ID A0A0D2E9L3_9EURO Unreviewed; 867 AA.
AC A0A0D2E9L3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN ORFNames=PV06_03094 {ECO:0000313|EMBL:KIW44639.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW44639.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW44639.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW44639.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) 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; KN847334; KIW44639.1; -; Genomic_DNA.
DR RefSeq; XP_016264855.1; XM_016403850.1.
DR AlphaFoldDB; A0A0D2E9L3; -.
DR STRING; 215243.A0A0D2E9L3; -.
DR GeneID; 27355168; -.
DR VEuPathDB; FungiDB:PV06_03094; -.
DR HOGENOM; CLU_003181_2_2_1; -.
DR OrthoDB; 150430at2759; -.
DR Proteomes; UP000053342; 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; 3.10.580.10; 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; PTHR45711; CHLORIDE CHANNEL PROTEIN; 1.
DR PANTHER; PTHR45711:SF6; CHLORIDE CHANNEL PROTEIN; 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|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:UP000053342};
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 136..157
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 215..236
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 320..344
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 397..415
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 436..452
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 521..543
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 587..611
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 768..823
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 94312 MW; 545A4AD753361BD9 CRC64;
MAPSDFDDGH HQLLSADAGA DISLSSPQQN LGTSSSTHQI TPDPVSSPSI TPSAEAGLPT
SDTRQPQSRN NGHGLKEELS SDWYVEGPGR RVGYDDLTAI DWIYEYTKER QRLRRLVALN
SGVVGQLRQL FEVSQIWLVL VATGISVGCV AAGINIASDW LSDIKTGYCK KGSGGGQFYL
NKQFCCWGHD DLSQCQDWTP WPAALGVGPA GGQYFISYIF FIVFAVLFAV SAGVLVQKYS
IYARHSGIPE IKTVLGGFVI RRFLGGWTLL AKSLGLCLSV SSGMWLGKEG PFVHLACCCA
NIIMKPFAAL SQNEARKREV LSAAAASGIS VAFGAPIGGV LFSLEQLSYY FPDKTMWQSF
VCAMVAAVTL QALNPFHTGK IALYQVTYTT IWHSFEIVPF VLLGITGGLF GGMFIKLNML
VSRMRKSQKY PLKERPLLEV LVVAAVSALV NFPNTFMRAQ LSELVYYLFA ECATIGNNDI
FGLCKATTAG ALSMLWLLIA ASVLGFLLAS ITFGLQIPAG IILPSLAIGA LYGRTVGVVM
ELIHKHFSTS LLFAACEPDV PCVIPGTYAI VGAASALAGV TRMTVSIVAI VFELTGALTY
VLPIMIAVML AKWIGDACST RGIYESWIQI NEYPYLDNKD DAAIPHVSVS GIMTRVEDMA
CLNGNQAYSI EKLRKLLRNT SFRGFPVVAF KDSAADAADM PSSPSHSPRE NTFLGYISRT
ELTFALDRVT NFTASARNSP AVTLQTPCYF NYHTDVISGH GVDLRPWMDQ TPITLNANSS
LQLAVHMFQN LGLRYLLFVD KGAFRGILTK KDVWWILSAT DDRRKRDEFV AGSGVLRGDV
DDDDGRDEAR GLLQQEDGGF EQQIAPT
//
