ID A0A0E0CQS9_9ORYZ Unreviewed; 790 AA.
AC A0A0E0CQS9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
OS Oryza meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI02G29500.2};
RN [1] {ECO:0000313|EnsemblPlants:OMERI02G29500.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI02G29500.2};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI02G29500.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361221}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361221}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC {ECO:0000256|ARBA:ARBA00009476, ECO:0000256|RuleBase:RU361221}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361221}.
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DR AlphaFoldDB; A0A0E0CQS9; -.
DR STRING; 40149.A0A0E0CQS9; -.
DR EnsemblPlants; OMERI02G29500.2; OMERI02G29500.2; OMERI02G29500.
DR Gramene; OMERI02G29500.2; OMERI02G29500.2; OMERI02G29500.
DR eggNOG; KOG0475; Eukaryota.
DR HOGENOM; CLU_015263_3_1_1; -.
DR Proteomes; UP000008021; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:UniProtKB-UniRule.
DR CDD; cd04592; CBS_pair_voltage-gated_CLC_euk_bac; 1.
DR CDD; cd00400; Voltage_gated_ClC; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR PANTHER; PTHR43427; CHLORIDE CHANNEL PROTEIN CLC-E; 1.
DR PANTHER; PTHR43427:SF3; CHLORIDE CHANNEL PROTEIN CLC-F; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
DR PROSITE; PS51371; CBS; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Chloride {ECO:0000256|RuleBase:RU361221};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|RuleBase:RU361221};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361221};
KW Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361221};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361221}; Transport {ECO:0000256|RuleBase:RU361221}.
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 184..205
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 276..302
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 358..381
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 393..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 465..488
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 503..528
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 535..554
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 622..679
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 84299 MW; 74A4E7969B977434 CRC64;
MSSRGSDDDD HASLLRSHPA AGAGAGSGSS SPCPSPRAVG GHHHHHQQHQ HADVEAAGEA
TVTASPRRSG GGGGVRGLLR HLDRRLSARG SGGRRSQQPP QQLDRSEPSP TSSPQQRERV
GEELGDGAPP EWALLLIGCL LGLATGICVA AFNRGVHVIH EWAWAGTPNE GAAWLRLQRL
ADTWHRILLI PVTGGVVVGM MHGLLEIFDQ LKLVKPPQKQ GINFLAAIFP TVNAVQAAVT
LGTGCSLGPE GPSVDIGKSC ANGCSEMMEN NRERRIALVA AGAAAGIASG FNAAVAGCFF
AIETVLRPLK AENSPPFTTA MIILASVISS TVSNVLLGER PAFIVPAYEL KSAAELPLYL
ILGMLCGAVS VVFGRLVVWF SNFFGYLKER YDFPIVVYPA LGGLGAGLIA LKYPGILYWG
FTNVEEILHT GKSASAPGIW LLTQLVAAKV VATALCKGSG LVGGLYAPSL MIGAAVGAVF
GGSAAYLINS AIPGNAAVAQ PQAYALVGMA ATLASVCSVP LTSVLLLFEL TKDYRILLPL
MGAVGLAIWV PSVVNQPKDG EPSRFRTPRR GYSSLSSEDR NSKSWRRGDC VNDLELTSLR
TDNYDTYNEE MLLDDLKVSQ AMSKSYVKIP TSATVTEALK LLHDKQQNCG LVVDCEDFLE
GIVTLGDIRR VGFELHGDSF TSGDQLKPAE NSSTISLCLT RGFQYEGNER GLLTCFPDTD
LTTAKNLMEA RGIKQLPVVK RGIGHRTEGK RKLIALLHYD SIGHCLREEI ENWKAIYQIK
EDFHLIANGH
//
