CFTR_RAT
ID CFTR_RAT Reviewed; 1476 AA.
AC P34158; Q2IBD3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Cystic fibrosis transmembrane conductance regulator;
DE Short=CFTR;
DE AltName: Full=ATP-binding cassette sub-family C member 7;
DE AltName: Full=Channel conductance-controlling ATPase;
DE EC=5.6.1.6 {ECO:0000250|UniProtKB:P13569};
DE AltName: Full=cAMP-dependent chloride channel;
GN Name=Cftr; Synonyms=Abcc7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12917688; DOI=10.1038/nature01858;
RA Thomas J.W., Touchman J.W., Blakesley R.W., Bouffard G.G.,
RA Beckstrom-Sternberg S.M., Margulies E.H., Blanchette M., Siepel A.C.,
RA Thomas P.J., McDowell J.C., Maskeri B., Hansen N.F., Schwartz M.S.,
RA Weber R.J., Kent W.J., Karolchik D., Bruen T.C., Bevan R., Cutler D.J.,
RA Schwartz S., Elnitski L., Idol J.R., Prasad A.B., Lee-Lin S.-Q.,
RA Maduro V.V.B., Summers T.J., Portnoy M.E., Dietrich N.L., Akhter N.,
RA Ayele K., Benjamin B., Cariaga K., Brinkley C.P., Brooks S.Y., Granite S.,
RA Guan X., Gupta J., Haghighi P., Ho S.-L., Huang M.C., Karlins E.,
RA Laric P.L., Legaspi R., Lim M.J., Maduro Q.L., Masiello C.A.,
RA Mastrian S.D., McCloskey J.C., Pearson R., Stantripop S., Tiongson E.E.,
RA Tran J.T., Tsurgeon C., Vogt J.L., Walker M.A., Wetherby K.D.,
RA Wiggins L.S., Young A.C., Zhang L.-H., Osoegawa K., Zhu B., Zhao B.,
RA Shu C.L., De Jong P.J., Lawrence C.E., Smit A.F., Chakravarti A.,
RA Haussler D., Green P., Miller W., Green E.D.;
RT "Comparative analyses of multi-species sequences from targeted genomic
RT regions.";
RL Nature 424:788-793(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RX PubMed=7526924; DOI=10.1093/hmg/3.7.1089;
RA Denamur E., Chehab F.F.;
RT "Analysis of the mouse and rat CFTR promoter regions.";
RL Hum. Mol. Genet. 3:1089-1094(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 482-988.
RX PubMed=1282491; DOI=10.1016/s0888-7543(05)80107-7;
RA Trezise A.E., Szpirer C., Buchwald M.;
RT "Localization of the gene encoding the cystic fibrosis transmembrane
RT conductance regulator (CFTR) in the rat to chromosome 4 and implications
RT for the evolution of mammalian chromosomes.";
RL Genomics 14:869-874(1992).
RN [4]
RP INTERACTION WITH GOPC.
RX PubMed=11707463; DOI=10.1074/jbc.m110177200;
RA Cheng J., Moyer B.D., Milewski M., Loffing J., Ikeda M., Mickle J.E.,
RA Cutting G.R., Li M., Stanton B.A., Guggino W.B.;
RT "A Golgi-associated PDZ domain protein modulates cystic fibrosis
RT transmembrane regulator plasma membrane expression.";
RL J. Biol. Chem. 277:3520-3529(2002).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12519745; DOI=10.1152/ajpcell.00227.2002;
RA Hallows K.R., Kobinger G.P., Wilson J.M., Witters L.A., Foskett J.K.;
RT "Physiological modulation of CFTR activity by AMP-activated protein kinase
RT in polarized T84 cells.";
RL Am. J. Physiol. 284:C1297-C1308(2003).
RN [6]
RP INTERACTION WITH SHANK2.
RX PubMed=14679199; DOI=10.1074/jbc.m312871200;
RA Kim J.Y., Han W., Namkung W., Lee J.H., Kim K.H., Shin H., Kim E.,
RA Lee M.G.;
RT "Inhibitory regulation of cystic fibrosis transmembrane conductance
RT regulator anion-transporting activities by Shank2.";
RL J. Biol. Chem. 279:10389-10396(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-808, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=29453757; DOI=10.1007/s10735-018-9759-2;
RA Sharma S., Hanukoglu A., Hanukoglu I.;
RT "Localization of epithelial sodium channel (ENaC) and CFTR in the germinal
RT epithelium of the testis, Sertoli cells, and spermatozoa.";
RL J. Mol. Histol. 49:195-208(2018).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=30659401; DOI=10.1007/s10735-019-09813-3;
RA Sharma S., Hanukoglu I.;
RT "Mapping the sites of localization of epithelial sodium channel (ENaC) and
RT CFTR in segments of the mammalian epididymis.";
RL J. Mol. Histol. 50:141-154(2019).
