PHCL2_DROME
ID PHCL2_DROME Reviewed; 526 AA.
AC Q9V9Y4; E3CTP9;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=pH-sensitive chloride channel 2 {ECO:0000303|PubMed:27172217};
DE AltName: Full=Ligand-gated chloride channel protein hodor {ECO:0000303|PubMed:32269334};
DE Flags: Precursor;
GN Name=pHCl-2 {ECO:0000303|PubMed:27172217, ECO:0000312|FlyBase:FBgn0039840};
GN Synonyms=hodor {ECO:0000303|PubMed:32269334};
GN ORFNames=CG11340 {ECO:0000312|FlyBase:FBgn0039840};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:ADO51077.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 92-526.
RA Carlson J., Booth B., Frise E., Sandler J., Wan K., Yu C., Celniker S.;
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27172217; DOI=10.1534/g3.116.029546;
RA Remnant E.J., Williams A., Lumb C., Yang Y.T., Chan J., Duchene S.,
RA Daborn P.J., Batterham P., Perry T.;
RT "Evolution, Expression, and Function of Nonneuronal Ligand-Gated Chloride
RT Channels in Drosophila melanogaster.";
RL G3 (Bethesda) 6:2003-2012(2016).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=27358471; DOI=10.1242/jeb.141069;
RA Feingold D., Starc T., O'Donnell M.J., Nilson L., Dent J.A.;
RT "The orphan pentameric ligand-gated ion channel pHCl-2 is gated by pH and
RT regulates fluid secretion in Drosophila Malpighian tubules.";
RL J. Exp. Biol. 219:2629-2638(2016).
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-255 AND GLU-296.
RX PubMed=32269334; DOI=10.1038/s41586-020-2111-5;
RA Redhai S., Pilgrim C., Gaspar P., Giesen L.V., Lopes T., Riabinina O.,
RA Grenier T., Milona A., Chanana B., Swadling J.B., Wang Y.F., Dahalan F.,
RA Yuan M., Wilsch-Brauninger M., Lin W.H., Dennison N., Capriotti P.,
RA Lawniczak M.K.N., Baines R.A., Warnecke T., Windbichler N., Leulier F.,
RA Bellono N.W., Miguel-Aliaga I.;
RT "An intestinal zinc sensor regulates food intake and developmental
RT growth.";
RL Nature 580:263-268(2020).
CC -!- FUNCTION: Ligand and pH-gated channel that mediates chloride transport
CC primarily in the mid-gut and thereby functions in larval metabolism and
CC fluid homeostasis (PubMed:32269334, PubMed:27358471, PubMed:27172217).
CC Channel opening is triggered by zinc binding or, to a lesser extent, an
CC increase in extracellular pH (PubMed:32269334, PubMed:27358471). Zinc-
CC dependent activity in the mid-gut is required for modulating Tor-
CC dependent metabolic programs that promote larval feeding and systematic
CC growth (PubMed:32269334). It may therefore act as an intestinal zinc
CC sensor that mediates larval growth and metabolism in response to
CC micronutrient availability (PubMed:32269334). Activates Tor signaling
CC via its activity in maintaining lysosome homeostasis in interstitial
CC cells and/or by its role in activating the release of insulin-like
CC peptides in the brain after feeding, via an unknown mechanism
CC (PubMed:32269334). Functions in lysosome homeostasis by regulating
CC chloride transport into enterocyte lysosomes to sustain V-ATPase
CC function which maintains lysosomal acidification and consequently
CC promotes Tor activation at the lysosome membrane (PubMed:32269334).
CC Also appears to play a role in regulating fluid secretion and osmotic
CC homeostasis in Malpighian tubules in response to the pH of
CC extracellular urine (PubMed:27358471). This function is important for
CC proper urine production during diuresis (PubMed:27358471).
CC {ECO:0000269|PubMed:27172217, ECO:0000269|PubMed:27358471,
CC ECO:0000269|PubMed:32269334}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:27358471,
CC ECO:0000269|PubMed:32269334};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29824;
CC Evidence={ECO:0000305|PubMed:32269334};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:27358471, ECO:0000269|PubMed:32269334}; Multi-pass
CC membrane protein {ECO:0000255}. Cell projection, microvillus membrane
CC {ECO:0000269|PubMed:32269334}; Multi-pass membrane protein
CC {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:32269334};
CC Multi-pass membrane protein {ECO:0000255}. Lysosome membrane
CC {ECO:0000269|PubMed:32269334}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Enriched on the apical side of gut interstitial
CC cells; on the brush-border and on the lysosomes.
CC {ECO:0000269|PubMed:32269334}.
CC -!- TISSUE SPECIFICITY: In third-instar larvae, expressed in the principal
CC cells of the excretory Malpighian tubules (at protein level)
CC (PubMed:32269334, PubMed:27358471). Also detected in the enterocytes of
CC the copper cell region and the iron cell region of the larval midgut
CC (at protein level) (PubMed:32269334). In the copper cell region
CC expression is confined to the interstitial cells and in the iron cell
CC region it is expressed in the anterior portion (at protein level)
CC (PubMed:32269334). Expressed in the Malpighian tubules and the middle
CC midgut of third instar larvae and adults (PubMed:27172217).
CC {ECO:0000269|PubMed:27172217, ECO:0000269|PubMed:27358471,
CC ECO:0000269|PubMed:32269334}.
