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8S3E

Structure of rabbit Slo1 in complex with gamma1/LRRC26

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005249molecular_functionvoltage-gated potassium channel activity
A0005267molecular_functionpotassium channel activity
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006813biological_processpotassium ion transport
A0015269molecular_functioncalcium-activated potassium channel activity
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
A0034702cellular_componentmonoatomic ion channel complex
A0045211cellular_componentpostsynaptic membrane
A0046872molecular_functionmetal ion binding
A0055085biological_processtransmembrane transport
A0060072molecular_functionlarge conductance calcium-activated potassium channel activity
A0071805biological_processpotassium ion transmembrane transport
B0005216molecular_functionmonoatomic ion channel activity
B0005249molecular_functionvoltage-gated potassium channel activity
B0005267molecular_functionpotassium channel activity
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006813biological_processpotassium ion transport
B0015269molecular_functioncalcium-activated potassium channel activity
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
B0034702cellular_componentmonoatomic ion channel complex
B0045211cellular_componentpostsynaptic membrane
B0046872molecular_functionmetal ion binding
B0055085biological_processtransmembrane transport
B0060072molecular_functionlarge conductance calcium-activated potassium channel activity
B0071805biological_processpotassium ion transmembrane transport
C0005216molecular_functionmonoatomic ion channel activity
C0005249molecular_functionvoltage-gated potassium channel activity
C0005267molecular_functionpotassium channel activity
C0005783cellular_componentendoplasmic reticulum
C0005789cellular_componentendoplasmic reticulum membrane
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0006813biological_processpotassium ion transport
C0015269molecular_functioncalcium-activated potassium channel activity
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
C0034702cellular_componentmonoatomic ion channel complex
C0045211cellular_componentpostsynaptic membrane
C0046872molecular_functionmetal ion binding
C0055085biological_processtransmembrane transport
C0060072molecular_functionlarge conductance calcium-activated potassium channel activity
C0071805biological_processpotassium ion transmembrane transport
D0005216molecular_functionmonoatomic ion channel activity
D0005249molecular_functionvoltage-gated potassium channel activity
D0005267molecular_functionpotassium channel activity
D0005783cellular_componentendoplasmic reticulum
D0005789cellular_componentendoplasmic reticulum membrane
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0006813biological_processpotassium ion transport
D0015269molecular_functioncalcium-activated potassium channel activity
D0016020cellular_componentmembrane
D0034220biological_processmonoatomic ion transmembrane transport
D0034702cellular_componentmonoatomic ion channel complex
D0045211cellular_componentpostsynaptic membrane
D0046872molecular_functionmetal ion binding
D0055085biological_processtransmembrane transport
D0060072molecular_functionlarge conductance calcium-activated potassium channel activity
D0071805biological_processpotassium ion transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00092
Number of Residues7
DetailsN6_MTASE N-6 Adenine-specific DNA methylases signature. VITNPPY
ChainResidueDetails
AVAL1033-TYR1039

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=Segment S0","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=Segment S1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues152
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=Segment S2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues68
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=Segment S3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Voltage-sensor; Name=Segment S4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=Segment S5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues88
DetailsIntramembrane: {"description":"Pore-forming; Name=P region","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=Segment S6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues568
DetailsDomain: {"description":"RCK N-terminal 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00543","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues80
DetailsRegion: {"description":"Segment S7"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues80
DetailsRegion: {"description":"Segment S8"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues16
DetailsRegion: {"description":"Heme-binding motif","evidences":[{"source":"UniProtKB","id":"Q12791","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues80
DetailsRegion: {"description":"Segment S9"}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues80
DetailsRegion: {"description":"Segment S10"}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues12
DetailsMotif: {"description":"Selectivity for potassium"}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues88
DetailsMotif: {"description":"Calcium bowl","evidences":[{"source":"UniProtKB","id":"B7ZC96","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues12
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"B7ZC96","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues8
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"Q12791","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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