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0TRPV2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTRPV2
DescriptionTransient receptor potential cation channel subfamily v member 2 (trpv2) (osm-9-like trp channel 2) (otrpc2) (vanilloid receptor-like protein 1) (vrl-1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005887 integral to plasma membrane (TAS)
0005216 ion channel activity (TAS)
0007600 sensory perception (TAS)
0006810 transport (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This group of proteins is found in sodium.otassium.nd calcium ion channels proteins. The proteins have 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some Na channels proteins the domain is repeated four times.hereas in others (e.g. K channels) the protein forms a tetramer in the membrane. A bacterial structure of the protein is known for the last two helices but is not included in the Pfam family due to it lacking the first four helices.
  IPR005821:Ion transport
The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers . The repeat has been found in proteins of diverse function such as transcriptional initiators.ell-cycle regulators.ytoskeletal.on transporters and signal transducers. The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures . Each repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90o angle. The repeats stack together to form an L-shaped structure .
  IPR002110:Ankyrin
The transient-receptor-potential calcium channel protein.RP-CC.as also been called the store-operated calcium channel (SOC) protein. The prototypical members include the Drosophila melanogaster retinal proteins TRP and TRPL . SOC members of the family mediate the entry of extracellular Ca2+ into cells in response to depletion of intracellular Ca2+ stores and agonist stimulated production of inositol-1.. trisphosphate (IP3). One member of the TRP-CC family.ammalian Htrp3.as been shown to form a tight complex with the IP3 receptor. This interaction is apparently required for IP3 to stimulate Ca2+ release via Htrp3.The vanilloid receptor subtype 1 (VR1).hich is the receptor for capsaicin and serves as a heat-activated ion channel in the pain pathway.s also a member of this family. The stretch-inhibitable non-selective cation channel (SIC) is identical to the vanilloid receptor throughout all of its first 700 residues.ut it exhibits a different sequence in its last 100 residues. VR1 and SIC transport monovalent cations as well as Ca2+. VR1 is about 10 times more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell death after chronic exposure to capsaicin.
  IPR004729:Transient receptor potential channel
Transient receptor potential (Trp) and related proteins are thought to be Ca2+ ion channel subunits that mediate capacitative Ca2+ entry in response to a range of external and internal cell stimuli. Such Ca2+ entry is thought to be an essential component of cellular responses to many hormones and growth factors.nd acts to replenish intracellular Ca2+ stores that have been emptied through the action of inositol triphosphate (IP3) and other agents. In non-excitable cells..e. those that lack voltage-gated Ca2+ channels.uch as hepatocytes.his mode of Ca2+ entry is thought to be an important step in generating the oscillations of intracellular Ca2+ concentration that characterise their response to stimulatory agents . Studies on the visual transduction system in Drosophila led to the molecular cloning of Trp and the cDNA of a related protein.rp-like.hich show similarity to voltage gated Ca2+ channels in the regions known as S3 through S6.ncluding the S5-S6 linker that forms the ion-selective channel pore . This provided evidence that Trp and/or related proteins might form mammalian capacitative Ca2+ entry channels. A number of Trp and Trp-like channel gene isoforms have now been cloned.ncluding several mammalian homologues. The Trp family is thought to encode at least 20 Ca2+-permeable channel proteins. Hydropathy analysis suggests that they share a common transmembrane (TM) topology. Each family member is predicted to possess 6 TM domains with intracellular N- and C-termini.hich is similar to the core structure of the pore-forming subunits of the voltage-gated Na+ and Ca2+ channels. By analogy with these proteins.hich have 4 linked domains of 6 TM segments.t is likely that Trp channels are homo- or heterotetramers of 4 single subunits . The Trp family can be divided on the basis of sequence similarity into 3 subfamilies: short (S).ong (L) and osm-like (O) Trp channels. The STrp subfamily includes Drosophila Trp and Trpl-like.nd the mammalian homologues TrpC1-7. Channels of the STrpC subfamily are activated following receptor-mediated stimulation of different isoforms of phospholipase C .Following the cloning of the vanilloid receptor (VR1).t least 4 otherrelated proteins have been identified. Together.hese form a distinctsubgroup of the Trp family. Members of the vanilloid receptor family (TRPV)are activated by a diverse range of stimuli.ncluding heat.rotons.ipids.horbols.hosphorylation.hanges in extracellular osmolarityand/or pressure.nd depletion of intracellular calcium stores . To date. vanilloid receptor-like proteins (VRL-1 and VRL-2) and at least 2epithelial calcium channels (ECAC) have been reported.
  IPR008347:Vanilloid receptor
IPR005821:Ion_trans 
Evalue:-13.958607673645 
Location:444-645IPR002110:Ank 
Evalue:-7.53760194778442 
Location:162-194IPR002110:Ank 
Evalue:-4.13076829910278 
Location:208-243IPR008347:TRPVRECEPTOR 
Evalue:0 
Location:103-130IPR008347:TRPVRECEPTOR 
Evalue:0 
Location:257-280IPR008347:TRPVRECEPTOR 
Evalue:0 
Location:132-153IPR008347:TRPVRECEPTOR 
Evalue:0 
Location:685-705IPR008347:TRPVRECEPTOR 
Evalue:0 
Location:363-383IPR008347:TRPVRECEPTOR 
Evalue:0 
Location:706-725IPR008347:TRPVRECEPTOR 
Evalue:0 
Location:405-421IPR002110:Ank 
Evalue:0.230448916554451 
Location:293-316
SequencesProtein: TRPV2_HUMAN (764 aa)
mRNA: NM_016113
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
KO assignmentK04971
  Level 3 annotation:
    transient receptor potential cation channel, subfamily V, member 2
  Level 2 annotation:
    Ion channels
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 87 residues, 16259612-16259872Exon2: 104 residues, 16261600-16261907Exon3: 46 residues, 16264153-16264287Exon4: 99 residues, 16266637-16266928Exon5: 101 residues, 16267507-16267806Exon6: 59 residues, 16270137-16270308Exon7: 54 residues, 16270760-16270916Exon8: 35 residues, 16271487-16271586Exon9: 25 residues, 16272355-16272426Exon10: 57 residues, 16272855-16273021Exon11: 24 residues, 16275822-16275889Exon12: 113 residues, 16276004-16276339Exon13: 43 residues, 16277612-16277737Exon14: 28 residues, 16278928-16279008Exon15: 73 residues, 16280827-16281040Exon16: 2 residues, -Jump to TRPV2_HUMAN  
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Loci Cluster (Details)Loci: 2986 16259612-16281040 ~-21K 15219(TRPV2)(+)Loci: 2985 15788955-15819935 ~-31K 15203(ADORA2B)(+)Link out to UCSC