ID A0A0E0GSA0_ORYNI Unreviewed; 942 AA.
AC A0A0E0GSA0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
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:ONIVA03G31920.1};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA03G31920.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA03G31920.1};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA03G31920.1}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA03G31920.1};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel. {ECO:0000256|ARBA:ARBA00026071}.
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}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0E0GSA0; -.
DR STRING; 4536.A0A0E0GSA0; -.
DR EnsemblPlants; ONIVA03G31920.1; ONIVA03G31920.1; ONIVA03G31920.
DR Gramene; ONIVA03G31920.1; ONIVA03G31920.1; ONIVA03G31920.
DR eggNOG; KOG0177; Eukaryota.
DR eggNOG; KOG0474; Eukaryota.
DR HOGENOM; CLU_312479_0_0_1; -.
DR OMA; FLKINMT; -.
DR Proteomes; UP000006591; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR GO; GO:0005802; C:trans-Golgi network; IEA:EnsemblPlants.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045824; P:negative regulation of innate immune response; IEA:EnsemblPlants.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:InterPro.
DR GO; GO:0009826; P:unidimensional cell growth; IEA:EnsemblPlants.
DR CDD; cd04591; CBS_pair_voltage-gated_CLC_euk_bac; 1.
DR CDD; cd03685; ClC_6_like; 1.
DR CDD; cd03758; proteasome_beta_type_2; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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 InterPro; IPR002251; Cl_channel_pln.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR035206; Proteasome_beta2.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11689; CHLORIDE CHANNEL PROTEIN CLC FAMILY MEMBER; 1.
DR PANTHER; PTHR11689:SF136; H(+)_CL(-) EXCHANGE TRANSPORTER 6; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR PRINTS; PR01120; CLCHANNELPLT.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703}; 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 Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000006591};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 71..94
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 114..136
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 265..284
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 317..342
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 398..416
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 539..599
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 650..708
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 942 AA; 103314 MW; A2DDC8080A1B8D15 CRC64;
MARLAWTRLP TADGAGAGAE GPGPVPASPS SAGYELFAGG VESLDYEVIE NYAYREEQAQ
RSKFWVPYYV MLKWLFSLLI GVGTGLAAIF INLAVENFSG WKYAATFAII QHSYFVGFFV
YIVFNLALVF SSVYIVTNFA PAAAGSGIPE IKGYLNGVDT HGILLFRTLV GKIFGSIGSV
GGGLALGKEG PLVHTGACIA SLLGQGGSAK YHLSSRWVRI FESDRDRRDL VTCGCAAGVA
AAFRAPVGGV LFALEEVTSW WRSHLMWRVF FTSAVVAVVV RSAMNWCKSG KCGHFGSGGF
IIWDISGGQE DYSYQELLPM AIIGVIGGLL GALFNQLTLY ITKWRRTYLH KKGKRVKFYC
SKDNEYNDLA TIFFNTQDDA IRNLFSAKTF HEYSAQSLIT FLVMFYSLAV VTFGTAVPAG
QFVPGIMIGS TYGRLVGMFV VKFYKKLNVE EGTYALLGAA SFLGGSMRMT VSLCVIMVEI
TNNLKLLPLI MLVLLISKAV GDFFNEGLYE VQAQLRGIPL LDSRPKQVMR NMSAKDACKN
QKVVSLPRVS RIVDIISVLR SNKHNGFPVV DRGQNGESLV IGLILRSHLL VLLQSKVDFQ
NSPFPCGPGI LNRHNTSDFV KPASSKGKSI DDIHLTEDEL GLYLDLAPFL NPSPYIVPED
MSLAKVYNLF RQLGLRHIFV VPRPSRVVGL ITRQDLLLEE NGNNVTTELQ STSVRLHFPD
ESAAAAAAAV MECVIGVVGR DFAVVAADTS AVQSILVHKT DEDKVMVLDS HKLMGASGEP
GDRVQFTEFI QKNLHLYQFR NNIPLSTAAT ANFTRGELAT ALRKNPYYVN VLLAGYDSDV
GASLYYIDYI ATFHKIEKGA FGYGSYFCLS LMDKLYRPDM SVEEAVDLVD KCIKEIRLRL
VVAPQNFIIK IVDKEGAREY ARRAYTDSPP EAATSEAATV AA
//
