P26361 (CFTR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Cftr
Synonyms:	Abcc7

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1476 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Interacts with MYO6, SLC9A3R1 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.
Subcellular location	Early endosome membrane; Multi-pass membrane protein By similarity. Cell membrane By similarity.
Tissue specificity	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.
Domain	The PDZ-binding motif mediates interactions with GOPC and with the SLC4A7, SLC9A3R1/EBP50 complex By similarity.
Post-translational modification	Ubiquitinated, leading to its degradation in the lysosome. Deubiquitination by USP10 in early endosomes, enhances its endocytic recycling 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.
Sequence similarities	Belongs to the ABC transporter superfamily. ABCC family. CFTR transporter (TC 3.A.1.202) subfamily. [View classification] Contains 2 ABC transmembrane type-1 domains. Contains 2 ABC transporter domains.

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell membrane Endosome Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Chloride Nucleotide-binding
Molecular function	Chloride channel Hydrolase Ion channel
PTM	Glycoprotein Lipoprotein Palmitate Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC bicarbonate transport Inferred from electronic annotation. Source: Compara cellular response to hormone stimulus Inferred from electronic annotation. Source: Compara cholesterol biosynthetic process Inferred from mutant phenotype PubMed 17085523. Source: MGI cholesterol transport Inferred from mutant phenotype PubMed 17085523. Source: MGI iodide transport Inferred from electronic annotation. Source: Compara lung development Inferred from electronic annotation. Source: Compara positive regulation of vasodilation Inferred from electronic annotation. Source: Compara response to cytokine stimulus Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to estrogen stimulus Inferred from electronic annotation. Source: Compara response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara transepithelial chloride transport Inferred from electronic annotation. Source: Compara vasodilation Inferred from electronic annotation. Source: Compara water transport Inferred from electronic annotation. Source: Compara
Cellular_component	apical plasma membrane Inferred from electronic annotation. Source: Compara basolateral plasma membrane Inferred from electronic annotation. Source: Compara chloride channel complex Inferred from electronic annotation. Source: UniProtKB-KW cytoplasmic vesicle membrane Inferred from electronic annotation. Source: Compara early endosome Inferred from sequence or structural similarity. Source: UniProtKB early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Sec complex Inferred from electronic annotation. Source: Compara microvillus Inferred from electronic annotation. Source: Compara plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW channel-conductance-controlling ATPase activity Inferred from electronic annotation. Source: EC chloride channel activity Inferred from sequence or structural similarity. Source: UniProtKB chloride channel inhibitor activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P26361-1)

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.

Isoform 2 (identifier: P26361-2)

The sequence of this isoform differs from the canonical sequence as follows:
     561-576: AVYKDADLYLLDSPFG → FLICLQTKDKVSLFRN
     577-1476: Missing.

Isoform 3 (identifier: P26361-3)

The sequence of this isoform differs from the canonical sequence as follows:
     561-600: AVYKDADLYL...VCKLMANKTR → QRTRSPYLEI...QYIKMLICTY
     601-1476: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1476

