- 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:46-111Annexin is a common name for a group of cellular
protein s. The annexins are a family of proteins, first described in the 1980s, that bindphospholipid 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 asignal peptide necessary for proteins to be transported out of the cell. Fact|date=June 2007Annexin 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 whichglucocorticoid s (primarilycortisol ) inhibitsinflammation .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|IPR015475Human 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/1465-6906/5/219External 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] inPROSITE
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