Summary: Latrophilin Cytoplasmic C-terminal region
This is the Wikipedia entry entitled "Latrophilin receptor". More...
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Latrophilin receptor Edit Wikipedia article
|EGF, latrophilin and seven transmembrane domain containing 1|
|Locus||Chr. 1 p33-p32|
|Alt. symbols||KIAA0821, CIRL1, LEC2|
|Locus||Chr. 19 p13.2|
|Alt. symbols||LPHH1, KIAA0786, LEC1|
|Locus||Chr. 1 p31.1|
|Alt. symbols||KIAA0768, LEC3|
|Locus||Chr. 4 q13.1|
The latrophilin receptors are a group of related G-protein coupled receptors from the class B secretin family. These receptors were originally identified based on their ability to bind alpha-latrotoxin.
Human proteins containing this domain
- Kreienkamp HJ, Soltau M, Richter D, Böckers T (2002). "Interaction of G-protein-coupled receptors with synaptic scaffolding proteins". Biochem. Soc. Trans. 30 (4): 464–8. doi:10.1042/BST0300464. PMID 12196116.
|This transmembrane receptor-related article is a stub. You can help Wikipedia by expanding it.|
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Latrophilin Cytoplasmic C-terminal region Provide feedback
This family consists of the cytoplasmic C-terminal region in latrophilin. Latrophilin is a synaptic Ca2+ independent alpha- latrotoxin (LTX) receptor and is a novel member of the secretin family of G-protein coupled receptors that are involved in secretion . Latrophilin mRNA is present only in neuronal tissue . Lactrophillin interacts with G-alpha O .
Lelianova VG, Davletov BA, Sterling A, Rahman MA, Grishin EV, Totty NF, Ushkaryov YA; , J Biol Chem 1997;272:21504-21508.: Alpha-latrotoxin receptor, latrophilin, is a novel member of the secretin family of G protein-coupled receptors. PUBMED:9261169 EPMC:9261169
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003334
G-protein-coupled receptors, GPCRs, constitute a vast protein family that encompasses a wide range of functions (including various autocrine, paracrine and endocrine processes). They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups. We use the term clan to describe the GPCRs, as they embrace a group of families for which there are indications of evolutionary relationship, but between which there is no statistically significant similarity in sequence [PUBMED:8170923]. The currently known clan members include the rhodopsin-like GPCRs, the secretin-like GPCRs, the cAMP receptors, the fungal mating pheromone receptors, and the metabotropic glutamate receptor family. There is a specialised database for GPCRs (http://www.gpcr.org/7tm/).
The secretin-like GPCRs include secretin [PUBMED:1646711], calcitonin [PUBMED:1658940], parathyroid hormone/parathyroid hormone-related peptides [PUBMED:1658941] and vasoactive intestinal peptide [PUBMED:1314625], all of which activate adenylyl cyclase and the phosphatidyl-inositol-calcium pathway. These receptors contain seven transmembrane regions, in a manner reminiscent of the rhodopsins and other receptors believed to interact with G-proteins (however there is no significant sequence identity between these families, the secretin-like receptors thus bear their own unique '7TM' signature). Their N terminus is probably located on the extracellular side of the membrane and potentially glycosylated. This N-terminal region contains a long conserved region which allow the binding of large peptidic ligand such as glucagon, secretin, VIP and PACAP; this region contains five conserved cysteines residues which could be involved in disulphide bond. The C-terminal region of these receptor is probably cytoplasmic. Every receptor gene in this family is encoded on multiple exons, and several of these genes are alternatively spliced to yield functionally distinct products.
Latrophilins are a family of secretin-like GPCRs that can be subdivided into 3 subtypes: LPH1, LPH2 and LPH3. LPH1 is a brain-specific calcium independent receptor of alpha-latrotoxin (LTX), a neurotoxin. It is the affinity of this form of the receptor for LTX that gives the family its name. LPH2 and LPH3, whilst sharing extensive sequence similarity to LPH1, do not bind LTX. LPH2 is distributed throughout most tissues, whereas LPH3 is also brain-specific [PUBMED:10025961]. The endogenous ligand(s) for these receptors are at present unknown. Binding of LTX to LPH1 stimulates exocytosis and the subsequent release of large amounts of neurotransmitters from neuronal and endocrine cells. The latrophilins possess up to 7 sites of alternative splicing; the resulting number of possible splice variants leads to a highly variable family of proteins.
This entry represents the C-terminal region of latrophilin.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||membrane (GO:0016020)|
|Molecular function||G-protein coupled receptor activity (GO:0004930)|
|Biological process||G-protein coupled receptor signaling pathway (GO:0007186)|
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Curation and family details
|Seed source:||Pfam-B_874 (release 5.2)|
|Author:||Bashton M, Bateman A|
|Number in seed:||3|
|Number in full:||436|
|Average length of the domain:||235.30 aa|
|Average identity of full alignment:||47 %|
|Average coverage of the sequence by the domain:||23.71 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
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