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InterPro: IPR001303 Class II aldolase/adducin, N-terminal

Protein matchesHelp
UniProtKB
Matches:
3596 proteins
AccessionHelp IPR001303 Aldolase_II/adducin_N
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR013447 Rhamnulose-1-phosphate aldolase
IPR017714 Methylthioribulose-1-phosphate dehydratase
Found in IPR004661 L-ribulose-5-phosphate 4-epimerase
IPR004782 L-fucose phosphate aldolase
IPR013454 Bifunctional rhamnulose-1-phosphate aldolase/alcohol dehydrogenase
GO Term annotationHelp
Function GO:0046872 metal ion binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This entry represents the alpha/beta/alpha domain found in class II aldolases and adducin, usually at the N terminus. These proteins form part of a family that includes: rhamnulose-1-phosphate aldolase (EC:4.1.2.19), L-fuculose phosphate aldolase (EC:4.1.2.17) [1, 2] that is involved in the third step in fucose metabolism, L-ribulose- 5-phosphate 4-epimerase (EC:5.1.3.4) involved in the third step of L-arabinose catabolism, a probable sugar isomerase SgbE, hypothetical proteins and the metazoan adducins which have not been ascribed any enzymatic function but which play a role in cell membrane cytoskeleton organisation.

Adducins are members of the Ig superfamily and encode cell surface sialoglycoproteins expressed by cytokine-activated endothelium. This type I membrane protein mediates leukocyte-endothelial cell adhesion and signal transduction, and may play a role in the development of artherosclerosis and rheumatoid arthritis. Adducin is a cell-membrane skeletal protein that was first purified from human erythrocytes and subsequently isolated from bovine brain membranes. Isoforms of this protein have been detected in lung, kidney, testes and liver. Erythrocyte adducin is a 200kDa heterodimer protein, composed of alpha and beta subunits, present at about 30,000 copies per cell. It binds with high affinity to Ca(2+)/calmodulin and is a substrate for protein kinases A and C. Both alpha-adducin and beta-adducin show alternative splicing. Thus, there may be several different heterodimeric or homodimeric forms of adducin, each with a different functional specificity. It is thought to play a role in assembly of the spectrin-actin lattice that underlies the plasma membrane [3]. Missense mutations in both the alpha- and beta-adducin genes that alter amino acids that are normally phosphorylated have been associated with the regulation of blood pressure in the Milan hypertensive strain (MHS) of rats. Gamma adducin was isolated from human foetal brain [4]. It shows a high degree of similarity to the alpha and beta adducins.

Structural linksHelp
SCOP: c.74.1.1
CATH: 3.40.225.10
Database linksHelp
PANDIT: PF00596
Blocks: IPB001303

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001303 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P35611 Alpha-adducin

P47095 Putative aldolase class 2 protein YJR024C

Q02645 Protein hu-li tai shao

Q20952 Adducin-related protein 2

Q9QYB5 Gamma-adducin

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001303 Class II aldolase/adducin, N-terminal
IPR017714 Methylthioribulose-1-phosphate dehydratase
SWISS-MODEL
ModBase

PublicationsHelp
1. Dreyer MK, Schulz GE.
The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli.
J. Mol. Biol. 231 549-53 1993 [PubMed: 8515438]
http://dx.doi.org/10.1006/jmbi.1993.1307
2. Dreyer MK, Schulz GE.
Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure.
J. Mol. Biol. 259 458-66 1996 [PubMed: 8676381]
http://dx.doi.org/10.1006/jmbi.1996.0332
3. Rabinovich PM, Beburov MIu, Linevich ZK, Stepanov AI.
[Amplification of the riboflavin operon genes of Bacillus subtilis in Escherichia coli cells]
Genetika 14 1696-1705 1978 [PubMed: 102560]
4. Katagiri T, Ozaki K, Fujiwara T, Shimizu F, Kawai A, Okuno S, Suzuki M, Nakamura Y, Takahashi E, Hirai Y.
Cloning, expression and chromosome mapping of adducin-like 70 (ADDL), a human cDNA highly homologous to human erythrocyte adducin.
Cytogenet. Cell Genet. 74 90-5 1996 [PubMed: 8893809]

Additional ReadingHelp
Grueninger D, Treiber N, Ziegler MO, Koetter JW, Schulze MS, Schulz GE.
Designed protein-protein association.
Science 319 2008 206-9 [PubMed: 18187656]
http://dx.doi.org/10.1126/science.1150421
Grueninger D, Schulz GE.
Antenna domain mobility and enzymatic reaction of L-rhamnulose-1-phosphate aldolase.
Biochemistry 47 2008 607-14 [PubMed: 18085797]
http://dx.doi.org/10.1021/bi7012799
Kroemer M, Schulz GE.
The structure of L-rhamnulose-1-phosphate aldolase (class II) solved by low-resolution SIR phasing and 20-fold NCS averaging.
Acta Crystallogr. D Biol. Crystallogr. 58 2002 824-32 [PubMed: 11976494]
http://dx.doi.org/10.1107/S0907444902004614
Luo Y, Samuel J, Mosimann SC, Lee JE, Tanner ME, Strynadka NC.
The structure of L-ribulose-5-phosphate 4-epimerase: an aldolase-like platform for epimerization.
Biochemistry 40 2001 14763-71 [PubMed: 11732895]
http://dx.doi.org/10.1021/bi0112513
Kroemer M, Merkel I, Schulz GE.
Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase.
Biochemistry 42 2003 10560-8 [PubMed: 12962479]
http://dx.doi.org/10.1021/bi0349266
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InterPro 23.1