Trpm3
entrez
226025
canonical
uniprot
J9SQF3
canonical
ensembl
ENSMUSG00000052387
resolver
ensp
ENSMUSP00000042184
resolver
ensp
ENSMUSP00000074328
resolver
ensp
ENSMUSP00000084857
resolver
ensp
ENSMUSP00000097160
resolver
ensp
ENSMUSP00000097162
resolver
ensp
ENSMUSP00000097164
resolver
ensp
ENSMUSP00000157503
resolver
ensp
ENSMUSP00000157511
resolver
ensp
ENSMUSP00000157607
resolver
ensp
ENSMUSP00000157646
resolver
ensp
ENSMUSP00000157673
resolver
ensp
ENSMUSP00000157909
resolver
ensp
ENSMUSP00000157917
resolver
ensp
ENSMUSP00000158045
resolver
ensp
ENSMUSP00000158135
resolver
ensp
ENSMUSP00000158494
resolver
ensp
ENSMUSP00000259822
resolver
ensp
ENSMUSP00000259836
resolver
enst
ENSMUST00000099564
resolver
enst
ENSMUST00000099566
resolver
enst
ENSMUST00000099569
resolver
enst
ENSMUST00000235522
resolver
enst
ENSMUST00000235712
resolver
enst
ENSMUST00000236372
resolver
enst
ENSMUST00000236804
resolver
enst
ENSMUST00000237223
resolver
genesymbol
Trpm3
resolver
genesymbol_syn
mKIAA1616
resolver
uniprot
A0A494B964
resolver
uniprot
A0A494B967
resolver
uniprot
A0A494BA79
resolver
uniprot
A0A494BAH7
resolver
uniprot
A0A494BAK8
resolver
uniprot
B2RUS0
resolver
uniprot
D3Z539
resolver
uniprot
E9PUC8
resolver
uniprot
F6M2J8
resolver
uniprot
F7CJ77
resolver
uniprot
J9S2Y6
resolver
uniprot
J9S2Z5
resolver
uniprot
J9S305
resolver
uniprot
J9S314
resolver
uniprot
J9SQE7
resolver
uniprot
J9SQF8
resolver
uniprot
J9SUA7
resolver
uniprot
J9SVL3
resolver
uniprot
J9T120
resolver
uniprot
J9T143
resolver
uniprot
J9T153
resolver
uniprot
J9T334
resolver
uniprot
J9T345
resolver
uniprot
Q5F4S6
resolver
uniprot
Q5F4S7
resolver
uniprot
Q5F4S8
resolver
uniprot
Q5F4S9
resolver
uniprot
Q5F4T0
resolver
uniprot
Q69ZE8
resolver
uniprot
Q8BIH6
resolver
uniprot_entry
A0A494B964_MOUSE
resolver
uniprot_entry
A0A494B967_MOUSE
resolver
uniprot_entry
A0A494BA79_MOUSE
resolver
uniprot_entry
A0A494BAH7_MOUSE
resolver
uniprot_entry
A0A494BAK8_MOUSE
resolver
uniprot_entry
D3Z539_MOUSE
resolver
uniprot_entry
E9PUC8_MOUSE
resolver
uniprot_entry
F7CJ77_MOUSE
resolver
uniprot_entry
J9S2Y6_MOUSE
resolver
uniprot_entry
J9S314_MOUSE
resolver
uniprot_entry
J9SVL3_MOUSE
resolver
uniprot_entry
J9T120_MOUSE
resolver
uniprot_entry
J9T143_MOUSE
resolver
uniprot_entry
J9T334_MOUSE
resolver
uniprot_entry
J9T345_MOUSE
resolver
uniprot_entry
Q69ZE8_MOUSE
resolver
uniprot_entry
Q8BIH6_MOUSE
resolver
uniprot_entry
TRPM3_MOUSE
resolver
uniprot_sec
B2RUS0
resolver
uniprot_sec
F6M2J8
resolver
uniprot_sec
J9S2Z5
resolver
uniprot_sec
J9S305
resolver
uniprot_sec
J9SQE7
resolver
uniprot_sec
J9SQF8
resolver
uniprot_sec
J9SUA7
resolver
uniprot_sec
J9T153
resolver
uniprot_sec
Q5F4S6
resolver
uniprot_sec
Q5F4S7
resolver
uniprot_sec
Q5F4S8
resolver
uniprot_sec
Q5F4S9
resolver
uniprot_sec
Q5F4T0
resolver
activity_regulation
ACTIVITY REGULATION: Activated by the neurosteroid pregnelonone sulfate (PregS). PregS activates the channel by shifting its current-voltage activation curve toward more negative membrane potentials and also potentiates temperature-induced activation (PubMed:18978782, PubMed:21555074, PubMed:24251620). Activated by heat (PubMed:21555074). Intracellular Ca(2+) inhibits TRPM3 probably via interaction with Ca(2+)/calmodulin (PubMed:29880196). Intracellular Mg(2+) inhibits TRPM3 activity (PubMed:15824111). Both intracellular