ID A0A2G5CIT7_AQUCA Unreviewed; 771 AA.
AC A0A2G5CIT7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN ORFNames=AQUCO_05400085v1 {ECO:0000313|EMBL:PIA30737.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA30737.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA30737.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) 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}.
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DR EMBL; KZ305071; PIA30737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5CIT7; -.
DR Proteomes; UP000230069; 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; cd04591; CBS_pair_voltage-gated_CLC_euk_bac; 1.
DR CDD; cd03685; ClC_6_like; 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 InterPro; IPR002251; Cl_channel_pln.
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; 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 PROSITE; PS51371; CBS; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000230069};
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 75..96
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 116..137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 231..254
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 266..285
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 318..339
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 449..467
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 473..492
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 504..529
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 589..650
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 704..760
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 771 AA; 85020 MW; BA7985F7970E6D40 CRC64;
MLSDHIQNGI ETAKLVWSRL PTSEEGESEE VNSSKRSDGT SVESLDYEVI ENYAYREEQA
QRGRLYVGYY VGVKWFFALL IGIGTGLAAV FINIAVENFA GWKFAATFAI IQKSYLAGFI
VYILINLALV FSSVFIITQF APAAAGSGIP EIKGYLNGVD THGILLFRTL IGKIFGSIGS
VGGGLALGKE GPLVHTGACI ASLLGQGGST KYHLSPRWLQ VFKSDRDRRD LVTCGCAAGV
AAAFRAPVGG VLFALEEVTS WWRSQLMWRV FFTSAIVAVV VRTAMGWCKS GKCGHFGSGG
FIIWDISGGQ DDYSFEELFP MAIIGIIGGL LGALFNQLTL YITYWRRKSL HKRGNRVKII
EACLISVITS IISFGLPLLR KCSPCPESDA NSDLECPRPP GMYGNYVNFY CSKDKEYNDL
ATIFFNTQDD AIRNLFSAKT IHEYSAQSLL TFLVMFYTLA VVTFGTAVPA GQFVPGIMIG
STYGRLVGMF VVKFYRKLNI EEGTYALLGA ASFLGGSMRM TVSLCVIMVE ITNNLKLLPL
IMLVLLISKA VGDAFNEGLY EEQAHLRGIP LLESRPKYHM RKMTAKEACR RQKVVSFPRV
VKVANVFSIL RSNKHNGFPV VDHGRNGEAL VIGLILRSHL LVLLQSKLDF QHSPLPCDLG
MGSIPIRHNF SEFVKPASST GLSIEDIHLT PDDFEMYIDL TPFLNPSPYV VPEDMSLTKV
YNLFRQLGLR HVFVVPRAPR VIGLITRKDL LVEENDDSAT VELQSTSSSE I
//