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8Y8P

Cryo-EM structure of AQP3 Y212F in POPC nanodisc

Functional Information from GO Data
ChainGOidnamespacecontents
A0002684biological_processpositive regulation of immune system process
A0002931biological_processresponse to ischemia
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0005911cellular_componentcell-cell junction
A0006833biological_processwater transport
A0015166molecular_functionpolyol transmembrane transporter activity
A0015204molecular_functionurea transmembrane transporter activity
A0015250molecular_functionwater channel activity
A0015254molecular_functionglycerol channel activity
A0015267molecular_functionchannel activity
A0015791biological_processpolyol transmembrane transport
A0015793biological_processglycerol transmembrane transport
A0015840biological_processurea transport
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0022857molecular_functiontransmembrane transporter activity
A0032526biological_processresponse to retinoic acid
A0042476biological_processodontogenesis
A0042802molecular_functionidentical protein binding
A0055085biological_processtransmembrane transport
A0070295biological_processrenal water absorption
A0071456biological_processcellular response to hypoxia
A0071918biological_processurea transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00221
Number of Residues9
DetailsMIP MIP family signature. HLNPAVTFA
ChainResidueDetails
AHIS81-ALA89

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"UniProtKB","id":"O14520","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues70
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"UniProtKB","id":"O14520","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"UniProtKB","id":"O14520","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues21
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"UniProtKB","id":"O14520","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues26
DetailsIntramembrane: {"description":"Discontinuously helical","evidences":[{"source":"UniProtKB","id":"O14520","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"UniProtKB","id":"O14520","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"UniProtKB","id":"O14520","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"UniProtKB","id":"O14520","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"UniProtKB","id":"O14520","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsMotif: {"description":"NPA 1","evidences":[{"source":"UniProtKB","id":"O14520","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsMotif: {"description":"NPA 2","evidences":[{"source":"UniProtKB","id":"O14520","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues3
DetailsSite: {"description":"Selectivity filter","evidences":[{"source":"UniProtKB","id":"O14520","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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