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8GCL

Cryo-EM structure of hAQP2 in DDM

Functional Information from GO Data
ChainGOidnamespacecontents
A0003091biological_processrenal water homeostasis
A0005372molecular_functionwater transmembrane transporter activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0006833biological_processwater transport
A0007015biological_processactin filament organization
A0015168molecular_functionglycerol transmembrane transporter activity
A0015250molecular_functionwater channel activity
A0015267molecular_functionchannel activity
A0015793biological_processglycerol transmembrane transport
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0030658cellular_componenttransport vesicle membrane
A0030659cellular_componentcytoplasmic vesicle membrane
A0031410cellular_componentcytoplasmic vesicle
A0048471cellular_componentperinuclear region of cytoplasm
A0051289biological_processprotein homotetramerization
A0055037cellular_componentrecycling endosome
A0055085biological_processtransmembrane transport
A0070062cellular_componentextracellular exosome
A0071280biological_processcellular response to copper ion
A0071288biological_processcellular response to mercury ion
A0072205biological_processmetanephric collecting duct development
A0098576cellular_componentlumenal side of membrane
Functional Information from PROSITE/UniProt
site_idPS00221
Number of Residues9
DetailsMIP MIP family signature. HINPAVTVA
ChainResidueDetails
AHIS66-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
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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