1476

Cystic fibrosis transmembrane conductance regulator

PRO_0000093424

Regions

Topological domain

1 – 80

80

Cytoplasmic Potential

Transmembrane

81 – 103

23

Helical; Name=1; Potential

Topological domain

104 – 117

14

Extracellular Potential

Transmembrane

118 – 138

21

Helical; Name=2; Potential

Topological domain

139 – 194

56

Cytoplasmic Potential

Transmembrane

195 – 215

21

Helical; Name=3; Potential

Topological domain

216 – 220

5

Extracellular Potential

Transmembrane

221 – 241

21

Helical; Name=4; Potential

Topological domain

242 – 307

66

Cytoplasmic Potential

Transmembrane

308 – 328

21

Helical; Name=5; Potential

Topological domain

329 – 330

2

Extracellular Potential

Transmembrane

331 – 350

20

Helical; Name=6; Potential

Topological domain

351 – 854

504

Cytoplasmic Potential

Transmembrane

855 – 875

21

Helical; Name=7; Potential

Topological domain

876 – 906

31

Extracellular Potential

Transmembrane

907 – 927

21

Helical; Name=8; Potential

Topological domain

928 – 985

58

Cytoplasmic Potential

Transmembrane

986 – 1006

21

Helical; Name=9; Potential

Topological domain

1007 – 1008

2

Extracellular Potential

Transmembrane

1009 – 1029

21

Helical; Name=10; Potential

Topological domain

1030 – 1097

68

Cytoplasmic Potential

Transmembrane

1098 – 1118

21

Helical; Name=11; Potential

Topological domain

1119 – 1123

5

Extracellular Potential

Transmembrane

1124 – 1144

21

Helical; Name=12; Potential

Topological domain

1145 – 1476

332

Cytoplasmic Potential

Domain

81 – 365

285

ABC transmembrane type-1 1

Domain

423 – 646

224

ABC transporter 1

Domain

854 – 1153

300

ABC transmembrane type-1 2

Domain

1208 – 1439

232

ABC transporter 2

Nucleotide binding

458 – 465

8

ATP 1 Potential

Nucleotide binding

1240 – 1247

8

ATP 2 Potential

Motif

1474 – 1476

3

PDZ-binding

Amino acid modifications

Modified residue

549

1

Phosphoserine By similarity

Modified residue

660

1

Phosphoserine By similarity

Modified residue

684

1

Phosphoserine By similarity

Modified residue

698

1

Phosphoserine By similarity

Modified residue

710

1

Phosphoserine By similarity

Modified residue

715

1

Phosphothreonine By similarity

Modified residue

732

1

Phosphoserine By similarity

Modified residue

763

1

Phosphoserine By similarity

Modified residue

785

1

Phosphoserine By similarity

Modified residue

790

1

Phosphoserine By similarity

Modified residue

808

1

Phosphoserine By similarity

Modified residue

1440

1

Phosphoserine By similarity

Modified residue

1452

1

Phosphoserine By similarity

Lipidation

524

1

S-palmitoyl cysteine By similarity

Lipidation

1391

1

S-palmitoyl cysteine By similarity

Glycosylation

889

1

N-linked (GlcNAc...) Potential

Glycosylation

895

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

561 – 600

40

AVYKD…ANKTR → QRTRSPYLEIRIFLCLFLYT RMKVCATTPEQYIKMLICTY in isoform 3.

VSP_000064

Alternative sequence

561 – 576

16

AVYKD…DSPFG → FLICLQTKDKVSLFRN in isoform 2.

VSP_000062

Alternative sequence

577 – 1476

900

Missing in isoform 2.

VSP_000063

Alternative sequence

601 – 1476

876

Missing in isoform 3.

VSP_000065

Experimental info

Sequence conflict

20 – 22

3

TTP → STA in AAF30300. Ref.3

Sequence conflict

30

1

H → Q in AAF30300. Ref.3

Sequence conflict

410 – 412

3

EKV → QKA in AAA37417. Ref.1

Sequence conflict

462

1

S → L in AAA37417. Ref.1

Sequence conflict

623

1

S → T in AAA37417. Ref.1

Sequence conflict

639

1

D → S in AAA37417. Ref.1

Secondary structure

1

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1476

Helix Strand Turn

Details...

