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P26361

- CFTR_MOUSE

UniProt

P26361 - CFTR_MOUSE

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Protein

Cystic fibrosis transmembrane conductance regulator

Gene

Cftr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in the transport of chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the SLC4A7 transporter. 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 similarity1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi458 – 4658ATP 1PROSITE-ProRule annotation
Nucleotide bindingi1240 – 12478ATP 2PROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. bicarbonate transmembrane transporter activity Source: UniProtKB
  3. channel-conductance-controlling ATPase activity Source: UniProtKB-EC
  4. chloride channel activity Source: UniProtKB
  5. chloride channel inhibitor activity Source: UniProtKB
  6. chloride transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  1. cellular response to cAMP Source: UniProtKB
  2. cellular response to hormone stimulus Source: Ensembl
  3. chloride transmembrane transport Source: GOC
  4. chloride transport Source: MGI
  5. cholesterol biosynthetic process Source: MGI
  6. cholesterol transport Source: MGI
  7. intracellular pH elevation Source: UniProtKB
  8. iodide transport Source: Ensembl
  9. lung development Source: Ensembl
  10. membrane hyperpolarization Source: UniProtKB
  11. positive regulation of vasodilation Source: Ensembl
  12. positive regulation of voltage-gated chloride channel activity Source: Ensembl
  13. response to cytokine Source: Ensembl
  14. response to drug Source: Ensembl
  15. response to estrogen Source: Ensembl
  16. response to peptide hormone Source: Ensembl
  17. sperm capacitation Source: UniProtKB
  18. transepithelial chloride transport Source: Ensembl
  19. vasodilation Source: Ensembl
  20. water transport Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chloride channel, Hydrolase, Ion channel

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

ATP-binding, Chloride, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.3.49. 3474.

Names & Taxonomyi

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:3.6.3.49)
cAMP-dependent chloride channel
Gene namesi
Name:Cftr
Synonyms:Abcc7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:88388. Cftr.

Subcellular locationi

Early endosome membrane By similarity; Multi-pass membrane protein PROSITE-ProRule annotation. Cell membrane By similarity
Note: In epithelial cells, detected on the apical side, but not associated with cilia.By similarity

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. basolateral plasma membrane Source: Ensembl
  3. cell surface Source: Ensembl
  4. chloride channel complex Source: UniProtKB-KW
  5. cytoplasmic vesicle membrane Source: Ensembl
  6. early endosome Source: UniProtKB
  7. endoplasmic reticulum Sec complex Source: Ensembl
  8. extracellular vesicular exosome Source: Ensembl
  9. microvillus Source: Ensembl
  10. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14761476Cystic fibrosis transmembrane conductance regulatorPRO_0000093424Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi524 – 5241S-palmitoyl cysteineBy similarity
Modified residuei549 – 5491PhosphoserineBy similarity
Modified residuei660 – 6601PhosphoserineBy similarity
Modified residuei684 – 6841PhosphoserineBy similarity
Modified residuei698 – 6981PhosphoserineBy similarity
Modified residuei710 – 7101PhosphoserineBy similarity
Modified residuei715 – 7151PhosphothreonineBy similarity
Modified residuei732 – 7321PhosphoserineBy similarity
Modified residuei763 – 7631PhosphoserineBy similarity
Modified residuei785 – 7851PhosphoserineBy similarity
Modified residuei790 – 7901PhosphoserineBy similarity
Modified residuei808 – 8081PhosphoserineBy similarity
Glycosylationi889 – 8891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi895 – 8951N-linked (GlcNAc...)Sequence Analysis
Lipidationi1391 – 13911S-palmitoyl cysteineBy similarity
Modified residuei1440 – 14401PhosphoserineBy similarity
Modified residuei1452 – 14521PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated, leading to its degradation in the lysosome. Deubiquitination by USP10 in early endosomes, enhances its endocytic recycling. Ubiquitinated by RNF185 during ER stress (By similarity).By similarity
Phosphorylated; activates the channel. It is not clear whether PKC phosphorylation itself activates the channel or permits activation by phosphorylation at PKA sites. Phosphorylated by AMPK (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP26361.

PTM databases

PhosphoSiteiP26361.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP26361.
ExpressionAtlasiP26361. baseline and differential.
GenevestigatoriP26361.

