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Entry version 130 (23 Feb 2022)
Sequence version 1 (30 May 2006)
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Protein

Cystic fibrosis transmembrane conductance regulator

Gene

cftr

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis (PubMed:20933420, PubMed:23487313, PubMed:25592226).

Mediates the transport of chloride ions across the cell membrane (By similarity).

Channel activity is coupled to ATP hydrolysis. The ion channel is also permeable to HCO3-; selectivity depends on the extracellular chloride concentration. Exerts its function also by modulating the activity of other ion channels and transporters. Contributes to the regulation of the pH and the ion content of the epithelial fluid layer (By similarity).

Required for normal fluid homeostasis in the gut (PubMed:20933420).

Required for normal volume expansion of Kupffer's vesicle during embryonic development and for normal establishment of left-right body patterning (PubMed:23487313, PubMed:26432887).

Required for normal resistance to infection by P.aeruginosa strain PA14 and strain SMC573 (PubMed:20732993).

By similarity1 Publication4 Publications

Miscellaneous

Mutations that lead to the production of a severely truncated protein that ends before the start of the fourth transmembrane domain disrupt normal left-right body patterning during embryogenesis and abolish lumen expansion of Kupffer's vesicle.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • ATP + H(2)O + closed Cl(-) channel = ADP + phosphate + open Cl(-) channel.UniRule annotation1 Publication EC:5.6.1.6

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.22 mM for ATP1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei402ATP 1By similarity1
Binding sitei492ATP 1By similarity1
Binding sitei1220ATP 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi457 – 464ATP 1PROSITE-ProRule annotation8
Nucleotide bindingi1245 – 1252ATP 2PROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChloride channel, Ion channel, Isomerase
Biological processIon transport, Transport
LigandATP-binding, Chloride, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
5.6.1.6, 928

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DRE-382556, ABC-family proteins mediated transport
R-DRE-5627083, RHO GTPases regulate CFTR trafficking
R-DRE-5689880, Ub-specific processing proteases
R-DRE-8856825, Cargo recognition for clathrin-mediated endocytosis
R-DRE-8856828, Clathrin-mediated endocytosis
R-DRE-9013406, RHOQ GTPase cycle
R-DRE-9646399, Aggrephagy

Protein family/group databases

Transport Classification Database

More...
TCDBi
3.A.1.202.2, the atp-binding cassette (abc) superfamily

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cystic fibrosis transmembrane conductance regulatorUniRule annotation (EC:5.6.1.6UniRule annotation1 Publication)
Alternative name(s):
ATP-binding cassette sub-family C member 7UniRule annotation
Channel conductance-controlling ATPaseUniRule annotation
cAMP-dependent chloride channelUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:cftrImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri7955 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesDanionidaeDanioninaeDanio
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000437 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 18

Organism-specific databases

Zebrafish Information Network genome database

More...
ZFINi
ZDB-GENE-050517-20, cftr

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 78Cytoplasmic1 PublicationAdd BLAST78
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei79 – 99Helical; Name=11 PublicationAdd BLAST21
Topological domaini100 – 123Extracellular1 PublicationAdd BLAST24
Transmembranei124 – 149Helical; Name=21 PublicationAdd BLAST26
Topological domaini150 – 195Cytoplasmic1 PublicationAdd BLAST46
Transmembranei196 – 216Helical; Name=31 PublicationAdd BLAST21
Topological domaini217 – 224Extracellular1 Publication8
Transmembranei225 – 245Helical; Name=41 PublicationAdd BLAST21
Topological domaini246 – 299Cytoplasmic1 PublicationAdd BLAST54
Transmembranei300 – 320Helical; Name=51 PublicationAdd BLAST21
Topological domaini321 – 340Extracellular1 PublicationAdd BLAST20
Transmembranei341 – 363Helical; Name=61 PublicationAdd BLAST23
Topological domaini364 – 856Cytoplasmic1 PublicationAdd BLAST493
Transmembranei857 – 877Helical; Name=71 PublicationAdd BLAST21
Topological domaini878 – 924Extracellular1 PublicationAdd BLAST47
Transmembranei925 – 946Discontinuously helical; Name=81 PublicationAdd BLAST22
Topological domaini947 – 996Cytoplasmic1 PublicationAdd BLAST50
Transmembranei997 – 1019Helical; Name=91 PublicationAdd BLAST23
Topological domaini1020 – 1021Extracellular1 Publication2
Transmembranei1022 – 1042Helical; Name=101 PublicationAdd BLAST21
Topological domaini1043 – 1103Cytoplasmic1 PublicationAdd BLAST61
Transmembranei1104 – 1124Helical; Name=111 PublicationAdd BLAST21
Topological domaini1125 – 1138Extracellular1 PublicationAdd BLAST14
Transmembranei1139 – 1159Helical; Name=121 PublicationAdd BLAST21
Topological domaini1160 – 1485Cytoplasmic1 PublicationAdd BLAST326

