ID W6PXR7_PENRF Unreviewed; 877 AA.
AC W6PXR7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN ORFNames=PROQFM164_S01g002849 {ECO:0000313|EMBL:CDM29038.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM29038.1};
RN [1] {ECO:0000313|EMBL:CDM29038.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM29038.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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; HG792015; CDM29038.1; -; Genomic_DNA.
DR AlphaFoldDB; W6PXR7; -.
DR STRING; 1365484.W6PXR7; -.
DR OMA; FLKINMT; -.
DR OrthoDB; 150430at2759; -.
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; 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; 2.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
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|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 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 110..131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 194..215
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 296..320
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 332..349
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 461..482
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 488..509
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 621..680
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 734..793
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 877 AA; 97221 MW; 6E429A7F4692DA73 CRC64;
MTSTRPSTTF NRSLSVSRER RSPRMPPSRS VPSPVDRRGD SDNQEAPAIP EEISGIKRYE
DFTTIDWVQD AVYEQSRRRA KRRSGTGFWD QEGILGWRRK MYESYDAGQA WLVVTLVGLA
IGLNSAVLNI ITEWLSDIKL GHCTTAFYLN ESFCCWGAEN GMFGRFYSAS CKLTFSIIGC
PEWKNWTSWW LLNYVFYFFG ALVLSSIAGV LVKSFAPYAA GSGISEIKCI IAGFVMKGFL
GAWTLLIKSI ALPLAIASGL SVGKEGPSVH FAVCTGNVIS RFFGKYKQNA SKTREILTAS
AAAGVAVAFG SPIGGVLFSL EEMANYFPLK TLWRSYFCAL VATSVLAAVN PFRTGQLVMF
QVEYDRTWHF FEFIFFIGLG VFGGLYGAFV MKWNLRMAAF RKKYLSQWPI TESVVLAGLT
AVLCYPNMFL KINMTAMMEI LFRECEGGHD YHGLCESKNR WSMVFSLAIA TVLRTVLVII
SYGCKVPAGI FVPSMAVGAS FGRMIGIMVQ ALHESFPQSA FFASCDPDVP CITPGTYAFL
GAGAALSGIM HLTISVTVIM FELTGALTYI LPTMIVVGVT KAVGDRFGSG GIADRMIWFN
GFPFLDNKED HVFNVPVSHA MTTGPLSVPA SDFPVREAEH LLNDNKFQGF PVVEDRTSKT
LVGYIGRTEL RYAIDRARNQ GMVAPNARCV FTKDAAEAAV ARRASVSHHS RSSDTFDAIQ
RSVGASFVDF SRYVDHTPLT VHPRHPLETV MEIFKKMGPR VILVEHRGKL IGLVTVKDCL
KYQFKVEAEE HTLAATSSSQ YSALGGQLNN PAPETLEDRL WRLIQTAAAF VSGKISRRPV
RPRDRTMPRQ PEHSDILEGR DDDAVVELED REDRPMI
//
