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0  structures 39  species 0  interactions 436  sequences 23  architectures

Family: Latrophilin (PF02354)

Summary: Latrophilin Cytoplasmic C-terminal region

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This is the Wikipedia entry entitled "Latrophilin receptor". More...

Latrophilin receptor Edit Wikipedia article

Latrophilin
Identifiers
Symbol Latrophilin
Pfam PF02354
InterPro IPR003334
EGF, latrophilin and seven transmembrane domain containing 1
Identifiers
Symbol ELTD1
Alt. symbols ETL
Entrez 64123
HUGO 20822
RefSeq NM_022159
UniProt Q9HBW9
Other data
Locus Chr. 1 p33-p32
latrophilin 1
Identifiers
Symbol LPHN1
Alt. symbols KIAA0821, CIRL1, LEC2
Entrez 22859
HUGO 20973
RefSeq NM_014921
UniProt O94910
Other data
Locus Chr. 19 p13.2
latrophilin 2
Identifiers
Symbol LPHN2
Alt. symbols LPHH1, KIAA0786, LEC1
Entrez 23266
HUGO 18582
OMIM 607018
RefSeq NM_012302
UniProt O95490
Other data
Locus Chr. 1 p31.1
latrophilin 3
Identifiers
Symbol LPHN3
Alt. symbols KIAA0768, LEC3
Entrez 23284
HUGO 20974
RefSeq NM_015236
UniProt Q9HAR2
Other data
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.[1]

[edit] Human proteins containing this domain

LPHN1; LPHN2; LPHN3;

[edit] References

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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 [1]. Latrophilin mRNA is present only in neuronal tissue [1]. Lactrophillin interacts with G-alpha O [1].

Literature references

  1. 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.

Gene Ontology

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Domain organisation

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Alignments

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

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Representative proteomes NCBI
(329)
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RP35
(16)
RP55
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RP75
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  Seed
(3)
Full
(436)
Representative proteomes NCBI
(329)
Meta
(0)
RP15
(4)
RP35
(16)
RP55
(60)
RP75
(132)
Alignment:
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  Seed
(3)
Full
(436)
Representative proteomes NCBI
(329)
Meta
(0)
RP15
(4)
RP35
(16)
RP55
(60)
RP75
(132)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_874 (release 5.2)
Previous IDs: none
Type: Family
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 information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 19.3 19.3
Trusted cut-off 69.2 20.3
Noise cut-off 18.7 18.7
Model length: 366
Family (HMM) version: 11
Download: download the raw HMM for this family

Species distribution

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