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Entry version 175 (18 Sep 2019)
Sequence version 3 (12 Jun 2007)
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Protein

Cystic fibrosis transmembrane conductance regulator

Gene

Cftr

Organism
Rattus norvegicus (Rat)
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. 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. 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 (By similarity).By similarity

<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 <a href="http://www.uniprot.org/help/function_section">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 sitei401ATP 1By similarity1
Binding sitei493ATP 1By similarity1
Binding sitei1215ATP 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi458 – 465ATPPROSITE-ProRule annotation8
Nucleotide bindingi458 – 465ATP 1PROSITE-ProRule annotationBy similarity8
Nucleotide bindingi1240 – 1247ATPPROSITE-ProRule annotation8
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

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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-382556 ABC-family proteins mediated transport
R-RNO-5627083 RHO GTPases regulate CFTR trafficking
R-RNO-5689880 Ub-specific processing proteases
R-RNO-8856825 Cargo recognition for clathrin-mediated endocytosis
R-RNO-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:5.6.1.6By 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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
2332 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 & Seán O’Donoghue; 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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3992

<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_00000934281 – 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 residuei698PhosphoserineBy similarity1
Modified residuei710PhosphoserineBy similarity1
Modified residuei715PhosphothreonineBy similarity1
Modified residuei732PhosphoserineBy similarity1
Modified residuei763PhosphoserineBy similarity1
Modified residuei785PhosphoserineBy similarity1
Modified residuei790PhosphoserineBy similarity1
Modified residuei808PhosphoserineCombined sources1
<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

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

More...
PaxDbi
P34158

PRoteomics IDEntifications database

More...
PRIDEi
P34158

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P34158

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

More...
PhosphoSitePlusi
P34158

<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 epithelial cells in nasopharynx, submandibular gland, pancreas and ileum (at protein level) (PubMed:12519745). Expressed in the epididymis (PubMed:30659401). In the caput section of the epididymis, expressed uniformly on both the luminal and basolateral sides of the ducts and on sperm in the caput lumen (at protein level) (PubMed:30659401). In the cauda, detected along the luminal border but not continuously and is also expressed on the basolateral surface (PubMed:30659401). Within the caudal lumen, detected on sperm (PubMed:30659401).2 Publications

<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 SLC4A7 through SLC9A3R1 (By similarity).

Interacts with SHANK2 (PubMed:14679199).

Interacts with SLC9A3R1 and MYO6.

Interacts (via C-terminus) with GOPC (via PDZ domain); this promotes CFTR internalization and thereby decreases channel activity (PubMed:11707463).

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 (By similarity).

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 similarity2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
246440, 3 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000010981

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P34158

<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

3D structure databases

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

More...
SMRi
P34158

Database of comparative protein structure models

More...
ModBasei
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_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
Domaini412 – 646ABC transporter 1PROSITE-ProRule annotationAdd BLAST235
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-binding1 Publication3

<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 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

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0054 Eukaryota
COG1132 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P34158

KEGG Orthology (KO)

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KOi
K05031

Database of Orthologous Groups

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OrthoDBi
138195at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P34158

TreeFam database of animal gene trees

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TreeFami
TF105200

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.1560.10, 2 hits

Integrated resource of protein families, domains and functional sites

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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

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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

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PRINTSi
PR01851 CYSFIBREGLTR

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00382 AAA, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52540 SSF52540, 2 hits
SSF90123 SSF90123, 2 hits