Interactioni

Subunit structurei

Interacts with MYO6 and GOPC. Interacts with SLC4A7 through SLC9A3R1. Interacts with SHANK2 (By similarity). Found in a complex with MYO5B and RAB11A (By similarity). Interacts with ANO1 (By similarity). Interacts with SLC26A3, SLC26A6 and SLC9A3R1. Interacts with SLC26A8 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
HSPA8P191205EBI-6115317,EBI-907802From a different organism.
Slc26a3Q9WVC83EBI-6115317,EBI-6895537
Slc26a6Q8CIW63EBI-6115317,EBI-6895517
Slc9a3r1P704413EBI-6115317,EBI-1184085

Protein-protein interaction databases

BioGridi198687. 2 interactions.
DIPiDIP-29618N.
IntActiP26361. 9 interactions.
MINTiMINT-2841263.

Structurei

Secondary structure

1
1476
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi392 – 4009
Helixi405 – 4128
Helixi423 – 4253
Helixi430 – 4356
Beta strandi439 – 44810
Beta strandi453 – 4597
Helixi464 – 4718
Beta strandi478 – 4836
Beta strandi488 – 4914
Beta strandi499 – 5013
Helixi502 – 5065
Turni507 – 5093
Helixi514 – 52310
Helixi527 – 5304
Helixi536 – 5383
Helixi543 – 5453
Helixi550 – 56314
Beta strandi567 – 5737
Helixi580 – 58910
Helixi590 – 5945
Turni595 – 5973
Beta strandi598 – 6036
Helixi607 – 6115
Beta strandi614 – 6207
Beta strandi623 – 6286
Helixi630 – 6367
Helixi638 – 6458
Beta strandi647 – 6493
Helixi650 – 6523
Helixi655 – 66814

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 389-670, 1198-1446.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26361.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8080CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini104 – 11714ExtracellularSequence AnalysisAdd
BLAST
Topological domaini139 – 19456CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini216 – 2205ExtracellularSequence Analysis
Topological domaini242 – 30766CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini329 – 3302ExtracellularSequence Analysis
Topological domaini351 – 854504CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini876 – 90631ExtracellularSequence AnalysisAdd
BLAST
Topological domaini928 – 98558CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1007 – 10082ExtracellularSequence Analysis
Topological domaini1030 – 109768CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1119 – 11235ExtracellularSequence Analysis
Topological domaini1145 – 1476332CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei81 – 10323Helical; Name=1PROSITE-ProRule annotationAdd
BLAST
Transmembranei118 – 13821Helical; Name=2PROSITE-ProRule annotationAdd
BLAST
Transmembranei195 – 21521Helical; Name=3PROSITE-ProRule annotationAdd
BLAST
Transmembranei221 – 24121Helical; Name=4PROSITE-ProRule annotationAdd
BLAST
Transmembranei308 – 32821Helical; Name=5PROSITE-ProRule annotationAdd
BLAST
Transmembranei331 – 35020Helical; Name=6PROSITE-ProRule annotationAdd
BLAST
Transmembranei855 – 87521Helical; Name=7PROSITE-ProRule annotationAdd
BLAST
Transmembranei907 – 92721Helical; Name=8PROSITE-ProRule annotationAdd
BLAST
Transmembranei986 – 100621Helical; Name=9PROSITE-ProRule annotationAdd
BLAST
Transmembranei1009 – 102921Helical; Name=10PROSITE-ProRule annotationAdd
BLAST
Transmembranei1098 – 111821Helical; Name=11PROSITE-ProRule annotationAdd
BLAST
Transmembranei1124 – 114421Helical; Name=12PROSITE-ProRule annotationAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 365285ABC transmembrane type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini423 – 646224ABC transporter 1PROSITE-ProRule annotationAdd
BLAST
Domaini854 – 1153300ABC transmembrane type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini1208 – 1439232ABC transporter 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1474 – 14763PDZ-binding

Domaini

The PDZ-binding motif mediates interactions with GOPC and with the SLC4A7, SLC9A3R1/EBP50 complex.By similarity

Sequence similaritiesi

Contains 2 ABC transmembrane type-1 domains.PROSITE-ProRule annotation
Contains 2 ABC transporter domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1132.
GeneTreeiENSGT00760000119056.
HOGENOMiHOG000185880.
HOVERGENiHBG004169.
InParanoidiP26361.
KOiK05031.
OMAiTLAMNIM.
OrthoDBiEOG7C2R0B.
PhylomeDBiP26361.
TreeFamiTF105200.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR005291. cAMP_cl_channel.
IPR025837. CFTR_reg_dom.
IPR009147. CysFib_conduc_TM.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00664. ABC_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
PF14396. CFTR_R. 1 hit.
[Graphical view]
PRINTSiPR01851. CYSFIBREGLTR.
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF90123. SSF90123. 3 hits.
TIGRFAMsiTIGR01271. CFTR_protein. 1 hit.
PROSITEiPS50929. ABC_TM1F. 2 hits.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

