro|IPR002390
*Annexin, type IV InterPro|IPR002391
*Annexin, type V InterPro|IPR002392
*Annexin, type VI InterPro|IPR002393
*Alpha giardin InterPro|IPR008088
*Annexin, type X InterPro|IPR008156
*Annexin, type VIII InterPro|IPR009115
*Annexin, type XXXI InterPro|IPR009116
*Annexin, type fungal XIV InterPro|IPR009117
*Annexin, type plant InterPro|IPR009118
*Annexin, type XIII InterPro|IPR009166
*Annexin, type VII InterPro|IPR013286
*Annexin like protein InterPro|IPR015472
*Annexin V InterPro|IPR015473
*Annexin XI InterPro|IPR015475

Human proteins containing this domain

ANXA1; ANXA10; ANXA11; ANXA13; ANXA2; ANXA3; ANXA4; ANXA5;
ANXA6; ANXA7; ANXA8; ANXA8L1; ANXA8L2; ANXA9;

References

Further reading

* [ 1] . cite journal |author=Bauer B, Engelbrecht S, Bakker-Grunwald T, Scholze H |title=Functional identification of alpha 1-giardin as an annexin of Giardia lamblia |journal=FEMS Microbiol. Lett. |volume=173 |issue=1 |pages=147–53 |year=1999 |month=April |pmid=10220891 |doi= |url=http://linkinghub.elsevier.com/retrieve/pii/S0378-1097(99)00064-6
* [ 2] . cite journal |author=Moss SE, Morgan RO |title=The annexins |journal=Genome Biol. |volume=5 |issue=4 |pages=219 |year=2004 |pmid=15059252 |doi=10.1186/gb-2004-5-4-219 |url=http://genomebiology.com/1465-6906/5/219

External links

* [http://www.annexins.org European Annexin Homepage] , acquired on 20 August 2005
* - Calculated spatial positions of annexins in membranes (the initially bound state)
* [http://www.expasy.org/cgi-bin/prosite-search-ac?PDOC00195 Annexins repeated domain] in PROSITE


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  • Annexin A5 — (or annexin V) is a cellular protein in the annexin group. The function of the protein is unknown, however annexin A5 has been proposed to play a role in the inhibition of blood coagulation by competing for phosphatidylserine binding sites with… …   Wikipedia

  • Annexin A1 — (or Lipocortin I) is a human protein encoded by the ANXA1 gene. PBB Summary section title = summary text = Annexin I belongs to a family of Ca(2+) dependent phospholipid binding proteins that have a molecular weight of approximately 35,000 to… …   Wikipedia

  • Annexin A2 — is a pleiotropic protein, meaning that its function is dependent on place and time in the body. PBB Summary section title = summary text = This gene encodes a member of the annexin family. Members of this calcium dependent phospholipid binding… …   Wikipedia

  • Annexin A3 — Annexin A3, also known as ANXA3, is a human gene.cite web | title = Entrez Gene: ANXA3 annexin A3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView TermToSearch=306| accessdate = ] PBB Summary section title = summary text …   Wikipedia

  • Annexin V — is the cause of a syndrome called the antiphospholipid antibody syndrome with abnormal blood clotting. The annexins are a family of proteins first described in 1990. All of the annexin proteins share the property of binding calcium and… …   Medical dictionary

  • Annexin 2 — is a protein shown to be involved in diverse cellular processes such as cell motility (especially that of the epithelial cells), linkage of membrane associated protein complexes to the actin cytoskeleton, endocytosis, fibrinolysis, ion channel… …   Wikipedia

  • Annexin II — Structure cristallographique modélisée de l annexine II Annexine II (autres noms : Annexin II, Annexin A2, Annexin 2, Lipocortin II, Calpactin I heavy chain, Chromobindin 8, p. 36, Placental anticoagulant protein IV). UniProtKB/Swiss… …   Wikipédia en Français

  • Annexin A5 affinity assay — Annexin A5 is a protein that binds in a calcium dependent manner to phosphatidylserine containing membrane surfaces. Cell surface expression of phosphatidylserine during cell deathApoptosis is a form of programmed cell death which is used by the… …   Wikipedia

  • annexin — noun Any of a group of cellular proteins found in all kingdoms (animal, plant and fungi) with the exception of the bacteria …   Wiktionary

  • annexin — an·nex·in (ə nekґsin) any of a family of Ca2+ dependent phospholipid binding proteins, which share a common primary structure in the C terminal region, four or eight repeats of an approximately 70 amino acid sequence. Proposed functions… …   Medical dictionary

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