Beta strand

392 – 400

9

Helix

405 – 412

8

Helix

423 – 425

3

Helix

430 – 435

6

Beta strand

439 – 448

10

Beta strand

453 – 459

7

Helix

464 – 471

8

Beta strand

478 – 483

6

Beta strand

488 – 491

4

Beta strand

499 – 501

3

Helix

502 – 506

5

Turn

507 – 509

3

Helix

514 – 523

10

Helix

527 – 530

4

Helix

536 – 538

3

Helix

543 – 545

3

Helix

550 – 563

14

Beta strand

567 – 573

7

Helix

580 – 589

10

Helix

590 – 594

5

Turn

595 – 597

3

Beta strand

598 – 603

6

Helix

607 – 611

5

Beta strand

614 – 620

7

Beta strand

623 – 628

6

Helix

630 – 636

7

Helix

638 – 645

8

Beta strand

647 – 649

3

Helix

650 – 652

3

Helix

655 – 668

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 31, 2002. Version 2. Checksum: 3D1B0BBDD80C1DA8	FASTA	1,476	167,870
	10 20 30 40 50 60 MQKSPLEKAS FISKLFFSWT TPILRKGYRH HLELSDIYQA PSADSADHLS EKLEREWDRE 70 80 90 100 110 120 QASKKNPQLI HALRRCFFWR FLFYGILLYL GEVTKAVQPV LLGRIIASYD PENKVERSIA 130 140 150 160 170 180 IYLGIGLCLL FIVRTLLLHP AIFGLHRIGM QMRTAMFSLI YKKTLKLSSR VLDKISIGQL 190 200 210 220 230 240 VSLLSNNLNK FDEGLALAHF IWIAPLQVTL LMGLLWDLLQ FSAFCGLGLL IILVIFQAIL 250 260 270 280 290 300 GKMMVKYRDQ RAAKINERLV ITSEIIDNIY SVKAYCWESA MEKMIENLRE VELKMTRKAA 310 320 330 340 350 360 YMRFFTSSAF FFSGFFVVFL SVLPYTVING IVLRKIFTTI SFCIVLRMSV TRQFPTAVQI 370 380 390 400 410 420 WYDSFGMIRK IQDFLQKQEY KVLEYNLMTT GIIMENVTAF WEEGFGELLE KVQQSNGDRK 430 440 450 460 470 480 HSSDENNVSF SHLCLVGNPV LKNINLNIEK GEMLAITGST GSGKTSLLML ILGELEASEG 490 500 510 520 530 540 IIKHSGRVSF CSQFSWIMPG TIKENIIFGV SYDEYRYKSV VKACQLQQDI TKFAEQDNTV 550 560 570 580 590 600 LGEGGVTLSG GQRARISLAR AVYKDADLYL LDSPFGYLDV FTEEQVFESC VCKLMANKTR 610 620 630 640 650 660 ILVTSKMEHL RKADKILILH QGSSYFYGTF SELQSLRPDF SSKLMGYDTF DQFTEERRSS 670 680 690 700 710 720 ILTETLRRFS VDDSSAPWSK PKQSFRQTGE VGEKRKNSIL NSFSSVRKIS IVQKTPLCID 730 740 750 760 770 780 GESDDLQEKR LSLVPDSEQG EAALPRSNMI ATGPTFPGRR RQSVLDLMTF TPNSGSSNLQ 790 800 810 820 830 840 RTRTSIRKIS LVPQISLNEV DVYSRRLSQD STLNITEEIN EEDLKECFLD DVIKIPPVTT 850 860 870 880 890 900 WNTYLRYFTL HKGLLLVLIW CVLVFLVEVA ASLFVLWLLK NNPVNSGNNG TKISNSSYVV 910 920 930 940 950 960 IITSTSFYYI FYIYVGVADT LLALSLFRGL PLVHTLITAS KILHRKMLHS ILHAPMSTIS 970 980 990 1000 1010 1020 KLKAGGILNR FSKDIAILDD FLPLTIFDFI QLVFIVIGAI IVVSALQPYI FLATVPGLVV 1030 1040 1050 1060 1070 1080 FILLRAYFLH TAQQLKQLES EGRSPIFTHL VTSLKGLWTL RAFRRQTYFE TLFHKALNLH 1090 1100 1110 1120 1130 1140 TANWFMYLAT