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Endosome, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Considerable lethality around 10 dpf (PubMed:25592226). No effect on initial pancreas development, but at 16 dpf mutants display loss of pancreatic acinar tissue (PubMed:25592226). At 22 dpf, most pancreatic acinar tissue has disappeared and has been replaced by fibrotic tissue that surrounds dilated, mucus-filled ducts (PubMed:25592226). Morpholino knockdown of the protein in 48 hpf embryos leads to impaired resistance to P.aeruginosa strain PA14 and strain SMC573, as shown by the increased bacterial burden, but there is no effect on resistance to E.tarda, B.cenocepacia, S.aureus MZ100, E.coli XL-10 and H.influenzae Hib EAGAN (PubMed:20732993). Morpholino knockdown of the protein causes an important reduction of the volume of Kupffer's vesicle during embryonic development (PubMed:26432887).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi205 – 206Missing in pd1048; abolishes trafficking to the cell membrane and leads to severe reduction of the size of the Kupffer's vesicle. 1 Publication2

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004396701 – 1485Cystic fibrosis transmembrane conductance regulatorAdd BLAST1485

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi897N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi903N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated; this activates the channel (PubMed:27912062). Dephosphorylation strongly decreases ATPase activity (PubMed:27912062). Phosphorylation at PKA sites activates the channel. Phosphorylation at PKC sites enhances the response to phosphorylation by PKA (By similarity).By similarity1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q1LX78

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in gut epithelium (at protein level) (PubMed:20933420). Detected in kidney, spleen, intestine and liver (PubMed:20732993). Detected in pancreatic duct epithelium at 5 dpf and throughout adult life (PubMed:25592226).2 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

First detected in developing pancreatic duct at 3 dpf (PubMed:25592226). Detected on Kupffer's vesicle during embryonic development (PubMed:23487313, PubMed:26432887). Detected on neural floorplate, brain and pronephric duct primordia in embryos at the 10 somite stage (PubMed:26432887).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSDARG00000041107, Expressed in testis and 20 other tissues

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer; does not require oligomerization for channel activity (By similarity).

Interacts with cse1l; this interaction may down-regulate cftr activity (PubMed:20933420).

By similarity1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
7955.ENSDARP00000060242

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11485
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q1LX78

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini83 – 353ABC transmembrane type-1 1PROSITE-ProRule annotationAdd BLAST271
Domaini424 – 645ABC transporter 1PROSITE-ProRule annotationAdd BLAST222
Domaini860 – 1163ABC transmembrane type-1 2PROSITE-ProRule annotationAdd BLAST304
Domaini1211 – 1444ABC transporter 2PROSITE-ProRule annotationAdd BLAST234

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni653 – 826Disordered R regionBy similarityAdd BLAST174
Regioni1452 – 1485DisorderedSequence analysisAdd BLAST34

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1483 – 1485PDZ-bindingBy similarity3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1455 – 1476Polar residuesSequence analysisAdd BLAST22

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Binds and hydrolyzes ATP via the two cytoplasmic ABC transporter nucleotide-binding domains. The two ATP-binding domains interact with each other, forming a head-to-tail dimer. Normal ATPase activity requires interaction between the two domains. The first ABC transporter nucleotide-binding domain has no ATPase activity by itself.By similarity
The disordered R region mediates channel activation when it is phosphorylated, but not in the absence of phosphorylation.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ABC transporter superfamily. ABCC family. CFTR transporter (TC 3.A.1.202) subfamily. [View classification]UniRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0054, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000158567

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000604_27_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q1LX78

Identification of Orthologs from Complete Genome Data

More...
OMAi
WRFTFYG

Database of Orthologous Groups

More...
OrthoDBi
138195at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q1LX78

TreeFam database of animal gene trees

More...
TreeFami
TF105200

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.1560.10, 2 hits
3.40.50.300, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003593, AAA+_ATPase
IPR011527, ABC1_TM_dom
IPR036640, ABC1_TM_sf
IPR003439, ABC_transporter-like_ATP-bd
IPR017871, ABC_transporter-like_CS
IPR009147, CFTR/ABCC7
IPR025837, CFTR_reg_dom
IPR027417, P-loop_NTPase

