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UniProtKB - P26361 (CFTR_MOUSE)

Entry version 188 (16 Jan 2019)
Sequence version 2 (31 Jan 2002)
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Protein

Cystic fibrosis transmembrane conductance regulator

Gene

Cftr

Organism
Mus musculus (Mouse)
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:26823428). Mediates the transport of chloride ions across the cell membrane (PubMed:20231442, PubMed:22265409). 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. Modulates the activity of the epithelial sodium channel (ENaC) complex, in part by regulating the cell surface expression of the ENaC complex. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the transporter SLC4A7. Can inhibit the chloride channel activity of ANO1 (By similarity). Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation (PubMed:21976599).By similarity5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei401ATP 1By similarity1
Binding sitei493ATP 1Combined sources1
Binding sitei1215ATP 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi458 – 465ATP 1PROSITE-ProRule annotationCombined sources8
Nucleotide bindingi1240 – 1247ATP 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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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, Hydrolase, Ion channel
Biological processIon transport, Transport
LigandATP-binding, Chloride, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.6.3.49 3474

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-382556 ABC-family proteins mediated transport
R-MMU-5627083 RHO GTPases regulate CFTR trafficking
R-MMU-5689880 Ub-specific processing proteases
R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis
R-MMU-8856828 Clathrin-mediated endocytosis

<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_and_taxonomy_section">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 regulator
Short name:
CFTR
Alternative name(s):
ATP-binding cassette sub-family C member 7
Channel conductance-controlling ATPase (EC:3.6.3.49By similarity)
cAMP-dependent chloride channel
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Cftr
Synonyms:Abcc7
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 6

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:88388 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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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 – 77CytoplasmicBy similarityAdd BLAST77
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei78 – 98Helical; Name=1By similarityAdd BLAST21
Topological domaini99 – 122ExtracellularBy similarityAdd BLAST24
Transmembranei123 – 146Helical; Name=2By similarityAdd BLAST24
Topological domaini147 – 195CytoplasmicBy similarityAdd BLAST49
Transmembranei196 – 216Helical; Name=3By similarityAdd BLAST21
Topological domaini217 – 222ExtracellularBy similarity6
Transmembranei223 – 243Helical; Name=4By similarityAdd BLAST21
Topological domaini244 – 298CytoplasmicBy similarityAdd BLAST55
Transmembranei299 – 319Helical; Name=5By similarityAdd BLAST21
Topological domaini320 – 339ExtracellularBy similarityAdd BLAST20
Transmembranei340 – 358Helical; Name=6By similarityAdd BLAST19
Topological domaini359 – 853CytoplasmicBy similarityAdd BLAST495
Transmembranei854 – 874Helical; Name=7By similarityAdd BLAST21
Topological domaini875 – 913ExtracellularBy similarityAdd BLAST39
Transmembranei914 – 934Discontinuously helical; Name=8By similarityAdd BLAST21
Topological domaini935 – 985CytoplasmicBy similarityAdd BLAST51
Transmembranei986 – 1006Helical; Name=9By similarityAdd BLAST21
Topological domaini1007 – 1008ExtracellularBy similarity2
Transmembranei1009 – 1029Helical; Name=10By similarityAdd BLAST21
Topological domaini1030 – 1090CytoplasmicBy similarityAdd BLAST61
Transmembranei1091 – 1111Helical; Name=11By similarityAdd BLAST21
Topological domaini1112 – 1125ExtracellularBy similarityAdd BLAST14
Transmembranei1126 – 1146Helical; Name=12By similarityAdd BLAST21
Topological domaini1147 – 1476CytoplasmicBy similarityAdd BLAST330

