Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00980
Entry Name
UniProt Accession
Theoretical PI
8.91
Molecular Weight
168141.56
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Cystic fibrosis transmembrane conductance regulator
Protein Synonyms/Alias
CFTR; ATP-binding cassette sub-family C member 7; Channel conductance-controlling ATPase; 3.6.3.49; cAMP-dependent chloride channel;
Gene Name
CFTR
Gene Synonyms/Alias
ABCC7;
Created Date
01-JAN-1990
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
524
Canonical
YRSVIKACQLEEDIS
[1]
S-Palmitoylation
1395
Canonical
LKQAFADCTVILCEH
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] McClure M, DeLucas LJ, Wilson L, Ray M, Rowe SM, Wu X, Dai Q, Hong JS,Sorscher EJ, Kappes JC, Barnes S. Purification of CFTR for mass spectrometryanalysis: identification of palmitoylation and other post-translationalmodifications. Protein Eng Des Sel. 2012 Jan;25(1):7-14. doi:10.1093/protein/gzr054. Epub 2011 Nov 25.[PMID:22119790]
Functional Description
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. Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation.
Sequence Annotation
Topological domain: 1 80 Cytoplasmic.
Transmembrane: 81 103 Helical; Name=1.
Topological domain: 104 117 Extracellular.
Transmembrane: 118 138 Helical; Name=2.
Topological domain: 139 194 Cytoplasmic.
Transmembrane: 195 215 Helical; Name=3.
Topological domain: 216 220 Extracellular.
Transmembrane: 221 241 Helical; Name=4.
Topological domain: 242 307 Cytoplasmic.
Transmembrane: 308 328 Helical; Name=5.
Topological domain: 329 330 Extracellular.
Transmembrane: 331 350 Helical; Name=6.
Topological domain: 351 859 Cytoplasmic.
Transmembrane: 860 880 Helical; Name=7.
Topological domain: 881 911 Extracellular.
Transmembrane: 912 932 Helical; Name=8.
Topological domain: 933 990 Cytoplasmic.
Transmembrane: 991 1011 Helical; Name=9.
Topological domain: 1012 1013 Extracellular.
Transmembrane: 1014 1034 Helical; Name=10.
Topological domain: 1035 1102 Cytoplasmic.
Transmembrane: 1103 1123 Helical; Name=11.
Topological domain: 1124 1128 Extracellular.
Transmembrane: 1129 1149 Helical; Name=12.
Topological domain: 1150 1480 Cytoplasmic.
Domain: 81 365 ABC transmembrane type-1 1.
Domain: 423 646 ABC transporter 1.
Domain: 859 1155 ABC transmembrane type-1 2.
Domain: 1210 1443 ABC transporter 2.
Nucleotide-binding: 458 465 ATP 1.
Nucleotide-binding: 1244 1251 ATP 2.
Motif: 1478 1480 PDZ-binding.
Modified residue: 291 291 Phosphothreonine.
Modified residue: 549 549 Phosphoserine.
Modified residue: 660 660 Phosphoserine; by PKA.
Modified residue: 686 686 Phosphoserine; by PKC.
Modified residue: 700 700 Phosphoserine; by PKA.
Modified residue: 712 712 Phosphoserine; by PKA.
Modified residue: 717 717 Phosphothreonine.
Modified residue: 737 737 Phosphoserine; by PKA.
Modified residue: 753 753 Phosphoserine; by PKA.
Modified residue: 768 768 Phosphoserine; by PKA.
Modified residue: 790 790 Phosphoserine; by PKC.
Modified residue: 795 795 Phosphoserine; by PKA.
Modified residue: 813 813 Phosphoserine; by PKA.
Modified residue: 1444 1444 Phosphoserine.
Modified residue: 1456 1456 Phosphoserine.
