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Entry version 119 (03 Jul 2019)
Sequence version 1 (01 May 1992)
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Protein

Cystic fibrosis transmembrane conductance regulator

Gene

CFTR

Organism
Squalus acanthias (Spiny dogfish)
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 (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 sitei402ATP 1By similarity1
Binding sitei435ATP 1By similarity1
Binding sitei494ATP 1By similarity1
Binding sitei1229ATP 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 bindingi459 – 466ATP 1PROSITE-ProRule annotation8
Nucleotide bindingi1254 – 1261ATP 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

<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)
Dogfish transmembrane conductance regulator
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, DFTR
<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>OrganismiSqualus acanthias (Spiny dogfish)
<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 identifieri7797 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiSqualimorphiiSqualiformesSqualidaeSqualus

<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 – 78CytoplasmicBy similarityAdd BLAST78
<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>Transmembranei79 – 99Helical; Name=1By similarityAdd BLAST21
Topological domaini100 – 123ExtracellularBy similarityAdd BLAST24
Transmembranei124 – 147Helical; Name=2By similarityAdd BLAST24
Topological domaini148 – 196CytoplasmicBy similarityAdd BLAST49
Transmembranei197 – 217Helical; Name=3By similarityAdd BLAST21
Topological domaini218 – 223ExtracellularBy similarity6
Transmembranei224 – 244Helical; Name=4By similarityAdd BLAST21
Topological domaini245 – 299CytoplasmicBy similarityAdd BLAST55
Transmembranei300 – 320Helical; Name=5By similarityAdd BLAST21
Topological domaini321 – 340ExtracellularBy similarityAdd BLAST20
Transmembranei341 – 359Helical; Name=6By similarityAdd BLAST19
Topological domaini360 – 867CytoplasmicBy similarityAdd BLAST508
Transmembranei868 – 888Helical; Name=7By similarityAdd BLAST21
Topological domaini889 – 932ExtracellularBy similarityAdd BLAST44
Transmembranei933 – 953Discontinuously helical; Name=8By similarityAdd BLAST21
Topological domaini954 – 1004CytoplasmicBy similarityAdd BLAST51
Transmembranei1005 – 1025Helical; Name=9By similarityAdd BLAST21
Topological domaini1026 – 1027ExtracellularBy similarity2
Transmembranei1028 – 1048Helical; Name=10By similarityAdd BLAST21
Topological domaini1049 – 1109CytoplasmicBy similarityAdd BLAST61
Transmembranei1110 – 1130Helical; Name=11By similarityAdd BLAST21
Topological domaini1131 – 1144ExtracellularBy similarityAdd BLAST14
Transmembranei1145 – 1165Helical; Name=12By similarityAdd BLAST21
Topological domaini1166 – 1492CytoplasmicBy similarityAdd BLAST327

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Endosome, Membrane

<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_00000934311 – 1492Cystic fibrosis transmembrane conductance regulatorAdd BLAST1492

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 and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi905N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi923N-linked (GlcNAc...) asparagineSequence analysis1

<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

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.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P26362

<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

Expressed in the rectal gland (at protein level).1 Publication

<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).

By similarity

<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
P26362

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>Domaini82 – 366ABC transmembrane type-1 1PROSITE-ProRule annotationAdd BLAST285
Domaini424 – 647ABC transporter 1PROSITE-ProRule annotationAdd BLAST224
Domaini868 – 1169ABC transmembrane type-1 2PROSITE-ProRule annotationAdd BLAST302
Domaini1220 – 1453ABC 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>Regioni655 – 840Intrinsically disordered R regionBy similarityAdd BLAST186

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

<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 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

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>. 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>Sequencei

<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.

