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{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
{{Infobox_gene}}


'''Mucolipin-1''' also known as '''TRPML1''' (transient receptor potential cation channel, mucolipin subfamily, member 1) is a [[protein]] that in humans is encoded by the ''MCOLN1'' [[gene]].<ref name="pmid16382100">{{cite journal |vauthors=Clapham DE, Julius D, Montell C, Schultz G | title = International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels | journal = Pharmacol. Rev. | volume = 57 | issue = 4 | pages = 427–50 |date=December 2005 | pmid = 16382100 | doi = 10.1124/pr.57.4.6 | s2cid = 17936350 }}</ref> It is a member of the small family of the [[TRPML]] channels, a subgroup of the large protein family of [[Transient receptor potential channel|TRP]] ion channels.
'''Mucolipin-1''' '''(ML1) '''also known as '''TRPML1''' (transient receptor potential cation channel, mucolipin subfamily, member 1) is a [[protein]] that in humans is encoded by the ''MCOLN1'' [[gene]].<ref name="pmid16382100">{{cite journal |vauthors=Clapham DE, Julius D, Montell C, Schultz G | title = International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels | journal = Pharmacol. Rev. | volume = 57 | issue = 4 | pages = 427–50 |date=December 2005 | pmid = 16382100 | doi = 10.1124/pr.57.4.6 | s2cid = 17936350 }}</ref> It is a member of the small family of the [[TRPML]] channels, a subgroup of the large protein family of [[Transient receptor potential channel|TRP]] ion channels.


TRPML1 is a 65 kDa protein associated with [[mucolipidosis type IV]]. Its predicted structure includes six transmembrane domains, a transient receptor potential (TRP) cation-channel domain, and an internal channel pore.<ref name="pmid17924347">{{cite journal |vauthors=Venugopal B, Browning MF, Curcio-Morelli C, Varro A, Michaud N, Nanthakumar N, Walkley SU, Pickel J, Slaugenhaupt SA | title = Neurologic, gastric, and {{sic|nolink=y|opthalmologic}} pathologies in a murine model of mucolipidosis type IV | journal = Am. J. Hum. Genet. | volume = 81 | issue = 5 | pages = 1070–83 |date=November 2007 | pmid = 17924347 | pmc = 2265643 | doi = 10.1086/521954 }}</ref> TRPML1 is believed to channel iron ions across the [[endosome]]/[[lysosome]] membrane into the cell and so its malfunction causes cellular iron deficiency.<ref>{{cite journal |vauthors= Dong X, Cheng X, Mills E, Delling M, Wang F, Kurz T, Xu H |title=The Type IV Mucolipidosis-Associated Protein TRPML1 is an Endo-lysosomal Iron Release Channel |journal=Nature |year=2008 |doi=10.1038/nature07311 |volume= 455 |pages= 992–6 |pmid= 18794901 |issue= 7215|pmc=4301259 }}</ref> It is important in lysosome function and plays a part in processes such as [[vesicular trafficking]], [[exocytosis]] and [[autophagy]].<ref name="pmid24756723">{{cite journal | vauthors = Wang W, Zhang X, Gao Q, Xu H | title = TRPML1: an ion channel in the lysosome | journal = Handbook of Experimental Pharmacology | volume = 222 | pages = 631–45 | date = 2014 | pmid = 24756723 | doi = 10.1007/978-3-642-54215-2_24 }}</ref><ref name="pmid28689729">{{cite journal | vauthors = Di Paola S, Scotto-Rosato A, Medina DL | title = TRPML1: The Ca(2+)retaker of the lysosome | journal = Cell Calcium | volume = 69 | pages = 112–121 | date = January 2018 | pmid = 28689729 | doi = 10.1016/j.ceca.2017.06.006 }}</ref>
TRPML1 is a 65 kDa protein associated with [[mucolipidosis type IV]]. Its predicted structure includes six transmembrane domains, a transient receptor potential (TRP) cation-channel domain, and an internal channel pore.<ref name="pmid17924347">{{cite journal |vauthors=Venugopal B, Browning MF, Curcio-Morelli C, Varro A, Michaud N, Nanthakumar N, Walkley SU, Pickel J, Slaugenhaupt SA | title = Neurologic, gastric, and {{sic|nolink=y|opthalmologic}} pathologies in a murine model of mucolipidosis type IV | journal = Am. J. Hum. Genet. | volume = 81 | issue = 5 | pages = 1070–83 |date=November 2007 | pmid = 17924347 | pmc = 2265643 | doi = 10.1086/521954 }}</ref> TRPML1 is believed to channel iron ions across the [[endosome]]/[[lysosome]] membrane into the cell and so its malfunction causes cellular iron deficiency.<ref>{{cite journal |vauthors= Dong X, Cheng X, Mills E, Delling M, Wang F, Kurz T, Xu H |title=The Type IV Mucolipidosis-Associated Protein TRPML1 is an Endo-lysosomal Iron Release Channel |journal=Nature |year=2008 |doi=10.1038/nature07311 |volume= 455 |pages= 992–6 |pmid= 18794901 |issue= 7215|pmc=4301259 |bibcode=2008Natur.455..992D }}</ref> It is important in lysosome function and plays a part in processes such as [[vesicular trafficking]], [[exocytosis]] and [[autophagy]].<ref name="pmid24756723">{{cite book | vauthors = Wang W, Zhang X, Gao Q, Xu H | title = Mammalian Transient Receptor Potential (TRP) Cation Channels | chapter = TRPML1: an ion channel in the lysosome | series = Handbook of Experimental Pharmacology | volume = 222 | pages = 631–45 | date = 2014 | pmid = 24756723 | doi = 10.1007/978-3-642-54215-2_24 | isbn = 978-3-642-54214-5 }}</ref><ref name="pmid28689729">{{cite journal | vauthors = Di Paola S, Scotto-Rosato A, Medina DL | title = TRPML1: The Ca(2+)retaker of the lysosome | journal = Cell Calcium | volume = 69 | pages = 112–121 | date = January 2018 | pmid = 28689729 | doi = 10.1016/j.ceca.2017.06.006 }}</ref>