CC -!- FUNCTION: Epithelial ion channel that plays an important role in the
CC regulation of epithelial ion and water transport and fluid homeostasis.
CC Mediates the transport of chloride ions across the cell membrane (By
CC similarity). Channel activity is coupled to ATP hydrolysis. The ion
CC channel is also permeable to HCO(3)(-); selectivity depends on the
CC extracellular chloride concentration. Exerts its function also by
CC modulating the activity of other ion channels and transporters.
CC Contributes to the regulation of the pH and the ion content of the
CC epithelial fluid layer. Modulates the activity of the epithelial sodium
CC channel (ENaC) complex, in part by regulating the cell surface
CC expression of the ENaC complex. May regulate bicarbonate secretion and
CC salvage in epithelial cells by regulating the transporter SLC4A7. Can
CC inhibit the chloride channel activity of ANO1 (By similarity). Plays a
CC role in the chloride and bicarbonate homeostasis during sperm
CC epididymal maturation and capacitation (By similarity).
CC {ECO:0000250|UniProtKB:P13569, ECO:0000250|UniProtKB:P26361}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + closed Cl(-) channel = ADP + phosphate + open
CC Cl(-) channel.; EC=5.6.1.6; Evidence={ECO:0000250|UniProtKB:P13569};
CC -!- SUBUNIT: Monomer; does not require oligomerization for channel
CC activity. May form oligomers in the membrane (By similarity). Interacts
CC with SLC4A7 through SLC9A3R1 (By similarity). Interacts with SHANK2
CC (PubMed:14679199). Interacts with SLC9A3R1 and MYO6. Interacts (via C-
CC terminus) with GOPC (via PDZ domain); this promotes CFTR
CC internalization and thereby decreases channel activity
CC (PubMed:11707463). Interacts with SLC4A7 through SLC9A3R1. Found in a
CC complex with MYO5B and RAB11A. Interacts with ANO1. Interacts with
CC SLC26A8 (By similarity). Interacts with AHCYL1; the interaction
CC increases CFTR activity (By similarity). Interacts with CSE1L (By
CC similarity). The core-glycosylated form interacts with GORASP2 (via PDZ
CC GRASP-type 1 domain) in respone to ER stress (By similarity). Interacts
CC with MARCHF2; the interaction leads to CFTR ubiqtuitination and
CC degradation (By similarity). {ECO:0000250|UniProtKB:P13569,
CC ECO:0000250|UniProtKB:P26361, ECO:0000269|PubMed:11707463,
CC ECO:0000269|PubMed:14679199}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P26361}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P13569}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P13569}. Cell membrane
CC {ECO:0000250|UniProtKB:P26361}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P13569}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P13569}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P13569}. Nucleus {ECO:0000269|PubMed:29453757}.
CC Note=The channel is internalized from the cell surface into an
CC endosomal recycling compartment, from where it is recycled to the cell
CC membrane (By similarity). In the oviduct and bronchus, detected on the
CC apical side of epithelial cells, but not associated with cilia (By
CC similarity). In Sertoli cells, a processed product is detected in the
CC nucleus (PubMed:29453757). ER stress induces GORASP2-mediated
CC unconventional (ER/Golgi-independent) trafficking of core-glycosylated
CC CFTR to cell membrane (By similarity). {ECO:0000250|UniProtKB:P13569,
CC ECO:0000269|PubMed:29453757}.
CC -!- TISSUE SPECIFICITY: Detected in epithelial cells in nasopharynx,
CC submandibular gland, pancreas and ileum (at protein level)
CC (PubMed:12519745). Expressed in the epididymis (PubMed:30659401). In
CC the caput section of the epididymis, expressed uniformly on both the
CC luminal and basolateral sides of the ducts and on sperm in the caput
CC lumen (at protein level) (PubMed:30659401). In the cauda, detected
CC along the luminal border but not continuously and is also expressed on
CC the basolateral surface (PubMed:30659401). Within the caudal lumen,
CC detected on sperm (PubMed:30659401). {ECO:0000269|PubMed:12519745,
CC ECO:0000269|PubMed:30659401}.
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 PDZ-binding motif mediates interactions with GOPC and with
CC the SLC4A7, SLC9A3R1/EBP50 complex. {ECO:0000250|UniProtKB:P13569}.
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: N-glycosylated. {ECO:0000250|UniProtKB:P13569}.
CC -!- PTM: Phosphorylated; cAMP treatment promotes phosphorylation and
CC activates the channel. Dephosphorylation decreases the ATPase activity
CC (in vitro). Phosphorylation at PKA sites activates the channel.
