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9PFB

Human OCTN2 bound to ipratropium in an inward-facing conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006814biological_processsodium ion transport
A0009609biological_processresponse to symbiotic bacterium
A0009925cellular_componentbasal plasma membrane
A0015199molecular_functionamino-acid betaine transmembrane transporter activity
A0015226molecular_functioncarnitine transmembrane transporter activity
A0015293molecular_functionsymporter activity
A0015651molecular_functionquaternary ammonium group transmembrane transporter activity
A0015695biological_processorganic cation transport
A0015697biological_processquaternary ammonium group transport
A0015837biological_processamine transport
A0015879biological_processcarnitine transport
A0016324cellular_componentapical plasma membrane
A0022857molecular_functiontransmembrane transporter activity
A0030165molecular_functionPDZ domain binding
A0031526cellular_componentbrush border membrane
A0034341biological_processresponse to type II interferon
A0034612biological_processresponse to tumor necrosis factor
A0042908biological_processxenobiotic transport
A0042910molecular_functionxenobiotic transmembrane transporter activity
A0060731biological_processpositive regulation of intestinal epithelial structure maintenance
A0070062cellular_componentextracellular exosome
A0070715biological_processsodium-dependent organic cation transport
A0150104biological_processtransport across blood-brain barrier
A1900749biological_process(R)-carnitine transport
A1901235molecular_function(R)-carnitine transmembrane transporter activity
A1902270biological_process(R)-carnitine transmembrane transport
A1902603biological_processcarnitine transmembrane transport
A1990961biological_processxenobiotic detoxification by transmembrane export across the plasma membrane
Functional Information from PROSITE/UniProt
site_idPS00216
Number of Residues17
DetailsSUGAR_TRANSPORT_1 Sugar transport proteins signature 1. SGQLSDRFGRKnvlfv.T
ChainResidueDetails
ASER160-THR176

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues123
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues122
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=11","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=12","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17509700","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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