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UniProtKB - P26361 (CFTR_MOUSE)

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Protein

Cystic fibrosis transmembrane conductance regulator

Gene

Cftr

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

Functioni

Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis (PubMed:26823428). Mediates the transport of chloride ions across the cell membrane (PubMed:20231442, PubMed:22265409). Channel activity is coupled to ATP hydrolysis. The ion channel is also permeable to HCO3-; selectivity depends on the extracellular chloride concentration. Exerts its function also by modulating the activity of other ion channels and transporters. Contributes to the regulation of the pH and the ion content of the epithelial fluid layer. Modulates the activity of the epithelial sodium channel (ENaC) complex, in part by regulating the cell surface expression of the ENaC complex. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the transporter SLC4A7. Can inhibit the chloride channel activity of ANO1 (By similarity). Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation (PubMed:21976599).By similarity5 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei401ATP 1By similarity1
Binding sitei493ATP 1Combined sources1
Binding sitei1215ATP 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi458 – 465ATP 1PROSITE-ProRule annotationCombined sources8
Nucleotide bindingi1240 – 1247ATP 2PROSITE-ProRule annotation8

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

  • 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
  • intracellular pH elevation Source: UniProtKB
  • iodide transport Source: MGI
  • 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 blood vessel diameter Source: MGI
  • positive regulation of cyclic nucleotide-gated ion channel activity Source: UniProtKB
  • 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
  • sperm capacitation Source: UniProtKB
  • transepithelial chloride transport Source: MGI
  • transepithelial water transport Source: UniProtKB
  • vasodilation Source: MGI
  • vesicle docking involved in exocytosis Source: UniProtKB
  • water transport Source: MGI
View the complete GO annotation on QuickGO ...

Keywordsi

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

Enzyme and pathway databases

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

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:3.6.3.49By similarity)
cAMP-dependent chloride channel
Gene namesi
Name:Cftr
Synonyms:Abcc7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:88388 Cftr

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 77CytoplasmicBy similarityAdd BLAST77
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

Pathology & Biotechi

Disruption phenotypei

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi508F → A, L or Q: Mildly impairs protein maturation. 1 Publication1
Mutagenesisi508F → C or M: No effect on protein maturation. 1 Publication1
Mutagenesisi508F → E, D, G, H, I, K, P, R or Y: Abolishes normal maturation. 1 Publication1
Mutagenesisi508F → N, S or V: Nearly abolishes normal maturation. 1 Publication1
Mutagenesisi508Missing : Impairs protein folding, due to small local changes that probably disrupt crucial interactions with the transmembrane domain. Abolishes normal maturation. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000934241 – 1476Cystic fibrosis transmembrane conductance regulatorAdd BLAST1476

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi524S-palmitoyl cysteineBy similarity1
Modified residuei549PhosphoserineBy similarity1
Modified residuei660PhosphoserineBy similarity1
Modified residuei670Phosphoserine; by PKABy similarity1
Modified residuei684PhosphoserineBy similarity1
Modified residuei698PhosphoserineCombined sources1
Modified residuei710PhosphoserineBy similarity1
Modified residuei715PhosphothreonineBy similarity1
Modified residuei732PhosphoserineBy similarity1
Modified residuei763PhosphoserineBy similarity1
Modified residuei785PhosphoserineBy similarity1
Modified residuei790PhosphoserineCombined sources1
Modified residuei808PhosphoserineBy similarity1
Glycosylationi889N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi895N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi1391S-palmitoyl cysteineBy similarity1
Modified residuei1440PhosphoserineBy similarity1
Modified residuei1452PhosphoserineBy similarity1

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

MaxQBiP26361
PaxDbiP26361
PeptideAtlasiP26361
PRIDEiP26361

PTM databases

iPTMnetiP26361
PhosphoSitePlusiP26361

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000041301
ExpressionAtlasiP26361 baseline and differential
GenevisibleiP26361 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).By similarity3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

