UniProtKB - P26361 (CFTR_MOUSE)
Cystic fibrosis transmembrane conductance regulator
Cftr
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 PublicationsCatalytic activityi
- ATP + H(2)O + closed Cl(-) channel = ADP + phosphate + open Cl(-) channel.By similarity EC:5.6.1.6
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 401 | ATP 1By similarity | 1 | |
Binding sitei | 493 | ATP 1Combined sources | 1 | |
Binding sitei | 1215 | ATP 2By similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 458 – 465 | ATP 1PROSITE-ProRule annotationCombined sources | 8 | |
Nucleotide bindingi | 1240 – 1247 | ATP 2PROSITE-ProRule annotation | 8 |
GO - Molecular functioni
- ABC-type transporter activity Source: InterPro
- ATPase-coupled transmembrane transporter activity Source: GO_Central
- ATP binding Source: UniProtKB-KW
- ATP hydrolysis activity Source: UniProtKB
- bicarbonate transmembrane transporter activity Source: UniProtKB
- chaperone binding Source: MGI
- chloride channel activity Source: UniProtKB
- chloride channel inhibitor activity Source: UniProtKB
- chloride transmembrane transporter activity Source: UniProtKB
- enzyme binding Source: MGI
- intracellularly ATP-gated chloride channel activity Source: UniProtKB
- isomerase activity Source: UniProtKB-KW
- PDZ domain binding Source: MGI
- Sec61 translocon complex binding Source: MGI
GO - Biological processi
- amelogenesis Source: ARUK-UCL
- bicarbonate transport Source: UniProtKB
- cellular response to cAMP Source: UniProtKB
- cellular response to forskolin Source: UniProtKB
- chloride transmembrane transport Source: UniProtKB
- chloride transport Source: MGI
- cholesterol biosynthetic process Source: MGI
- cholesterol transport Source: MGI
- enamel mineralization Source: MGI
- intracellular pH elevation Source: UniProtKB
- lung development Source: MGI
- membrane hyperpolarization Source: UniProtKB
- multicellular organismal water homeostasis Source: UniProtKB
- negative regulation of type B pancreatic cell development Source: MGI
- negative regulation of vascular associated smooth muscle cell apoptotic process Source: MGI
- positive regulation of cyclic nucleotide-gated ion channel activity Source: UniProtKB
- positive regulation of enamel mineralization Source: ARUK-UCL
- positive regulation of establishment of Sertoli cell barrier Source: MGI
- positive regulation of exocytosis Source: UniProtKB
- positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
- positive regulation of mast cell activation Source: MGI
- positive regulation of voltage-gated chloride channel activity Source: MGI
- response to amiloride Source: MGI
- response to endoplasmic reticulum stress Source: UniProtKB
- response to xenobiotic stimulus Source: MGI
- sodium ion transmembrane transport Source: MGI
- sperm capacitation Source: UniProtKB
- transepithelial chloride transport Source: MGI
- transepithelial water transport Source: UniProtKB
- transmembrane transport Source: GO_Central
- vasodilation Source: MGI
- vesicle docking involved in exocytosis Source: UniProtKB
- water transport Source: MGI
Keywordsi
Molecular function | Chloride channel, Ion channel, Isomerase |
Biological process | Ion transport, Transport |
Ligand | ATP-binding, Chloride, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 2.7.4.3, 3474 5.6.1.6, 3474 |
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 R-MMU-9013406, RHOQ GTPase cycle R-MMU-9646399, Aggrephagy |
Names & Taxonomyi
Protein namesi | Recommended name: Cystic fibrosis transmembrane conductance regulatorShort 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 |
Gene namesi | Name:Cftr Synonyms:Abcc7 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:88388, Cftr |
VEuPathDBi | HostDB:ENSMUSG00000041301 |
Subcellular locationi
Plasma membrane
- Apical cell membrane 2 Publications; Multi-pass membrane protein By similarity
- Cell membrane 2 Publications; Multi-pass membrane protein By similarity
Endosome
- Early endosome membrane By similarity; Multi-pass membrane protein By similarity
- Recycling endosome membrane By similarity; Multi-pass membrane protein By similarity
Nucleus
- Nucleus By similarity
Endoplasmic reticulum
- Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
