Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

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 Residues72
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMET1-TRP11
ASER68-GLY70
ALEU85-SER92
ALEU156-ASP165
ALEU227-LYS271

site_idSWS_FT_FI2
Number of Residues17
DetailsTRANSMEM: Helical; Name=Helix 1 => ECO:0000250|UniProtKB:P29972
ChainResidueDetails
AARG12-ILE29

site_idSWS_FT_FI3
Number of Residues51
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AGLY30-VAL48
AALA112-VAL135
ALEU184-TYR188
ASER202-PHE208

site_idSWS_FT_FI4
Number of Residues18
DetailsTRANSMEM: Helical; Name=Helix 2 => ECO:0000250|UniProtKB:P29972
ChainResidueDetails
AGLN49-GLN67

site_idSWS_FT_FI5
Number of Residues25
DetailsINTRAMEM: INTRAMEM => ECO:0000250|UniProtKB:P29972
ChainResidueDetails
AHIS71-GLY84
ATHR189-SER201

site_idSWS_FT_FI6
Number of Residues18
DetailsTRANSMEM: Helical; Name=Helix 3 => ECO:0000250|UniProtKB:P29972
ChainResidueDetails
AVAL93-THR111

site_idSWS_FT_FI7
Number of Residues19
DetailsTRANSMEM: Helical; Name=Helix 4 => ECO:0000250|UniProtKB:P29972
ChainResidueDetails
AASN136-VAL155

site_idSWS_FT_FI8
Number of Residues17
DetailsTRANSMEM: Helical; Name=Helix 5 => ECO:0000250|UniProtKB:P29972
ChainResidueDetails
ALEU166-LEU183

site_idSWS_FT_FI9
Number of Residues17
DetailsTRANSMEM: Helical; Name=Helix 6 => ECO:0000250|UniProtKB:P29972
ChainResidueDetails
AGLN209-VAL226

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q02013
ChainResidueDetails
ASER249
ASER264

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q02013
ChainResidueDetails
ATYR255

site_idSWS_FT_FI12
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN42

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon