Summary: Transient receptor ion channel II
Transient receptor ion channel II Provide feedback
This domain is found in the transient receptor ion channel (Trp) family of proteins. There is strong evidence that Trp proteins are structural elements of calcium-ion entry channels activated by G protein-coupled receptors . This domain does not tend to appear with the TRP domain (PF06011) but is often found to the C-terminus of Ankyrin repeats (PF00023).
Vannier B, Peyton M, Boulay G, Brown D, Qin N, Jiang M, Zhu X, Birnbaumer L; , Proc Natl Acad Sci U S A 1999;96:2060-2064.: Mouse trp2, the homologue of the human trpc2 pseudogene, encodes mTrp2, a store depletion-activated capacitative Ca2+ entry channel. PUBMED:10051594 EPMC:10051594
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR013555
TRP (transient receptor potential) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [PUBMED:18535090].
TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies [PUBMED:20025796]: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin), whose only member is the transmembrane protein 1, TRPP(polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogenous properties and complex regulation.
TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [PUBMED:20861159].
This domain is found in some Trp proteins, and is generally located C-terminal to ankyrin repeats (INTERPRO).
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
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Curation and family details
|Seed source:||Pfam-B_1032 (release 18.0)|
|Number in seed:||18|
|Number in full:||680|
|Average length of the domain:||62.10 aa|
|Average identity of full alignment:||55 %|
|Average coverage of the sequence by the domain:||7.46 %|
|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:||6|
|Download:||download the raw HMM for this family|
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