LRWFQMRIDM IFVLFFIVVT FISILTTGEG EGTAGIILTL AMNIMSTLQW 1150 1160 1170 1180 1190 1200 AVNSSIDTDS LMRSVSRVFK FIDIQTEESM YTQIIKELPR EGSSDVLVIK NEHVKKSDIW 1210 1220 1230 1240 1250 1260 PSGGEMVVKD LTVKYMDDGN AVLENISFSI SPGQRVGLLG RTGSGKSTLL SAFLRMLNIK 1270 1280 1290 1300 1310 1320 GDIEIDGVSW NSVTLQEWRK AFGVITQKVF IFSGTFRQNL DPNGKWKDEE IWKVADEVGL 1330 1340 1350 1360 1370 1380 KSVIEQFPGQ LNFTLVDGGY VLSHGHKQLM CLARSVLSKA KIILLDEPSA HLDPITYQVI 1390 1400 1410 1420 1430 1440 RRVLKQAFAG CTVILCEHRI EAMLDCQRFL VIEESNVWQY DSLQALLSEK SIFQQAISSS 1450 1460 1470 EKMRFFQGRH SSKHKPRTQI TALKEETEEE VQETRL
	Isoform 2 [UniParc]. Checksum: 5EED7EC29AD39CFC	FASTA	576	65,799
	10 20 30 40 50 60 MQKSPLEKAS FISKLFFSWT TPILRKGYRH HLELSDIYQA PSADSADHLS EKLEREWDRE 70 80 90 100 110 120 QASKKNPQLI HALRRCFFWR FLFYGILLYL GEVTKAVQPV LLGRIIASYD PENKVERSIA 130 140 150 160 170 180 IYLGIGLCLL FIVRTLLLHP AIFGLHRIGM QMRTAMFSLI YKKTLKLSSR VLDKISIGQL 190 200 210 220 230 240 VSLLSNNLNK FDEGLALAHF IWIAPLQVTL LMGLLWDLLQ FSAFCGLGLL IILVIFQAIL 250 260 270 280 290 300 GKMMVKYRDQ RAAKINERLV ITSEIIDNIY SVKAYCWESA MEKMIENLRE VELKMTRKAA 310 320 330 340 350 360 YMRFFTSSAF FFSGFFVVFL SVLPYTVING IVLRKIFTTI SFCIVLRMSV TRQFPTAVQI 370 380 390 400 410 420 WYDSFGMIRK IQDFLQKQEY KVLEYNLMTT GIIMENVTAF WEEGFGELLE KVQQSNGDRK 430 440 450 460 470 480 HSSDENNVSF SHLCLVGNPV LKNINLNIEK GEMLAITGST GSGKTSLLML ILGELEASEG 490 500 510 520 530 540 IIKHSGRVSF CSQFSWIMPG TIKENIIFGV SYDEYRYKSV VKACQLQQDI TKFAEQDNTV 550 560 570 LGEGGVTLSG GQRARISLAR FLICLQTKDK VSLFRN
	Isoform 3 [UniParc]. Checksum: C8E6AE26516811C4	FASTA	600	68,782
	10 20 30 40 50 60 MQKSPLEKAS FISKLFFSWT TPILRKGYRH HLELSDIYQA PSADSADHLS EKLEREWDRE 70 80 90 100 110 120 QASKKNPQLI HALRRCFFWR FLFYGILLYL GEVTKAVQPV LLGRIIASYD PENKVERSIA 130 140 150 160 170 180 IYLGIGLCLL FIVRTLLLHP AIFGLHRIGM QMRTAMFSLI YKKTLKLSSR VLDKISIGQL 190 200 210 220 230 240 VSLLSNNLNK FDEGLALAHF IWIAPLQVTL LMGLLWDLLQ FSAFCGLGLL IILVIFQAIL 250 260 270 280 290 300 GKMMVKYRDQ RAAKINERLV ITSEIIDNIY SVKAYCWESA MEKMIENLRE VELKMTRKAA 310 320 330 340 350 360 YMRFFTSSAF FFSGFFVVFL SVLPYTVING IVLRKIFTTI SFCIVLRMSV TRQFPTAVQI 370 380 390 400 410 420 WYDSFGMIRK IQDFLQKQEY KVLEYNLMTT GIIMENVTAF WEEGFGELLE KVQQSNGDRK 430 440 450 460 470 480 HSSDENNVSF SHLCLVGNPV LKNINLNIEK GEMLAITGST GSGKTSLLML ILGELEASEG 490 500 510 520 530 540 IIKHSGRVSF CSQFSWIMPG TIKENIIFGV SYDEYRYKSV VKACQLQQDI TKFAEQDNTV 550 560 570 580 590 600 LGEGGVTLSG GQRARISLAR QRTRSPYLEI RIFLCLFLYT RMKVCATTPE QYIKMLICTY

