View source for TRPML

{{Short description|Protein family}}
'''TRPML''' (transient receptor potential cation channel, mucolipin subfamily) comprises a group of three evolutionarily related proteins that belongs to the large family of [[transient receptor potential]] [[ion channel]]s.  The three proteins [[TRPML1]], [[TRPML2]] and [[TRPML3]] are encoded by the mucolipin-1 (''[[MCOLN1]]''), mucolipin-2 (''[[MCOLN2]]'') and mucolipin-3 (''[[MCOLN3]]'') genes, respectively.

The three members of the TRPML ("ML" for mucolipin) sub-family are not extremely well characterized.<ref name=Nilius_2007>{{cite journal |vauthors=Nilius B, Owsianik G, Voets T, Peters JA |title=Transient receptor potential cation channels in disease |journal=Physiol. Rev. |volume=87 |issue=1 |pages=165–217 |year=2007 |pmid=17237345 |doi=10.1152/physrev.00021.2006|url=https://lirias.kuleuven.be/handle/123456789/137085 |url-access=subscription }}</ref> [[Mucolipin-1|TRPML1]] is known to be localized in late [[endosome]]s.<ref name = "Colletti_2011" >{{cite book | editor = Islam MS | title = Transient Receptor Potential Channels |date=January 2011 | volume = 704 | publisher = Springer |  location = Berlin | pages = 700  | series = Advances in Experimental Medicine and Biology | isbn = 978-94-007-0264-6 | vauthors = Colletti GA, Kiselyov K | chapter = Chapter 11: TRPML1 }}</ref> This subunit also contains a lipase domain between its S1 and S2 segments. While the function of this domain is unknown it has been proposed that it is involved in channel regulation. Physiological studies have described TRPML1 channels as [[proton]] leak channels in [[lysosome]]s responsible for preventing these organelles from becoming too acidic.<ref name = "Colletti_2011" /> [[MCOLN2|TRPML2]] and [[MCOLN3|TRPML3]] more poorly characterized than [[MCOLN1|TRPML1]].<ref name = "Flores_2011" >{{cite book | editor = Islam MS | title = Transient Receptor Potential Channels |date=January 2011 | volume = 704 | publisher = Springer |  location = Berlin | pages = 700  | series = Advances in Experimental Medicine and Biology | isbn = 978-94-007-0264-6 | vauthors = Flores EN, García-Añoveros J | chapter = Chapter 12: TRPML2 }}</ref><ref name = "Noben-Trauth_2011" >{{cite book | editor = Islam MS | title = Transient Receptor Potential Channels |date=January 2011 | volume = 704 | publisher = Springer |  location = Berlin | pages = 700  | series = Advances in Experimental Medicine and Biology | isbn = 978-94-007-0264-6 | author = Noben-Trauth K | chapter = Chapter 13: TRPML3 }}</ref>

Deficiencies can lead to enlarged vesicles.<ref>{{cite journal |vauthors=Qian F, Noben-Trauth K |title=Cellular and molecular function of mucolipins (TRPML) and polycystin 2 (TRPP2) |journal=Pflügers Arch. |volume=451 |issue=1 |pages=277–85 |year=2005 |pmid=15971078 |doi=10.1007/s00424-005-1469-4|s2cid=23165191 }}</ref>

==Genes==
* {{Gene|MCOLN1}} ([[Mucolipin-1|TRPML1]])
* {{Gene|MCOLN2}} ([[MCOLN2|TRPML2]])
* {{Gene|MCOLN3}} ([[MCOLN3|TRPML3]])

== References ==
{{Reflist}}

==External links==
*{{cite web | url = http://www.iuphar-db.org/IC/FamilyMenuForward?familyId=12 | title = Transient Receptor Potential Channels | work = IUPHAR Database of Receptors and Ion Channels | publisher = International Union of Basic and Clinical Pharmacology | access-date = 2008-12-17 | archive-date = 2021-10-25 | archive-url = https://web.archive.org/web/20211025112234/https://www.iuphar-db.org/IC/FamilyMenuForward?familyId=12 | url-status = dead }}
* {{cite web | url = http://www.trpchannel.org | title = TRIP Database | work = a manually curated database of protein-protein interactions for mammalian TRP channels}}

{{Ion channels|g4}}
{{Transient receptor potential channel modulators}}

[[Category:Membrane proteins]]
[[Category:Ion channels]]