PHCL2_ANOGA
ID PHCL2_ANOGA Reviewed; 617 AA.
AC A0A1S4H2E2;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=pH-sensitive chloride channel 2 {ECO:0000250|UniProtKB:Q9V9Y4};
DE AltName: Full=Ligand-gated chloride channel protein hodor {ECO:0000303|PubMed:32269334};
DE Flags: Precursor;
GN Name=pHCl-2 {ECO:0000250|UniProtKB:Q9V9Y4};
GN Synonyms=hodor {ECO:0000303|PubMed:32269334};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [2] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
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 in the mid-gut and thereby may function in larval metabolism and fluid
CC homeostasis. Channel opening is triggered by zinc binding or, to a
CC lesser extent, an increase in extracellular pH.
CC {ECO:0000250|UniProtKB:Q9V9Y4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q9V9Y4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29824;
CC Evidence={ECO:0000250|UniProtKB:Q9V9Y4};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9V9Y4};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Adults are infertile.
CC {ECO:0000269|PubMed:32269334}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC {ECO:0000305}.
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DR EMBL; AAAB01008980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A1S4H2E2; -.
DR SMR; A0A1S4H2E2; -.
DR VEuPathDB; VectorBase:AGAP009616; -.
DR Proteomes; UP000007062; Chromosome 3R.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProt.
DR GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
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 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..617
FT /note="pH-sensitive chloride channel 2"
FT /id="PRO_5022251841"
FT TOPO_DOM 29..387
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 388..408
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 415..434
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..447
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 448..468
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..596
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 597..617
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT REGION 82..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 617 AA; 68733 MW; 2995A8AD5119A734 CRC64;
MHSPGAAAYV FLQCLVALVA AVIAQSGADQ PPTTVVEVTA HGSVSMTPPT PRSPLLNETE
LVELNQPGST AVFVALPTNP PTVSVDSSST TTVASTQEPT STTERTMSPE EIQKLLLPPA
TVEADILHVN ATDDNRPDAK SSGKDSECPT LEGADHLSQT QLLTRLTHVC RYDRLERPKR
ESINGTNGPV KVYARAYIYF MQNLEAHDLQ FKIHALLQFR YVDPRLVFRE VAPNRTKPIM
GEQSLRDLLW VPHVFLANER SSDILGTAEK DILTSISPDG TVIVSTRISA TLYCWMNLQK
FPFDEQHCST VLESWMYNED DLVLLWEHKS PVTLAPELHL TEYVLLEMFT NETVINADLS
DLRHGAFAGN YSSLSFTVHL AREMGFYMMD YFIPSIMLVA ISWVTFWLQA DQSAPRITLG
TSTMLTFITL ASAQGKTLPK VSYIKASEIW FLGCTGFIFG SLVEFAFVNT IWRRKRNVEV
KKVNSKHVLK QAITPRPARK DMSGLHKSHS CTSLADSATT VSANSFNNYL TVHSIPQKSP
SSATLPIIST TDVDRAMTEA SNVTIQIEGQ TSNVNGNGWT TMTPQEVAIW IDKRSRFVFP
IAFVIFNIFY WTFVYYV
