ID A0A498J0F2_MALDO Unreviewed; 787 AA.
AC A0A498J0F2;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN ORFNames=DVH24_034734 {ECO:0000313|EMBL:RXH87834.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH87834.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH87834.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH87834.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXH87834.1}.
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DR EMBL; RDQH01000336; RXH87834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498J0F2; -.
DR STRING; 3750.A0A498J0F2; -.
DR Proteomes; UP000290289; Chromosome 10.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
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:SF6; CHLORIDE CHANNEL PROTEIN CLC-E; 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:UP000290289};
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 122..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 286..310
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 330..348
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 369..395
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 407..424
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 518..543
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 549..567
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 644..700
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 21..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..111
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 787 AA; 84599 MW; 6CA5D1C428066D6D CRC64;
MRGLDCIWRF PNAHSRRHLC PLVSPPPSSP PPRKTVLLFS PTSNTQTRTI DTKNASAGYT
SKTRTSKPIK NGRALTPRPP LSLPQTQQTQ QQNDDNDNAE EQEEEEEDED ESRAQGRGRG
NWTIVLSSSL VGLLTGIGVV LFNYSVNEIR DVFWGGMPQR GASWLREEYV GDTWKQVILV
PASGGLIVAI LNFLRDALED GSQDNNGNEQ GGEKGENLLV KMGMPVSVFD GLKAASRPFL
KAIAACVTLG TGNSLGPEGP SVEIGTSIAK GVGAVFDKSS QRRLSLVAAG SAAGIASGFN
AAVSGCFFAV ESVLWPSPPD SSSISLVNTT SMVILSAVIA SVVSEVGLGS EPAFKVPYYD
FRSPTELPLY LLLGVLCGLV SLTLSKCTSY MLVFVDNLHK TMGLPKFLFP IMGGLAVGLM
ALAYPEILYR GFENVDLLLE SRPLEKCLSA DLLLQLVVVK IGATSLSRAS GLVGGFYAPS
LFIGAATGMA YGKFISSAVA QSSPILHLSV LEVASPQAYG LVGMAATLAG VCQVPLTSVL
LLFELTQDYR IVLPLLGAVG LSSWITSGQT RRKDNLKTKK LKQGKSSGNQ QPEVPSPSAS
GLSSSNAFTS NASNLCELES SLCIDGSDIN TENLEKRISV SEAMRTRYVT VLMDTLLTEA
VTLMLAEKQP CAMIVDDDHI LIGLLTLRDI QEFSNKYAKS RRQRPKELIV SEMCSSDGEV
CRVPWTATPA MTLLSAQNIM NKYGMNQIPV VTQHVQDHRG HLSFSNQRIP LQVTNTGCTD
LLIKQNT
//