Note: The channel is internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane. In the oviduct and bronchus, detected on the apical side of epithelial cells, but not associated with cilia. In Sertoli cells, a processed product is detected in the nucleus. ER stress induces GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (PubMed:21884936).By similarity1 Publication
Cytosol
- cytosol Source: UniProtKB
Endoplasmic reticulum
- endoplasmic reticulum membrane Source: UniProtKB
Endosome
- early endosome Source: UniProtKB
- early endosome membrane Source: UniProtKB-SubCell
- recycling endosome Source: MGI
- recycling endosome membrane Source: UniProtKB-SubCell
Nucleus
- nucleus Source: UniProtKB
Plasma Membrane
- apical plasma membrane Source: UniProtKB
- basolateral plasma membrane Source: MGI
- integral component of plasma membrane Source: UniProtKB
- plasma membrane Source: UniProtKB
Other locations
- cell surface Source: MGI
- chloride channel complex Source: UniProtKB-KW
- cytoplasm Source: MGI
- cytoplasmic vesicle membrane Source: MGI
- dendrite Source: MGI
- integral component of membrane Source: UniProtKB
- membrane Source: GO_Central
- microvillus Source: MGI
- neuronal cell body Source: MGI
- protein-containing complex Source: MGI
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 77 | CytoplasmicBy similarityAdd BLAST | 77 | |
Transmembranei | 78 – 98 | Helical; Name=1By similarityAdd BLAST | 21 | |
Topological domaini | 99 – 122 | ExtracellularBy similarityAdd BLAST | 24 | |
Transmembranei | 123 – 146 | Helical; Name=2By similarityAdd BLAST | 24 | |
Topological domaini | 147 – 195 | CytoplasmicBy similarityAdd BLAST | 49 | |
Transmembranei | 196 – 216 | Helical; Name=3By similarityAdd BLAST | 21 | |
Topological domaini | 217 – 222 | ExtracellularBy similarity | 6 | |
Transmembranei | 223 – 243 | Helical; Name=4By similarityAdd BLAST | 21 | |
Topological domaini | 244 – 298 | CytoplasmicBy similarityAdd BLAST | 55 | |
Transmembranei | 299 – 319 | Helical; Name=5By similarityAdd BLAST | 21 | |
Topological domaini | 320 – 339 | ExtracellularBy similarityAdd BLAST | 20 | |
Transmembranei | 340 – 358 | Helical; Name=6By similarityAdd BLAST | 19 | |
Topological domaini | 359 – 853 | CytoplasmicBy similarityAdd BLAST | 495 | |
Transmembranei | 854 – 874 | Helical; Name=7By similarityAdd BLAST | 21 | |
Topological domaini | 875 – 913 | ExtracellularBy similarityAdd BLAST | 39 | |
Transmembranei | 914 – 934 | Discontinuously helical; Name=8By similarityAdd BLAST | 21 | |
Topological domaini | 935 – 985 | CytoplasmicBy similarityAdd BLAST | 51 | |
Transmembranei | 986 – 1006 | Helical; Name=9By similarityAdd BLAST | 21 | |
Topological domaini | 1007 – 1008 | ExtracellularBy similarity | 2 | |
Transmembranei | 1009 – 1029 | Helical; Name=10By similarityAdd BLAST | 21 | |
Topological domaini | 1030 – 1090 | CytoplasmicBy similarityAdd BLAST | 61 | |
Transmembranei | 1091 – 1111 | Helical; Name=11By similarityAdd BLAST | 21 | |
Topological domaini | 1112 – 1125 | ExtracellularBy similarityAdd BLAST | 14 | |
Transmembranei | 1126 – 1146 | Helical; Name=12By similarityAdd BLAST | 21 | |
Topological domaini | 1147 – 1476 | CytoplasmicBy similarityAdd BLAST | 330 |
Keywords - Cellular componenti
Cell membrane, Endoplasmic reticulum, Endosome, Membrane, NucleusPathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 508 | F → A, L or Q: Mildly impairs protein maturation. 1 Publication | 1 | |
Mutagenesisi | 508 | F → C or M: No effect on protein maturation. 1 Publication | 1 | |
Mutagenesisi | 508 | F → E, D, G, H, I, K, P, R or Y: Abolishes normal maturation. 1 Publication | 1 | |
Mutagenesisi | 508 | F → N, S or V: Nearly abolishes normal maturation. 1 Publication | 1 | |
Mutagenesisi | 508 | Missing : 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 Publications | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000093424 | 1 – 1476 | Cystic fibrosis transmembrane conductance regulatorAdd BLAST | 1476 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 524 | S-palmitoyl cysteineBy similarity | 1 | |
Modified residuei | 549 | PhosphoserineBy similarity | 1 | |
Modified residuei | 660 | PhosphoserineBy similarity | 1 | |
Modified residuei | 670 | Phosphoserine; by PKABy similarity | 1 | |
Modified residuei | 684 | PhosphoserineBy similarity | 1 | |
