ID A0A395ICE7_ASPHC Unreviewed; 871 AA.
AC A0A395ICE7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN ORFNames=BO97DRAFT_439556 {ECO:0000313|EMBL:RAL17726.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL17726.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL17726.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL17726.1,
RC ECO:0000313|Proteomes:UP000248961};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-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|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; KZ824267; RAL17726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395ICE7; -.
DR STRING; 1450537.A0A395ICE7; -.
DR VEuPathDB; FungiDB:BO97DRAFT_439556; -.
DR OrthoDB; 150430at2759; -.
DR Proteomes; UP000248961; 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; cd04591; CBS_pair_voltage-gated_CLC_euk_bac; 1.
DR CDD; cd03684; ClC_3_like; 1.
DR Gene3D; 3.10.580.20; -; 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; CHLORIDE CHANNEL PROTEIN; 1.
DR PANTHER; PTHR45711:SF6; CHLORIDE CHANNEL PROTEIN; 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|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:UP000248961};
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 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 254..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 356..380
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 473..490
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 552..571
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 591..612
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 618..642
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 776..834
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 95947 MW; C61BB9A5775049A7 CRC64;
MSLPHLEPGT EARASPSQSY SDDPSSRSEP PNSHTYPQSS RASLSGGLDE PISFKRKQKQ
RSRFSISRLF PGESTSTRDT GFGSPNRNRQ PPHSRSPPPR DFPSSNGNAN HKDSGFLDWY
VEGPGRRVGY DDLTAIDWIF EYTKERQRKR LLYANGQGLV GYTRKILDAS NVWIVLIATG
ILVGIIAACI DVSSDWLADL KTGYCKNGAG GGRFYLNRSF CCWGHDDINN CLDWTPWRTA
FGVTSRDGGY TVDYVLYILY SVFFAVCACI LVRTYAIYAK HSGIPEIKTV LGGFVIRHFM
GPWTLAIKSL GLCLSVASGM WLGKEGPLVH VACCCASLMM KPFHSLNHNE ARKREVLSAA
AAAGISVAFG APIGGVLFSL EQLSYYFPDK TMWQSFVCAM VASVTLHALD PFRTGNIVLY
QVKYTRGWHR FEIIPFVILG IVGGLYGAFF IRLNMKIADW RRSRSIPRPI LEVSVVALLN
SLINFPNLFM KAQNSELVHS LFAECGTATD DPFGFCKTGA VSASTVALLL SAAILGFFLA
SITFGLDIPA GIILPSIAIG ALYGRALGIV FRMWQQAFPK FFLFGSCEPD IPCVTPGIYA
IIGAASALGG ATRMTVSIVV IMFELTGALT YVIPIMIAVM LSKWCGDIFG KRGIYESWIQ
LKEYPFLDHR DDSAPPDVYA HKVMTTVDDL TVITAVGHTI DTLRNLLMTT SYRGYPVVTD
MANPVLLGYI SRNELSYGLK YSASPSDHEL SGTTQVFFTH QPFADPGETL DLRPWMDQTP
ITLNSNTTFL IVLRMFQRLG LRYVLFADKG VLQGLLTKKD VWSIVSGPGF HKDEALLERT
FTQPSAAEEV GLLDGDDGTS LASSIERRQS L
//