The PANTHER Classification System

More...
PANTHERi
PTHR24223:SF19, PTHR24223:SF19, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00664, ABC_membrane, 2 hits
PF00005, ABC_tran, 2 hits
PF14396, CFTR_R, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01851, CYSFIBREGLTR

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382, AAA, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 2 hits
SSF90123, SSF90123, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01271, CFTR_protein, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50929, ABC_TM1F, 2 hits
PS00211, ABC_TRANSPORTER_1, 1 hit
PS50893, ABC_TRANSPORTER_2, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q1LX78-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQRSPVEDAN CLSRYFFWWT NPIMRKGFKE KLRPSDVYQA PSQDAADILA
60 70 80 90 100
ERLEKEWDRE VASGKKKPSL LRAMARCYIK PFLLFGFLLY IGEATKTVQP
110 120 130 140 150
QLLGRIIASF DPAHEPERAN GYFLAFGLGL LFTARFLLLQ PAMFGLHHLG
160 170 180 190 200
MQIRIALFSI IYKKTLKLSS RVLDKISTGQ LVSLMSANLG KFDQSLGMAH
210 220 230 240 250
FIWISPLQCI LCTGLIWELI DVNSFCALAA ISLLGVLQAF LSHKMGPYKA
260 270 280 290 300
QKVLLTNKRL ALTSEIMENL HSVKAYGWEE IMETLIKNIR QDEVKLTRKI
310 320 330 340 350
GSLRYFYSSA YFFSAIFVIV AAVVPHALSR GINLRRIFTT LSYCMVLRMT
360 370 380 390 400
VTRQLPGSIQ MWYDTMRLIW KIEEFLSKEE YKLMEYDLSI TELELQDVTA
410 420 430 440 450
SWDEGPGELL ERIKQENKAN GHHNGDAGLF FTNLYVAPVL KDISLKLKKG
460 470 480 490 500
EMLAVTGSMG SGKSSLLMTI LGELVPSSGK IRHSGRISYS SQTAWIMPGT
510 520 530 540 550
IRDNILFGLT YDEYRYKSVV KACQLEEDLA ALPEKDKTPM AEGGLNLSGG
560 570 580 590 600
QKARVALARA VYRDADLYLL DAPFTHLDIA TEKEIFDKCL CKLMASKTRI
610 620 630 640 650
LVTNKIEHLK RADKILLLHN GESFFYGTFP ELQSERPDFS SLLLGLEAYD
660 670 680 690 700
NISAERRCSI LTETLHRVSV DESAGMQPER SAFRQVPPTK PMYIDERKAS
710 720 730 740 750
VIVNPLGVAR KASFIQVPEE EVRRTLPDRK FSLVPENELV DESFMGSDVY
760 770 780 790 800
HNHGVHMAGQ RRQSVLAFMT NAQGQGRREH LQSSFRRRLS VVPQSELASE
810 820 830 840 850
LDIYTRRLSD STYDMTGILE EENIEACLTD EIDEIEETFE TTKWNTYVRY
860 870 880 890 900
VSNNKSLLYV LIFILFIAAI EIAGSVAGIF LITDELWREE HQRSEPNMTK
910 920 930 940 950
HSNASSSGQT YAITVTPTSS YYILYIYVAT SESLLAMGFF RGLPFVHTTI
960 970 980 990 1000
TISKKLHQKM LHAVLSAPMS VLNTMKTGRI MNRFTKDMAT IDDMLPLLMF
1010 1020 1030 1040 1050
DFVQLTVVVV GCILVVSIVR PYIFLAATPL AIIFIVMRKY FLRTGQQLKQ
1060 1070 1080 1090 1100
LETEARSPIF SHLIMSLKGL WTIRAFERQA YFEALFHKTL NTHTATWFLY
1110 1120 1130 1140 1150
LSTLRWFLFR ADILFVFFFT LAAWIAVGTN QDKPGEIGII ICLAMLILGT
1160 1170 1180 1190 1200
FQWCVATSIA VDGMMRSVDR VFKFIDLPSE TPKPDKGKDS DLIIENVDAQ
1210 1220 1230 1240 1250
ADSSWPHRGQ IEVRNLTVKY TEAGHAVLKN LSFSAEGRQR VGILGRTGSG
1260 1270 1280 1290 1300
KSSLFNALLK LVYTDGEISI DGVNWNKMPL QKWRKAFGVV PQKVFIFTGP
1310 1320 1330 1340 1350
LRMNLDPYGC HSDEELWRVA EEVGLKTVIE QFPDKLDFQL EYGGYVLSNG
1360 1370 1380 1390 1400
HKQLICLARS ILSGARILLL DEPSAHLDPV TIKVLKKTLR QSFSTCTILL
1410 1420 1430 1440 1450
SEHKVEPLLE CQSFLMMDKG QVKTYDSIQK LLNETSHLKQ AISPAERLKL
1460 1470 1480
FPRRNSSMRT PQSKLSSVTQ TLQEEAEDNI QDTRL
Length:1,485
Mass (Da):168,400
Last modified:May 30, 2006 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i62601EBC307A3B8A
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0R4ID63A0A0R4ID63_DANRE
Cystic fibrosis transmembrane condu...
cftr
1,485Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti658C → S in AAI71654 (Ref. 2) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
BX470130 Genomic DNA No translation available.
BC171654 mRNA Translation: AAI71654.1