References

[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]	"Comparative genomic sequence analysis of the human and mouse cystic fibrosis transmembrane conductance regulator genes." Ellsworth R.E., Jamison D.C., Touchman J.W., Chissoe S.L., Braden Maduro V.V., Bouffard G.G., Dietrich N.L., Beckstrom-Sternberg S.M., Iyer L.M., Weintraub L.A., Cotton M., Courtney L., Edwards J., Maupin R., Ozersky P., Rohlfing T., Wohldmann P., Miner T. , Kemp K., Kramer J., Korf I., Pepin K., Antonacci-Fulton L., Fulton R.S., Minx P., Hillier L.W., Wilson R.K., Waterston R.H., Miller W., Green E.D. Proc. Natl. Acad. Sci. U.S.A. 97:1172-1177(2000) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00113739.
IPI00227785.
IPI00227786.

PIR

A39901.
A40303.
I49593.
I58115.
I78527.

RefSeq

NP_066388.1. NM_021050.2.

UniGene

Mm.15621.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P26361.

SMR

P26361. Positions 87-700, 943-1446.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29618N.

IntAct

P26361. 1 interaction.

MINT

MINT-2841263.

PTM databases

PhosphoSite

P26361.

Proteomic databases

PRIDE

P26361.

Protocols and materials databases

DNASU

12638.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000045706; ENSMUSP00000049228; ENSMUSG00000041301.
ENSMUST00000115405; ENSMUSP00000111064; ENSMUSG00000041301.
ENSMUST00000140407; ENSMUSP00000116957; ENSMUSG00000041301.

GeneID

12638.

KEGG

mmu:12638.

UCSC

uc009bai.1. mouse.

Organism-specific databases

CTD

1080.

MGI

MGI:88388. Cftr.

Phylogenomic databases

eggNOG

COG1132.

GeneTree

ENSGT00700000104147.

HOGENOM

HOG000185880.

HOVERGEN

HBG004169.

InParanoid

P26361.

KO

K05031.

OMA

WRKAFGV.

OrthoDB

EOG4KKZ25.

Enzyme and pathway databases

BRENDA

3.6.3.49. 3474.

Gene expression databases

ArrayExpress

P26361.

Bgee

P26361.

Genevestigator

P26361.

Family and domain databases

InterPro

IPR003593. AAA+_ATPase.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR017940. ABC_transporter_type1.
IPR001140. ABC_transptr_TM_dom.
IPR011527. ABC_transptrTM_dom_typ1.
IPR005291. cAMP_cl_channel.
IPR025837. CFTR_reg_dom.
IPR009147. CysFib_conduc_TM.
[Graphical view]

Pfam

PF00664. ABC_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
PF14396. CFTR_R. 1 hit.
[Graphical view]

PRINTS

PR01851. CYSFIBREGLTR.

SMART

SM00382. AAA. 2 hits.
[Graphical view]

SUPFAM

SSF90123. ABC_TM_1. 2 hits.

TIGRFAMs

TIGR01271. CFTR_protein. 1 hit.

PROSITE

PS50929. ABC_TM1F. 2 hits.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P26361.

NextBio

281830.

SOURCE

Search...

Entry information

Entry name

CFTR_MOUSE

Accession

Primary (citable) accession number: P26361
Secondary accession number(s): Q63893, Q63894, Q9JKQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 31, 2002
Last modified:	May 1, 2013
This is version 136 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program