TIGRFAMs; a protein family database

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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>. 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_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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P34158-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQKSPLEKAS FISKLFFSWT TPILRKGYRH HLELSDIYQA PSSDSADHLS
60 70 80 90 100
EKLEREWDRE QASKKKPQLI HALRRCFVWR FVFYGVLLYL GEVTKAVQPV
110 120 130 140 150
LLGRIIASYD PDNTEERSIA IYLGIGLCLL FIVRTLLLHP AIFGLHHIGM
160 170 180 190 200
QMRIAMFSLI YKKTLKLSSR VLDKISIGQL ISLLSNNLNK FDEGLALAHF
210 220 230 240 250
IWIAPLQVVL LMGLLWDLLQ FSAFCGLGLL IVLVIFQAIL GKMMVKYRDK
260 270 280 290 300
RAAKINERLV ITSEVIDNIY SVKAYCWESA MEKIIESLRE EELKMTRRSA
310 320 330 340 350
YMRFFTSSAF FFSGFFVVFL SVLPYTVING IVLRKIFTTI SFCIVLRMSV
360 370 380 390 400
TRQFPTAVQI WYDSLGMIRK IQDFLQTQEY KVLEYNLMFT GLVMENVTAF
410 420 430 440 450
WEEGFQELLE KVQLNNDDRK TSNGENHLSF SHLCLVGNPV LKNINLNIKK
460 470 480 490 500
GEMLAITGST GAGKTSLLML ILGELEASEG IIKHSGRVSF SSQISWIMPG
510 520 530 540 550
TIKENIIFGV SYDEYRYKSV VKACQLQEDI TKFAEQDNTV LGEGGVTLSG
560 570 580 590 600
GQRARISLAR AVYKDADLYL LDSPFGYLDV LTEEQIFESC VCKLMASKTR
610 620 630 640 650
ILVTSKMEQL KKADKILILH EGSSYFYGTF SELQSLRPDF SSKLMGYDTF
660 670 680 690 700
DQFTEERRSS ILTETLRRFS VDDASTTWNK AKQSFRQTGE FGEKRKNSIL
710 720 730 740 750
SSFSSVKKIS IVQKTPLSIE GESDDLQERR LSLVPDSEHG EAALPRSNMI
760 770 780 790 800
TAGPTFPGRR RQSVLDLMTF TPSSVSSSLQ RTRASIRKIS LAPRISLKEE
810 820 830 840 850
DIYSRRLSQD STLNITEEIN EEDLKECFFD DMVKIPTVTT WNTYLRYFTL
860 870 880 890 900
HRGLFAVLIW CVLVFLVEVA ASLFVLWLLK NNPVNGGNNG TKIANTSYVV
910 920 930 940 950
VITSSSFYYI FYIYVGVADT LLALSLFRGL PLVHTLITAS KILHRKMLHS
960 970 980 990 1000
ILHAPMSTFN KLKAGGILNR FSKDIAILDD FLPLTIFDFI QLLFIVVGAI
1010 1020 1030 1040 1050
IVVSALQPYI FLATVPGLAV FILLRAYFLH TSQQLKQLES EGRSPIFTHL
1060 1070 1080 1090 1100
VTSLKGLWTL RAFRRQTYFE TLFHKALNLH TANWFMYLAT LRWFQMRIDM
1110 1120 1130 1140 1150
IFVLFFIVVT FISILTTGEG EGTTGIILTL AMNIMSTLQW AVNSSIDTDS
1160 1170 1180 1190 1200
LMRSVSRVFK FIDIQTEESI CTKIMKELHS EDSPNALVIK NEHVKKCDTW
1210 1220 1230 1240 1250
PSGGEMVVKD LTVKYVDDGN AILENISFSI SPGQRVGLLG RTGSGKSTLL
1260 1270 1280 1290 1300
SAFLRMLNIK GEIQIDGVSW NSMTLQEWRK AFGVITQKVF IFSGTFRQNL
1310 1320 1330 1340 1350
DPNGKWRDEE IWKVADQVGL KSVIEQFPGQ LNFTLVDGGY VLSHGHKQLM
1360 1370 1380 1390 1400
CLARSVLSKA KIILLDEPSA NLDPITYQVI RRVLRQAFAG CTVVLCEHRI
1410 1420 1430 1440 1450
EAMLDCQRFL VIEQGNVWQY ESLQALLSEK SVFQRALSSS EKMKLFHGRH
1460 1470
SSKQKPRTQI TAVKEETEEE VQETRL
Length:1,476
Mass (Da):167,830
Last modified:June 12, 2007 - v3
<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:iB2B2A25EB5107640
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
A0A0G2K3B1A0A0G2K3B1_RAT
Cystic fibrosis transmembrane condu...
Cftr
1,665Annotation 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 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 conflicti987 – 988FD → LT in AAA40918 (PubMed:1282491).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
DP000027 Genomic DNA Translation: AAR16315.1
L26098 Genomic DNA Translation: AAA73561.1
M89906 mRNA Translation: AAA40918.1

Protein sequence database of the Protein Information Resource

More...
PIRi
I84733

NCBI Reference Sequences

More...
RefSeqi
NP_113694.1, NM_031506.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24255

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:24255

<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
DP000027 Genomic DNA Translation: AAR16315.1
L26098 Genomic DNA Translation: AAA73561.1
M89906 mRNA Translation: AAA40918.1
PIRiI84733
RefSeqiNP_113694.1, NM_031506.1

3D structure databases

SMRiP34158
ModBaseiSearch...

Protein-protein interaction databases

BioGridi246440, 3 interactors
STRINGi10116.ENSRNOP00000010981

Chemistry databases

BindingDBiP34158
ChEMBLiCHEMBL3992

PTM databases

iPTMnetiP34158
PhosphoSitePlusiP34158

Proteomic databases

PaxDbiP34158
PRIDEiP34158

Genome annotation databases

GeneIDi24255
KEGGirno:24255

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1080
RGDi2332 Cftr

Phylogenomic databases

eggNOGiKOG0054 Eukaryota
COG1132 LUCA
InParanoidiP34158
KOiK05031
OrthoDBi138195at2759
PhylomeDBiP34158
TreeFamiTF105200

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P34158

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...

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_RAT
<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: P34158
Secondary accession number(s): Q2IBD3
<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: February 1, 1994
Last sequence update: June 12, 2007
Last modified: September 18, 2019
This is version 175 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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