ID A0A0E0GCA5_ORYNI Unreviewed; 802 AA.
AC A0A0E0GCA5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA02G33300.1};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA02G33300.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA02G33300.1};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA02G33300.1}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA02G33300.1};
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; A0A0E0GCA5; -.
DR STRING; 4536.A0A0E0GCA5; -.
DR EnsemblPlants; ONIVA02G33300.1; ONIVA02G33300.1; ONIVA02G33300.
DR Gramene; ONIVA02G33300.1; ONIVA02G33300.1; ONIVA02G33300.
DR eggNOG; KOG0475; Eukaryota.
DR HOGENOM; CLU_015263_3_1_1; -.
DR OMA; TQAGKEC; -.
DR Proteomes; UP000006591; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:UniProtKB-UniRule.
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 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:UP000006591};
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 125..145
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 200..221
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 292..318
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 374..397
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 409..427
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 481..504
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 519..544
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 551..570
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 638..695
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..603
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 69..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 85661 MW; FD10C30A953246E4 CRC64;
MSSRGGEDDD HASLLRSHPA AGAGAGSGSS SPCPSPRAVG GHHHNQHADV EAVGEATVTA
SPRRSGGVRG LLRHLDRRLS ARGSGGRRSQ QPPQQLDRPE PSPTSSPQQR ERVGEELGDG
APPEWALLLI GCLLGLATGI CVAAFNRGVS ISLVLLTDWK LDYPLQVEST GVHVIHEWAW
AGTPNEGAAW LRLQRLADTW HRILLIPVTG GVVVGMMHGL LEIFDQLKLV KPPQKQGINF
LAAIFPTVNA VQAAVTLGTG CSLGPEGPSV DIGKSCANGC SEMMENNRER RIALVAAGAA
AGIASGFNAA VAGCFFAIET VLRPLKAENS PPFTTAMIIL ASVISSTVSN VLLGERPAFI
VPAYELKSAA ELPLYLILGM LCGAVSVVFG RLVVWFSNFF GYLKERYDFP IVVYPALGGL
GAGLIALKYP GILYWGFTNV EEILHTGKSA SAPGIWLLTQ LAAAKVVATA LCKGSGLVGG
LYAPSLMIGA AVGAVFGGSA GYLINSAVPG NAAVAQPQAY ALVGMAATLA SVCSVPLTSV
LLLFELTKDY RILLPLMGAV GLAIWVPSVV NQSKDGEPSR FRTPRRGYSS LSSEDRNSKS
WRRGDSVNDL ELTSLRTDNY DTYNEEMLLD DLKVSQAMSK SYVKIPTSAM VTEALKLLHD
KQQNCGLVVD CEDFLEGIVT LGDIRRMGFE LHGDSFTSGD QLKPAVKTKQ FTQAGKECVL
INGDVAGKFF NHIIVSYSRI PARGIKQLPV VKRGVGHRTE GKRKLIALLH YDSIGHCLRE
EIENWKAIYQ IKEDFHLIAN GH
//
