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9OVV

Heteromeric GluA1/A2-CNIH1 in the activated state, composite map of LBD-TMD

Functional Information from GO Data
ChainGOidnamespacecontents
E0000139cellular_componentGolgi membrane
E0005515molecular_functionprotein binding
E0005789cellular_componentendoplasmic reticulum membrane
E0006955biological_processimmune response
E0007165biological_processsignal transduction
E0012507cellular_componentER to Golgi transport vesicle membrane
E0033116cellular_componentendoplasmic reticulum-Golgi intermediate compartment membrane
E0038024molecular_functioncargo receptor activity
F0000139cellular_componentGolgi membrane
F0005515molecular_functionprotein binding
F0005789cellular_componentendoplasmic reticulum membrane
F0006955biological_processimmune response
F0007165biological_processsignal transduction
F0012507cellular_componentER to Golgi transport vesicle membrane
F0033116cellular_componentendoplasmic reticulum-Golgi intermediate compartment membrane
F0038024molecular_functioncargo receptor activity
G0000139cellular_componentGolgi membrane
G0005515molecular_functionprotein binding
G0005789cellular_componentendoplasmic reticulum membrane
G0006955biological_processimmune response
G0007165biological_processsignal transduction
G0012507cellular_componentER to Golgi transport vesicle membrane
G0033116cellular_componentendoplasmic reticulum-Golgi intermediate compartment membrane
G0038024molecular_functioncargo receptor activity
H0000139cellular_componentGolgi membrane
H0005515molecular_functionprotein binding
H0005789cellular_componentendoplasmic reticulum membrane
H0006955biological_processimmune response
H0007165biological_processsignal transduction
H0012507cellular_componentER to Golgi transport vesicle membrane
H0033116cellular_componentendoplasmic reticulum-Golgi intermediate compartment membrane
H0038024molecular_functioncargo receptor activity
Functional Information from PROSITE/UniProt
site_idPS01340
Number of Residues15
DetailsCORNICHON Cornichon family signature. IafdELktDYkNPID
ChainResidueDetails
EILE29-ASP43

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues30
DetailsIntramembrane: {"description":"Helical; Pore-forming","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsIntramembrane: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=M4","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P42262","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"7877986","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"8848293","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues8
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues80
DetailsTransmembrane: {"description":"Helical"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues30
DetailsIntramembrane: {"description":"Helical; Pore-forming"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsIntramembrane: {}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues10
DetailsTopological domain: {"description":"Cytoplasmic"}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=M4"}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11086992","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16483599","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FTJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CMO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues6
DetailsSite: {"description":"Interaction with the cone snail toxin Con-ikot-ikot","evidences":[{"source":"PubMed","id":"25103405","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues2
DetailsSite: {"description":"Crucial to convey clamshell closure to channel opening","evidences":[{"source":"PubMed","id":"25103405","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PKG","evidences":[{"source":"PubMed","id":"8848293","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues240
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues96
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues176
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

256158

PDB entries from 2026-07-08

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