Protein Length
1480 AA.
Protein Sequence
(Canonical)
MQRSPLEKAS VVSKLFFSWT RPILRKGYRQ RLELSDIYQI PSVDSADNLS EKLEREWDRE  60
LASKKNPKLI NALRRCFFWR FMFYGIFLYL GEVTKAVQPL LLGRIIASYD PDNKEERSIA  120
IYLGIGLCLL FIVRTLLLHP AIFGLHHIGM QMRIAMFSLI YKKTLKLSSR VLDKISIGQL  180
VSLLSNNLNK FDEGLALAHF VWIAPLQVAL LMGLIWELLQ ASAFCGLGFL IVLALFQAGL  240
GRMMMKYRDQ RAGKISERLV ITSEMIENIQ SVKAYCWEEA MEKMIENLRQ TELKLTRKAA  300
YVRYFNSSAF FFSGFFVVFL SVLPYALIKG IILRKIFTTI SFCIVLRMAV TRQFPWAVQT  360
WYDSLGAINK IQDFLQKQEY KTLEYNLTTT EVVMENVTAF WEEGFGELFE KAKQNNNNRK  420
TSNGDDSLFF SNFSLLGTPV LKDINFKIER GQLLAVAGST GAGKTSLLMV IMGELEPSEG  480
KIKHSGRISF CSQFSWIMPG TIKENIIFGV SYDEYRYRSV IKACQLEEDI SKFAEKDNIV  540
LGEGGITLSG GQRARISLAR AVYKDADLYL LDSPFGYLDV LTEKEIFESC VCKLMANKTR  600
ILVTSKMEHL KKADKILILH EGSSYFYGTF SELQNLQPDF SSKLMGCDSF DQFSAERRNS  660
ILTETLHRFS LEGDAPVSWT ETKKQSFKQT GEFGEKRKNS ILNPINSIRK FSIVQKTPLQ  720
MNGIEEDSDE PLERRLSLVP DSEQGEAILP RISVISTGPT LQARRRQSVL NLMTHSVNQG  780
QNIHRKTTAS TRKVSLAPQA NLTELDIYSR RLSQETGLEI SEEINEEDLK ECFFDDMESI  840
PAVTTWNTYL RYITVHKSLI FVLIWCLVIF LAEVAASLVV LWLLGNTPLQ DKGNSTHSRN  900
NSYAVIITST SSYYVFYIYV GVADTLLAMG FFRGLPLVHT LITVSKILHH KMLHSVLQAP  960
MSTLNTLKAG GILNRFSKDI AILDDLLPLT IFDFIQLLLI VIGAIAVVAV LQPYIFVATV  1020
PVIVAFIMLR AYFLQTSQQL KQLESEGRSP IFTHLVTSLK GLWTLRAFGR QPYFETLFHK  1080
ALNLHTANWF LYLSTLRWFQ MRIEMIFVIF FIAVTFISIL TTGEGEGRVG IILTLAMNIM  1140
STLQWAVNSS IDVDSLMRSV SRVFKFIDMP TEGKPTKSTK PYKNGQLSKV MIIENSHVKK  1200
DDIWPSGGQM TVKDLTAKYT EGGNAILENI SFSISPGQRV GLLGRTGSGK STLLSAFLRL  1260
LNTEGEIQID GVSWDSITLQ QWRKAFGVIP QKVFIFSGTF RKNLDPYEQW SDQEIWKVAD  1320
EVGLRSVIEQ FPGKLDFVLV DGGCVLSHGH KQLMCLARSV LSKAKILLLD EPSAHLDPVT  1380
YQIIRRTLKQ AFADCTVILC EHRIEAMLEC QQFLVIEENK VRQYDSIQKL LNERSLFRQA  1440
ISPSDRVKLF PHRNSSKCKS KPQIAALKEE TEEEVQDTRL                        1480
FASTA
(Canonical)
>LipidDB-9606-00980|P13569
MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRE
LASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIA
IYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQL
VSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGL
GRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAA
YVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQT
WYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRK
TSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEG
KIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIV
LGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTR
ILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNS
ILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQ
MNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQG
QNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESI
PAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRN
NSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAP
MSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATV
PVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHK
ALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIM
STLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKK
DDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL
LNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVAD
EVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVT
YQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQA
ISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL
Gene Ontology
GO:0016324; C:apical plasma membrane; IDA:UniProtKB
GO:0016323; C:basolateral plasma membrane; NAS:UniProtKB
GO:0009986; C:cell surface; IDA:UniProtKB
GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW
GO:0030659; C:cytoplasmic vesicle membrane; IEA:Ensembl
GO:0005769; C:early endosome; IDA:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005902; C:microvillus; IEA:Ensembl
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0043234; C:protein complex; IDA:UniProtKB
GO:0005524; F:ATP binding; TAS:ProtInc
GO:0005224; F:ATP-binding and phosphorylation-dependent chloride channel activity; TAS:ProtInc
GO:0015106; F:bicarbonate transmembrane transporter activity; ISS:UniProtKB
GO:0005260; F:channel-conductance-controlling ATPase activity; NAS:UniProtKB
GO:0005254; F:chloride channel activity; IDA:UniProtKB
GO:0019869; F:chloride channel inhibitor activity; IDA:UniProtKB
GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB
GO:0019899; F:enzyme binding; IPI:UniProtKB
GO:0030165; F:PDZ domain binding; IDA:UniProtKB
GO:0071320; P:cellular response to cAMP; ISS:UniProtKB
GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl
GO:1902476; P:chloride transmembrane transport; IDA:GOC
GO:0006695; P:cholesterol biosynthetic process; IEA:Ensembl
GO:0030301; P:cholesterol transport; IEA:Ensembl
GO:0051454; P:intracellular pH elevation; ISS:UniProtKB
GO:0015705; P:iodide transport; IEA:Ensembl
GO:0030324; P:lung development; IEA:Ensembl
GO:0060081; P:membrane hyperpolarization; ISS:UniProtKB
GO:0045909; P:positive regulation of vasodilation; IEA:Ensembl
GO:1902943; P:positive regulation of voltage-gated chloride channel activity; IDA:UniProt
GO:0007585; P:respiratory gaseous exchange; TAS:ProtInc
GO:0034097; P:response to cytokine; IEA:Ensembl
GO:0042493; P:response to drug; IEA:Ensembl
GO:0043627; P:response to estrogen; IEA:Ensembl
GO:0043434; P:response to peptide hormone; IEA:Ensembl
GO:0048240; P:sperm capacitation; ISS:UniProtKB
GO:0030321; P:transepithelial chloride transport; IEA:Ensembl
GO:0055085; P:transmembrane transport; TAS:Reactome
GO:0006810; P:transport; TAS:ProtInc
GO:0042311; P:vasodilation; IEA:Ensembl
GO:0006833; P:water transport; IEA:Ensembl
Interpro
InterPro; IPR003593; AAA+_ATPase
InterPro; IPR011527; ABC1_TM_dom
InterPro; IPR003439; ABC_transporter-like
InterPro; IPR017871; ABC_transporter_CS
InterPro; IPR001140; ABC_transptr_TM_dom
InterPro; IPR005291; cAMP_cl_channel
InterPro; IPR025837; CFTR_reg_dom
InterPro; IPR009147; CysFib_conduc_TM
InterPro; IPR027417; P-loop_NTPase
Pfam
Pfam; PF00664; ABC_membrane;
Pfam; PF00005; ABC_tran;
Pfam; PF14396; CFTR_R;
SMART
SMART; SM00382; AAA;
PROSITE
PROSITE; PS50929; ABC_TM1F;
PROSITE; PS00211; ABC_TRANSPORTER_1;
PROSITE; PS50893; ABC_TRANSPORTER_2;
PRINTS
PRINTS; PR01851; CYSFIBREGLTR;