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Endosome, Membrane, Nucleus

<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

Mice are born at the expected Mendelian rate, but about 80% die within two to five days after birth due to peritonitis (PubMed:7685652). Those that survive fail to thrive, appear runted and weigh about half as much as wild-type littermates (PubMed:7685652). Many of the surviving pups die when they start ingesting solid food, due to intestinal blockage caused by excessive mucus accumulation (PubMed:7685652). None survive for more than about 45 days after birth (PubMed:7685652). Intestinal crypts in the jejunum and ileum are filled with excessive mucus (PubMed:7685652). Excessive accumulation of mucus is also seen in colon (PubMed:7685652). In contrast, their lungs do not present pathological mucus accumulation (PubMed:7685652). Likewise, only five out of ten animals show dilatation and blockage of several small pancreatic ducts (PubMed:7685652). Besides, mutant mice present defects in their lacrimal glands that make them more susceptible to develop eye infections (PubMed:7685652). In caecum epithelium, forskolin-sensitive ion transport is nearly abolished (PubMed:7685652).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi508F → A, L or Q: Mildly impairs protein maturation. 1 Publication1
Mutagenesisi508F → C or M: No effect on protein maturation. 1 Publication1
Mutagenesisi508F → E, D, G, H, I, K, P, R or Y: Abolishes normal maturation. 1 Publication1
Mutagenesisi508F → N, S or V: Nearly abolishes normal maturation. 1 Publication1
Mutagenesisi508Missing : Impairs protein folding, due to small local changes that probably disrupt crucial interactions with the transmembrane domain. Abolishes normal maturation. Impairs trafficking to the apical cell membrane. 3 Publications1

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000934241 – 1476Cystic fibrosis transmembrane conductance regulatorAdd BLAST1476

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi524S-palmitoyl cysteineBy similarity1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei549PhosphoserineBy similarity1
Modified residuei660PhosphoserineBy similarity1
Modified residuei670Phosphoserine; by PKABy similarity1
Modified residuei684PhosphoserineBy similarity1
Modified residuei698PhosphoserineCombined sources1
Modified residuei710PhosphoserineBy similarity1
Modified residuei715PhosphothreonineBy similarity1
Modified residuei732PhosphoserineBy similarity1
Modified residuei763PhosphoserineBy similarity1
Modified residuei785PhosphoserineBy similarity1
Modified residuei790PhosphoserineCombined sources1
Modified residuei808PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi889N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi895N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi1391S-palmitoyl cysteineBy similarity1
Modified residuei1440PhosphoserineBy similarity1
Modified residuei1452PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

N-glycosylated.By similarity
Phosphorylated; cAMP treatment promotes phosphorylation and activates the channel. Dephosphorylation decreases the ATPase activity (in vitro). Phosphorylation at PKA sites activates the channel. Phosphorylation at PKC sites enhances the response to phosphorylation by PKA. Phosphorylated by AMPK; this inhibits channel activity.By similarity
Ubiquitinated, leading to its degradation in the lysosome. Deubiquitination by USP10 in early endosomes enhances its endocytic recycling to the cell membrane. Ubiquitinated by RNF185 during ER stress.By similarity

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P26361

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

More...PaxDbi		P26361

PeptideAtlas

More...PeptideAtlasi		P26361

PRoteomics IDEntifications database

More...PRIDEi		P26361

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P26361

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P26361

<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

Isoform 1 is expressed in a variety of epithelial tissues including colon, kidney, lung, small intestine, pancreatic duct and testis. Isoforms 2 and 3 are expressed only in testis.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000041301 Expressed in 126 organ(s), highest expression level in paneth cell

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P26361 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P26361 MM

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer; does not require oligomerization for channel activity. May form oligomers in the membrane (By similarity). Interacts with SLC26A3, SLC26A6 and SLC9A3R1 (PubMed:21976599). Interacts with SHANK2 (By similarity). Interacts with MYO6 (By similarity). Interacts (via C-terminus) with GOPC (via PDZ domain); this promotes CFTR internalization and thereby decreases channel activity. Interacts with SLC4A7 through SLC9A3R1. Found in a complex with MYO5B and RAB11A. Interacts with ANO1. Interacts with SLC26A8 (By similarity). Interacts with AHCYL1; the interaction increases CFTR activity (PubMed:19033647, PubMed:23542070). Interacts with CSE1L (By similarity). The core-glycosylated form interacts with GORASP2 (via PDZ GRASP-type 1 domain) in respone to ER stress (By similarity).By similarity3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		198687, 2 interactors

Database of interacting proteins

More...DIPi		DIP-29618N

Protein interaction database and analysis system

More...IntActi		P26361, 10 interactors

Molecular INTeraction database

More...MINTi		P26361

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000049228

<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

11476
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1Q3HX-ray2.50A/B/C/D389-673[»]
1R0WX-ray2.20A/B/C/D389-673[»]
1R0XX-ray2.20A/B/C/D389-673[»]
1R0YX-ray2.55A/B/C/D389-673[»]
1R0ZX-ray2.35A/B/C/D389-673[»]
1R10X-ray3.00A/B389-673[»]
1XF9X-ray2.70A/B/C/D389-670[»]
1XFAX-ray3.10A/B389-670[»]
3SI7X-ray2.25A/B/C/D389-673[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P26361

