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Mucolipin-3 (Transient receptor potential channel mucolipin 3) (TRPML3)

 MCLN3_MOUSE             Reviewed;         553 AA.
Q8R4F0; Q8BS73; Q8BSG1; Q8CDB2;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
25-OCT-2017, entry version 113.
RecName: Full=Mucolipin-3;
AltName: Full=Transient receptor potential channel mucolipin 3;
Short=TRPML3;
Name=Mcoln3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANTS THR-362
AND PRO-419.
STRAIN=C57BL/6J;
PubMed=12403827; DOI=10.1073/pnas.222425399;
Di Palma F., Belyantseva I.A., Kim H.J., Vogt T.F., Kachar B.,
Noben-Trauth K.;
"Mutations in Mcoln3 associated with deafness and pigmentation defects
in varitint-waddler (Va) mice.";
Proc. Natl. Acad. Sci. U.S.A. 99:14994-14999(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
Falardeau J.L., Kennedy J.C., Acierno J.S. Jr., Slaugenhaupt S.A.;
"Cloning of the mouse Mcoln3 gene.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo, Mesonephros, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
FUNCTION, MUTAGENESIS OF 458-ASP-ASP-459, AND CHARACTERIZATION OF
VARIANT PRO-419.
PubMed=17989217; DOI=10.1073/pnas.0709096104;
Xu H., Delling M., Li L., Dong X., Clapham D.E.;
"Activating mutation in a mucolipin transient receptor potential
channel leads to melanocyte loss in varitint-waddler mice.";
Proc. Natl. Acad. Sci. U.S.A. 104:18321-18326(2007).
[5]
CHARACTERIZATION OF VARIANT PRO-419.
PubMed=18048323; DOI=10.1073/pnas.0709846104;
Grimm C., Cuajungco M.P., van Aken A.F., Schnee M., Joers S.,
Kros C.J., Ricci A.J., Heller S.;
"A helix-breaking mutation in TRPML3 leads to constitutive activity
underlying deafness in the varitint-waddler mouse.";
Proc. Natl. Acad. Sci. U.S.A. 104:19583-19588(2007).
[6]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=18801844; DOI=10.1113/jphysiol.2008.156992;
van Aken A.F., Atiba-Davies M., Marcotti W., Goodyear R.J.,
Bryant J.E., Richardson G.P., Noben-Trauth K., Kros C.J.;
"TRPML3 mutations cause impaired mechano-electrical transduction and
depolarization by an inward-rectifier cation current in auditory hair
cells of varitint-waddler mice.";
J. Physiol. (Lond.) 586:5403-5418(2008).
[7]
DISRUPTION PHENOTYPE.
PubMed=21179200; DOI=10.1371/journal.pone.0014317;
Joers S., Grimm C., Becker L., Heller S.;
"Genetic inactivation of Trpml3 does not lead to hearing and
vestibular impairment in mice.";
PLoS ONE 5:E14317-E14317(2010).
[8]
FUNCTION, INTERACTION WITH GABARAPL2, AND SUBCELLULAR LOCATION.
PubMed=24269818; DOI=10.1016/j.bbrc.2013.11.044;
Choi S., Kim H.J.;
"The Ca2+ channel TRPML3 specifically interacts with the mammalian
ATG8 homologue GATE16 to regulate autophagy.";
Biochem. Biophys. Res. Commun. 443:56-61(2014).
-!- FUNCTION: Nonselective cation channel probably playing a role in
the regulation of membrane trafficking events. Acts as Ca(2+)-
permeable cation channel with inwardly rectifying activity
(PubMed:17989217). Mediates release of Ca(2+) from endosomes to
the cytoplasm, contributes to endosomal acidification and is
involved in the regulation of membrane trafficking and fusion in
the endosomal pathway (By similarity). Does not seem to act as
mechanosensory transduction channel in inner ear sensory hair
cells. Proposed to play a critical role at the cochlear
stereocilia ankle-link region during hair-bundle growth
(PubMed:18801844). Involved in the regulation of autophagy.
Through association with GABARAPL2 may be involved in
autophagosome formation possibly providing Ca(2+) for the fusion
process (PubMed:24269818). Through a possible and probably tissue-
specific heteromerization with MCOLN1 may be at least in part
involved in many lysosome-dependent cellular events. Possible
heteromeric ion channel assemblies with TRPV5 show pharmacological
similarity with TRPML3 (By similarity).
{ECO:0000250|UniProtKB:Q8TDD5, ECO:0000269|PubMed:17989217,
ECO:0000269|PubMed:18801844, ECO:0000269|PubMed:24269818}.
