ID G1N9K2_MELGA Unreviewed; 1403 AA.
AC G1N9K2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 2.
DT 13-APR-2016, entry version 40.
DE RecName: Full=Cystic fibrosis transmembrane conductance regulator {ECO:0000256|RuleBase:RU362037};
DE EC=3.6.3.49 {ECO:0000256|RuleBase:RU362037};
DE AltName: Full=ATP-binding cassette sub-family C member 7 {ECO:0000256|RuleBase:RU362037};
DE AltName: Full=Channel conductance-controlling ATPase {ECO:0000256|RuleBase:RU362037};
DE AltName: Full=cAMP-dependent chloride channel {ECO:0000256|RuleBase:RU362037};
DE Flags: Fragment;
GN Name=CFTR {ECO:0000313|Ensembl:ENSMGAP00000009096};
OS Meleagris gallopavo (Common turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC Phasianidae; Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000009096, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000009096, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A.,
RA de Jong P., Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D.,
RA Lee M.K., Lee T., Mane S., Marcais G., Marz M., McElroy A.P.,
RA Modise T., Nefedov M., Notredame C., Paton I.R., Payne W.S.,
RA Pertea G., Prickett D., Puiu D., Qioa D., Raineri E., Ruffier M.,
RA Salzberg S.L., Schatz M.C., Scheuring C., Schmidt C.J., Schroeder S.,
RA Searle S.M., Smith E.J., Smith J., Sonstegard T.S., Stadler P.F.,
RA Tafer H., Tu Z.J., Van Tassell C.P., Vilella A.J., Williams K.P.,
RA Yorke J.A., Zhang L., Zhang H.B., Zhang X., Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000009096}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2011) to UniProtKB.
CC -!- FUNCTION: Involved in the transport of chloride ions.
CC {ECO:0000256|RuleBase:RU362037}.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC {ECO:0000256|RuleBase:RU362037}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000256|RuleBase:RU362037}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU362037}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
CC family. CFTR transporter (TC 3.A.1.202) subfamily.
CC {ECO:0000256|RuleBase:RU362037}.
CC -!- SIMILARITY: Contains 2 ABC transmembrane type-1 domains.
CC {ECO:0000256|RuleBase:RU362037}.
CC -!- SIMILARITY: Contains 2 ABC transporter domains.
CC {ECO:0000256|RuleBase:RU363033}.
CC -!- CAUTION: The sequence shown here is derived from an Ensembl
CC automatic analysis pipeline and should be considered as
CC preliminary data. {ECO:0000313|Ensembl:ENSMGAP00000009096}.
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DR STRING; 9103.ENSMGAP00000009096; -.
DR Ensembl; ENSMGAT00000009910; ENSMGAP00000009096; ENSMGAG00000008826.
DR eggNOG; KOG0054; Eukaryota.
DR eggNOG; COG1132; LUCA.
DR GeneTree; ENSGT00820000126974; -.
DR InParanoid; G1N9K2; -.
DR OMA; NALRRCF; -.
DR OrthoDB; EOG7C2R0B; -.
DR TreeFam; TF105200; -.
DR Proteomes; UP000001645; Chromosome 1.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031205; C:endoplasmic reticulum Sec complex; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0005260; F:channel-conductance-controlling ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0019869; F:chloride channel inhibitor activity; IEA:Ensembl.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:Ensembl.
DR GO; GO:0030301; P:cholesterol transport; IEA:Ensembl.
DR GO; GO:0051454; P:intracellular pH elevation; IEA:Ensembl.
DR GO; GO:0060081; P:membrane hyperpolarization; IEA:Ensembl.
DR GO; GO:1902161; P:positive regulation of cyclic nucleotide-gated ion channel activity; IEA:Ensembl.
DR GO; GO:0045921; P:positive regulation of exocytosis; IEA:Ensembl.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:1902943; P:positive regulation of voltage-gated chloride channel activity; IEA:Ensembl.
DR GO; GO:0048240; P:sperm capacitation; IEA:Ensembl.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR003439; ABC_transporter-like.
DR InterPro; IPR017871; ABC_transporter_CS.
DR InterPro; IPR009147; CFTR/ABCC7.
DR InterPro; IPR025837; CFTR_reg_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF19; PTHR24223:SF19; 3.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU363033};
KW Chloride {ECO:0000256|RuleBase:RU362037};
KW Chloride channel {ECO:0000256|RuleBase:RU362037};
KW Complete proteome {ECO:0000313|Proteomes:UP000001645};
KW Hydrolase {ECO:0000256|RuleBase:RU362037};
KW Ion channel {ECO:0000256|RuleBase:RU362037};
KW Ion transport {ECO:0000256|RuleBase:RU362037};
KW Membrane {ECO:0000256|RuleBase:RU362037};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033};
KW Phosphoprotein {ECO:0000256|RuleBase:RU362037};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW Transmembrane {ECO:0000256|RuleBase:RU362037};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362037};
KW Transport {ECO:0000256|RuleBase:RU362037}.
FT TRANSMEM 59 78 Helical. {ECO:0000256|RuleBase:RU362037}.