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

More...SMRi		P26361

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P26361

<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_and_domains_section">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>Domaini81 – 365ABC transmembrane type-1 1PROSITE-ProRule annotationAdd BLAST285
Domaini423 – 646ABC transporter 1PROSITE-ProRule annotationAdd BLAST224
Domaini854 – 1153ABC transmembrane type-1 2PROSITE-ProRule annotationAdd BLAST300
Domaini1208 – 1439ABC transporter 2PROSITE-ProRule annotationAdd BLAST232

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>Regioni654 – 826Intrinsically disordered R regionBy similarityAdd BLAST173
Regioni1382 – 1476Interaction with GORASP2By similarityAdd BLAST95

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>Motifi1474 – 1476PDZ-bindingBy similarity3

<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 (By similarity). The first ABC transporter nucleotide-binding domain has no ATPase activity by itself (PubMed:14685259, PubMed:15619636).By similarity2 Publications
The PDZ-binding motif mediates interactions with GOPC and with the SLC4A7, SLC9A3R1/EBP50 complex.By similarity
The R region is intrinsically disordered. It 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]Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0054 Eukaryota
COG1132 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000158567

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000185880

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG004169

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P26361

KEGG Orthology (KO)

More...KOi		K05031

Identification of Orthologs from Complete Genome Data

More...OMAi		RCFFWKF

Database of Orthologous Groups

More...OrthoDBi		138195at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P26361

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

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
IPR017871 ABC_transporter_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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P26361-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MQKSPLEKAS FISKLFFSWT TPILRKGYRH HLELSDIYQA PSADSADHLS 
        60         70         80         90        100
EKLEREWDRE QASKKNPQLI HALRRCFFWR FLFYGILLYL GEVTKAVQPV 
       110        120        130        140        150
LLGRIIASYD PENKVERSIA IYLGIGLCLL FIVRTLLLHP AIFGLHRIGM 
       160        170        180        190        200
QMRTAMFSLI YKKTLKLSSR VLDKISIGQL VSLLSNNLNK FDEGLALAHF 
       210        220        230        240        250
IWIAPLQVTL LMGLLWDLLQ FSAFCGLGLL IILVIFQAIL GKMMVKYRDQ 
       260        270        280        290        300
RAAKINERLV ITSEIIDNIY SVKAYCWESA MEKMIENLRE VELKMTRKAA 
       310        320        330        340        350
YMRFFTSSAF FFSGFFVVFL SVLPYTVING IVLRKIFTTI SFCIVLRMSV 
       360        370        380        390        400
TRQFPTAVQI WYDSFGMIRK IQDFLQKQEY KVLEYNLMTT GIIMENVTAF 
       410        420        430        440        450
WEEGFGELLE KVQQSNGDRK HSSDENNVSF SHLCLVGNPV LKNINLNIEK 
       460        470        480        490        500
GEMLAITGST GSGKTSLLML ILGELEASEG IIKHSGRVSF CSQFSWIMPG 
       510        520        530        540        550
TIKENIIFGV SYDEYRYKSV VKACQLQQDI TKFAEQDNTV LGEGGVTLSG 
       560        570        580        590        600
GQRARISLAR AVYKDADLYL LDSPFGYLDV FTEEQVFESC VCKLMANKTR 
       610        620        630        640        650
ILVTSKMEHL RKADKILILH QGSSYFYGTF SELQSLRPDF SSKLMGYDTF 
       660        670        680        690        700
DQFTEERRSS ILTETLRRFS VDDSSAPWSK PKQSFRQTGE VGEKRKNSIL 
       710        720        730        740        750
NSFSSVRKIS IVQKTPLCID GESDDLQEKR LSLVPDSEQG EAALPRSNMI 
       760        770        780        790        800
ATGPTFPGRR RQSVLDLMTF TPNSGSSNLQ RTRTSIRKIS LVPQISLNEV 
       810        820        830        840        850
DVYSRRLSQD STLNITEEIN EEDLKECFLD DVIKIPPVTT WNTYLRYFTL 
       860        870        880        890        900
HKGLLLVLIW CVLVFLVEVA ASLFVLWLLK NNPVNSGNNG TKISNSSYVV 
       910        920        930        940        950
IITSTSFYYI FYIYVGVADT LLALSLFRGL PLVHTLITAS KILHRKMLHS 
       960        970        980        990       1000
ILHAPMSTIS KLKAGGILNR FSKDIAILDD FLPLTIFDFI QLVFIVIGAI 
      1010       1020       1030       1040       1050
IVVSALQPYI FLATVPGLVV FILLRAYFLH TAQQLKQLES EGRSPIFTHL 
      1060       1070       1080       1090       1100
VTSLKGLWTL RAFRRQTYFE TLFHKALNLH TANWFMYLAT LRWFQMRIDM 
      1110       1120       1130       1140       1150
IFVLFFIVVT FISILTTGEG EGTAGIILTL AMNIMSTLQW AVNSSIDTDS 
      1160       1170       1180       1190       1200
LMRSVSRVFK FIDIQTEESM YTQIIKELPR EGSSDVLVIK NEHVKKSDIW 
      1210       1220       1230       1240       1250
PSGGEMVVKD LTVKYMDDGN AVLENISFSI SPGQRVGLLG RTGSGKSTLL 
      1260       1270       1280       1290       1300
SAFLRMLNIK GDIEIDGVSW NSVTLQEWRK AFGVITQKVF IFSGTFRQNL 
      1310       1320       1330       1340       1350
DPNGKWKDEE IWKVADEVGL KSVIEQFPGQ LNFTLVDGGY VLSHGHKQLM 
      1360       1370       1380       1390       1400
CLARSVLSKA KIILLDEPSA HLDPITYQVI RRVLKQAFAG CTVILCEHRI 
      1410       1420       1430       1440       1450
EAMLDCQRFL VIEESNVWQY DSLQALLSEK SIFQQAISSS EKMRFFQGRH 
      1460       1470 
SSKHKPRTQI TALKEETEEE VQETRL
Length:1,476
Mass (Da):167,870
Last modified:January 31, 2002 - v2
<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:i3D1B0BBDD80C1DA8
GO
Isoform 2 (identifier: P26361-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     561-576: AVYKDADLYLLDSPFG → FLICLQTKDKVSLFRN
     577-1476: Missing.