-!- ENZYME REGULATION: Inhibited by lumenal H(+) and Na(+). The
channel pore shows dynamic behavior and undergoes spontaneous,
Ca(2+)-dependent modulation when conducting Ca(2+).
{ECO:0000250|UniProtKB:Q8TDD5}.
-!- SUBUNIT: Forms homooligomeric complexes; probably tetrameric. Can
heterooligomerize with MCOLN1; heteromeric assemblies have
different channel properties as compared to the respective
homooligomers and may be tissue-specific. May heterooligomerize
with TRPV5 to form a functional distinct ion channel (By
similarity). Interacts with GABARAPL2 (PubMed:24269818).
{ECO:0000250|UniProtKB:Q8TDD5, ECO:0000269|PubMed:24269818}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}. Early endosome membrane
{ECO:0000250|UniProtKB:Q8TDD5}; Multi-pass membrane protein. Late
endosome membrane {ECO:0000269|PubMed:17989217}; Multi-pass
membrane protein. Cytoplasmic vesicle, autophagosome membrane
{ECO:0000269|PubMed:24269818}; Multi-pass membrane protein. Cell
projection, stereocilium membrane {ECO:0000269|PubMed:18801844};
Multi-pass membrane protein. Note=Recycles between the plasma
membrane and intracellular compartments by a dynamin-dependent
endocytic pathway (By similarity). In the cochlea located at the
base of stereocilia near the position of the ankle links.
{ECO:0000250|UniProtKB:Q8TDD5, ECO:0000269|PubMed:18801844}.
-!- TISSUE SPECIFICITY: Expressed in the cochlea; particularly in the
inner and outer hair cells (at protein level).
{ECO:0000269|PubMed:12403827, ECO:0000269|PubMed:18801844}.
-!- DOMAIN: The most N-terminal extracellular/lumenal domain (referred
to as I-II linker or polycystin-mucolipin domain) contributes to a
structure with a four-fold rotational symmetry in a tetrameric
assembly; the structure contains a central highly electronegative
pore with a 14 A diameter. The pore is critical for Ca(2+) and pH
regulation. The protruding structure formed by the I-II linkers
may contain all the interaction sites with lipids and proteins in
the endolysosomal lumen. {ECO:0000250|UniProtKB:Q9GZU1}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8TDD5}.
-!- DISEASE: Note=Defects in Mcoln3 are the cause of the varitin-
waddler (Va) phenotype. Classical Va mice exhibit early-onset
hearing loss, vestibular defects, pigmentation abnormalities and
perinatal lethality. The phenotype varitin-waddler Jackcon (Va-J),
which arose in a cross segregating for Va, is similar but less
severe.
-!- DISRUPTION PHENOTYPE: No severe auditory and vestibular phenotype;
does not lead to circling behavior, balance impairment or hearing
loss. {ECO:0000269|PubMed:21179200}.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
Polycystin subfamily. MCOLN3 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC27146.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAC28123.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAC28916.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY083531; AAM08924.1; -; mRNA.
EMBL; AF475086; AAL84623.1; -; mRNA.
EMBL; AK030819; BAC27146.1; ALT_INIT; mRNA.
EMBL; AK033008; BAC28123.1; ALT_INIT; mRNA.
EMBL; AK035029; BAC28916.1; ALT_INIT; mRNA.
CCDS; CCDS17900.1; -.
RefSeq; NP_598921.1; NM_134160.1.
RefSeq; XP_006501144.1; XM_006501081.2.
RefSeq; XP_006501145.1; XM_006501082.3.
RefSeq; XP_006501146.1; XM_006501083.3.
RefSeq; XP_006501147.1; XM_006501084.3.
UniGene; Mm.114683; -.
ProteinModelPortal; Q8R4F0; -.
SMR; Q8R4F0; -.
STRING; 10090.ENSMUSP00000038801; -.
GuidetoPHARMACOLOGY; 503; -.
TCDB; 1.A.5.3.2; the polycystin cation channel (pcc) family.
iPTMnet; Q8R4F0; -.
PhosphoSitePlus; Q8R4F0; -.
MaxQB; Q8R4F0; -.
PaxDb; Q8R4F0; -.
PRIDE; Q8R4F0; -.
Ensembl; ENSMUST00000039450; ENSMUSP00000038801; ENSMUSG00000036853.
GeneID; 171166; -.
KEGG; mmu:171166; -.
UCSC; uc008rqx.1; mouse.
CTD; 55283; -.
MGI; MGI:1890500; Mcoln3.
eggNOG; KOG3733; Eukaryota.
eggNOG; ENOG410Z1HH; LUCA.
GeneTree; ENSGT00390000017126; -.
HOGENOM; HOG000232158; -.
HOVERGEN; HBG052430; -.