CC Phosphorylation at PKC sites enhances the response to phosphorylation
CC by PKA. Phosphorylated by AMPK; this inhibits channel activity.
CC {ECO:0000250|UniProtKB:P13569}.
CC -!- PTM: Ubiquitinated, leading to its degradation in the lysosome.
CC Deubiquitination by USP10 in early endosomes enhances its endocytic
CC recycling to the cell membrane. Ubiquitinated by RNF185 during ER
CC stress. Ubiquitinated by MARCHF2 (By similarity).
CC {ECO:0000250|UniProtKB:P13569}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC CFTR transporter (TC 3.A.1.202) subfamily. {ECO:0000305}.
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DR EMBL; DP000027; AAR16315.1; -; Genomic_DNA.
DR EMBL; L26098; AAA73561.1; -; Genomic_DNA.
DR EMBL; M89906; AAA40918.1; -; mRNA.
DR PIR; I84733; I84733.
DR RefSeq; NP_113694.1; NM_031506.1.
DR AlphaFoldDB; P34158; -.
DR SMR; P34158; -.
DR BioGRID; 246440; 3.
DR STRING; 10116.ENSRNOP00000010981; -.
DR BindingDB; P34158; -.
DR ChEMBL; CHEMBL3992; -.
DR GlyGen; P34158; 2 sites.
DR iPTMnet; P34158; -.
DR PhosphoSitePlus; P34158; -.
DR PaxDb; P34158; -.
DR PRIDE; P34158; -.
DR GeneID; 24255; -.
DR KEGG; rno:24255; -.
DR CTD; 1080; -.
DR RGD; 2332; Cftr.
DR eggNOG; KOG0054; Eukaryota.
DR InParanoid; P34158; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; P34158; -.
DR TreeFam; TF105200; -.
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-9646399; Aggrephagy.
DR PRO; PR:P34158; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
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; ISS: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:0005902; C:microvillus; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0055037; C:recycling endosome; ISO:RGD.
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; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS: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:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
DR GO; GO:0019869; F:chloride channel inhibitor activity; ISS:UniProtKB.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
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:0030165; F:PDZ domain binding; ISO:RGD.
DR GO; GO:0106138; F:Sec61 translocon complex binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0097186; P:amelogenesis; ISO:RGD.
DR GO; GO:0015701; P:bicarbonate transport; IMP:RGD.
DR GO; GO:0071454; P:cellular response to anoxia; IEP:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IEP:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006821; P:chloride transport; IMP:RGD.
DR GO; GO:0006695; P:cholesterol biosynthetic process; ISO:RGD.
DR GO; GO:0030301; P:cholesterol transport; ISO:RGD.
DR GO; GO:0070166; P:enamel mineralization; IMP:RGD.
DR GO; GO:0051454; P:intracellular pH elevation; ISS:UniProtKB.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0030324; P:lung development; IMP:RGD.
DR GO; GO:0060081; P:membrane hyperpolarization; ISS:UniProtKB.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; ISS:UniProtKB.
DR GO; GO:2000077; P:negative regulation of type B pancreatic cell development; IMP:RGD.
DR GO; GO:1905460; P:negative regulation of vascular associated smooth muscle cell apoptotic process; IMP:RGD.
DR GO; GO:1902161; P:positive regulation of cyclic nucleotide-gated ion channel activity; ISO:RGD.
DR GO; GO:0070175; P:positive regulation of enamel mineralization; ISO:RGD.
DR GO; GO:1904446; P:positive regulation of establishment of Sertoli cell barrier; IMP:RGD.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:RGD.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:RGD.
DR GO; GO:0033005; P:positive regulation of mast cell activation; IMP:RGD.
DR GO; GO:1902943; P:positive regulation of voltage-gated chloride channel activity; ISO:RGD.
DR GO; GO:0036253; P:response to amiloride; IMP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:RGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IMP:RGD.
DR GO; GO:0048240; P:sperm capacitation; ISS:UniProtKB.
DR GO; GO:0030321; P:transepithelial chloride transport; IMP:RGD.
DR GO; GO:0035377; P:transepithelial water transport; ISS:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0042311; P:vasodilation; IDA:RGD.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; ISO:RGD.
DR GO; GO:0006833; P:water transport; IMP:RGD.
