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PPK11_DROME
ID   PPK11_DROME             Reviewed;         516 AA.
AC   Q9VL84; Q86LH0;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Pickpocket protein 11;
DE            Short=PPK11 {ECO:0000303|PubMed:12571352, ECO:0000312|EMBL:AAO47368.1};
GN   Name=ppk11; ORFNames=CG34058, CG4110;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAO47368.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=12571352; DOI=10.1073/pnas.252785099;
RA   Liu L., Johnson W.A., Welsh M.J.;
RT   "Drosophila DEG/ENaC pickpocket genes are expressed in the tracheal system,
RT   where they may be involved in liquid clearance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:2128-2133(2003).
RN   [2] {ECO:0000312|EMBL:AAF52812.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4] {ECO:0000305}
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12848938; DOI=10.1016/s0896-6273(03)00394-5;
RA   Liu L., Leonard A.S., Motto D.G., Feller M.A., Price M.P., Johnson W.A.,
RA   Welsh M.J.;
RT   "Contribution of Drosophila DEG/ENaC genes to salt taste.";
RL   Neuron 39:133-146(2003).
CC   -!- FUNCTION: Part of a complex that plays a role in tracheal liquid
CC       clearance. In both larvae and adults, contributes to the behavioral
CC       response to salt. Probable role in sodium transport.
CC       {ECO:0000269|PubMed:12571352, ECO:0000269|PubMed:12848938,
CC       ECO:0000303|PubMed:12571352}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in embryonic and larval tracheal systems
CC       in the dorsal trunk and transverse connective (TC), but not in the
CC       junction between the dorsal trunk and TC, and in several tracheal
CC       branches and terminal cells. In larvae, also expressed in ventral pits.
CC       Expressed in the taste-sensing terminal organ of the larval head. In
CC       adult, expressed in hairs on the tibia, femur, tarsi of the leg and
CC       wing margin. {ECO:0000269|PubMed:12571352,
CC       ECO:0000269|PubMed:12848938}.
CC   -!- DEVELOPMENTAL STAGE: Expression is first detected during late
CC       embryogenesis, at stage 15 in the dorsal trunk. At stage 16, expression
CC       is observed in the TC and extends into the primary branches. By stage
CC       17, expression is more extensive in the primary branches and in some
CC       secondary branches. {ECO:0000269|PubMed:12571352}.
CC   -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC       1.A.6) family. {ECO:0000305}.
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DR   EMBL; AY226542; AAO47368.1; -; mRNA.
DR   EMBL; AE014134; AAF52812.2; -; Genomic_DNA.
DR   RefSeq; NP_001334672.1; NM_001347761.1.
DR   AlphaFoldDB; Q9VL84; -.
DR   BioGRID; 60396; 2.
DR   STRING; 7227.FBpp0100162; -.
DR   PaxDb; Q9VL84; -.
DR   EnsemblMetazoa; FBtr0100831; FBpp0100162; FBgn0065109.
DR   GeneID; 34299; -.
DR   KEGG; dme:Dmel_CG34058; -.
DR   UCSC; CG34058-RA; d. melanogaster.
DR   CTD; 34299; -.
DR   FlyBase; FBgn0065109; ppk11.
DR   VEuPathDB; VectorBase:FBgn0065109; -.
DR   eggNOG; KOG4294; Eukaryota.
DR   GeneTree; ENSGT00940000171214; -.
DR   HOGENOM; CLU_024950_1_1_1; -.
DR   InParanoid; Q9VL84; -.
DR   OMA; RQQIRYR; -.
DR   PhylomeDB; Q9VL84; -.
DR   Reactome; R-DME-2672351; Stimuli-sensing channels.
DR   BioGRID-ORCS; 34299; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 34299; -.
DR   PRO; PR:Q9VL84; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0065109; Expressed in open tracheal system trachea and 6 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0015280; F:ligand-gated sodium channel activity; IBA:GO_Central.
DR   GO; GO:0005272; F:sodium channel activity; ISS:FlyBase.
DR   GO; GO:0035002; P:liquid clearance, open tracheal system; IMP:FlyBase.
DR   GO; GO:0060025; P:regulation of synaptic activity; IMP:FlyBase.
DR   GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR   GO; GO:0035199; P:salt aversion; IMP:UniProtKB.
DR   GO; GO:0050914; P:sensory perception of salty taste; IMP:FlyBase.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006814; P:sodium ion transport; ISS:FlyBase.
DR   InterPro; IPR001873; ENaC.
DR   InterPro; IPR020903; ENaC_CS.
DR   PANTHER; PTHR11690; PTHR11690; 1.
DR   Pfam; PF00858; ASC; 2.
DR   PROSITE; PS01206; ASC; 1.
PE   2: Evidence at transcript level;
KW   Ion channel; Ion transport; Membrane; Reference proteome; Sodium;
KW   Sodium channel; Sodium transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..516
FT                   /note="Pickpocket protein 11"
FT                   /id="PRO_0000420125"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        454..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   516 AA;  59999 MW;  2C7784ABBD219FB1 CRC64;
     MSDVPGEDSP THFYPVNFEN YLRPKQSIKC QPLQRFKKPN ERATNLYRNL KRLKILRWYN
     RVSKRFEEFP LPKFLGFLQA RNDDGLCKRK TGFEIYCEMA SIHGFHIFVG AKTWQRILWW
     LLICNAVLLS FTLVIMSLSM SKETPTIRFI DTMMKPTAEV PFPAVTICGF NTKEWMNSSQ
     IVNQRNASWL ELLEDLALPI CPQIKICQWD NRMVNCLDQL QPIWTLDQRL CCSFNYNKQL
     FSSYLGVSFV LRSNDEILQS SKSAGFEVLI HESHEIPNGA TPRVFVPGES DAHIMLRPYI
     NRFTKNLKGL SLQKRGCYFS TERRLILSDV YNQINCLAEC RTESILKSCG CIPPKSPIEK
     SWLICDLKQM QCVIDFDHDE IISGEQKNCD CLPPCEFNRY EFQSDIRFIK GMINNSIVNT
     SNQETTNEVR VRVYYDSAIA EELLLDVYEN WLTFIGTFGG ITGLFMGCSF VSVFELIFFS
     CVRPTCNWLT RQQILWRRRR NQRVGITESR SLGPAN
 
 
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