==Ligands==
==Ligands==
;Agonists
;Agonists
* [[ML-SA1]]
* [[ML-SA1]]
* [[MK6-83]]<ref name="pmid29019983">{{cite journal | vauthors = Schmiege P, Fine M, Blobel G, Li X | title = Human TRPML1 channel structures in open and closed conformations | journal = Nature | volume = 550 | issue = 7676 | pages = 366–370 | date = October 2017 | pmid = 29019983 | pmc = 5920536 | doi = 10.1038/nature24036 }}</ref>
* [[MK6-83]]<ref name="pmid29019983">{{cite journal | vauthors = Schmiege P, Fine M, Blobel G, Li X | title = Human TRPML1 channel structures in open and closed conformations | journal = Nature | volume = 550 | issue = 7676 | pages = 366–370 | date = October 2017 | pmid = 29019983 | pmc = 5920536 | doi = 10.1038/nature24036 | bibcode = 2017Natur.550..366S }}</ref>


==See also==
==See also==
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{{Ion channels|g4}}
{{Ion channels|g4}}
{{Transient receptor potential channel modulators}}
{{Transient receptor potential channel modulators}}


{{biochem-stub}}

Latest revision as of 17:09, 3 October 2024

MCOLN1
Identifiers
AliasesMCOLN1, MG-2, ML4, MLIV, MST080, MSTP080, TRP-ML1, TRPM-L1, TRPML1, mucolipin 1, ML1, mucolipin TRP cation channel 1
External IDsOMIM: 605248; MGI: 1890498; HomoloGene: 10744; GeneCards: MCOLN1; OMA:MCOLN1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

57192

94178

Ensembl

ENSG00000090674

ENSMUSG00000004567

UniProt

Q9GZU1

Q99J21

RefSeq (mRNA)

NM_020533

NM_053177

RefSeq (protein)

NP_065394

NP_444407

Location (UCSC)Chr 19: 7.52 – 7.53 MbChr 8: 3.55 – 3.57 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Mucolipin-1 (ML1) also known as TRPML1 (transient receptor potential cation channel, mucolipin subfamily, member 1) is a protein that in humans is encoded by the MCOLN1 gene.[5] It is a member of the small family of the TRPML channels, a subgroup of the large protein family of TRP ion channels.

TRPML1 is a 65 kDa protein associated with mucolipidosis type IV. Its predicted structure includes six transmembrane domains, a transient receptor potential (TRP) cation-channel domain, and an internal channel pore.[6] TRPML1 is believed to channel iron ions across the endosome/lysosome membrane into the cell and so its malfunction causes cellular iron deficiency.[7] It is important in lysosome function and plays a part in processes such as vesicular trafficking, exocytosis and autophagy.[8][9]

Ligands

[edit]
Agonists

See also

[edit]
  • transient receptor potential cation channel, mucolipin subfamily, member 2 (MCOLN2)
  • transient receptor potential cation channel, mucolipin subfamily, member 3 (MCOLN3)
  • mucolipidosis type IV
  • TRPML

References

[edit]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000090674 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000004567 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Clapham DE, Julius D, Montell C, Schultz G (December 2005). "International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels". Pharmacol. Rev. 57 (4): 427–50. doi:10.1124/pr.57.4.6. PMID 16382100. S2CID 17936350.
  6. ^ Venugopal B, Browning MF, Curcio-Morelli C, Varro A, Michaud N, Nanthakumar N, Walkley SU, Pickel J, Slaugenhaupt SA (November 2007). "Neurologic, gastric, and opthalmologic [sic] pathologies in a murine model of mucolipidosis type IV". Am. J. Hum. Genet. 81 (5): 1070–83. doi:10.1086/521954. PMC 2265643. PMID 17924347.
  7. ^ Dong X, Cheng X, Mills E, Delling M, Wang F, Kurz T, Xu H (2008). "The Type IV Mucolipidosis-Associated Protein TRPML1 is an Endo-lysosomal Iron Release Channel". Nature. 455 (7215): 992–6. Bibcode:2008Natur.455..992D. doi:10.1038/nature07311. PMC 4301259. PMID 18794901.
  8. ^ Wang W, Zhang X, Gao Q, Xu H (2014). "TRPML1: an ion channel in the lysosome". Mammalian Transient Receptor Potential (TRP) Cation Channels. Handbook of Experimental Pharmacology. Vol. 222. pp. 631–45. doi:10.1007/978-3-642-54215-2_24. ISBN 978-3-642-54214-5. PMID 24756723.
  9. ^ Di Paola S, Scotto-Rosato A, Medina DL (January 2018). "TRPML1: The Ca(2+)retaker of the lysosome". Cell Calcium. 69: 112–121. doi:10.1016/j.ceca.2017.06.006. PMID 28689729.
  10. ^ Schmiege P, Fine M, Blobel G, Li X (October 2017). "Human TRPML1 channel structures in open and closed conformations". Nature. 550 (7676): 366–370. Bibcode:2017Natur.550..366S. doi:10.1038/nature24036. PMC 5920536. PMID 29019983.
[edit]
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