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
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 223TTP → STA in AAF30300. (PubMed:10655503)Curated
Sequence conflicti30 – 301H → Q in AAF30300. (PubMed:10655503)Curated
Sequence conflicti410 – 4123EKV → QKA in AAA37417. (PubMed:1712752)Curated
Sequence conflicti462 – 4621S → L in AAA37417. (PubMed:1712752)Curated
Sequence conflicti623 – 6231S → T in AAA37417. (PubMed:1712752)Curated
Sequence conflicti639 – 6391D → S in AAA37417. (PubMed:1712752)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei561 – 60040AVYKD…ANKTR → QRTRSPYLEIRIFLCLFLYT RMKVCATTPEQYIKMLICTY in isoform 3. CuratedVSP_000064Add
BLAST
Alternative sequencei561 – 57616AVYKD…DSPFG → FLICLQTKDKVSLFRN in isoform 2. CuratedVSP_000062Add
BLAST
Alternative sequencei577 – 1476900Missing in isoform 2. CuratedVSP_000063Add
BLAST
Alternative sequencei601 – 1476876Missing in isoform 3. CuratedVSP_000065Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

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]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. [P26361-1 ]
XP_006505041.1. XM_006504978.1. [P26361-1 ]
UniGenei Mm.15621.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P26361.
SMRi P26361. Positions 389-670, 1198-1446.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198687. 2 interactions.
DIPi DIP-29618N.
IntActi P26361. 9 interactions.
MINTi MINT-2841263.

PTM databases

PhosphoSitei P26361.

Proteomic databases

PRIDEi P26361.

Protocols and materials databases

DNASUi 12638.
Structural Biology Knowledgebase Search...

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.

Phylogenomic databases

eggNOGi COG1132.
GeneTreei ENSGT00760000119056.
HOGENOMi HOG000185880.
HOVERGENi HBG004169.
InParanoidi P26361.
KOi K05031.
OMAi TLAMNIM.
OrthoDBi EOG7C2R0B.
PhylomeDBi P26361.
TreeFami TF105200.

Enzyme and pathway databases

BRENDAi 3.6.3.49. 3474.

Miscellaneous databases

EvolutionaryTracei P26361.
NextBioi 281830.
PROi P26361.
SOURCEi Search...

Gene expression databases

Bgeei P26361.
ExpressionAtlasi P26361. baseline and differential.
Genevestigatori P26361.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR005291. cAMP_cl_channel.
IPR025837. CFTR_reg_dom.
IPR009147. CysFib_conduc_TM.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00664. ABC_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
PF14396. CFTR_R. 1 hit.
[Graphical view ]
PRINTSi PR01851. CYSFIBREGLTR.
SMARTi SM00382. AAA. 2 hits.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
SSF90123. SSF90123. 3 hits.
TIGRFAMsi TIGR01271. CFTR_protein. 1 hit.
PROSITEi PS50929. ABC_TM1F. 2 hits.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
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Publicationsi

  1. "Cloning the mouse homolog of the human cystic fibrosis transmembrane conductance regulator gene."
    Tata F., Stanier P., Wicking C., Halford S., Kruyer H., Lench N.J., Scambler P.J., Hansen C., Braman J.C., Williamson R., Wainwright B.J.
    Genomics 10:301-307(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning and sequence analysis of the murine cDNA for the cystic fibrosis transmembrane conductance regulator."
    Yorifuji T., Lemna W.K., Ballard C.F., Rosenbloom C.L., Rozmahel R., Plavsic N., Tsui L.-C., Beaudet A.L.
    Genomics 10:547-550(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Analysis of the mouse and rat CFTR promoter regions."
    Denamur E., Chehab F.F.
    Hum. Mol. Genet. 3:1089-1094(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
  5. "Cystic fibrosis transmembrane conductance regulator splice variants are not conserved and fail to produce chloride channels."
    Delaney S.J., Rich D.P., Thomson S.A., Hargrave M.R., Lovelock P.K., Welsh M.J., Wainwright B.J.
    Nat. Genet. 4:426-431(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 549-600, ALTERNATIVE SPLICING.
    Tissue: Testis.
  6. "Participation of the Cl-/HCO(3)- exchangers SLC26A3 and SLC26A6, the Cl- channel CFTR, and the regulatory factor SLC9A3R1 in mouse sperm capacitation."
    Chavez J.C., Hernandez-Gonzalez E.O., Wertheimer E., Visconti P.E., Darszon A., Trevino C.L.
    Biol. Reprod. 86:1-14(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SLC26A3; SLC26A6 AND SLC9A3R1.

Entry informationi

Entry nameiCFTR_MOUSE
AccessioniPrimary (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: October 29, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3