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Database: UniProt
Entry: C1GVL8_PARBA
LinkDB: C1GVL8_PARBA
Original site: C1GVL8_PARBA 
ID   C1GVL8_PARBA            Unreviewed;       923 AA.
AC   C1GVL8;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 2.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN   ORFNames=PAAG_02295 {ECO:0000313|EMBL:EEH40240.2};
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH40240.2, ECO:0000313|Proteomes:UP000002059};
RN   [1] {ECO:0000313|EMBL:EEH40240.2, ECO:0000313|Proteomes:UP000002059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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; KN293996; EEH40240.2; -; Genomic_DNA.
DR   RefSeq; XP_015701644.1; XM_015844596.1.
DR   AlphaFoldDB; C1GVL8; -.
DR   SMR; C1GVL8; -.
DR   STRING; 502779.C1GVL8; -.
DR   GeneID; 9098936; -.
DR   KEGG; pbl:PAAG_02295; -.
DR   VEuPathDB; FungiDB:PAAG_02295; -.
DR   eggNOG; KOG0475; Eukaryota.
DR   HOGENOM; CLU_003181_2_2_1; -.
DR   OMA; FLKINMT; -.
DR   OrthoDB; 150430at2759; -.
DR   Proteomes; UP000002059; Partially assembled 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000002059};
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        116..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        182..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        284..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        361..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        399..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        449..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   TRANSMEM        476..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361221"
FT   DOMAIN          609..668
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          759..816
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          681..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          863..907
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        681..734
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   923 AA;  101855 MW;  FB50A4C899A07C59 CRC64;
     MNPPGSYSSA HPQRPRSLSA RSRYPPTNNA RVHTSSTEAA RERRPTITAS RRPSIRDEIN
     EIKRYEDFTT IDWVQDAVHE QARRRAKRRD GLQFWDQEGT LGWRRKVSES YDAGQAWLVV
     TIVGAAIGLN AGFLSIVTEW LADIKLGHCE TGFYLNESFC CWGADDGCPE WRPWTSFAPL
     NYIAYFIFAV LFAFSSAVLV NSFAPYAAGS GISEIKVIIA GFIMKGFLGS RTLIIKSLTL
     PLAIASGLSV GKEGPSVHFA VCTGNVISRW FSKYTRNAAK TREILTATAG AGVAVAFGSP
     IGGVLFSLEE MASYFPLKTL WRSYFCALVA TGVLAAMNPF RTGQLVMFQV KYDRTWHSFE
     LIFFVLLGIF GGLYGAFVIK WNLRAQAFRK KYLSQHPIIE ATVLAGLTAL ICYPNMFLRI
     NMTEMMEILF RECEGAHDYN GICDTKNRWS MVLSLAIATT LRALLCIISY GCKVPAGIFV
     PSMAIGASFG RMVGILVQAL YERFPDSKFF ASCEPDVPCI TPGTYAFLGA GAALSGIMHL
     TISITIIMFE LTGALTYILP TMIVVGVTKA VSDSFGRGGI ADRMIWFNGF PFLDSKEDHI
     FNVPVSHAMT SKPAVLTATD FPVFEAEKLL RQHKYQGFPI VEDLTNNVVI GYIGRTELQY
     AINRAKREGL LSPNAKCRFT TAPSATSHRH RTTPSTNSLT LEISTARQGF GSSSSSSSRS
     DERNNTNIDT NADHRPPSRT FDDIATSTGI RSIDFSQYVD LAPLTVHPRL PLETVMEVFK
     KMGPRVILVE HRGRLSGLVT VKDCLKYQFK VEGRDGGGIG VGASANGGLG EGIIEQKAWE
     FIQWVTRKVM FWKTVAGEGG AQGRLRFSSR DGDGDLGGGQ RQGQRQGGRE PLRSRNSSDI
     IDGTEELDGF MELENRREGR ELL
//
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