and extracellular protons block TRPM3 through probable binding sites in the pore region (By similarity). Positively regulated by phosphoinositide phosphoinositol 4,5-biphosphate (PI(4,5)P2) (By similarity). Strongly inhibited by activation of G(i)-coupled receptors via direct binding with G-beta/gamma-subunits of heterotrimeric G proteins (PubMed:36283409). {ECO:0000250|UniProtKB:Q9HCF6, ECO:0000269|PubMed:15824111, ECO:0000269|PubMed:18978782, ECO:0000269|PubMed:21555074, ECO:0000269|PubMed:24251620, ECO:0000269|PubMed:29880196, ECO:0000269|PubMed:36283409}.; ACTIVITY REGULATION: [Isoform 8]: Insensitive to pregnenolone sulfate (PregS) or heat. {ECO:0000269|PubMed:32780479}.; ACTIVITY REGULATION: [Isoform 10]: Not inhibited by G-beta/gamma-subunits of heterotrimeric G proteins. {ECO:0000269|PubMed:33122432}.; ACTIVITY REGULATION: [Isoform 7]: Not inhibited by G-beta/gamma-subunits of heterotrimeric G proteins. {ECO:0000269|PubMed:33122432}.
uniprot
proteins
amino_acid_sequence
MPGPWGTVYFLGTAQICSFLSSRWNLEGVMNQTDASRPLNWTIRKLCHAAFLPSVRLLKAQKSWIERAFYKRECVHIIPSTKDPHRCCCGRLIGQHVGLTPSISVLQNEKNESRLSRNDIQSEKWSISKHTQLSPTDAFGTIEFQGGGHSNKAMYVRVSFDTKPDLLLHLMTKEWQLELPKLLISVHGGLQNFELQPKLKQVFGKGLIKAAMTTGAWIFTGGVNTGVIRHVGDALKDHASKSRGKICTIGIAPWGIVENQEDLIGRDVVRPYQTMSNPMSKLTVLNSMHSHFILADNGTTGKYGAEVKLRRQLEKHISLQKINTRCLPFFSLDSRLFYSFWGSCQLDPIGIGQGVPVVALIVEGGPNVISIVLEYLRDTPPVPVVVCDGSGRASDILAFGHKYSEEGGLINESLRDQLLVTIQKTFTYTRTQAQHLFIILMECMKKKELITVFRMGSEGHQDIDLAILTALLKGANASAPDQLSLALAWNRVDIARSQIFIYGQQWPVGSLEQAMLDALVLDRVDFVKLLIENGVSMHRFLTISRLEELYNTRHGPSNTLYHLVRDVKKGNLPPDYRISLIDIGLVIEYLMGGAYRCNYTRKRFRTLYHNLFGPKRPKALKLLGMEDDIPLRRGRKTTKKREEEVDIDLDDPEINHFPFPFHELMVWAVLMKRQKMALFFWQHGEEAMAKALVACKLCKAMAHEASENDMVDDISQELNHNSRDFGQLAVELLDQSYKQDEQLAMKLLTYELKNWSNATCLQLAVAAKHRDFIAHTCSQMLLTDMWMGRLRMRKNSGLKVILGILLPPSILSLEFKNKDDMPYMTQAQEIHLQEKEPEEPEKPTKEKDEEDMELTAMLGRSNGESSRKKDEEEVQSRHRLIPVGRKIYEFYNAPIVKFWFYTLAYIGYLMLFNYIVLVKMERWPSTQEWIVISYIFTLGIEKMREILMSEPGKLLQKVKVWLQEYWNVTDLIAILLFSVGMILRLQDQPFRSDGRVIYCVNIIYWYIRLLDIFGVNKYLGPYVMMIGKMMIDMMYFVIIMLVVLMSFGVARQAILFPNEEPSWKLAKNIFYMPYWMIYGEVFADQIDPPCGQNETREDGKTIQLPPCKTGAWIVPAIMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQRYQLIMTFHERPVLPPPLIIFSHMTMIFQHVCCRWRKHESDQDERDYGLKLFITDDELKKVHDFEEQCIEEYFREKDDRFNSSNDERIRVTSERVENMSMRLEEVNEREHSMKASLQTVDIRLAQLEDLIGRMATALERLTGLERAESNKIRSRTSSDCTDAAYIVRQSSFNSQEGNTFKLQESIDPAGEETISPTSPTLMPRMRSHSFYSVNVKDKGGIEKLESIFKERSLSLHRATSSHSVAKEPKAPAAPANTLAIVPDSRRPSSCIDIYVSAMDELHCDIEPLDNSMNILGLGEPSFSALAPSTTPSSSAYATLAPTDRPPSRSIDFEDLTSMDTRSFSSDYTHLPECQNPWDTDPPTYHTIERSKSSRYLATTPFLLEEAPIVKSHSFMFSPSRSYYANFGVPVKTAEYTSITDCIDTRCVNAPQAIADRATFPGGLGDKVEDLSCCHPEREAELSHPSSDSEENEARGQRAANPISSQEAENADRTLSNNITVPKIERANSYSAEEPNVPYAHTRKSFSISDKLDRQRNTASLRNPFQRSKSSKPEGRGDSLSMRRLSRTSAFHSFESKHN
uniprot
proteins
function
FUNCTION: Constitutively active, non-selective divalent cation-conducting channel that is permeable to Ca(2+), Mn(2+), and Mg(2+), with a high permeability for Ca(2+) (PubMed:15824111, PubMed:20401728, PubMed:32780479). However, can be enhanced by increasing temperature and by ligands, including the endogenous neurosteroid pregnenolone sulfate and sphingosine-1 and suppressed by intracellular Mg(2+) (PubMed:20401728, PubMed:21555074). Implicated in a variety of cellular processes, including insulin/peptide secretion, vascular constriction and