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 ATP-binding; Cell membrane; Chloride; Chloride channel;
KW Endoplasmic reticulum; Endosome; Glycoprotein; Ion channel; Ion transport;
KW Isomerase; Lipoprotein; Membrane; Nucleotide-binding; Nucleus; Palmitate;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..1476
FT /note="Cystic fibrosis transmembrane conductance regulator"
FT /id="PRO_0000093428"
FT TOPO_DOM 1..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 78..98
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 99..122
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 123..146
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 147..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 196..216
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 217..222
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 223..243
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 244..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 299..319
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 320..339
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 340..358
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 359..853
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 854..874
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 875..913
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 914..934
FT /note="Discontinuously helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 935..985
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 986..1006
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 1007..1008
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 1009..1029
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 1030..1090
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 1091..1111
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 1112..1125
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TRANSMEM 1126..1146
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT TOPO_DOM 1147..1476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT DOMAIN 81..365
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 412..646
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 854..1153
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1208..1439
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 654..826
FT /note="Disordered R region"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT REGION 1382..1476
FT /note="Interaction with GORASP2"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT REGION 1445..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1474..1476
FT /note="PDZ-binding"
FT /evidence="ECO:0000269|PubMed:11707463"
FT COMPBIAS 1459..1476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT BINDING 458..465
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P26361,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 458..465
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P26361"
FT BINDING 1215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT BINDING 1240..1247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1240..1247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 670
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 715
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 790
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT MOD_RES 1452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT LIPID 524
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT LIPID 1391
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P13569"
FT CARBOHYD 889
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 987..988
FT /note="FD -> LT (in Ref. 3; AAA40918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1476 AA; 167830 MW; B2B2A25EB5107640 CRC64;
MQKSPLEKAS FISKLFFSWT TPILRKGYRH HLELSDIYQA PSSDSADHLS EKLEREWDRE
QASKKKPQLI HALRRCFVWR FVFYGVLLYL GEVTKAVQPV LLGRIIASYD PDNTEERSIA
IYLGIGLCLL FIVRTLLLHP AIFGLHHIGM QMRIAMFSLI YKKTLKLSSR VLDKISIGQL
ISLLSNNLNK FDEGLALAHF IWIAPLQVVL LMGLLWDLLQ FSAFCGLGLL IVLVIFQAIL
GKMMVKYRDK RAAKINERLV ITSEVIDNIY SVKAYCWESA MEKIIESLRE EELKMTRRSA
YMRFFTSSAF FFSGFFVVFL SVLPYTVING IVLRKIFTTI SFCIVLRMSV TRQFPTAVQI
WYDSLGMIRK IQDFLQTQEY KVLEYNLMFT GLVMENVTAF WEEGFQELLE KVQLNNDDRK
TSNGENHLSF SHLCLVGNPV LKNINLNIKK GEMLAITGST GAGKTSLLML ILGELEASEG
IIKHSGRVSF SSQISWIMPG TIKENIIFGV SYDEYRYKSV VKACQLQEDI TKFAEQDNTV
LGEGGVTLSG GQRARISLAR AVYKDADLYL LDSPFGYLDV LTEEQIFESC VCKLMASKTR
ILVTSKMEQL KKADKILILH EGSSYFYGTF SELQSLRPDF SSKLMGYDTF DQFTEERRSS
ILTETLRRFS VDDASTTWNK AKQSFRQTGE FGEKRKNSIL SSFSSVKKIS IVQKTPLSIE
GESDDLQERR LSLVPDSEHG EAALPRSNMI TAGPTFPGRR RQSVLDLMTF TPSSVSSSLQ
RTRASIRKIS LAPRISLKEE DIYSRRLSQD STLNITEEIN EEDLKECFFD DMVKIPTVTT
WNTYLRYFTL HRGLFAVLIW CVLVFLVEVA ASLFVLWLLK NNPVNGGNNG TKIANTSYVV
VITSSSFYYI FYIYVGVADT LLALSLFRGL PLVHTLITAS KILHRKMLHS ILHAPMSTFN
KLKAGGILNR FSKDIAILDD FLPLTIFDFI QLLFIVVGAI IVVSALQPYI FLATVPGLAV
FILLRAYFLH TSQQLKQLES EGRSPIFTHL VTSLKGLWTL RAFRRQTYFE TLFHKALNLH
TANWFMYLAT LRWFQMRIDM IFVLFFIVVT FISILTTGEG EGTTGIILTL AMNIMSTLQW
AVNSSIDTDS LMRSVSRVFK FIDIQTEESI CTKIMKELHS EDSPNALVIK NEHVKKCDTW
PSGGEMVVKD LTVKYVDDGN AILENISFSI SPGQRVGLLG RTGSGKSTLL SAFLRMLNIK
GEIQIDGVSW NSMTLQEWRK AFGVITQKVF IFSGTFRQNL DPNGKWRDEE IWKVADQVGL
KSVIEQFPGQ LNFTLVDGGY VLSHGHKQLM CLARSVLSKA KIILLDEPSA NLDPITYQVI
RRVLRQAFAG CTVVLCEHRI EAMLDCQRFL VIEQGNVWQY ESLQALLSEK SVFQRALSSS
EKMKLFHGRH SSKQKPRTQI TAVKEETEEE VQETRL
