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4OJ2

The structure of aquaporin

Functional Information from GO Data
ChainGOidnamespacecontents
X0003091biological_processrenal water homeostasis
X0005372molecular_functionwater transmembrane transporter activity
X0005515molecular_functionprotein binding
X0005737cellular_componentcytoplasm
X0005794cellular_componentGolgi apparatus
X0005886cellular_componentplasma membrane
X0006833biological_processwater transport
X0007015biological_processactin filament organization
X0015168molecular_functionglycerol transmembrane transporter activity
X0015250molecular_functionwater channel activity
X0015267molecular_functionchannel activity
X0015793biological_processglycerol transmembrane transport
X0016020cellular_componentmembrane
X0016323cellular_componentbasolateral plasma membrane
X0016324cellular_componentapical plasma membrane
X0030658cellular_componenttransport vesicle membrane
X0030659cellular_componentcytoplasmic vesicle membrane
X0031410cellular_componentcytoplasmic vesicle
X0048471cellular_componentperinuclear region of cytoplasm
X0051289biological_processprotein homotetramerization
X0055037cellular_componentrecycling endosome
X0055085biological_processtransmembrane transport
X0070062cellular_componentextracellular exosome
X0071280biological_processcellular response to copper ion
X0071288biological_processcellular response to mercury ion
X0072205biological_processmetanephric collecting duct development
X0098576cellular_componentlumenal side of membrane
Functional Information from PROSITE/UniProt
site_idPS00221
Number of Residues9
DetailsMIP MIP family signature. HINPAVTVA
ChainResidueDetails
XHIS66-ALA74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues118
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"24733887","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NEF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"24733887","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues21
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"24733887","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues21
DetailsIntramembrane: {"description":"Discontinuously helical","evidences":[{"source":"PubMed","id":"24733887","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NEF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsMotif: {"description":"NPA 1","evidences":[{"source":"PubMed","id":"24733887","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsMotif: {"description":"NPA 2","evidences":[{"source":"PubMed","id":"24733887","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"PubMed","id":"12194985","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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