CFTR_DANRE
ID CFTR_DANRE Reviewed; 1485 AA.
AC Q1LX78; B7ZVN9;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cystic fibrosis transmembrane conductance regulator {ECO:0000255|RuleBase:RU362037};
DE EC=5.6.1.6 {ECO:0000255|RuleBase:RU362037, ECO:0000269|PubMed:27912062};
DE AltName: Full=ATP-binding cassette sub-family C member 7 {ECO:0000255|RuleBase:RU362037};
DE AltName: Full=Channel conductance-controlling ATPase {ECO:0000255|RuleBase:RU362037};
DE AltName: Full=cAMP-dependent chloride channel {ECO:0000255|RuleBase:RU362037};
GN Name=cftr {ECO:0000312|ZFIN:ZDB-GENE-050517-20};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Ensembl:ENSDARP00000060242};
RN [1] {ECO:0000312|Ensembl:ENSDARP00000060242, ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Ensembl:ENSDARP00000060242,
RC ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000312|EMBL:AAI71654.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20933420; DOI=10.1016/j.cub.2010.09.012;
RA Bagnat M., Navis A., Herbstreith S., Brand-Arzamendi K., Curado S.,
RA Gabriel S., Mostov K., Huisken J., Stainier D.Y.;
RT "Cse1l is a negative regulator of CFTR-dependent fluid secretion.";
RL Curr. Biol. 20:1840-1845(2010).
RN [4]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=20732993; DOI=10.1128/iai.00302-10;
RA Phennicie R.T., Sullivan M.J., Singer J.T., Yoder J.A., Kim C.H.;
RT "Specific resistance to Pseudomonas aeruginosa infection in zebrafish is
RT mediated by the cystic fibrosis transmembrane conductance regulator.";
RL Infect. Immun. 78:4542-4550(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 205-SER-PRO-206.
RX PubMed=23487313; DOI=10.1242/dev.091819;
RA Navis A., Marjoram L., Bagnat M.;
RT "Cftr controls lumen expansion and function of Kupffer's vesicle in
RT zebrafish.";
RL Development 140:1703-1712(2013).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=26432887; DOI=10.1242/bio.014076;
RA Roxo-Rosa M., Jacinto R., Sampaio P., Lopes S.S.;
RT "The zebrafish Kupffer's vesicle as a model system for the molecular
RT mechanisms by which the lack of Polycystin-2 leads to stimulation of
RT CFTR.";
RL Biol. Open 4:1356-1366(2015).
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND TISSUE SPECIFICITY.
RX PubMed=25592226; DOI=10.1016/j.ydbio.2014.12.034;
RA Navis A., Bagnat M.;
RT "Loss of cftr function leads to pancreatic destruction in larval
RT zebrafish.";
RL Dev. Biol. 399:237-248(2015).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.73 ANGSTROMS), CATALYTIC ACTIVITY,
RP TOPOLOGY, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27912062; DOI=10.1016/j.cell.2016.11.014;
RA Zhang Z., Chen J.;
RT "Atomic structure of the cystic fibrosis transmembrane conductance
RT regulator.";
RL Cell 167:1586-1597(2016).
CC -!- FUNCTION: Epithelial ion channel that plays an important role in the
CC regulation of epithelial ion and water transport and fluid homeostasis
CC (PubMed:20933420, PubMed:23487313, PubMed:25592226). Mediates the
CC transport of chloride ions across the cell membrane (By similarity).
CC Channel activity is coupled to ATP hydrolysis. The ion channel is also
CC permeable to HCO(3)(-); selectivity depends on the extracellular
CC chloride concentration. Exerts its function also by modulating the
CC activity of other ion channels and transporters. Contributes to the
CC regulation of the pH and the ion content of the epithelial fluid layer
CC (By similarity). Required for normal fluid homeostasis in the gut
CC (PubMed:20933420). Required for normal volume expansion of Kupffer's
CC vesicle during embryonic development and for normal establishment of
CC left-right body patterning (PubMed:23487313, PubMed:26432887). Required
CC for normal resistance to infection by P.aeruginosa strain PA14 and
CC strain SMC573 (PubMed:20732993). {ECO:0000250|UniProtKB:P13569,
CC ECO:0000269|PubMed:20732993, ECO:0000269|PubMed:20933420,
CC ECO:0000269|PubMed:23487313, ECO:0000269|PubMed:26432887,
CC ECO:0000305|PubMed:25592226}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + closed Cl(-) channel = ADP + phosphate + open
CC Cl(-) channel.; EC=5.6.1.6; Evidence={ECO:0000255|RuleBase:RU362037,
CC ECO:0000269|PubMed:27912062};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.22 mM for ATP {ECO:0000269|PubMed:27912062};
CC -!- SUBUNIT: Monomer; does not require oligomerization for channel activity
CC (By similarity). Interacts with cse1l; this interaction may down-
CC regulate cftr activity (PubMed:20933420).