InParanoid; Q8R4F0; -.
KO; K04994; -.
OMA; CGWLILG; -.
OrthoDB; EOG091G026A; -.
PhylomeDB; Q8R4F0; -.
TreeFam; TF317783; -.
Reactome; R-MMU-3295583; TRP channels.
PRO; PR:Q8R4F0; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000036853; -.
CleanEx; MM_MCOLN3; -.
ExpressionAtlas; Q8R4F0; baseline and differential.
Genevisible; Q8R4F0; MM.
GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0060171; C:stereocilium membrane; IEA:UniProtKB-SubCell.
GO; GO:0042491; P:auditory receptor cell differentiation; IMP:MGI.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
GO; GO:0007626; P:locomotory behavior; IMP:MGI.
InterPro; IPR013122; PKD1_2_channel.
Pfam; PF08016; PKD_channel; 1.
1: Evidence at protein level;
Cell membrane; Cell projection; Complete proteome;
Cytoplasmic vesicle; Disease mutation; Disulfide bond; Endosome;
Glycoprotein; Ion channel; Ion transport; Membrane;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 553 Mucolipin-3.
/FTId=PRO_0000215368.
TOPO_DOM 1 62 Cytoplasmic. {ECO:0000305}.
TRANSMEM 63 83 Helical. {ECO:0000255}.
TOPO_DOM 84 283 Extracellular. {ECO:0000305}.
TRANSMEM 284 304 Helical. {ECO:0000255}.
TOPO_DOM 305 336 Cytoplasmic. {ECO:0000305}.
TRANSMEM 337 357 Helical. {ECO:0000255}.
TOPO_DOM 358 374 Extracellular. {ECO:0000305}.
TRANSMEM 375 395 Helical. {ECO:0000255}.
TOPO_DOM 396 414 Cytoplasmic. {ECO:0000305}.
TRANSMEM 415 435 Helical. {ECO:0000255}.
TOPO_DOM 436 480 Extracellular. {ECO:0000305}.
TRANSMEM 481 501 Helical. {ECO:0000255}.
TOPO_DOM 502 553 Cytoplasmic. {ECO:0000305}.
REGION 104 118 Extracellular/lumenal pore loop.
{ECO:0000250|UniProtKB:Q9GZU1}.
DISULFID 159 185 {ECO:0000250|UniProtKB:Q9GZU1}.
DISULFID 238 269 {ECO:0000250|UniProtKB:Q9GZU1}.
VARIANT 362 362 I -> T (in Va-J).
{ECO:0000269|PubMed:12403827}.
VARIANT 419 419 A -> P (in Va and Va-J; constitutive
active cation channel localized to plasma
membrane). {ECO:0000269|PubMed:12403827,
ECO:0000269|PubMed:17989217,
ECO:0000269|PubMed:18048323}.
MUTAGEN 458 459 DD->KK: Abolishes channel activity.
{ECO:0000269|PubMed:17989217}.
CONFLICT 193 193 A -> D (in Ref. 3; BAC27146).
{ECO:0000305}.
CONFLICT 467 467 M -> K (in Ref. 3; BAC27146).
{ECO:0000305}.
CONFLICT 543 543 P -> A (in Ref. 3; BAC28916).
{ECO:0000305}.
SEQUENCE 553 AA; 63748 MW; 8E257B05D96DF536 CRC64;
MANPEVLVSS CRARQDESPC TFHPSSSPSE QLLLEDQMRR KLKFFFMNPC EKFWARGRKP
WKLAIQILKI AMVTIQLVLF GLSNQMVVAF KEENTIAFKH LFLKGYMDRM DDTYAVYTQS
EVYDQIIFAV TQYLQLQNIS VGNHAYENKG TKQSAMAICQ HFYRQGTICP GNDTFDIDPE
VETECFLVEP DEASHLGTPG ENKLNLSLDF HRLLTVELQF KLKAINLQTV RHQELPDCYD
FTLTITFDNK AHSGRIKISL DNDISIKECK DWHVSGSIQK NTHYMMIFDA FVILTCLASL
VLCARSVIRG LQLQQEFVNF FLLHYKKEVS ASDQMEFING WYIMIIISDI LTIVGSVLKM
EIQAKSLTSY DVCSILLGTS TMLVWLGVIR YLGFFAKYNL LILTLQAALP NVMRFCCCAA
MIYLGYCFCG WIVLGPYHEK FRSLNRVSEC LFSLINGDDM FSTFAKMQQK SYLVWLFSRV
YLYSFISLFI YMILSLFIAL ITDTYETIKH YQQDGFPETE LRKFIAECKD LPNSGKYRLE
DDPPGSLLCC CKK


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