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6C96

Cryo-EM structure of mouse TPC1 channel in the apo state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005248molecular_functionvoltage-gated sodium channel activity
A0005262molecular_functioncalcium channel activity
A0005764cellular_componentlysosome
A0005765cellular_componentlysosomal membrane
A0005768cellular_componentendosome
A0006811biological_processmonoatomic ion transport
A0006816biological_processcalcium ion transport
A0010008cellular_componentendosome membrane
A0010508biological_processpositive regulation of autophagy
A0015280molecular_functionligand-gated sodium channel activity
A0016020cellular_componentmembrane
A0019722biological_processcalcium-mediated signaling
A0019905molecular_functionsyntaxin binding
A0022832molecular_functionvoltage-gated channel activity
A0031901cellular_componentearly endosome membrane
A0034220biological_processmonoatomic ion transmembrane transport
A0034702cellular_componentmonoatomic ion channel complex
A0035725biological_processsodium ion transmembrane transport
A0036019cellular_componentendolysosome
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0055038cellular_componentrecycling endosome membrane
A0055085biological_processtransmembrane transport
A0070588biological_processcalcium ion transmembrane transport
A0072345molecular_functionNAADP-sensitive calcium-release channel activity
A0075509biological_processendocytosis involved in viral entry into host cell
A0080025molecular_functionphosphatidylinositol-3,5-bisphosphate binding
A0097682molecular_functionintracellularly phosphatidylinositol-3,5-bisphosphate-gated monatomic cation channel activity
B0005216molecular_functionmonoatomic ion channel activity
B0005248molecular_functionvoltage-gated sodium channel activity
B0005262molecular_functioncalcium channel activity
B0005764cellular_componentlysosome
B0005765cellular_componentlysosomal membrane
B0005768cellular_componentendosome
B0006811biological_processmonoatomic ion transport
B0006816biological_processcalcium ion transport
B0010008cellular_componentendosome membrane
B0010508biological_processpositive regulation of autophagy
B0015280molecular_functionligand-gated sodium channel activity
B0016020cellular_componentmembrane
B0019722biological_processcalcium-mediated signaling
B0019905molecular_functionsyntaxin binding
B0022832molecular_functionvoltage-gated channel activity
B0031901cellular_componentearly endosome membrane
B0034220biological_processmonoatomic ion transmembrane transport
B0034702cellular_componentmonoatomic ion channel complex
B0035725biological_processsodium ion transmembrane transport
B0036019cellular_componentendolysosome
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0055038cellular_componentrecycling endosome membrane
B0055085biological_processtransmembrane transport
B0070588biological_processcalcium ion transmembrane transport
B0072345molecular_functionNAADP-sensitive calcium-release channel activity
B0075509biological_processendocytosis involved in viral entry into host cell
B0080025molecular_functionphosphatidylinositol-3,5-bisphosphate binding
B0097682molecular_functionintracellularly phosphatidylinositol-3,5-bisphosphate-gated monatomic cation channel activity
Functional Information from PROSITE/UniProt
site_idPS00307
Number of Residues7
DetailsLECTIN_LEGUME_BETA Legume lectins beta-chain signature. LAVVFDT
ChainResidueDetails
ALEU317-THR323

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=S1 of repeat I","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues202
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=S2 of repeat I","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues342
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=S3 of repeat I","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues36
DetailsTransmembrane: {"description":"Helical; Name=S4 of repeat I","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=S5 of repeat I","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues92
DetailsIntramembrane: {"description":"Helical; Pore-forming","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=S6 of repeat I","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=S1 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=S2 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues44
DetailsTransmembrane: {"description":"Helical; Name=S3 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues28
DetailsTransmembrane: {"description":"Helical; Name=S4 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=S5 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=S6 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues48
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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