Show »
Length:576
Mass (Da):65,799
Checksum:i5EED7EC29AD39CFC
GO
Isoform 3 (identifier: P26361-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     561-600: AVYKDADLYL...VCKLMANKTR → QRTRSPYLEI...QYIKMLICTY
     601-1476: Missing.

Show »
Length:600
Mass (Da):68,782
Checksum:iC8E6AE26516811C4
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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PVD7E9PVD7_MOUSE
Cystic fibrosis transmembrane condu...
Cftr
1,446Annotation score:

Annotation score:3 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>
F6U9G7F6U9G7_MOUSE
Cystic fibrosis transmembrane condu...
Cftr
529Annotation score:

Annotation score:1 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 conflicti20 – 22TTP → STA in AAF30300 (PubMed:10655503).Curated3
Sequence conflicti30H → Q in AAF30300 (PubMed:10655503).Curated1
Sequence conflicti410 – 412EKV → QKA in AAA37417 (PubMed:1712752).Curated3
Sequence conflicti462S → L in AAA37417 (PubMed:1712752).Curated1
Sequence conflicti623S → T in AAA37417 (PubMed:1712752).Curated1
Sequence conflicti639D → S in AAA37417 (PubMed:1712752).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_000064561 – 600AVYKD…ANKTR → QRTRSPYLEIRIFLCLFLYT RMKVCATTPEQYIKMLICTY in isoform 3. CuratedAdd BLAST40
Alternative sequenceiVSP_000062561 – 576AVYKD…DSPFG → FLICLQTKDKVSLFRN in isoform 2. CuratedAdd BLAST16
Alternative sequenceiVSP_000063577 – 1476Missing in isoform 2. CuratedAdd BLAST900
Alternative sequenceiVSP_000065601 – 1476Missing in isoform 3. CuratedAdd BLAST876

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
M69298 mRNA Translation: AAA37417.1
M60493 mRNA Translation: AAA18903.1
AF162137 Genomic DNA Translation: AAF30300.1
L04873 Genomic DNA Translation: AAA73562.1
S65942, S65940, S65941 Genomic DNA Translation: AAB28393.1
S65942 Genomic DNA Translation: AAB28391.1
S65941, S65940 Genomic DNA Translation: AAB28392.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS19930.1 [P26361-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A39901
A40303
I49593
I58115
I78527

