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5UAR

Dephosphorylated, ATP-free cystic fibrosis transmembrane conductance regulator (CFTR) from zebrafish

Replaces:  5TSI
Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002679biological_processrespiratory burst involved in defense response
A0005254molecular_functionchloride channel activity
A0005260molecular_functionintracellularly ATP-gated chloride channel activity
A0005524molecular_functionATP binding
A0005768cellular_componentendosome
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006821biological_processchloride transport
A0006833biological_processwater transport
A0007507biological_processheart development
A0008354biological_processgerm cell migration
A0015106molecular_functionbicarbonate transmembrane transporter activity
A0015701biological_processbicarbonate transport
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0016853molecular_functionisomerase activity
A0016887molecular_functionATP hydrolysis activity
A0030217biological_processT cell differentiation
A0031016biological_processpancreas development
A0031901cellular_componentearly endosome membrane
A0034220biological_processmonoatomic ion transmembrane transport
A0034707cellular_componentchloride channel complex
A0035162biological_processembryonic hemopoiesis
A0035377biological_processtransepithelial water transport
A0042742biological_processdefense response to bacterium
A0045087biological_processinnate immune response
A0050891biological_processmulticellular organismal-level water homeostasis
A0055038cellular_componentrecycling endosome membrane
A0055085biological_processtransmembrane transport
A0060063biological_processSpemann organizer formation at the embryonic shield
A0070121biological_processKupffer's vesicle development
A0090022biological_processregulation of neutrophil chemotaxis
A0097535biological_processlymphoid lineage cell migration into thymus
A0098660biological_processinorganic ion transmembrane transport
A0140359molecular_functionABC-type transporter activity
A1902476biological_processchloride transmembrane transport
A1904322biological_processcellular response to forskolin
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue D10 A 1502
ChainResidue
AARG1038

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKARVALARAV
ChainResidueDetails
ALEU547-VAL561

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues284
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"27912062","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"27912062","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues63
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"27912062","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"27912062","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"27912062","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"27912062","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"27912062","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"27912062","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"27912062","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues21
DetailsTransmembrane: {"description":"Discontinuously helical; Name=8","evidences":[{"source":"PubMed","id":"27912062","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"27912062","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PubMed","id":"27912062","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PubMed","id":"27912062","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PubMed","id":"27912062","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues270
DetailsDomain: {"description":"ABC transmembrane type-1 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P13569","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

240291

PDB entries from 2025-08-13

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