dilation, noxious heat sensing, inflammatory and spontaneous pain sensitivity (PubMed:21555074, PubMed:30853321, PubMed:33478988). In neurons of the dorsal root ganglia, functions as thermosensitive channel for the detection of noxious heat and spontaneous pain (PubMed:21555074, PubMed:33478988). Suggested to function as an ionotropic steroid receptor in beta-cell, indeed pregnenolone sulfate leads to Ca(2+) influx and enhanced insulin secretion (PubMed:18978782). Mediates Zn(2+) uptake into the lumen of pancreatic beta cell secretory granules, thereby regulating insulin secretion (PubMed:20401728). Forms heteromultimeric ion channels with TRPM1 which are permeable for Ca(2+) and Zn(2+) ions (By similarity). Exists as multiple splice variants which differ significantly in their biophysical properties (PubMed:15824111, PubMed:22961981). {ECO:0000250|UniProtKB:Q9HCF6, ECO:0000269|PubMed:15824111, ECO:0000269|PubMed:18978782, ECO:0000269|PubMed:20401728, ECO:0000269|PubMed:21555074, ECO:0000269|PubMed:22961981, ECO:0000269|PubMed:30853321, ECO:0000269|PubMed:32780479, ECO:0000269|PubMed:33478988}.; FUNCTION: [Isoform 8]: Displays strongly reduced permeability for divalent cations and high selectivity toward monovalent cations. {ECO:0000269|PubMed:15824111}.; FUNCTION: [Isoform 14]: No channel activity. {ECO:0000269|PubMed:22961981}.; FUNCTION: [Isoform 15]: No channel activity. {ECO:0000269|PubMed:22961981}.
uniprot
proteins
mass_dalton
197458
uniprot
proteins
mutagenesis
MUTAGEN 198; /note="K->A,P,G: Reduces calmodulin-binding by more than 50%."; /evidence="ECO:0000269|PubMed:29880196"; MUTAGEN 200; /note="K->A,P,G: Reduces calmodulin-binding by more than 50%."; /evidence="ECO:0000269|PubMed:29880196"; MUTAGEN 205; /note="K->A,P,G: Reduces calmodulin-binding by more than 50%."; /evidence="ECO:0000269|PubMed:29880196"; MUTAGEN 209; /note="K->A,P,G: Reduces calmodulin-binding by more than 50%."; /evidence="ECO:0000269|PubMed:29880196
uniprot
proteins
protein_family
LTrpC subfamily
uniprot
proteins
protein_family
TRPM3 sub-subfamily
uniprot
proteins
protein_family
Transient receptor (TC 1.A.4) family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15824111
uniprot
proteins
pubmed
18978782
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20401728
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21555074
uniprot
proteins
pubmed
22961981
uniprot
proteins
pubmed
24251620
uniprot
proteins
pubmed
29880196
uniprot
proteins
pubmed
30853321
uniprot
proteins
pubmed
32780479
uniprot
proteins
pubmed
33122432
uniprot
proteins
pubmed
33478988
uniprot
proteins
pubmed
36283409
uniprot
proteins
sequence_length
1732
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9HCF6}; Multi-pass membrane protein {ECO:0000269|PubMed:36283409}.
uniprot
proteins
transmembrane_region
TRANSMEM 895..918; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:36283409"; TRANSMEM 926..948; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:36283409"; TRANSMEM 965..985; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:36283409"; TRANSMEM 990..1013; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:36283409"; TRANSMEM 1029..1056; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:36283409"; TRANSMEM 1112..1137; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:36283409
uniprot
proteins