NCBI Reference Sequences

More...RefSeqi		NP_066388.1, NM_021050.2 [P26361-1]
XP_006505040.1, XM_006504977.1 [P26361-1]
XP_006505041.1, XM_006504978.1 [P26361-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Mm.15621

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000045706; ENSMUSP00000049228; ENSMUSG00000041301 [P26361-1]
ENSMUST00000115405; ENSMUSP00000111064; ENSMUSG00000041301 [P26361-3]
ENSMUST00000140407; ENSMUSP00000116957; ENSMUSG00000041301 [P26361-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		12638

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:12638

UCSC genome browser

More...UCSCi		uc009bai.1 mouse [P26361-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
M69298 mRNA Translation: AAA37417.1
M60493 mRNA Translation: AAA18903.1
AF162137 Genomic DNA Translation: AAF30300.1
L04873 Genomic DNA Translation: AAA73562.1
S65942, S65940, S65941 Genomic DNA Translation: AAB28393.1
S65942 Genomic DNA Translation: AAB28391.1
S65941, S65940 Genomic DNA Translation: AAB28392.1
CCDSiCCDS19930.1 [P26361-1]
PIRiA39901
A40303
I49593
I58115
I78527
RefSeqiNP_066388.1, NM_021050.2 [P26361-1]
XP_006505040.1, XM_006504977.1 [P26361-1]
XP_006505041.1, XM_006504978.1 [P26361-1]
UniGeneiMm.15621

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q3HX-ray2.50A/B/C/D389-673[»]
1R0WX-ray2.20A/B/C/D389-673[»]
1R0XX-ray2.20A/B/C/D389-673[»]
1R0YX-ray2.55A/B/C/D389-673[»]
1R0ZX-ray2.35A/B/C/D389-673[»]
1R10X-ray3.00A/B389-673[»]
1XF9X-ray2.70A/B/C/D389-670[»]
1XFAX-ray3.10A/B389-670[»]
3SI7X-ray2.25A/B/C/D389-673[»]
ProteinModelPortaliP26361
SMRiP26361
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198687, 2 interactors
DIPiDIP-29618N
IntActiP26361, 10 interactors
MINTiP26361
STRINGi10090.ENSMUSP00000049228

PTM databases

iPTMnetiP26361
PhosphoSitePlusiP26361

Proteomic databases

MaxQBiP26361
PaxDbiP26361
PeptideAtlasiP26361
PRIDEiP26361

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		12638
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045706; ENSMUSP00000049228; ENSMUSG00000041301 [P26361-1]
ENSMUST00000115405; ENSMUSP00000111064; ENSMUSG00000041301 [P26361-3]
ENSMUST00000140407; ENSMUSP00000116957; ENSMUSG00000041301 [P26361-2]
GeneIDi12638
KEGGimmu:12638
UCSCiuc009bai.1 mouse [P26361-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1080
MGIiMGI:88388 Cftr

Phylogenomic databases

eggNOGiKOG0054 Eukaryota
COG1132 LUCA
GeneTreeiENSGT00940000158567
HOGENOMiHOG000185880
HOVERGENiHBG004169
InParanoidiP26361
KOiK05031
OMAiRCFFWKF
OrthoDBi138195at2759
PhylomeDBiP26361
TreeFamiTF105200

Enzyme and pathway databases

BRENDAi3.6.3.49 3474
ReactomeiR-MMU-382556 ABC-family proteins mediated transport
R-MMU-5627083 RHO GTPases regulate CFTR trafficking
R-MMU-5689880 Ub-specific processing proteases
R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis
R-MMU-8856828 Clathrin-mediated endocytosis

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Cftr mouse
EvolutionaryTraceiP26361

Protein Ontology

More...PROi		PR:P26361

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000041301 Expressed in 126 organ(s), highest expression level in paneth cell
ExpressionAtlasiP26361 baseline and differential
GenevisibleiP26361 MM

Family and domain databases

Gene3Di1.20.1560.10, 2 hits
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR011527 ABC1_TM_dom
IPR036640 ABC1_TM_sf
IPR003439 ABC_transporter-like
IPR017871 ABC_transporter_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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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_MOUSE
<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: P26361
Secondary accession number(s): Q63893, Q63894, Q9JKQ6
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 31, 2002
Last modified: January 16, 2019
This is version 188 of the entry and version 2 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, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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