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

Structurei

Secondary structure

11476
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi392 – 400Combined sources9
Helixi405 – 412Combined sources8
Helixi423 – 425Combined sources3
Helixi430 – 435Combined sources6
Beta strandi439 – 448Combined sources10
Beta strandi453 – 459Combined sources7
Helixi464 – 471Combined sources8
Beta strandi478 – 483Combined sources6
Beta strandi488 – 491Combined sources4
Beta strandi499 – 501Combined sources3
Helixi502 – 506Combined sources5
Turni507 – 509Combined sources3
Helixi514 – 523Combined sources10
Helixi527 – 530Combined sources4
Helixi536 – 538Combined sources3
Helixi543 – 545Combined sources3
Helixi550 – 563Combined sources14
Beta strandi567 – 573Combined sources7
Helixi580 – 589Combined sources10
Helixi590 – 594Combined sources5
Turni595 – 597Combined sources3
Beta strandi598 – 603Combined sources6
Helixi607 – 611Combined sources5
Beta strandi614 – 620Combined sources7
Beta strandi623 – 628Combined sources6
Helixi630 – 636Combined sources7
Helixi638 – 645Combined sources8
Beta strandi647 – 649Combined sources3
Helixi650 – 652Combined sources3
Helixi655 – 668Combined sources14

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP26361

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini81 – 365ABC transmembrane type-1 1PROSITE-ProRule annotationAdd BLAST285
Domaini423 – 646ABC transporter 1PROSITE-ProRule annotationAdd BLAST224
Domaini854 – 1153ABC transmembrane type-1 2PROSITE-ProRule annotationAdd BLAST300
Domaini1208 – 1439ABC transporter 2PROSITE-ProRule annotationAdd BLAST232

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni654 – 826Intrinsically disordered R regionBy similarityAdd BLAST173

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1474 – 1476PDZ-bindingBy similarity3

Domaini

Binds and hydrolyzes ATP via the two cytoplasmic ABC transporter nucleotide-binding domains. The two ATP-binding domains interact with each other, forming a head-to-tail dimer. Normal ATPase activity requires interaction between the two domains (By similarity). The first ABC transporter nucleotide-binding domain has no ATPase activity by itself (PubMed:14685259, PubMed:15619636).By similarity2 Publications
The PDZ-binding motif mediates interactions with GOPC and with the SLC4A7, SLC9A3R1/EBP50 complex.By similarity
The R region is intrinsically disordered. It mediates channel activation when it is phosphorylated, but not in the absence of phosphorylation.By similarity

Sequence similaritiesi

Belongs to the ABC transporter superfamily. ABCC family. CFTR transporter (TC 3.A.1.202) subfamily. [View classification]Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0054 Eukaryota
COG1132 LUCA
GeneTreeiENSGT00880000137856
HOGENOMiHOG000185880
HOVERGENiHBG004169
InParanoidiP26361
KOiK05031
OMAiLAHFVWI
OrthoDBiEOG091G00K4
PhylomeDBiP26361
TreeFamiTF105200

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, 3 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

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000064561 – 600AVYKD…ANKTR → QRTRSPYLEIRIFLCLFLYT RMKVCATTPEQYIKMLICTY in isoform 3. CuratedAdd BLAST40
Alternative sequenceiVSP_000062561 – 576AVYKD…DSPFG → FLICLQTKDKVSLFRN in isoform 2. CuratedAdd BLAST16
Alternative sequenceiVSP_000063577 – 1476Missing in isoform 2. CuratedAdd BLAST900
Alternative sequenceiVSP_000065601 – 1476Missing in isoform 3. CuratedAdd BLAST876

Sequence databases

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

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

Similar proteinsi

Entry informationi

Entry nameiCFTR_MOUSE
AccessioniPrimary (citable) accession number: P26361
Secondary accession number(s): Q63893, Q63894, Q9JKQ6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 31, 2002
Last modified: June 20, 2018
This is version 184 of the entry and version 2 of the sequence. See 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

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