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9B91

Cryo-EM structure of the human TRPM4 channel subunit in complex with calcium and ATP at 37 degrees Celsius

Functional Information from GO Data
ChainGOidnamespacecontents
A0002250biological_processadaptive immune response
A0002407biological_processdendritic cell chemotaxis
A0002724biological_processregulation of T cell cytokine production
A0005216molecular_functionmonoatomic ion channel activity
A0005227molecular_functioncalcium-activated cation channel activity
A0005262molecular_functioncalcium channel activity
A0005272molecular_functionsodium channel activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005516molecular_functioncalmodulin binding
A0005524molecular_functionATP binding
A0005654cellular_componentnucleoplasm
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006816biological_processcalcium ion transport
A0007204biological_processpositive regulation of cytosolic calcium ion concentration
A0008284biological_processpositive regulation of cell population proliferation
A0010460biological_processpositive regulation of heart rate
A0016020cellular_componentmembrane
A0016925biological_processprotein sumoylation
A0019722biological_processcalcium-mediated signaling
A0030001biological_processmetal ion transport
A0030502biological_processnegative regulation of bone mineralization
A0034220biological_processmonoatomic ion transmembrane transport
A0034706cellular_componentsodium channel complex
A0035774biological_processpositive regulation of insulin secretion involved in cellular response to glucose stimulus
A0043025cellular_componentneuronal cell body
A0045600biological_processpositive regulation of fat cell differentiation
A0045668biological_processnegative regulation of osteoblast differentiation
A0045907biological_processpositive regulation of vasoconstriction
A0046872molecular_functionmetal ion binding
A0051289biological_processprotein homotetramerization
A0055085biological_processtransmembrane transport
A0070588biological_processcalcium ion transmembrane transport
A0071318biological_processcellular response to ATP
A0086045biological_processmembrane depolarization during AV node cell action potential
A0086047biological_processmembrane depolarization during Purkinje myocyte cell action potential
A0086048biological_processmembrane depolarization during bundle of His cell action potential
A0086091biological_processregulation of heart rate by cardiac conduction
A0090263biological_processpositive regulation of canonical Wnt signaling pathway
A0098655biological_processmonoatomic cation transmembrane transport
A0098662biological_processinorganic cation transmembrane transport
A0098719biological_processsodium ion import across plasma membrane
A0098911biological_processregulation of ventricular cardiac muscle cell action potential
A1903949biological_processpositive regulation of atrial cardiac muscle cell action potential
A1904179biological_processpositive regulation of adipose tissue development
A1904199biological_processpositive regulation of regulation of vascular associated smooth muscle cell membrane depolarization
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1000
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:29211723, ECO:0000269|PubMed:29217581
ChainResidueDetails
AMET1-ILE782
AGLY836-SER863
ATHR911-VAL930
AALA1041-ASP1214

site_idSWS_FT_FI2
Number of Residues123
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:29211723, ECO:0000269|PubMed:29217581
ChainResidueDetails
APHE783-VAL803
ALEU815-GLY835
ATRP864-THR884
ALEU887-PHE910
APHE931-LEU951
AVAL1020-ILE1040

site_idSWS_FT_FI3
Number of Residues56
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:29211723, ECO:0000269|PubMed:29217581
ChainResidueDetails
AASP804-GLU814
APRO885-GLY886
ALEU952-LEU963
AVAL985-LEU1019

site_idSWS_FT_FI4
Number of Residues20
DetailsINTRAMEM: Pore-forming => ECO:0000269|PubMed:29211723, ECO:0000269|PubMed:29217581
ChainResidueDetails
AARG964-ASP984

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q7TN37
ChainResidueDetails
AARG171

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:38750366, ECO:0007744|PDB:9B90, ECO:0007744|PDB:9B91
ChainResidueDetails
AARG214

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:38750366, ECO:0007744|PDB:9B90
ChainResidueDetails
ALEU225

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:38750366, ECO:0007744|PDB:9B8Y, ECO:0007744|PDB:9B91
ChainResidueDetails
AASP270

site_idSWS_FT_FI9
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:38750366, ECO:0007744|PDB:9B8W, ECO:0007744|PDB:9B8Y
ChainResidueDetails
AALA392
AASP395
AGLU396

site_idSWS_FT_FI10
Number of Residues2
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:Q7TN37
ChainResidueDetails
AARG421
AGLY448

site_idSWS_FT_FI11
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:29217581, ECO:0007744|PDB:6BQV
ChainResidueDetails
AGLU828

site_idSWS_FT_FI12
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:29217581, ECO:0000269|PubMed:38750366, ECO:0007744|PDB:6BQV, ECO:0007744|PDB:9B92
ChainResidueDetails
AGLN831
AASN865

site_idSWS_FT_FI13
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:38750366, ECO:0000305|PubMed:29217581, ECO:0007744|PDB:6BQV, ECO:0007744|PDB:9B92
ChainResidueDetails
AASP868

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000305|PubMed:15590641
ChainResidueDetails
ASER1145
ASER1152

site_idSWS_FT_FI15
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:29217581
ChainResidueDetails
AASN992

227344

PDB entries from 2024-11-13

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