CC {ECO:0000250|UniProtKB:P13569, ECO:0000269|PubMed:20933420}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:20933420, ECO:0000269|PubMed:23487313,
CC ECO:0000269|PubMed:25592226}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:27912062}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:27912062}. Cell membrane
CC {ECO:0000269|PubMed:23487313, ECO:0000305|PubMed:27912062}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:27912062}. Recycling endosome
CC membrane {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:27912062}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:27912062}. Note=The channel is internalized from
CC the cell surface into an endosomal recycling compartment, from where it
CC is recycled to the cell membrane. {ECO:0000250|UniProtKB:P13569}.
CC -!- TISSUE SPECIFICITY: Detected in gut epithelium (at protein level)
CC (PubMed:20933420). Detected in kidney, spleen, intestine and liver
CC (PubMed:20732993). Detected in pancreatic duct epithelium at 5 dpf and
CC throughout adult life (PubMed:25592226). {ECO:0000269|PubMed:20732993,
CC ECO:0000269|PubMed:25592226}.
CC -!- DEVELOPMENTAL STAGE: First detected in developing pancreatic duct at 3
CC dpf (PubMed:25592226). Detected on Kupffer's vesicle during embryonic
CC development (PubMed:23487313, PubMed:26432887). Detected on neural
CC floorplate, brain and pronephric duct primordia in embryos at the 10
CC somite stage (PubMed:26432887). {ECO:0000269|PubMed:23487313,
CC ECO:0000269|PubMed:25592226, ECO:0000269|PubMed:26432887}.
CC -!- DOMAIN: Binds and hydrolyzes ATP via the two cytoplasmic ABC
CC transporter nucleotide-binding domains. The two ATP-binding domains
CC interact with each other, forming a head-to-tail dimer. Normal ATPase
CC activity requires interaction between the two domains. The first ABC
CC transporter nucleotide-binding domain has no ATPase activity by itself.
CC {ECO:0000250|UniProtKB:P13569, ECO:0000250|UniProtKB:P26361}.
CC -!- DOMAIN: The disordered R region mediates channel activation when it is
CC phosphorylated, but not in the absence of phosphorylation.
CC {ECO:0000250|UniProtKB:P13569}.
CC -!- PTM: Phosphorylated; this activates the channel (PubMed:27912062).
CC Dephosphorylation strongly decreases ATPase activity (PubMed:27912062).
CC Phosphorylation at PKA sites activates the channel. Phosphorylation at
CC PKC sites enhances the response to phosphorylation by PKA (By
CC similarity). {ECO:0000250|UniProtKB:P13569,
CC ECO:0000269|PubMed:27912062}.
CC -!- DISRUPTION PHENOTYPE: Considerable lethality around 10 dpf
CC (PubMed:25592226). No effect on initial pancreas development, but at 16
CC dpf mutants display loss of pancreatic acinar tissue (PubMed:25592226).
CC At 22 dpf, most pancreatic acinar tissue has disappeared and has been
CC replaced by fibrotic tissue that surrounds dilated, mucus-filled ducts
CC (PubMed:25592226). Morpholino knockdown of the protein in 48 hpf
CC embryos leads to impaired resistance to P.aeruginosa strain PA14 and
CC strain SMC573, as shown by the increased bacterial burden, but there is
CC no effect on resistance to E.tarda, B.cenocepacia, S.aureus MZ100,
CC E.coli XL-10 and H.influenzae Hib EAGAN (PubMed:20732993). Morpholino
CC knockdown of the protein causes an important reduction of the volume of
CC Kupffer's vesicle during embryonic development (PubMed:26432887).
CC {ECO:0000269|PubMed:20732993, ECO:0000269|PubMed:25592226,
CC ECO:0000269|PubMed:26432887}.
CC -!- MISCELLANEOUS: Mutations that lead to the production of a severely
CC truncated protein that ends before the start of the fourth
CC transmembrane domain disrupt normal left-right body patterning during
CC embryogenesis and abolish lumen expansion of Kupffer's vesicle.
CC {ECO:0000269|PubMed:23487313}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC CFTR transporter (TC 3.A.1.202) subfamily.
CC {ECO:0000255|RuleBase:RU362037}.
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DR EMBL; BX470130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC171654; AAI71654.1; -; mRNA.
DR RefSeq; NP_001038348.1; NM_001044883.1.
DR PDB; 5UAR; EM; 3.73 A; A=1-1485.
DR PDB; 5W81; EM; 3.37 A; A=1-1485.
DR PDBsum; 5UAR; -.
DR PDBsum; 5W81; -.
DR AlphaFoldDB; Q1LX78; -.
DR SMR; Q1LX78; -.
DR STRING; 7955.ENSDARP00000060242; -.
