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IPR008373 is a Saposin.
<p>Sphingolipids are bioactive compounds found in lower and higher eukaryotes. They are involved in the regulation of various cellular functions, such as growth, differentiation and apoptosis, and are believed to be essential in a healthy diet. Sphigolipids are degraded in the lysosome, and the products from their hydrolysis are used in other biosynthetic and regulatory pathways in the host.</p> <p>There are a number of lysosomal enzymes involved in the breakdown of sphinogolipids, and these act in sequence to degrade the moieties [[cite:PUB00011688]]. These enzymes require co-proteins called sphingolipid activator proteins, (SAPs or saposins), to stabilise and activate them as necessary. SAPs are non-enzymatic and usually have a low molecular weight. They are conserved across a wide range of eukaryotes and contain specific saposin domains that aid in the activation of hydrolase enzymes. There have been four human saposins described so far, sharing significant similarity with each other and with other eukaryotic SAP proteins.</p> <p>Mutations in SAP genes have been linked to a number of conditions. A defect in the saposin B region leads to metachromatic leucodystrophy (MLD), while a single nucleotide polymorphism in the SAP-C region may give rise to Gaucher disease [[cite:PUB00011689]]. More recently, an opportunistic protozoan parasite protein has shown similarity both to the higher and lower eukaryotic saposins. The pore-forming protein isolated from virulent Naegleria fowleri (Brain eating amoeba) has been dubbed Naegleriapore A. It also shares structural similarity with cytolytic bacterial peptides, although this similarity does not extend to the sequence level.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
GO term | Namespace | Name | Definition | Relationships |
---|---|---|---|---|
Cellular component | Lysosome | A small lytic vacuole that has cell cycle-independent morphology and is found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. | ||
Biological process | Sphingolipid metabolic process | The chemical reactions and pathways involving sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid). |
Transcript | Name | Description | Predicted domains | Domain count |
---|---|---|---|---|
– | PREDICTED: proactivator polypeptide-like 1-like isoform X1 [Cicer arietinum] gi|502146403|ref|XP_004506438.1| | 18 | ||
– | Saposin B domain protein; TAIR: AT3G51730.1 saposin B domain-containing protein; Swiss-Prot: sp|P07602|SAP_HUMAN Prosaposin; TrEMBL-Plants: tr|I3TAH9|I3TAH9_LOTJA Uncharacterized protein; Found in the gene: LotjaGi3g1v0094300 | 21 | ||
– | Saposin B domain protein; TAIR: AT3G51730.1 saposin B domain-containing protein; Swiss-Prot: sp|P07602|SAP_HUMAN Prosaposin; TrEMBL-Plants: tr|I3TAH9|I3TAH9_LOTJA Uncharacterized protein; Found in the gene: LotjaGi3g1v0094300 | 21 | ||
– | Saposin B domain protein; TAIR: AT3G51730.1 saposin B domain-containing protein; Swiss-Prot: sp|P07602|SAP_HUMAN Prosaposin; TrEMBL-Plants: tr|I3TAH9|I3TAH9_LOTJA Uncharacterized protein; Found in the gene: LotjaGi3g1v0094300 | 21 |
A list of co-occurring predicted domains within the L. japonicus gene space:
Predicted domain | Source | Observations | Saturation (%) |
---|---|---|---|
SignalP-noTM | SignalP_GRAM_NEGATIVE | 1 | 25.00 |