Modified residuei | 698 | PhosphoserineCombined sources | 1 | |
Modified residuei | 710 | PhosphoserineBy similarity | 1 | |
Modified residuei | 715 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 732 | PhosphoserineBy similarity | 1 | |
Modified residuei | 763 | PhosphoserineBy similarity | 1 | |
Modified residuei | 785 | PhosphoserineBy similarity | 1 | |
Modified residuei | 790 | PhosphoserineCombined sources | 1 | |
Modified residuei | 808 | PhosphoserineBy similarity | 1 | |
Glycosylationi | 889 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 895 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Lipidationi | 1391 | S-palmitoyl cysteineBy similarity | 1 | |
Modified residuei | 1440 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1452 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugationProteomic databases
MaxQBi | P26361 |
PaxDbi | P26361 |
PeptideAtlasi | P26361 |
PRIDEi | P26361 |
ProteomicsDBi | 281397 [P26361-1] 281398 [P26361-2] 281399 [P26361-3] |
PTM databases
GlyGeni | P26361, 2 sites |
iPTMneti | P26361 |
PhosphoSitePlusi | P26361 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSMUSG00000041301, Expressed in paneth cell and 160 other tissues |
ExpressionAtlasi | P26361, baseline and differential |
Genevisiblei | P26361, MM |
Interactioni
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).
Interacts with MARCHF2; the interaction leads to CFTR ubiqtuitination and degradation (By similarity).
By similarity3 PublicationsBinary interactionsi
P26361
With | #Exp. | IntAct |
---|---|---|
Slc26a3 [Q9WVC8] | 3 | EBI-6115317,EBI-6895537 |
Slc26a6 [Q8CIW6] | 3 | EBI-6115317,EBI-6895517 |
Slc9a3r1 [P70441] | 3 | EBI-6115317,EBI-1184085 |
HSPA8 [P19120] from Bos taurus. | 5 | EBI-6115317,EBI-907802 |
GO - Molecular functioni
- chaperone binding Source: MGI
- enzyme binding Source: MGI
- PDZ domain binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 198687, 12 interactors |
DIPi | DIP-29618N |
IntActi | P26361, 10 interactors |
MINTi | P26361 |
STRINGi | 10090.ENSMUSP00000049228 |
Miscellaneous databases
RNActi | P26361, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P26361 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P26361 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 81 – 365 | ABC transmembrane type-1 1PROSITE-ProRule annotationAdd BLAST | 285 | |
Domaini | 423 – 646 | ABC transporter 1PROSITE-ProRule annotationAdd BLAST | 224 | |
Domaini | 854 – 1153 | ABC transmembrane type-1 2PROSITE-ProRule annotationAdd BLAST | 300 | |
Domaini | 1208 – 1439 | ABC transporter 2PROSITE-ProRule annotationAdd BLAST | 232 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 654 – 826 | Disordered R regionBy similarityAdd BLAST | 173 | |
Regioni | 1382 – 1476 | Interaction with GORASP2By similarityAdd BLAST | 95 | |
Regioni | 1446 – 1476 | DisorderedSequence analysisAdd BLAST | 31 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 1474 – 1476 | PDZ-bindingBy similarity | 3 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 1458 – 1476 | Basic and acidic residuesSequence analysisAdd BLAST | 19 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Repeat, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG0054, Eukaryota |
GeneTreei | ENSGT00940000158567 |
HOGENOMi | CLU_000604_27_14_1 |
InParanoidi | P26361 |
OMAi | WRFTFYG |
OrthoDBi | 138195at2759 |
PhylomeDBi | P26361 |
TreeFami | TF105200 |
Family and domain databases
Gene3Di | 1.20.1560.10, 2 hits 3.40.50.300, 2 hits |
InterProi | View protein in InterPro IPR003593, AAA+_ATPase IPR011527, ABC1_TM_dom IPR036640, ABC1_TM_sf IPR003439, ABC_transporter-like_ATP-bd IPR017871, ABC_transporter-like_CS IPR009147, CFTR/ABCC7 IPR025837, CFTR_reg_dom IPR027417, P-loop_NTPase |
PANTHERi | PTHR24223:SF19, PTHR24223:SF19, 1 hit |
Pfami | View protein in Pfam PF00664, ABC_membrane, 2 hits PF00005, ABC_tran, 2 hits PF14396, CFTR_R, 1 hit |
PRINTSi | PR01851, CYSFIBREGLTR |
SMARTi | View protein in SMART SM00382, AAA, 2 hits |
SUPFAMi | SSF52540, SSF52540, 2 hits SSF90123, SSF90123, 2 hits |
TIGRFAMsi | TIGR01271, CFTR_protein, 1 hit |
PROSITEi | View protein in PROSITE PS50929, ABC_TM1F, 2 hits PS00211, ABC_TRANSPORTER_1, 1 hit PS50893, ABC_TRANSPORTER_2, 2 hits |
s (3+)i Sequence
Sequence statusi: Complete.