DR TCDB; 3.A.1.202.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q1LX78; -.
DR Ensembl; ENSDART00000060243; ENSDARP00000060242; ENSDARG00000041107.
DR GeneID; 559080; -.
DR KEGG; dre:559080; -.
DR CTD; 1080; -.
DR ZFIN; ZDB-GENE-050517-20; cftr.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000158567; -.
DR HOGENOM; CLU_000604_27_1_1; -.
DR InParanoid; Q1LX78; -.
DR OMA; NIRQEEM; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q1LX78; -.
DR TreeFam; TF105200; -.
DR BRENDA; 5.6.1.6; 928.
DR Reactome; R-DRE-382556; ABC-family proteins mediated transport.
DR Reactome; R-DRE-5627083; RHO GTPases regulate CFTR trafficking.
DR Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR Reactome; R-DRE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DRE-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DRE-9013406; RHOQ GTPase cycle.
DR Reactome; R-DRE-9646399; Aggrephagy.
DR PRO; PR:Q1LX78; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000041107; Expressed in testis and 6 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ZFIN.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IDA:ZFIN.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
DR GO; GO:0005260; F:intracellularly ATP-gated chloride channel activity; ISS:UniProtKB.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0015701; P:bicarbonate transport; ISS:UniProtKB.
DR GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
DR GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:ZFIN.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:ZFIN.
DR GO; GO:0008354; P:germ cell migration; IMP:ZFIN.
DR GO; GO:0070121; P:Kupffer's vesicle development; IMP:ZFIN.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; ISS:UniProtKB.
DR GO; GO:0031016; P:pancreas development; IMP:ZFIN.
DR GO; GO:0090022; P:regulation of neutrophil chemotaxis; IMP:ZFIN.
DR GO; GO:0002679; P:respiratory burst involved in defense response; IMP:ZFIN.
DR GO; GO:0035377; P:transepithelial water transport; ISS:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR009147; CFTR/ABCC7.
DR InterPro; IPR025837; CFTR_reg_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF19; PTHR24223:SF19; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14396; CFTR_R; 1.
DR PRINTS; PR01851; CYSFIBREGLTR.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR TIGRFAMs; TIGR01271; CFTR_protein; 1.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Chloride; Chloride channel;
KW Endoplasmic reticulum; Endosome; Glycoprotein; Ion channel; Ion transport;
KW Isomerase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1485
FT /note="Cystic fibrosis transmembrane conductance regulator"
FT /id="PRO_0000439670"
FT TOPO_DOM 1..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TRANSMEM 79..99
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TOPO_DOM 100..123
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TRANSMEM 124..149
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TOPO_DOM 150..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TRANSMEM 196..216
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TOPO_DOM 217..224
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TRANSMEM 225..245
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TOPO_DOM 246..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TRANSMEM 300..320
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TOPO_DOM 321..340
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TRANSMEM 341..363
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TOPO_DOM 364..856
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TRANSMEM 857..877
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TOPO_DOM 878..924
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TRANSMEM 925..946
FT /note="Discontinuously helical; Name=8"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TOPO_DOM 947..996
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TRANSMEM 997..1019
FT /note="Helical; Name=9"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TOPO_DOM 1020..1021
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TRANSMEM 1022..1042
FT /note="Helical; Name=10"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TOPO_DOM 1043..1103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TRANSMEM 1104..1124
FT /note="Helical; Name=11"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TOPO_DOM 1125..1138
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TRANSMEM 1139..1159
FT /note="Helical; Name=12"
FT /evidence="ECO:0000269|PubMed:27912062"
FT TOPO_DOM 1160..1485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27912062"
FT DOMAIN 83..353
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 424..645
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 860..1163
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1211..1444
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 653..826
FT /note="Disordered R region"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT REGION 1452..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1483..1485
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT COMPBIAS 1455..1476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT BINDING 457..464
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT BINDING 1220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT BINDING 1245..1252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 903
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 205..206
FT /note="Missing: In pd1048; abolishes trafficking to the
FT cell membrane and leads to severe reduction of the size of
FT the Kupffer's vesicle."