P26362-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQRSPIEKAN AFSKLFFRWP RPILKKGYRQ KLELSDIYQI PSSDSADELS
60 70 80 90 100
EMLEREWDRE LATSKKNPKL VNALRRCFFW RFLFYGILLY FVEFTKAVQP
110 120 130 140 150
LCLGRIIASY NAKNTYEREI AYYLALGLCL LFVVRTLFLH PAVFGLQHLG
160 170 180 190 200
MQMRIALFSL IYKKILKMSS RVLDKIDTGQ LVSLLSNNLN KFDEGVAVAH
210 220 230 240 250
FVWIAPVQVV LLMGLIWNEL TEFVFCGLGF LIMLALFQAW LGKKMMQYRD
260 270 280 290 300
KRAGKINERL AITSEIIDNI QSVKVYCWED AMEKIIDDIR QVELKLTRKV
310 320 330 340 350
AYCRYFSSSA FFFSGFFVVF LSVVPYAFIH TIKLRRIFTT ISYNIVLRMT
360 370 380 390 400
VTRQFPSAIQ TWYDSLGAIR KIQDFLHKDE HKTVEYNLTT KEVEMVNVTA
410 420 430 440 450
SWDEGIGELF EKVKQNDSER KMANGDDGLF FSNFSLHVTP VLKNISFKLE
460 470 480 490 500
KGELLAIAGS TGSGKSSLLM MIMGELEPSD GKIKHSGRIS YSPQVPWIMP
510 520 530 540 550
GTIKDNIIFG LSYDEYRYTS VVNACQLEED ITVFPNKDKT VLGDGGITLS
560 570 580 590 600
GGQRARISLA RALYKDADLY LLDSPFSHLD VTTEKDIFES CLCKLMVNKT
610 620 630 640 650
RILVTSKLEH LKKADKILLL HEGHCYFYGT FSELQGEKPD FSSQLLGSVH
660 670 680 690 700
FDSFSAERRN SILTETFRRC SVSSGDGAGL GSYSETRKAS FKQPPPEFNE
710 720 730 740 750
KRKSSLIVNP ITSNKKFSLV QTAMSYPQTN GMEDATSEPG ERHFSLIPEN
760 770 780 790 800
ELGEPTKPRS NIFKSELPFQ AHRRQSVLAL MTHSSTSPNK IHARRSAVRK
810 820 830 840 850
MSMLSQTNFA SSEIDIYSRR LSEDGSFEIS EEINEEDLKE CFADEEEIQN
860 870 880 890 900
VTTTWSTYLR YVTTNRNLVF VLILCLVIFL AEVAASLAGL WIISGLAINT
910 920 930 940 950
GSQTNDTSTD LSHLSVFSKF ITNGSHYYIF YIYVGLADSF LALGVIRGLP
960 970 980 990 1000
LVHTLVTVSK DLHKQMLHSV LQGPMTAFNK MKAGRILNRF IKDTAIIDDM
1010 1020 1030 1040 1050
LPLTVFDFVQ LILIVVGAIC VVSVLQPYTL LAAIPVAVIF IMLRAYFLRT
1060 1070 1080 1090 1100
SQQLKQLESE ARSPIFSHLI TSLRGLWTVR AFGRQSYFET LFHKALNLHT
1110 1120 1130 1140 1150
ANWFLYLSTL RWFQMRIDIV FVLFFIAVTF IAIATHDVGE GQVGIILTLA
1160 1170 1180 1190 1200
MNITSTLQWA VNSSIDVDGL MRSVSRVFKY IDIPPEGSET KNRHNANNPS
1210 1220 1230 1240 1250
DVLVIENKHL TKEWPSGGQM MVNNLTAKYT SDGRAVLQDL SFSVNAGQRV
1260 1270 1280 1290 1300
GLLGRTGAGK STLLSALLRL LSTEGEIQID GISWNSVSLQ KWRKAFGVIP
1310 1320 1330 1340 1350
QKVFVFSGTF RKNLDPYEQW SDEEIWKVTE EVGLKSMIEQ FPDKLNFVLV
1360 1370 1380 1390 1400
DGGYILSNGH KQLMCLARSI LSKAKILLLD EPTAHLDPVT FQIIRKTLKH
1410 1420 1430 1440 1450
TFSNCTVILS EHRVEALLEC QQFLVIEGCS VKQFDALQKL LTEASLFKQV
1460 1470 1480 1490
FGHLDRAKLF TAHRRNSSKR KTRPKISALQ EEAEEDLQET RL
Length:1,492
Mass (Da):169,385
Last modified:May 1, 1992 - 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:i0E49CA89968FC2F9
GO

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
M83785 mRNA Translation: AAA49616.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A39322

<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
M83785 mRNA Translation: AAA49616.1
PIRiA39322

3D structure databases

SMRiP26362
ModBaseiSearch...

Proteomic databases

PRIDEiP26362

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_SQUAC
<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: P26362
<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: May 1, 1992
Last modified: July 3, 2019
This is version 119 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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