NCBI Reference Sequences

More...
RefSeqi
NP_001038348.1, NM_001044883.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSDART00000060243; ENSDARP00000060242; ENSDARG00000041107

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
559080

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dre:559080

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX470130 Genomic DNA No translation available.
BC171654 mRNA Translation: AAI71654.1
RefSeqiNP_001038348.1, NM_001044883.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5UARelectron microscopy3.73A1-1485[»]
5W81electron microscopy3.37A1-1485[»]
SMRiQ1LX78
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000060242

Protein family/group databases

TCDBi3.A.1.202.2, the atp-binding cassette (abc) superfamily

Proteomic databases

PaxDbiQ1LX78

Genome annotation databases

EnsembliENSDART00000060243; ENSDARP00000060242; ENSDARG00000041107
GeneIDi559080
KEGGidre:559080

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1080
ZFINiZDB-GENE-050517-20, cftr

Phylogenomic databases

eggNOGiKOG0054, Eukaryota
GeneTreeiENSGT00940000158567
HOGENOMiCLU_000604_27_1_1
InParanoidiQ1LX78
OMAiWRFTFYG
OrthoDBi138195at2759
PhylomeDBiQ1LX78
TreeFamiTF105200

Enzyme and pathway databases

BRENDAi5.6.1.6, 928
ReactomeiR-DRE-382556, ABC-family proteins mediated transport
R-DRE-5627083, RHO GTPases regulate CFTR trafficking
R-DRE-5689880, Ub-specific processing proteases
R-DRE-8856825, Cargo recognition for clathrin-mediated endocytosis
R-DRE-8856828, Clathrin-mediated endocytosis
R-DRE-9013406, RHOQ GTPase cycle
R-DRE-9646399, Aggrephagy

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q1LX78

Gene expression databases

BgeeiENSDARG00000041107, Expressed in testis and 20 other tissues

Family and domain databases

Gene3Di1.20.1560.10, 2 hits
3.40.50.300, 2 hits
InterProiView protein in InterPro
IPR003593, AAA+_ATPase
IPR011527, ABC1_TM_dom
IPR036640, ABC1_TM_sf
IPR003439, ABC_transporter-like_ATP-bd
IPR017871, ABC_transporter-like_CS
IPR009147, CFTR/ABCC7
IPR025837, CFTR_reg_dom
IPR027417, P-loop_NTPase
PANTHERiPTHR24223:SF19, PTHR24223:SF19, 1 hit
PfamiView protein in Pfam
PF00664, ABC_membrane, 2 hits
PF00005, ABC_tran, 2 hits
PF14396, CFTR_R, 1 hit
PRINTSiPR01851, CYSFIBREGLTR
SMARTiView protein in SMART
SM00382, AAA, 2 hits
SUPFAMiSSF52540, SSF52540, 2 hits
SSF90123, SSF90123, 2 hits
TIGRFAMsiTIGR01271, CFTR_protein, 1 hit
PROSITEiView protein in PROSITE
PS50929, ABC_TM1F, 2 hits
PS00211, ABC_TRANSPORTER_1, 1 hit
PS50893, ABC_TRANSPORTER_2, 2 hits

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCFTR_DANRE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q1LX78
Secondary accession number(s): B7ZVN9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 12, 2017
Last sequence update: May 30, 2006
Last modified: February 23, 2022
This is version 130 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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