FT /evidence="ECO:0000269|PubMed:23487313"
FT CONFLICT 658
FT /note="C -> S (in Ref. 2; AAI71654)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 11..16
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:5W81"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 46..62
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 70..97
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 120..165
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 178..194
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 201..216
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 222..268
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 270..276
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 280..328
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 336..352
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 354..376
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 394..400
FT /evidence="ECO:0007829|PDB:5W81"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 439..446
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 452..456
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 463..471
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 477..482
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 487..490
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 501..506
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 514..522
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 526..530
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 532..536
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 544..547
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 549..562
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 579..588
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 589..593
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 597..602
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 606..611
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 612..619
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 622..627
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 629..634
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 635..637
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 845..853
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 855..885
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 922..934
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 939..965
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 969..974
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 977..993
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 995..1018
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1023..1055
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1057..1068
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1070..1075
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1079..1125
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1138..1147
FT /evidence="ECO:0007829|PDB:5W81"
FT TURN 1148..1150
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1151..1165
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1167..1175
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 1211..1221
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 1227..1235
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 1240..1245
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1251..1258
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 1262..1264
FT /evidence="ECO:0007829|PDB:5W81"
FT TURN 1275..1277
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1280..1285
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 1287..1290
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1301..1305
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1313..1322
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1326..1330
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 1332..1334
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 1342..1347
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1349..1363
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 1366..1371
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1379..1392
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 1393..1395
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 1397..1401
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1408..1410
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 1411..1417
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 1419..1427
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1428..1434
FT /evidence="ECO:0007829|PDB:5W81"
FT STRAND 1437..1439
FT /evidence="ECO:0007829|PDB:5W81"
FT TURN 1440..1442
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1447..1450
FT /evidence="ECO:0007829|PDB:5W81"
FT HELIX 1453..1456
FT /evidence="ECO:0007829|PDB:5W81"
SQ SEQUENCE 1485 AA; 168400 MW; 62601EBC307A3B8A CRC64;
MQRSPVEDAN CLSRYFFWWT NPIMRKGFKE KLRPSDVYQA PSQDAADILA ERLEKEWDRE
VASGKKKPSL LRAMARCYIK PFLLFGFLLY IGEATKTVQP QLLGRIIASF DPAHEPERAN
GYFLAFGLGL LFTARFLLLQ PAMFGLHHLG MQIRIALFSI IYKKTLKLSS RVLDKISTGQ
LVSLMSANLG KFDQSLGMAH FIWISPLQCI LCTGLIWELI DVNSFCALAA ISLLGVLQAF
LSHKMGPYKA QKVLLTNKRL ALTSEIMENL HSVKAYGWEE IMETLIKNIR QDEVKLTRKI
GSLRYFYSSA YFFSAIFVIV AAVVPHALSR GINLRRIFTT LSYCMVLRMT VTRQLPGSIQ
MWYDTMRLIW KIEEFLSKEE YKLMEYDLSI TELELQDVTA SWDEGPGELL ERIKQENKAN
GHHNGDAGLF FTNLYVAPVL KDISLKLKKG EMLAVTGSMG SGKSSLLMTI LGELVPSSGK
IRHSGRISYS SQTAWIMPGT IRDNILFGLT YDEYRYKSVV KACQLEEDLA ALPEKDKTPM
AEGGLNLSGG QKARVALARA VYRDADLYLL DAPFTHLDIA TEKEIFDKCL CKLMASKTRI
LVTNKIEHLK RADKILLLHN GESFFYGTFP ELQSERPDFS SLLLGLEAYD NISAERRCSI
LTETLHRVSV DESAGMQPER SAFRQVPPTK PMYIDERKAS VIVNPLGVAR KASFIQVPEE
EVRRTLPDRK FSLVPENELV DESFMGSDVY HNHGVHMAGQ RRQSVLAFMT NAQGQGRREH
LQSSFRRRLS VVPQSELASE LDIYTRRLSD STYDMTGILE EENIEACLTD EIDEIEETFE
TTKWNTYVRY VSNNKSLLYV LIFILFIAAI EIAGSVAGIF LITDELWREE HQRSEPNMTK
HSNASSSGQT YAITVTPTSS YYILYIYVAT SESLLAMGFF RGLPFVHTTI TISKKLHQKM
LHAVLSAPMS VLNTMKTGRI MNRFTKDMAT IDDMLPLLMF DFVQLTVVVV GCILVVSIVR
PYIFLAATPL AIIFIVMRKY FLRTGQQLKQ LETEARSPIF SHLIMSLKGL WTIRAFERQA
YFEALFHKTL NTHTATWFLY LSTLRWFLFR ADILFVFFFT LAAWIAVGTN QDKPGEIGII
ICLAMLILGT FQWCVATSIA VDGMMRSVDR VFKFIDLPSE TPKPDKGKDS DLIIENVDAQ
ADSSWPHRGQ IEVRNLTVKY TEAGHAVLKN LSFSAEGRQR VGILGRTGSG KSSLFNALLK
LVYTDGEISI DGVNWNKMPL QKWRKAFGVV PQKVFIFTGP LRMNLDPYGC HSDEELWRVA
EEVGLKTVIE QFPDKLDFQL EYGGYVLSNG HKQLICLARS ILSGARILLL DEPSAHLDPV
TIKVLKKTLR QSFSTCTILL SEHKVEPLLE CQSFLMMDKG QVKTYDSIQK LLNETSHLKQ
AISPAERLKL FPRRNSSMRT PQSKLSSVTQ TLQEEAEDNI QDTRL