FT TRANSMEM 106 124 Helical. {ECO:0000256|RuleBase:RU362037}.
FT TRANSMEM 182 203 Helical. {ECO:0000256|RuleBase:RU362037}.
FT TRANSMEM 209 228 Helical. {ECO:0000256|RuleBase:RU362037}.
FT TRANSMEM 291 314 Helical. {ECO:0000256|RuleBase:RU362037}.
FT TRANSMEM 849 874 Helical. {ECO:0000256|RuleBase:RU362037}.
FT TRANSMEM 906 925 Helical. {ECO:0000256|RuleBase:RU362037}.
FT TRANSMEM 945 964 Helical. {ECO:0000256|RuleBase:RU362037}.
FT TRANSMEM 976 998 Helical. {ECO:0000256|RuleBase:RU362037}.
FT TRANSMEM 1004 1023 Helical. {ECO:0000256|RuleBase:RU362037}.
FT TRANSMEM 1095 1113 Helical. {ECO:0000256|RuleBase:RU362037}.
FT DOMAIN 73 310 ABC transmembrane type-1.
FT {ECO:0000259|PROSITE:PS50929}.
FT DOMAIN 410 633 ABC transporter. {ECO:0000259|PROSITE:
FT PS50893}.
FT DOMAIN 850 1145 ABC transmembrane type-1.
FT {ECO:0000259|PROSITE:PS50929}.
FT DOMAIN 1198 1403 ABC transporter. {ECO:0000259|PROSITE:
FT PS50893}.
FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSMGAP00000009096}.
SQ SEQUENCE 1403 AA; 158740 MW; 29C3D4D883E3FD0D CRC64;
FFFRWTKPIL KKGYRQRLEL SDIYQIPSAD SADNLSEKLE REWDRELATS KKKPKLINAL
RRCFFWKFMF YGILLYLGEV TKSVQPLLLG RIIASYDPDN FSERSIAYYL GIGLCLLFLV
RTLLIHPSIF GLHHIGMQIR IALFSLIYKK TLKLSSKVLD KISTGQLVSL LSNNLNKFDE
GLALAHFVWI APLQVALLMG LLWDMLQASA FAGLAFLIVM AFFQAWLGQM MMKYRDRRAG
KINERLVITS EIIENIQSVK AYCWEDAMEK MIESLRETEL KLTRKAAYVR YFNSSAFFFS
GFFVVFLAVV PYAVTKGIIL RKIFTTISFC IVLRMTVTRQ FPGSVQTWYD SIGAINKIQD
FLLKEEYKAL EYNLTTTGVE VDKVTAFWDE GIGELFVKAK QENNNSKAPS NDNNLFFSNF
PLHASPVLQD INFKIEKGEL LAVSGSTGSG KTSLLMLIMG ELEPSQGKIK HSGRISFSPQ
VSWIMPGTIK ENIIFGVSYD EYRYKSVIQA CQLEEDILKF PDKDYTVLGE GGIILSGGQR
ARISLARAVY KDADLYLMDS PFGYLDIFTE KEIFESCVCK LMANKTRILV TSKLEHLKIA
DKILILHEGS CYFYGTFSEL QGQRPDFSSE LMGFDSFDQF SAERRNSIIT ETLRRFSFEG
ESMGSRNEIK KQSFKQTSDF NDKRKNSIII NPLNAGRKLS IMQKNGTQVN GLEDGHVDPS
ERRISLVPDL EQGDVGLPRS NMLNSDHMLQ SRRRQSVLSL MTGTSVNQGP HVSKKGSTTF
RKMSMVPQTN LSSEIDIYTR RLSRDSILDI TDEINEDDLK ECFTDDAESM GTVTTWNTYF
RYITIHKSLI FVLILCVIIF LLEVAASLVL LLFLQKAAKI NETQPENATS DSPPVIITDT
SSYYMIYIYV GIADTLLAMG IFRGLPLVHT LITVSKTLHQ KMVHAVLYAP MSAFNSLKAG
GILNRFSKDT AILDDLLPLT VFDLIQLILI VIGAITVVSI LQPYIFLASV PVIAAFIVLR
AYFLHTSQQL KQLESEARSP IFTHLVTSLK GLWTLRAFGR QPYFETLFHK ALNLHTANWF
LYLSTLRWFQ MRIEMIFVVF FSAVAFISII TTGDGPGRVG IILTLAMNIM GTLQWAVNSS
IDVDSLMRSV SRIFKFIDMP TEEMKTIKPQ KNNQFSDALV IENRHVKDEK NWPSGGQMTV
TDLTARYTEG GTAVLENISF SISSGQTVGL LGRTGSGKST LLFAFLRLLN TEGDIRIDGI
SWNTVSLQQW RKAFGVIPQK VFIFSGTFRK NLDPYGQWND EEIWKVAEEV GLKSVIEQFP
GQLDFVLVDG GCVLSHGHKQ LMCLARSVLS KAKILLLDEP SAHLDPITSQ VIRKTLKHAF
ADCTVILSEH RLEAILECQR FLV
//