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketE9PVD7 | E9PVD7_MOUSE | Cystic fibrosis transmembrane condu... | Cftr | 1,446 | Annotation score: | ||
F6U9G7 | F6U9G7_MOUSE | Cystic fibrosis transmembrane condu... | Cftr | 529 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 20 – 22 | TTP → STA in AAF30300 (PubMed:10655503).Curated | 3 | |
Sequence conflicti | 30 | H → Q in AAF30300 (PubMed:10655503).Curated | 1 | |
Sequence conflicti | 410 – 412 | EKV → QKA in AAA37417 (PubMed:1712752).Curated | 3 | |
Sequence conflicti | 462 | S → L in AAA37417 (PubMed:1712752).Curated | 1 | |
Sequence conflicti | 623 | S → T in AAA37417 (PubMed:1712752).Curated | 1 | |
Sequence conflicti | 639 | D → S in AAA37417 (PubMed:1712752).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_000064 | 561 – 600 | AVYKD…ANKTR → QRTRSPYLEIRIFLCLFLYT RMKVCATTPEQYIKMLICTY in isoform 3. CuratedAdd BLAST | 40 | |
Alternative sequenceiVSP_000062 | 561 – 576 | AVYKD…DSPFG → FLICLQTKDKVSLFRN in isoform 2. CuratedAdd BLAST | 16 | |
Alternative sequenceiVSP_000063 | 577 – 1476 | Missing in isoform 2. CuratedAdd BLAST | 900 | |
Alternative sequenceiVSP_000065 | 601 – 1476 | Missing in isoform 3. CuratedAdd BLAST | 876 |
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 |
CCDSi | CCDS19930.1 [P26361-1] |
PIRi | A39901 A40303 I49593 I58115 I78527 |
RefSeqi | NP_066388.1, NM_021050.2 [P26361-1] XP_006505040.1, XM_006504977.1 XP_006505041.1, XM_006504978.1 |
Genome annotation databases
Ensembli | ENSMUST00000045706; ENSMUSP00000049228; ENSMUSG00000041301 [P26361-1] ENSMUST00000115405; ENSMUSP00000111064; ENSMUSG00000041301 [P26361-3] ENSMUST00000140407; ENSMUSP00000116957; ENSMUSG00000041301 [P26361-2] |
GeneIDi | 12638 |
KEGGi | mmu:12638 |
UCSCi | uc009bai.1, mouse [P26361-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
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 |
CCDSi | CCDS19930.1 [P26361-1] |
PIRi | A39901 A40303 I49593 I58115 I78527 |
RefSeqi | NP_066388.1, NM_021050.2 [P26361-1] XP_006505040.1, XM_006504977.1 XP_006505041.1, XM_006504978.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1Q3H | X-ray | 2.50 | A/B/C/D | 389-673 | [»] | |
1R0W | X-ray | 2.20 | A/B/C/D | 389-673 | [»] | |
1R0X | X-ray | 2.20 | A/B/C/D | 389-673 | [»] | |
1R0Y | X-ray | 2.55 | A/B/C/D | 389-673 | [»] | |
1R0Z | X-ray | 2.35 | A/B/C/D | 389-673 | [»] | |
1R10 | X-ray | 3.00 | A/B | 389-673 | [»] | |
1XF9 | X-ray | 2.70 | A/B/C/D | 389-670 | [»] | |
1XFA | X-ray | 3.10 | A/B | 389-670 | [»] | |
3SI7 | X-ray | 2.25 | A/B/C/D | 389-673 | [»] | |
SMRi | P26361 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 198687, 12 interactors |
DIPi | DIP-29618N |
IntActi | P26361, 10 interactors |
MINTi | P26361 |
STRINGi | 10090.ENSMUSP00000049228 |
PTM databases
