ID A0A0L6X2Z4_9AGAR Unreviewed; 880 AA.
AC A0A0L6X2Z4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN ORFNames=J132_06279 {ECO:0000313|EMBL:KNZ82207.1};
OS Termitomyces sp. J132.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC Termitomyces.
OX NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ82207.1, ECO:0000313|Proteomes:UP000053712};
RN [1] {ECO:0000313|Proteomes:UP000053712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA Hu H., Poulsen M.;
RT "The genome of Termitomyces.";
RL Submitted (JAN-2014) 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|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 EMBL; KQ412169; KNZ82207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6X2Z4; -.
DR OrthoDB; 150430at2759; -.
DR Proteomes; UP000053712; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:UniProtKB-UniRule.
DR CDD; cd03684; ClC_3_like; 1.
DR Gene3D; 3.10.580.20; -; 1.
DR Gene3D; 3.90.1280.20; -; 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; PTHR45711:SF9; ANION_PROTON EXCHANGE TRANSPORTER GEF1; 1.
DR PANTHER; PTHR45711; CHLORIDE CHANNEL PROTEIN; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SMART; SM00116; CBS; 1.
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|ARBA:ARBA00023214, ECO:0000256|RuleBase:RU361221};
KW Ion transport {ECO:0000256|RuleBase:RU361221};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361221};
KW Reference proteome {ECO:0000313|Proteomes:UP000053712};
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..99
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 141..159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 180..206
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 218..234
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 246..270
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 355..376
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 471..496
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 502..521
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 681..741
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 880 AA; 96938 MW; 307B0DB2D2972E07 CRC64;
MHPAEGLDDD ELEQIRRYED FTTIDWIQDS ILERNRRIRT AHSYSAPARV RRGPGRSWFW
LWSQVRKAMD MGQSWFVVSL AGMVIGVNAA IISIITQWLS DIKFGYCSDG WWLNQQFCCW
EIEGEDVDGC DSWHPWSNVM MGRWTVFVFF ATLFSFVAAH LVRSMAKYAA GSGISEIKCI
LAGFVMQGYL GFATVVIKSI TLPLVIASGL SVGKEGPSVH VACCIGSLVA GLFKKFSLSI
GKMREIVTAA SAAGVAVAFG SPIGGVLFSI EEMSHGFSIK TMWRSFLCAL VATVTLSAMN
PFRTGKLVLF QITYDRDWHF FEIMFYVILG IFGGLYGAFM VKFNLQVAAF RRKHLANHGV
AEAVTLATLT AMIGYFNRFL RMDMTSSMAI LFRECEGGGN IGNLCQTPAQ WRISNSLFLA
TIIRIGLVVI SYGCKVPAGI FVPSMAIGAT FGRMIGILVK AMERAYTGHG IFAVCAPDIP
CITPGTYAFL GAAAALSGVM RITVTVVVIM FELTGALNYI LPTMIVLLVT KAVGDFLGTN
GIADEMIRFN GFPFLEKEDH AYNVSVSAVM RTGMHTLMES GMDVKQIEDI LEATHVKGFP
IESADGLRHI IGYIGRTELR YVLDRAKKMP RVDDDTRCHF APHDSEHSIH SVSFGIEEEA
AGTSFFESAL SEGGIRFWPW VNLTPITVSP ELPLEIVMQL FKRMGRVLPR VILVENHGVL
MGLVTVKDVL KFIATKPSHE LSWDDRGGLD GLLEESLFCS PIAMAHSSNT TTSSSQQHYS
SSLAAYTLKQ LSAAHAALDN DEQATAKLPA TVKMYGHHVS KRSTGARNHS TFCDPKQTKL
PQKRLLNLPH RSVPAPSNQP KLDSLRILSI PHVGSLVCFL
//