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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1J4N

Crystal Structure of the AQP1 water channel

Functional Information from GO Data
ChainGOidnamespacecontents
A0003097biological_processrenal water transport
A0005223molecular_functionintracellularly cGMP-activated cation channel activity
A0005267molecular_functionpotassium channel activity
A0005372molecular_functionwater transmembrane transporter activity
A0005634cellular_componentnucleus
A0005886cellular_componentplasma membrane
A0005903cellular_componentbrush border
A0006833biological_processwater transport
A0006884biological_processcell volume homeostasis
A0006972biological_processhyperosmotic response
A0008519molecular_functionammonium channel activity
A0009925cellular_componentbasal plasma membrane
A0009992biological_processintracellular water homeostasis
A0015168molecular_functionglycerol transmembrane transporter activity
A0015250molecular_functionwater channel activity
A0015267molecular_functionchannel activity
A0015670biological_processcarbon dioxide transport
A0015793biological_processglycerol transmembrane transport
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0019725biological_processcellular homeostasis
A0019934biological_processcGMP-mediated signaling
A0021670biological_processlateral ventricle development
A0022857molecular_functiontransmembrane transporter activity
A0030184molecular_functionnitric oxide transmembrane transporter activity
A0030185biological_processnitric oxide transport
A0030950biological_processestablishment or maintenance of actin cytoskeleton polarity
A0031526cellular_componentbrush border membrane
A0031965cellular_componentnuclear membrane
A0032127cellular_componentdense core granule membrane
A0034644biological_processcellular response to UV
A0035377biological_processtransepithelial water transport
A0035378biological_processcarbon dioxide transmembrane transport
A0035379molecular_functioncarbon dioxide transmembrane transporter activity
A0042383cellular_componentsarcolemma
A0043066biological_processnegative regulation of apoptotic process
A0045177cellular_componentapical part of cell
A0045766biological_processpositive regulation of angiogenesis
A0046878biological_processpositive regulation of saliva secretion
A0048146biological_processpositive regulation of fibroblast proliferation
A0055085biological_processtransmembrane transport
A0070301biological_processcellular response to hydrogen peroxide
A0071260biological_processcellular response to mechanical stimulus
A0071280biological_processcellular response to copper ion
A0071288biological_processcellular response to mercury ion
A0071300biological_processcellular response to retinoic acid
A0071320biological_processcellular response to cAMP
A0071456biological_processcellular response to hypoxia
A0071472biological_processcellular response to salt stress
A0071474biological_processcellular hyperosmotic response
A0071549biological_processcellular response to dexamethasone stimulus
A0071805biological_processpotassium ion transmembrane transport
A0072488biological_processammonium transmembrane transport
A0098655biological_processmonoatomic cation transmembrane transport
A0170014cellular_componentankyrin-1 complex
Functional Information from PROSITE/UniProt
site_idPS00221
Number of Residues9
DetailsMIP MIP family signature. HLNPAVTLG
ChainResidueDetails
AHIS76-GLY84
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=Helix 1","evidences":[{"source":"UniProtKB","id":"P29972","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues51
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=Helix 2","evidences":[{"source":"UniProtKB","id":"P29972","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues25
DetailsIntramembrane: {"evidences":[{"source":"UniProtKB","id":"P29972","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=Helix 3","evidences":[{"source":"UniProtKB","id":"P29972","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=Helix 4","evidences":[{"source":"UniProtKB","id":"P29972","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=Helix 5","evidences":[{"source":"UniProtKB","id":"P29972","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=Helix 6","evidences":[{"source":"UniProtKB","id":"P29972","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsMotif: {"description":"NPA 1","evidences":[{"source":"UniProtKB","id":"P29972","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsMotif: {"description":"NPA 2","evidences":[{"source":"UniProtKB","id":"P29972","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q02013","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2025-07-16

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