CC -!- DISRUPTION PHENOTYPE: Larval lethal (PubMed:32269334). Larval
CC development is delayed due to decreased food intake and reduced
CC systematic insulin signaling (PubMed:32269334). However, escapers
CC eventually attain a normal size during the pupal and adult stages
CC (PubMed:32269334). Unlike in wild-type larvae, mutants do not develop a
CC preference for zinc supplemented food or eat more when fed a zinc rich
CC diet (PubMed:32269334). The copper cell region of the larval midgut
CC displays developmental and functional defects such as reduced luminal
CC acidity, increased bacterial titers and enlarged cell volume
CC (PubMed:32269334). The interstitial cells also display increased cell
CC volume due to reduced basal infolding (PubMed:32269334). They also
CC display an increased tolerance to copper but not zinc, likely due to
CC increased cell acidity which has been found to decrease copper uptake
CC (PubMed:27172217). Postembryonic knockdown specifically in interstitial
CC and Malpighian tubule principal cells also results in reduced food
CC intake and increased time to pupation, whereas knockdown only in
CC principal cells, iron cells or copper cells has no effect on larval
CC development (PubMed:32269334). Mutants display a further increase in
CC developmental delay in a Tor RNAi-mediated background
CC (PubMed:32269334). {ECO:0000269|PubMed:27172217,
CC ECO:0000269|PubMed:32269334}.
CC -!- MISCELLANEOUS: The name 'hodor' is an acronym for 'hold on, don't
CC rush', referring to the developmental delay phenotype in mutants.
CC {ECO:0000303|PubMed:32269334}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADO51077.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF57144.1; -; Genomic_DNA.
DR EMBL; AE014297; ALI30655.1; -; Genomic_DNA.
DR EMBL; BT125715; ADO51077.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001303470.1; NM_001316541.1.
DR RefSeq; NP_651861.1; NM_143604.3.
DR AlphaFoldDB; Q9V9Y4; -.
DR SMR; Q9V9Y4; -.
DR IntAct; Q9V9Y4; 1.
DR STRING; 7227.FBpp0085128; -.
DR GlyGen; Q9V9Y4; 8 sites.
DR PaxDb; Q9V9Y4; -.
DR EnsemblMetazoa; FBtr0085766; FBpp0085128; FBgn0039840.
DR EnsemblMetazoa; FBtr0347502; FBpp0312576; FBgn0039840.
DR GeneID; 43703; -.
DR KEGG; dme:Dmel_CG11340; -.
DR UCSC; CG11340-RA; d. melanogaster.
DR CTD; 43703; -.
DR FlyBase; FBgn0039840; pHCl-2.
DR VEuPathDB; VectorBase:FBgn0039840; -.
DR eggNOG; KOG3644; Eukaryota.
DR GeneTree; ENSGT00940000168665; -.
DR HOGENOM; CLU_010920_0_1_1; -.
DR InParanoid; Q9V9Y4; -.
DR OMA; MLWVPHI; -.
DR OrthoDB; 1260459at2759; -.
DR PhylomeDB; Q9V9Y4; -.
DR Reactome; R-DME-112314; Neurotransmitter receptors and postsynaptic signal transmission.
DR BioGRID-ORCS; 43703; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43703; -.
DR PRO; PR:Q9V9Y4; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039840; Expressed in adult Malpighian tubule (Drosophila) and 9 other tissues.
DR Genevisible; Q9V9Y4; DM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:1902495; C:transmembrane transporter complex; IDA:FlyBase.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IDA:UniProtKB.
DR GO; GO:0061778; F:intracellular chloride channel activity; IDA:UniProtKB.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0061797; F:pH-gated chloride channel activity; IDA:FlyBase.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0106219; F:zinc ion sensor activity; IDA:UniProtKB.
DR GO; GO:0071294; P:cellular response to zinc ion; IMP:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IDA:FlyBase.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:2001151; P:regulation of renal water transport; IMP:FlyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00253; GABAARECEPTR.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Chloride; Chloride channel; Endosome;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Lysosome; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..526
FT /note="pH-sensitive chloride channel 2"
FT /id="PRO_5015100030"
FT TOPO_DOM 19..300
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 301..321
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 328..347
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..360
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 361..381
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..505
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 506..526
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT REGION 463..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 255
FT /note="E->K: Results in zinc-elicited currents with
FT increased rise time and deactivation kinetics in Xenopus
FT oocytes; when associated with F-296."
FT /evidence="ECO:0000269|PubMed:32269334"
FT MUTAGEN 296
FT /note="E->F: Results in zinc-elicited currents with
FT increased rise time and deactivation kinetics in Xenopus
FT oocytes; when associated with K-255."
FT /evidence="ECO:0000269|PubMed:32269334"
FT CONFLICT 299
FT /note="Y -> H (in Ref. 3; ADO51077)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 59826 MW; BC78EC5EC219F596 CRC64;
MDTLGIFVLI SYLGLSSAAG VHLGDLQQNL AANGSVVVSP LNTTDAFSVS INLSQSTVNN
CPSLKNAESM ALMELLTRLT APCRYDRMVP PVVHNKDGEE VPMDIYARFY IYVMKNLDSS
DLQFTVQGLL QLRYLDPRLA FSSYLPNRRQ PIMGESELKK MLWVPHIFLT NEQASTVLGT
SAKDELTSIY PNGTVLTSTR LQATLYCWMN FQKFPFDEQK CKTTLESWMY NTTLVQLHWE
TDNPVSFDKQ LQLTEYNLIG SLYNESIRVS NESYMSHGSL EGNYSIISFT VLLTREVGYY
VIDYFLPSIM IVTISWVSFW LQADQTPART TLGCTTLLSF ITLSLSQENN LMKVSYVTMS
EVWFLVCTIF IFGSLVEFAF VNTIWRRNND LQLKKRTTKY IVKSTFVPHL KKHRRHGYRR
TDSTMSTMST TSMDKTCGPN NTVITIETPI IIGGSLSRED SAISLDEQDE TSTSESSDSS
KEKPAQTFAT MTPKEVSLWI DRKMRFVFPL SFIVFNALFW TLVYCL