GlyGeni | P26361, 2 sites |
iPTMneti | P26361 |
PhosphoSitePlusi | P26361 |
Proteomic databases
MaxQBi | P26361 |
PaxDbi | P26361 |
PeptideAtlasi | P26361 |
PRIDEi | P26361 |
ProteomicsDBi | 281397 [P26361-1] 281398 [P26361-2] 281399 [P26361-3] |
Protocols and materials databases
Antibodypediai | 4530, 1075 antibodies from 41 providers |
DNASUi | 12638 |
Genome annotation databases
Ensembli | ENSMUST00000045706; ENSMUSP00000049228; ENSMUSG00000041301 [P26361-1] ENSMUST00000115405; ENSMUSP00000111064; ENSMUSG00000041301 [P26361-3] ENSMUST00000140407; ENSMUSP00000116957; ENSMUSG00000041301 [P26361-2] |
GeneIDi | 12638 |
KEGGi | mmu:12638 |
UCSCi | uc009bai.1, mouse [P26361-1] |
Organism-specific databases
CTDi | 1080 |
MGIi | MGI:88388, Cftr |
VEuPathDBi | HostDB:ENSMUSG00000041301 |
Phylogenomic databases
eggNOGi | KOG0054, Eukaryota |
GeneTreei | ENSGT00940000158567 |
HOGENOMi | CLU_000604_27_14_1 |
InParanoidi | P26361 |
OMAi | WRFTFYG |
OrthoDBi | 138195at2759 |
PhylomeDBi | P26361 |
TreeFami | TF105200 |
Enzyme and pathway databases
BRENDAi | 2.7.4.3, 3474 5.6.1.6, 3474 |
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 R-MMU-9013406, RHOQ GTPase cycle R-MMU-9646399, Aggrephagy |
Miscellaneous databases
BioGRID-ORCSi | 12638, 2 hits in 64 CRISPR screens |
ChiTaRSi | Cftr, mouse |
EvolutionaryTracei | P26361 |
PROi | PR:P26361 |
RNActi | P26361, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000041301, Expressed in paneth cell and 160 other tissues |
ExpressionAtlasi | P26361, baseline and differential |
Genevisiblei | P26361, MM |
Family and domain databases
Gene3Di | 1.20.1560.10, 2 hits 3.40.50.300, 2 hits |
InterProi | View protein in InterPro IPR003593, AAA+_ATPase IPR011527, ABC1_TM_dom IPR036640, ABC1_TM_sf IPR003439, ABC_transporter-like_ATP-bd IPR017871, ABC_transporter-like_CS IPR009147, CFTR/ABCC7 IPR025837, CFTR_reg_dom IPR027417, P-loop_NTPase |
PANTHERi | PTHR24223:SF19, PTHR24223:SF19, 1 hit |
Pfami | View protein in Pfam PF00664, ABC_membrane, 2 hits PF00005, ABC_tran, 2 hits PF14396, CFTR_R, 1 hit |
PRINTSi | PR01851, CYSFIBREGLTR |
SMARTi | View protein in SMART SM00382, AAA, 2 hits |
SUPFAMi | SSF52540, SSF52540, 2 hits SSF90123, SSF90123, 2 hits |
TIGRFAMsi | TIGR01271, CFTR_protein, 1 hit |
PROSITEi | View protein in PROSITE PS50929, ABC_TM1F, 2 hits PS00211, ABC_TRANSPORTER_1, 1 hit PS50893, ABC_TRANSPORTER_2, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | CFTR_MOUSE | |
Accessioni | P26361Primary (citable) accession number: P26361 Secondary accession number(s): Q63893, Q63894, Q9JKQ6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 1, 1992 |
Last sequence update: | January 31, 2002 | |
Last modified: | February 23, 2022 | |
This is version 206 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families